Copper
Explore a selection of our essential drug information below, or:
Identification
- Summary
Copper is a transition metal found in a variety of supplements and vitamins, including intravenous solutions for total parenteral nutrition (TPN).
- Brand Names
- Paragard T 380a, Vitafol-one
- Generic Name
- Copper
- DrugBank Accession Number
- DB09130
- Background
Copper is a transition metal and a trace element in the body. It is important to the function of many enzymes including cytochrome c oxidase, monoamine oxidase and superoxide dismutase Label. Copper is commonly used in contraceptive intrauterine devices (IUD) 5.
- Type
- Small Molecule
- Groups
- Approved, Investigational
- Structure
- Weight
- Average: 63.546
Monoisotopic: 62.929601079 - Chemical Formula
- Cu
- Synonyms
- cobre
- cuivre
- cuprum
- Kupfer
Pharmacology
- Indication
For use in the supplementation of total parenteral nutrition and in contraception with intrauterine devices Label 5.
Reduce drug development failure ratesBuild, train, & validate machine-learning modelswith evidence-based and structured datasets.Build, train, & validate predictive machine-learning models with structured datasets.- Associated Therapies
- Contraindications & Blackbox Warnings
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- Pharmacodynamics
Copper is incorporated into many enzymes throughout the body as an essential part of their function 2. Copper ions are known to reduce fertility when released from copper-containing IUDs 3.
- Mechanism of action
Copper is absorbed from the gut via high affinity copper uptake protein and likely through low affinity copper uptake protein and natural resistance-associated macrophage protein-2 4. It is believed that copper is reduced to the Cu1+ form prior to transport. Once inside the enterocyte, it is bound to copper transport protein ATOX1 which shuttles the ion to copper transporting ATPase-1 on the golgi membrane which take up copper into the golgi apparatus. Once copper has been secreted by enterocytes into the systemic circulation it remain largely bound by ceruloplasmin (65-90%), albumin (18%), and alpha 2-macroglobulin (12%).
Copper is an essential element in the body and is incorporated into many oxidase enzymes as a cofactor 2. It is also a component of zinc/copper super oxide dismutase, giving it an anti-oxidant role. Copper defiency occurs in Occipital Horn Syndrome and Menke's disease both of which are associated with impaired development of connective tissue due to the lack of copper to act as a cofactor in protein-lysine-6-oxidase. Menke's disease is also associated with progressive neurological impairment leading to death in infancy. The precise mechanisms of the effects of copper deficiency are vague due to the wide range of enzymes which use the ion as a cofactor.
Copper appears to reduce the viabilty and motility of spermatozoa 3. This reduces the likelihood of fertilization with a copper IUD, producing copper's contraceptive effect 3. The exact mechanism of copper's effect on sperm are unknown.
- Absorption
Copper absorption varies inversely with intake. Absorption range is 12-65%.
- Volume of distribution
Not Available
- Protein binding
Copper is nearly entirely bound by ceruloplasmin (65-90%), plasma albumin (18%), and alpha 2-macroglobulin (12%) 4.
- Metabolism
- Not Available
- Route of elimination
Copper appears to be eliminated primarily through bile 1.
- Half-life
Not Available
- Clearance
Not Available
- Adverse Effects
- Improve decision support & research outcomesWith structured adverse effects data, including: blackbox warnings, adverse reactions, warning & precautions, & incidence rates. View sample adverse effects data in our new Data Library!Improve decision support & research outcomes with our structured adverse effects data.
- Toxicity
Copper toxicity is belevied to be due to fenton-type redox reactions occuring with high copper concentrations which produce damaging reactive oxygen species 1.
- Pathways
- Not Available
- Pharmacogenomic Effects/ADRs
- Not Available
Interactions
- Drug Interactions
- This information should not be interpreted without the help of a healthcare provider. If you believe you are experiencing an interaction, contact a healthcare provider immediately. The absence of an interaction does not necessarily mean no interactions exist.
Drug Interaction Integrate drug-drug
interactions in your softwareConjugated estrogens Conjugated estrogens can cause an increase in the absorption of Copper resulting in an increased serum concentration and potentially a worsening of adverse effects. Dienestrol Dienestrol can cause an increase in the absorption of Copper resulting in an increased serum concentration and potentially a worsening of adverse effects. Estradiol Estradiol can cause an increase in the absorption of Copper resulting in an increased serum concentration and potentially a worsening of adverse effects. Estradiol acetate Estradiol acetate can cause an increase in the absorption of Copper resulting in an increased serum concentration and potentially a worsening of adverse effects. Estriol Estriol can cause an increase in the absorption of Copper resulting in an increased serum concentration and potentially a worsening of adverse effects. - Food Interactions
- No interactions found.
Products
- Drug product information from 10+ global regionsOur datasets provide approved product information including:dosage, form, labeller, route of administration, and marketing period.Access drug product information from over 10 global regions.
- Active Moieties
Name Kind UNII CAS InChI Key Cupric oxide unknown V1XJQ704R4 1317-38-0 KKCXRELNMOYFLS-UHFFFAOYSA-N - Brand Name Prescription Products
Name Dosage Strength Route Labeller Marketing Start Marketing End Region Image ParaGard T 380A Intrauterine device 313.4 mg/1 Intrauterine CooperSurgical, Inc. 2017-11-02 Not applicable US ParaGard T 380A Intrauterine device 313.4 mg/1 Intrauterine CooperSurgical, Inc. 2024-08-15 Not applicable US ParaGard T 380A Intrauterine device 313.4 mg/1 Intrauterine Teva Women's Health 2004-01-01 2024-04-30 US ParaGard T380A Intrauterine device 311 mg/1 Intrauterine Duramed Pharmaceuticals, Inc. 2007-08-04 2007-08-04 US - Over the Counter Products
Name Dosage Strength Route Labeller Marketing Start Marketing End Region Image Antibacterial PVC film Film 0.3 g/100g Topical DH Investment Co Ltd 2020-06-27 Not applicable US Chela Copper Tab 3mg Tablet 3 mg / tab Oral Nu Life Nutrition Ltd. 1986-12-31 2000-03-03 Canada Chelated Copper Supplement - Tab 2mg Tablet 2 mg / tab Oral Albion 1996-09-06 2001-09-07 Canada Chelazome Copper Cap 5mg Capsule 5 mg Oral Trophic Canada Ltd. 1987-12-31 2008-08-29 Canada Copper Chelate - 5mg Tab Tablet 5 mg Oral Professional Health Products 1995-12-31 2010-05-10 Canada - Mixture Products
Name Ingredients Dosage Route Labeller Marketing Start Marketing End Region Image 24 Multivitamins + Minerals Copper (1 mg) + Ascorbic acid (150 mg) + Beta carotene (10000 unit) + Biotin (25 mcg) + Calcium (130 mg) + Cholecalciferol (400 unit) + Choline bitartrate (25 mg) + Chromium (20 mcg) + Cyanocobalamin (25 mcg) + Ferrous fumarate (15 mg) + Folic acid (.8 mg) + Inositol (25 mg) + Magnesium (65 mg) + Manganese cation (2 mg) + Molybdenum (20 mcg) + Niacin (25 mg) + Calcium pantothenate (25 mg) + Potassium (15 mg) + Potassium Iodide (.1 mg) + Pyridoxine hydrochloride (25 mg) + Racemethionine (25 mg) + Riboflavin (25 mg) + Selenium (20 mcg) + Thiamine hydrochloride (25 mg) + Vanadium (20 mcg) + Vitamin A palmitate (5000 unit) + Vitamin E (50 unit) + Zinc (10 mg) Tablet Oral Stanley Pharmaceuticals, A Division Of Vita Health Products Inc. 1997-04-30 2002-07-31 Canada 4Life Targeted Vitamin & Mineral Complex Capsule Copper (0.5 mg) + Ascorbic acid (50.76 mg) + Beta carotene (630 IU) + Chromium (0.07 mg) + Cyanocobalamin (0.002 mg) + Folic acid (0.1 mg) + Magnesium (46.4 mg) + Niacin (5 mg) + Potassium (12.5 mg) + Pyridoxine (0.5 mg) + Selenium (0.013 mg) + Vanadium (0.15 mg) + Vitamin E (25.5 IU) + Zinc (2.5 mg) Capsule Oral Forlife Research Imports Sdn. Bhd. 2020-09-08 Not applicable Malaysia 50 Plus Multiple Vitamins & Minerals Copper (2 mg) + Ascorbic acid (90 mg) + Biotin (45 mcg) + Calcium (200 mg) + Cholecalciferol (400 unit) + Chromium (10 mcg) + Cyanocobalamin (25 mcg) + Folic acid (0.4 mg) + Magnesium (100 mg) + Manganese cation (5 mg) + Molybdenum (25 mcg) + Nicotinamide (40 mg) + Pantothenic acid (10 mg) + Potassium Iodide (0.15 mg) + Pyridoxine hydrochloride (3 mg) + Riboflavin (3.2 mg) + Selenium (25 mcg) + Thiamine mononitrate (2.25 mg) + Vanadium (10 mcg) + Vitamin A palmitate (6000 unit) + Zinc (15 mg) Tablet Oral Gfr Pharma Ltd. 2002-10-20 2004-06-15 Canada A.R.T.H. Away Formula Copper (0.232 mg) + Calcium (24 mg) + Cholecalciferol (45 unit) + Folic acid (0.025 mg) + Manganese cation (0.58 mg) + Pyridoxine hydrochloride (0.5 mg) + Selenium (1.54 mcg) + Zinc (0.63 mg) Capsule Oral Abundance Naturally Ltd 1999-02-01 2006-06-16 Canada A/o-26 - Caplet Copper (1 mg) + Beta carotene (7500 unit) + Calcium (75 mg) + Calcium ascorbate (250 mg) + DL-alpha tocopheryl acetate (100 unit) + Folic acid (.4 mg) + Manganese cation (2.5 mg) + Racemethionine (50 mg) + Selenium (100 mcg) + Zinc (7.5 mg) Tablet Oral Enviro Tech International Canada 1996-12-19 1999-07-26 Canada - Unapproved/Other Products
Name Ingredients Dosage Route Labeller Marketing Start Marketing End Region Image Antibacterial PVC film Copper (0.3 g/100g) Film Topical DH Investment Co Ltd 2020-06-27 Not applicable US Cavan-EC SOD DHA Copper (2 mg/1) + Ascorbic acid (130 mg/1) + Beta carotene (3000 [iU]/1) + Calcium (230 mg/1) + Cholecalciferol (410 [iU]/1) + Cyanocobalamin (12 ug/1) + Folic acid (1 mg/1) + Magnesium (25 mg/1) + Nicotinamide (20 mg/1) + Omega-3 fatty acids (440 mg/1) + Pyridoxine hydrochloride (28 mg/1) + Riboflavin (4 mg/1) + Sodium feredetate (30 mg/1) + Thiamine mononitrate (1.8 mg/1) + Vitamin E (30 mg/1) + Zinc (26 mg/1) Kit Oral Seton Pharmaceuticals 2010-01-10 2014-07-15 US CitraNatal Assure Copper (2 mg/1) + Ascorbic acid (120 mg/1) + Calcium citrate tetrahydrate (125 mg/1) + Cholecalciferol (400 [iU]/1) + Doconexent (300 mg/1) + Docusate sodium (50 mg/1) + Folic acid (1 mg/1) + Icosapent (0.75 mg/1) + Iodine (150 ug/1) + Iron (35 mg/1) + Nicotinamide (20 mg/1) + Pyridoxine hydrochloride (25 mg/1) + Riboflavin (3.4 mg/1) + Thiamine chloride (3 mg/1) + Vitamin E (30 [iU]/1) + Zinc (25 mg/1) Kit Oral Mission Pharmacal 2008-11-19 Not applicable US CitraNatal Assure Copper (2 mg/1) + Ascorbic acid (120 mg/1) + Calcium citrate tetrahydrate (124 mg/1) + Cholecalciferol (400 [iU]/1) + Doconexent (300 mg/1) + Docusate sodium (50 mg/1) + Folic acid (1 mg/1) + Icosapent (0.75 mg/1) + Iodine (150 ug/1) + Iron (35 mg/1) + Nicotinamide (20 mg/1) + Pyridoxine hydrochloride (25 mg/1) + Riboflavin (3.4 mg/1) + Thiamine chloride (3 mg/1) + Vitamin E (30 [iU]/1) + Zinc (25 mg/1) Capsule; Kit; Tablet, coated Oral Mission Pharmacal Company 2014-04-30 Not applicable US CitraNatal Essence Copper (2 mg/1) + Ascorbic acid (120 mg/1) + Calcium citrate tetrahydrate (140 mg/1) + Cholecalciferol (400 [iU]/1) + Doconexent (300 mg/1) + Folic acid (1 mg/1) + Icosapent (0.75 mg/1) + Iodine (150 ug/1) + Iron (35 mg/1) + Nicotinamide (20 mg/1) + Pyridoxine hydrochloride (25 mg/1) + Riboflavin (3.4 mg/1) + Thiamine chloride (3 mg/1) + Vitamin E (30 [iU]/1) + Zinc (25 mg/1) Kit Oral Mission Pharmacal Company 2020-07-07 Not applicable US
Categories
- Drug Categories
- Chemical TaxonomyProvided by Classyfire
- Description
- This compound belongs to the class of inorganic compounds known as homogeneous transition metal compounds. These are inorganic compounds containing only metal atoms,with the largest atom being a transition metal atom.
- Kingdom
- Inorganic compounds
- Super Class
- Homogeneous metal compounds
- Class
- Homogeneous transition metal compounds
- Sub Class
- Not Available
- Direct Parent
- Homogeneous transition metal compounds
- Alternative Parents
- Not Available
- Substituents
- Homogeneous transition metal
- Molecular Framework
- Not Available
- External Descriptors
- elemental copper (CHEBI:30052)
- Affected organisms
- Not Available
Chemical Identifiers
- UNII
- 789U1901C5
- CAS number
- 7440-50-8
- InChI Key
- RYGMFSIKBFXOCR-UHFFFAOYSA-N
- InChI
- InChI=1S/Cu
- IUPAC Name
- copper
- SMILES
- [Cu]
References
- General References
- Bost M, Houdart S, Oberli M, Kalonji E, Huneau JF, Margaritis I: Dietary copper and human health: Current evidence and unresolved issues. J Trace Elem Med Biol. 2016 May;35:107-15. doi: 10.1016/j.jtemb.2016.02.006. Epub 2016 Mar 5. [Article]
- Tapiero H, Townsend DM, Tew KD: Trace elements in human physiology and pathology. Copper. Biomed Pharmacother. 2003 Nov;57(9):386-98. [Article]
- Ortiz ME, Croxatto HB: Copper-T intrauterine device and levonorgestrel intrauterine system: biological bases of their mechanism of action. Contraception. 2007 Jun;75(6 Suppl):S16-30. Epub 2007 Mar 29. [Article]
- van den Berghe PV, Klomp LW: New developments in the regulation of intestinal copper absorption. Nutr Rev. 2009 Nov;67(11):658-72. doi: 10.1111/j.1753-4887.2009.00250.x. [Article]
- Product Monograph: Copper IUD [Link]
- External Links
- FDA label
- Download (139 KB)
- MSDS
- Download (107 KB)
Clinical Trials
- Clinical Trials
Clinical Trial & Rare Diseases Add-on Data Package
Explore 4,000+ rare diseases, orphan drugs & condition pairs, clinical trial why stopped data, & more. Preview package Phase Status Purpose Conditions Count Start Date Why Stopped 100+ additional columns Unlock 175K+ rows when you subscribe.View sample dataNot Available Active Not Recruiting Not Available Contraception / Contraceptive implant therapy / Emergency Contraception / IUD therapy 1 somestatus stop reason just information to hide Not Available Active Not Recruiting Diagnostic Breast Cancer / Colon Cancer / Extrahepatic Bile Duct Cancer / Gallbladder Cancer / Gastrointestinal Tract Cancer / Liver and Intrahepatic Biliary Tract Cancer / Lung Cancer / Metastatic Cancer / Pancreatic Cancer / Rectal Cancer / Thyroid Gland Medullary Carcinoma / Unspecified Adult Solid Tumor, Protocol Specific 1 somestatus stop reason just information to hide Not Available Completed Not Available Contraception 1 somestatus stop reason just information to hide Not Available Completed Not Available Coronavirus Disease 2019 (COVID‑19) 1 somestatus stop reason just information to hide Not Available Completed Not Available Emergency Contraception 1 somestatus stop reason just information to hide
Pharmacoeconomics
- Manufacturers
- Not Available
- Packagers
- Not Available
- Dosage Forms
Form Route Strength Injection, solution, concentrate Intravenous Film Topical 0.3 g/100g Tablet Oral 3 mg / tab Tablet Oral 2 mg / tab Capsule Oral 5 mg Capsule; kit; tablet, coated Oral Kit Oral Tablet Oral 5 mg Tablet, chewable Oral Tablet, film coated Oral Tablet, effervescent Oral Liquid Oral Liquid Intravenous Tablet Oral Capsule Oral Intrauterine device Intrauterine 313.4 mg/1 Intrauterine device Intrauterine 311 mg/1 Capsule, coated Oral Capsule, gelatin coated Oral Capsule Tablet, coated Oral Tablet, extended release Oral Powder, for solution Oral Tablet Capsule, liquid filled; kit Oral Capsule, liquid filled Oral Powder Oral - Prices
- Not Available
- Patents
- Not Available
Properties
- State
- Solid
- Experimental Properties
Property Value Source melting point (°C) 1083 MSDS boiling point (°C) 2597 MSDS water solubility 8.96g/mL MSDS - Predicted Properties
Property Value Source Water Solubility 0.0 mg/mL ALOGPS logP -1.3 ALOGPS logP 0.16 Chemaxon logS 1.08 ALOGPS Physiological Charge 0 Chemaxon Hydrogen Acceptor Count 0 Chemaxon Hydrogen Donor Count 0 Chemaxon Polar Surface Area 0 Å2 Chemaxon Rotatable Bond Count 0 Chemaxon Refractivity 0 m3·mol-1 Chemaxon Polarizability 1.78 Å3 Chemaxon Number of Rings 0 Chemaxon Bioavailability 1 Chemaxon Rule of Five Yes Chemaxon Ghose Filter No Chemaxon Veber's Rule Yes Chemaxon MDDR-like Rule No Chemaxon - Predicted ADMET Features
- Not Available
Spectra
- Mass Spec (NIST)
- Not Available
- Spectra
- Not Available
- Chromatographic Properties
Collision Cross Sections (CCS)
Not Available
Targets
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Binder
- General Function
- Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis (PubMed:25122912). Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(o) and JIP. Inhibits G(o) alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity). By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapses in axons (PubMed:17062754, PubMed:23011729). Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1
- Specific Function
- DNA binding
- Gene Name
- APP
- Uniprot ID
- P05067
- Uniprot Name
- Amyloid-beta precursor protein
- Molecular Weight
- 86942.715 Da
References
- Tapiero H, Townsend DM, Tew KD: Trace elements in human physiology and pathology. Copper. Biomed Pharmacother. 2003 Nov;57(9):386-98. [Article]
- Suzuki K, Miura T, Takeuchi H: Inhibitory effect of copper(II) on zinc(II)-induced aggregation of amyloid beta-peptide. Biochem Biophys Res Commun. 2001 Jul 27;285(4):991-6. [Article]
- White AR, Multhaup G, Galatis D, McKinstry WJ, Parker MW, Pipkorn R, Beyreuther K, Masters CL, Cappai R: Contrasting, species-dependent modulation of copper-mediated neurotoxicity by the Alzheimer's disease amyloid precursor protein. J Neurosci. 2002 Jan 15;22(2):365-76. [Article]
- Hesse L, Beher D, Masters CL, Multhaup G: The beta A4 amyloid precursor protein binding to copper. FEBS Lett. 1994 Jul 25;349(1):109-16. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Allosteric modulator
- General Function
- Catalyzes the hydrolysis of S-adenosyl-L-homocysteine to form adenosine and homocysteine (PubMed:10933798). Binds copper ions (By similarity)
- Specific Function
- adenosylhomocysteinase activity
- Gene Name
- AHCY
- Uniprot ID
- P23526
- Uniprot Name
- Adenosylhomocysteinase
- Molecular Weight
- 47715.715 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling
- Specific Function
- DNA binding
- Gene Name
- H2BC4
- Uniprot ID
- P62807
- Uniprot Name
- Histone H2B type 1-C/E/F/G/I
- Molecular Weight
- 13906.035 Da
References
- She YM, Narindrasorasak S, Yang S, Spitale N, Roberts EA, Sarkar B: Identification of metal-binding proteins in human hepatoma lines by immobilized metal affinity chromatography and mass spectrometry. Mol Cell Proteomics. 2003 Dec;2(12):1306-18. Epub 2003 Oct 7. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively (PubMed:11724794, PubMed:3170585). Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate (PubMed:11724794, PubMed:3170585). Modulates the organization and assembly of the cytoskeleton (By similarity). Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (By similarity). Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes (PubMed:23071094). Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation (PubMed:23071094). Also plays a role in innate immunity by promoting TNF-induced NF-kappa-B activation and type I interferon production, via interaction with TRAF2 and TRAF3, respectively (PubMed:23332158, PubMed:27387501). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis (By similarity). Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity)
- Specific Function
- aspartic-type endopeptidase inhibitor activity
- Gene Name
- GAPDH
- Uniprot ID
- P04406
- Uniprot Name
- Glyceraldehyde-3-phosphate dehydrogenase
- Molecular Weight
- 36053.0 Da
References
- She YM, Narindrasorasak S, Yang S, Spitale N, Roberts EA, Sarkar B: Identification of metal-binding proteins in human hepatoma lines by immobilized metal affinity chromatography and mass spectrometry. Mol Cell Proteomics. 2003 Dec;2(12):1306-18. Epub 2003 Oct 7. [Article]
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and farnesyl pyrophosphate kinase, histidine protein kinase and 3'-5' exonuclease activities. Involved in cell proliferation, differentiation and development, signal transduction, G protein-coupled receptor endocytosis, and gene expression. Required for neural development including neural patterning and cell fate determination. During GZMA-mediated cell death, works in concert with TREX1. NME1 nicks one strand of DNA and TREX1 removes bases from the free 3' end to enhance DNA damage and prevent DNA end reannealing and rapid repair
- Specific Function
- 3'-5' exonuclease activity
- Gene Name
- NME1
- Uniprot ID
- P15531
- Uniprot Name
- Nucleoside diphosphate kinase A
- Molecular Weight
- 17148.635 Da
References
- She YM, Narindrasorasak S, Yang S, Spitale N, Roberts EA, Sarkar B: Identification of metal-binding proteins in human hepatoma lines by immobilized metal affinity chromatography and mass spectrometry. Mol Cell Proteomics. 2003 Dec;2(12):1306-18. Epub 2003 Oct 7. [Article]
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity)
- Specific Function
- chromatin DNA binding
- Gene Name
- H1-4
- Uniprot ID
- P10412
- Uniprot Name
- Histone H1.4
- Molecular Weight
- 21865.02 Da
References
- She YM, Narindrasorasak S, Yang S, Spitale N, Roberts EA, Sarkar B: Identification of metal-binding proteins in human hepatoma lines by immobilized metal affinity chromatography and mass spectrometry. Mol Cell Proteomics. 2003 Dec;2(12):1306-18. Epub 2003 Oct 7. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2) (PubMed:9497357). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity)
- Specific Function
- cadherin binding
- Gene Name
- PRDX1
- Uniprot ID
- Q06830
- Uniprot Name
- Peroxiredoxin-1
- Molecular Weight
- 22110.19 Da
References
- She YM, Narindrasorasak S, Yang S, Spitale N, Roberts EA, Sarkar B: Identification of metal-binding proteins in human hepatoma lines by immobilized metal affinity chromatography and mass spectrometry. Mol Cell Proteomics. 2003 Dec;2(12):1306-18. Epub 2003 Oct 7. [Article]
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- S100A8 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. It can induce neutrophil chemotaxis and adhesion. Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions. The intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase. Participates also in regulatory T-cell differentiation together with CD69 (PubMed:26296369). Activates NADPH-oxidase by facilitating the enzyme complex assembly at the cell membrane, transferring arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX. The extracellular functions involve pro-inflammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities. Its pro-inflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER). Binding to TLR4 and AGER activates the MAP-kinase and NF-kappa-B signaling pathways resulting in the amplification of the pro-inflammatory cascade. Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth. Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3. Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK. Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants. Can act as a potent amplifier of inflammation in autoimmunity as well as in cancer development and tumor spread. The iNOS-S100A8/A9 transnitrosylase complex directs selective inflammatory stimulus-dependent S-nitrosylation of GAPDH and probably multiple targets such as ANXA5, EZR, MSN and VIM by recognizing a [IL]-x-C-x-x-[DE] motif; S100A8 seems to contribute to S-nitrosylation site selectivity
- Specific Function
- arachidonic acid binding
- Gene Name
- S100A8
- Uniprot ID
- P05109
- Uniprot Name
- Protein S100-A8
- Molecular Weight
- 10834.43 Da
References
- She YM, Narindrasorasak S, Yang S, Spitale N, Roberts EA, Sarkar B: Identification of metal-binding proteins in human hepatoma lines by immobilized metal affinity chromatography and mass spectrometry. Mol Cell Proteomics. 2003 Dec;2(12):1306-18. Epub 2003 Oct 7. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement membrane and in the consequent activation of signaling transduction pathways. May play a role in cell fate determination and tissue morphogenesis. Acts as a PPP1R16B-dependent substrate of PPP1CA
- Specific Function
- DNA binding
- Gene Name
- RPSA
- Uniprot ID
- P08865
- Uniprot Name
- Small ribosomal subunit protein uS2
- Molecular Weight
- 32853.79 Da
References
- She YM, Narindrasorasak S, Yang S, Spitale N, Roberts EA, Sarkar B: Identification of metal-binding proteins in human hepatoma lines by immobilized metal affinity chromatography and mass spectrometry. Mol Cell Proteomics. 2003 Dec;2(12):1306-18. Epub 2003 Oct 7. [Article]
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. May play a role in the repair of noise-induced stereocilia gaps thereby maintains hearing sensitivity following loud noise damage (By similarity)
- Specific Function
- ATP binding
- Gene Name
- ACTG1
- Uniprot ID
- P63261
- Uniprot Name
- Actin, cytoplasmic 2
- Molecular Weight
- 41792.48 Da
References
- She YM, Narindrasorasak S, Yang S, Spitale N, Roberts EA, Sarkar B: Identification of metal-binding proteins in human hepatoma lines by immobilized metal affinity chromatography and mass spectrometry. Mol Cell Proteomics. 2003 Dec;2(12):1306-18. Epub 2003 Oct 7. [Article]
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Glycolytic enzyme the catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate (PubMed:1369209, PubMed:29775581). In addition to glycolysis, involved in various processes such as growth control, hypoxia tolerance and allergic responses (PubMed:10802057, PubMed:12666133, PubMed:2005901, PubMed:29775581). May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons (PubMed:12666133). Stimulates immunoglobulin production (PubMed:1369209)
- Specific Function
- cadherin binding
- Gene Name
- ENO1
- Uniprot ID
- P06733
- Uniprot Name
- Alpha-enolase
- Molecular Weight
- 47168.555 Da
References
- She YM, Narindrasorasak S, Yang S, Spitale N, Roberts EA, Sarkar B: Identification of metal-binding proteins in human hepatoma lines by immobilized metal affinity chromatography and mass spectrometry. Mol Cell Proteomics. 2003 Dec;2(12):1306-18. Epub 2003 Oct 7. [Article]
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Translation elongation factor that catalyzes the GTP-dependent binding of aminoacyl-tRNA (aa-tRNA) to the A-site of ribosomes during the elongation phase of protein synthesis (PubMed:26593721, PubMed:26651998, PubMed:36123449, PubMed:36264623, PubMed:36638793). Base pairing between the mRNA codon and the aa-tRNA anticodon promotes GTP hydrolysis, releasing the aa-tRNA from EEF1A1 and allowing its accommodation into the ribosome (PubMed:26593721, PubMed:26651998, PubMed:36123449, PubMed:36264623, PubMed:36638793). The growing protein chain is subsequently transferred from the P-site peptidyl tRNA to the A-site aa-tRNA, extending it by one amino acid through ribosome-catalyzed peptide bond formation (PubMed:26593721, PubMed:26651998, PubMed:36123449, PubMed:36264623). Also plays a role in the positive regulation of IFNG transcription in T-helper 1 cells as part of an IFNG promoter-binding complex with TXK and PARP1 (PubMed:17177976)
- Specific Function
- GTP binding
- Gene Name
- EEF1A1
- Uniprot ID
- P68104
- Uniprot Name
- Elongation factor 1-alpha 1
- Molecular Weight
- 50140.565 Da
References
- She YM, Narindrasorasak S, Yang S, Spitale N, Roberts EA, Sarkar B: Identification of metal-binding proteins in human hepatoma lines by immobilized metal affinity chromatography and mass spectrometry. Mol Cell Proteomics. 2003 Dec;2(12):1306-18. Epub 2003 Oct 7. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Together with KRT19, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle
- Specific Function
- protein-containing complex binding
- Gene Name
- KRT8
- Uniprot ID
- P05787
- Uniprot Name
- Keratin, type II cytoskeletal 8
- Molecular Weight
- 53703.76 Da
References
- She YM, Narindrasorasak S, Yang S, Spitale N, Roberts EA, Sarkar B: Identification of metal-binding proteins in human hepatoma lines by immobilized metal affinity chromatography and mass spectrometry. Mol Cell Proteomics. 2003 Dec;2(12):1306-18. Epub 2003 Oct 7. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations and following phosphorylation by FAM20C, functions as a chaperone that inhibits aggregation of misfolded proteins (PubMed:32149426). At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts as a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307)
- Specific Function
- actin binding
- Gene Name
- P4HB
- Uniprot ID
- P07237
- Uniprot Name
- Protein disulfide-isomerase
- Molecular Weight
- 57115.795 Da
References
- She YM, Narindrasorasak S, Yang S, Spitale N, Roberts EA, Sarkar B: Identification of metal-binding proteins in human hepatoma lines by immobilized metal affinity chromatography and mass spectrometry. Mol Cell Proteomics. 2003 Dec;2(12):1306-18. Epub 2003 Oct 7. [Article]
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Protein disulfide isomerase that catalyzes the formation, isomerization, and reduction or oxidation of disulfide bonds in client proteins and functions as a protein folding chaperone (PubMed:11825568, PubMed:16193070, PubMed:27897272, PubMed:36104323, PubMed:7487104). Core component of the major histocompatibility complex class I (MHC I) peptide loading complex where it functions as an essential folding chaperone for TAPBP. Through TAPBP, assists the dynamic assembly of the MHC I complex with high affinity antigens in the endoplasmic reticulum. Therefore, plays a crucial role in the presentation of antigens to cytotoxic T cells in adaptive immunity (PubMed:35948544, PubMed:36104323)
- Specific Function
- cysteine-type endopeptidase activity
- Gene Name
- PDIA3
- Uniprot ID
- P30101
- Uniprot Name
- Protein disulfide-isomerase A3
- Molecular Weight
- 56781.84 Da
References
- She YM, Narindrasorasak S, Yang S, Spitale N, Roberts EA, Sarkar B: Identification of metal-binding proteins in human hepatoma lines by immobilized metal affinity chromatography and mass spectrometry. Mol Cell Proteomics. 2003 Dec;2(12):1306-18. Epub 2003 Oct 7. [Article]
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (PubMed:11422376, PubMed:1346131). The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable)
- Specific Function
- apolipoprotein A-I binding
- Gene Name
- HSPD1
- Uniprot ID
- P10809
- Uniprot Name
- 60 kDa heat shock protein, mitochondrial
- Molecular Weight
- 61054.17 Da
References
- She YM, Narindrasorasak S, Yang S, Spitale N, Roberts EA, Sarkar B: Identification of metal-binding proteins in human hepatoma lines by immobilized metal affinity chromatography and mass spectrometry. Mol Cell Proteomics. 2003 Dec;2(12):1306-18. Epub 2003 Oct 7. [Article]
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Has peptide-independent ATPase activity
- Specific Function
- ATP binding
- Gene Name
- HSPA13
- Uniprot ID
- P48723
- Uniprot Name
- Heat shock 70 kDa protein 13
- Molecular Weight
- 51927.08 Da
References
- She YM, Narindrasorasak S, Yang S, Spitale N, Roberts EA, Sarkar B: Identification of metal-binding proteins in human hepatoma lines by immobilized metal affinity chromatography and mass spectrometry. Mol Cell Proteomics. 2003 Dec;2(12):1306-18. Epub 2003 Oct 7. [Article]
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (PubMed:2294010, PubMed:23769672, PubMed:23990668, PubMed:28332555). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (PubMed:1550958, PubMed:19538957). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1 (By similarity). Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent activation of ERN1/IRE1 (By similarity). Plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). May function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. Appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. May also play a role in apoptosis and cell proliferation (PubMed:26045166)
- Specific Function
- ATP binding
- Gene Name
- HSPA5
- Uniprot ID
- P11021
- Uniprot Name
- Endoplasmic reticulum chaperone BiP
- Molecular Weight
- 72332.425 Da
References
- She YM, Narindrasorasak S, Yang S, Spitale N, Roberts EA, Sarkar B: Identification of metal-binding proteins in human hepatoma lines by immobilized metal affinity chromatography and mass spectrometry. Mol Cell Proteomics. 2003 Dec;2(12):1306-18. Epub 2003 Oct 7. [Article]
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Molecular chaperone that functions in the processing and transport of secreted proteins (By similarity). When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD) (PubMed:18264092). Has ATPase activity (By similarity). May participate in the unfolding of cytosolic leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1 to facilitate their translocation into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) and secretion; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059)
- Specific Function
- ATP binding
- Gene Name
- HSP90B1
- Uniprot ID
- P14625
- Uniprot Name
- Endoplasmin
- Molecular Weight
- 92468.06 Da
References
- She YM, Narindrasorasak S, Yang S, Spitale N, Roberts EA, Sarkar B: Identification of metal-binding proteins in human hepatoma lines by immobilized metal affinity chromatography and mass spectrometry. Mol Cell Proteomics. 2003 Dec;2(12):1306-18. Epub 2003 Oct 7. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation
- Specific Function
- enzyme binding
- Gene Name
- TF
- Uniprot ID
- P02787
- Uniprot Name
- Serotransferrin
- Molecular Weight
- 77049.175 Da
References
- She YM, Narindrasorasak S, Yang S, Spitale N, Roberts EA, Sarkar B: Identification of metal-binding proteins in human hepatoma lines by immobilized metal affinity chromatography and mass spectrometry. Mol Cell Proteomics. 2003 Dec;2(12):1306-18. Epub 2003 Oct 7. [Article]
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Luo LZ, Jin HW, Huang L, Huang HQ: Different binding affinities of Pb2+ and Cu2+ to glycosylation variants of human serum transferrin interfere with the detection of carbohydrate-deficient transferrin. Biol Trace Elem Res. 2011 Dec;144(1-3):487-95. doi: 10.1007/s12011-011-9150-6. Epub 2011 Jul 27. [Article]
- Kind
- Protein
- Organism
- Mouse
- Pharmacological action
- Unknown
- General Function
- Plays a role in the maintenance of the appropriate processing of 47S/45S pre-rRNA to 32S/30S pre-rRNAs and their subsequent processing to produce 18S and 28S rRNAs (By similarity). Also acts at the level of transcription regulation. Along with PRMT5, binds embryonic globin promoter (By similarity). Represses the expression of embryonic globin Hbb-y gene (PubMed:25092918). In neuroblastoma cells, may also repress the expression of oxidative stress genes, including CHAC1, HMOX1, SLC7A11, ULBP1 and that encoding the small nucleolar RNA SNORD41 (By similarity). Preferentially binds to a DNA motif containing 5'-GGTTAT-3' (By similarity). Negatively regulates the antiviral innate immune response by targeting IRF3 and impairing its DNA-binding activity (By similarity). In addition, inhibits NF-kappa-B-mediated expression of pro-inflammatory cytokines (By similarity). Stimulates phagocytosis of photoreceptor outer segments by retinal pigment epithelial cells (PubMed:25735755). Prevents NCL self-cleavage, maintaining a normal steady-state level of NCL protein in undifferentiated embryonic stem cells (ESCs), which in turn is essential for ESC self-renewal (PubMed:19489080).
- Specific Function
- DNA binding
- Gene Name
- Lyar
- Uniprot ID
- Q08288
- Uniprot Name
- Cell growth-regulating nucleolar protein
- Molecular Weight
- 43735.435 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399). The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules (PubMed:23636399). The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain (PubMed:23636399). The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:23636399). Plays a role in the assembly and function of the 40S ribosomal subunit (By similarity). Mutations in this protein affects the control of translational fidelity (By similarity). Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly (By similarity)
- Specific Function
- cadherin binding
- Gene Name
- RPS2
- Uniprot ID
- P15880
- Uniprot Name
- Small ribosomal subunit protein uS5
- Molecular Weight
- 31324.22 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Plays a role in preventing exon skipping, ensuring the accuracy of splicing and regulating alternative splicing. Interacts with other spliceosomal components, via the RS domains, to form a bridge between the 5'- and 3'-splice site binding components, U1 snRNP and U2AF. Can stimulate binding of U1 snRNP to a 5'-splice site-containing pre-mRNA. Binds to purine-rich RNA sequences, either the octamer, 5'-RGAAGAAC-3' (r=A or G) or the decamers, AGGACAGAGC/AGGACGAAGC. Binds preferentially to the 5'-CGAGGCG-3' motif in vitro. Three copies of the octamer constitute a powerful splicing enhancer in vitro, the ASF/SF2 splicing enhancer (ASE) which can specifically activate ASE-dependent splicing. Isoform ASF-2 and isoform ASF-3 act as splicing repressors. May function as export adapter involved in mRNA nuclear export through the TAP/NXF1 pathway
- Specific Function
- DNA topoisomerase binding
- Gene Name
- SRSF1
- Uniprot ID
- Q07955
- Uniprot Name
- Serine/arginine-rich splicing factor 1
- Molecular Weight
- 27744.335 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Heterogeneous nuclear ribonucleoprotein (hnRNP) that associates with nascent pre-mRNAs, packaging them into hnRNP particles. The hnRNP particle arrangement on nascent hnRNA is non-random and sequence-dependent and serves to condense and stabilize the transcripts and minimize tangling and knotting. Packaging plays a role in various processes such as transcription, pre-mRNA processing, RNA nuclear export, subcellular location, mRNA translation and stability of mature mRNAs (PubMed:19099192). Forms hnRNP particles with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus. Involved in transport of specific mRNAs to the cytoplasm in oligodendrocytes and neurons: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) or the A2RE11 (derivative 11 nucleotide oligonucleotide) sequence motifs present on some mRNAs, and promotes their transport to the cytoplasm (PubMed:10567417). Specifically binds single-stranded telomeric DNA sequences, protecting telomeric DNA repeat against endonuclease digestion (By similarity). Also binds other RNA molecules, such as primary miRNA (pri-miRNAs): acts as a nuclear 'reader' of the N6-methyladenosine (m6A) mark by specifically recognizing and binding a subset of nuclear m6A-containing pri-miRNAs. Binding to m6A-containing pri-miRNAs promotes pri-miRNA processing by enhancing binding of DGCR8 to pri-miRNA transcripts (PubMed:26321680). Involved in miRNA sorting into exosomes following sumoylation, possibly by binding (m6A)-containing pre-miRNAs (PubMed:24356509). Acts as a regulator of efficiency of mRNA splicing, possibly by binding to m6A-containing pre-mRNAs (PubMed:26321680). Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (PubMed:20010808). Also plays a role in the activation of the innate immune response (PubMed:31320558). Mechanistically, senses the presence of viral DNA in the nucleus, homodimerizes and is demethylated by JMJD6 (PubMed:31320558). In turn, translocates to the cytoplasm where it activates the TBK1-IRF3 pathway, leading to interferon alpha/beta production (PubMed:31320558)
- Specific Function
- G-rich strand telomeric DNA binding
- Gene Name
- HNRNPA2B1
- Uniprot ID
- P22626
- Uniprot Name
- Heterogeneous nuclear ribonucleoproteins A2/B1
- Molecular Weight
- 37429.71 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- This protein is a component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Mediates pre-mRNA alternative splicing regulation. Inhibits, together with CUGBP1, insulin receptor (IR) pre-mRNA exon 11 inclusion in myoblast. Binds to the IR RNA. Binds poly(RG)
- Specific Function
- identical protein binding
- Gene Name
- HNRNPH1
- Uniprot ID
- P31943
- Uniprot Name
- Heterogeneous nuclear ribonucleoprotein H
- Molecular Weight
- 49229.25 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Involved in the splicing process and participates in early heat shock-induced splicing arrest. Due to their great structural variations the different isoforms may possess different functions in the splicing reaction
- Specific Function
- RNA binding
- Gene Name
- HNRNPH3
- Uniprot ID
- P31942
- Uniprot Name
- Heterogeneous nuclear ribonucleoprotein H3
- Molecular Weight
- 36926.445 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Treponema denticola (strain ATCC 35405 / CIP 103919 / DSM 14222)
- Pharmacological action
- Unknown
- General Function
- Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
- Specific Function
- cobalt-precorrin-5B C1-methyltransferase activity
- Gene Name
- cbiD
- Uniprot ID
- P61987
- Uniprot Name
- Cobalt-precorrin-5B C(1)-methyltransferase
- Molecular Weight
- 39699.48 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Splicing factor binding to exonic or intronic sites and acting as either an activator or repressor of exon inclusion. Exhibits a binding preference for CA-rich elements (PubMed:11809897, PubMed:22570490, PubMed:24164894, PubMed:25623890, PubMed:26051023). Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and associated with most nascent transcripts (PubMed:2687284). Associates, together with APEX1, to the negative calcium responsive element (nCaRE) B2 of the APEX2 promoter (PubMed:11809897). As part of a ribonucleoprotein complex composed at least of ZNF827, HNRNPK and the circular RNA circZNF827 that nucleates the complex on chromatin, may negatively regulate the transcription of genes involved in neuronal differentiation (PubMed:33174841). Regulates alternative splicing of a core group of genes involved in neuronal differentiation, likely by mediating H3K36me3-coupled transcription elongation and co-transcriptional RNA processing via interaction with CHD8
- Specific Function
- mRNA binding
- Gene Name
- HNRNPL
- Uniprot ID
- P14866
- Uniprot Name
- Heterogeneous nuclear ribonucleoprotein L
- Molecular Weight
- 64132.45 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- DNA- and RNA binding protein, involved in several nuclear processes. Essential pre-mRNA splicing factor required early in spliceosome formation and for splicing catalytic step II, probably as a heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and specifically binds to intronic polypyrimidine tracts. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45, a phosphorylated form is sequestered by THRAP3 from the pre-mRNA in resting T-cells; T-cell activation and subsequent reduced phosphorylation is proposed to lead to release from THRAP3 allowing binding to pre-mRNA splicing regulatotry elements which represses exon inclusion. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. May be involved in a pre-mRNA coupled splicing and polyadenylation process as component of a snRNP-free complex with SNRPA/U1A. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. SFPQ may be involved in homologous DNA pairing; in vitro, promotes the invasion of ssDNA between a duplex DNA and produces a D-loop formation. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1; in vitro, stimulates dissociation of TOP1 from DNA after cleavage and enhances its jumping between separate DNA helices. The SFPQ-NONO heteromer binds DNA (PubMed:25765647). The SFPQ-NONO heteromer may be involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends; in vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. SFPQ is involved in transcriptional regulation. Functions as a transcriptional activator (PubMed:25765647). Transcriptional repression is mediated by an interaction of SFPQ with SIN3A and subsequent recruitment of histone deacetylases (HDACs). The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional activity. SFPQ isoform Long binds to the DNA binding domains (DBD) of nuclear hormone receptors, like RXRA and probably THRA, and acts as a transcriptional corepressor in absence of hormone ligands. Binds the DNA sequence 5'-CTGAGTC-3' in the insulin-like growth factor response element (IGFRE) and inhibits IGF-I-stimulated transcriptional activity. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation (By similarity). Required for the assembly of nuclear speckles (PubMed:25765647). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728)
- Specific Function
- chromatin binding
- Gene Name
- SFPQ
- Uniprot ID
- P23246
- Uniprot Name
- Splicing factor, proline- and glutamine-rich
- Molecular Weight
- 76149.15 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Component of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs (PubMed:10882114, PubMed:11533230, PubMed:32494006, PubMed:34822310). The 17S U2 SnRNP complex (1) directly participates in early spliceosome assembly and (2) mediates recognition of the intron branch site during pre-mRNA splicing by promoting the selection of the pre-mRNA branch-site adenosine, the nucleophile for the first step of splicing (PubMed:10882114, PubMed:11533230, PubMed:32494006, PubMed:34822310). Within the 17S U2 SnRNP complex, SF3A2 is part of the SF3A subcomplex that contributes to the assembly of the 17S U2 snRNP, and the subsequent assembly of the pre-spliceosome 'E' complex and the pre-catalytic spliceosome 'A' complex (PubMed:10882114, PubMed:11533230). Involved in pre-mRNA splicing as a component of pre-catalytic spliceosome 'B' complexes, including the Bact complex (PubMed:29360106, PubMed:29361316, PubMed:30315277). Interacts directly with the duplex formed by U2 snRNA and the intron (PubMed:29360106)
- Specific Function
- RNA binding
- Gene Name
- SF3A2
- Uniprot ID
- Q15428
- Uniprot Name
- Splicing factor 3A subunit 2
- Molecular Weight
- 49255.355 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Scaffolding protein involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes. Component of the 40S ribosomal subunit involved in translational repression (PubMed:23636399). Involved in the initiation of the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation, by promoting ubiquitination of a subset of 40S ribosomal subunits (PubMed:28132843). Binds to and stabilizes activated protein kinase C (PKC), increasing PKC-mediated phosphorylation. May recruit activated PKC to the ribosome, leading to phosphorylation of EIF6. Inhibits the activity of SRC kinases including SRC, LCK and YES1. Inhibits cell growth by prolonging the G0/G1 phase of the cell cycle. Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK heterodimer. Facilitates ligand-independent nuclear translocation of AR following PKC activation, represses AR transactivation activity and is required for phosphorylation of AR by SRC. Modulates IGF1R-dependent integrin signaling and promotes cell spreading and contact with the extracellular matrix. Involved in PKC-dependent translocation of ADAM12 to the cell membrane. Promotes the ubiquitination and proteasome-mediated degradation of proteins such as CLEC1B and HIF1A. Required for VANGL2 membrane localization, inhibits Wnt signaling, and regulates cellular polarization and oriented cell division during gastrulation. Required for PTK2/FAK1 phosphorylation and dephosphorylation. Regulates internalization of the muscarinic receptor CHRM2. Promotes apoptosis by increasing oligomerization of BAX and disrupting the interaction of BAX with the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity. Regulates cell surface expression of some GPCRs such as TBXA2R. Plays a role in regulation of FLT1-mediated cell migration. Involved in the transport of ABCB4 from the Golgi to the apical bile canalicular membrane (PubMed:19674157). Promotes migration of breast carcinoma cells by binding to and activating RHOA (PubMed:20499158). Acts as an adapter for the dephosphorylation and inactivation of AKT1 by promoting recruitment of PP2A phosphatase to AKT1 (By similarity)
- Specific Function
- BH3 domain binding
- Gene Name
- RACK1
- Uniprot ID
- P63244
- Uniprot Name
- Small ribosomal subunit protein RACK1
- Molecular Weight
- 35076.47 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. Association with IGSF8 regulates the immune synapse formation and is required for efficient T-cell activation (PubMed:22689882)
- Specific Function
- actin filament binding
- Gene Name
- ACTN1
- Uniprot ID
- P12814
- Uniprot Name
- Alpha-actinin-1
- Molecular Weight
- 103056.695 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the hydrolysis of N-acetylated amino acids to acetate and free amino acids
- Specific Function
- aminoacylase activity
- Gene Name
- ACY1
- Uniprot ID
- Q03154
- Uniprot Name
- Aminoacylase-1
- Molecular Weight
- 45884.705 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis
- Specific Function
- calcium ion binding
- Gene Name
- ANXA4
- Uniprot ID
- P09525
- Uniprot Name
- Annexin A4
- Molecular Weight
- 35882.36 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade
- Specific Function
- calcium ion binding
- Gene Name
- ANXA5
- Uniprot ID
- P08758
- Uniprot Name
- Annexin A5
- Molecular Weight
- 35936.375 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (PubMed:7876246). Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export (PubMed:11149926). Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity). Present in the cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation and might participate in the block to polyspermy (By similarity)
- Specific Function
- calcium ion binding
- Gene Name
- CALR
- Uniprot ID
- P27797
- Uniprot Name
- Calreticulin
- Molecular Weight
- 48141.2 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the final rate-limiting step of glycolysis by mediating the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP (PubMed:15996096, PubMed:1854723, PubMed:20847263). The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production (PubMed:15996096, PubMed:1854723, PubMed:20847263). The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival (PubMed:15996096, PubMed:1854723, PubMed:20847263)
- Specific Function
- ATP binding
- Gene Name
- PKM
- Uniprot ID
- P14618
- Uniprot Name
- Pyruvate kinase PKM
- Molecular Weight
- 57936.38 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols (PubMed:10510318, PubMed:30538128). Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides and bile acids, with a preference for negatively charged substrates, such as glucuronate and succinic semialdehyde (PubMed:10510318, PubMed:30538128). Functions as a detoxifiying enzyme by reducing a range of toxic aldehydes (By similarity). Reduces methylglyoxal and 3-deoxyglucosone, which are present at elevated levels under hyperglycemic conditions and are cytotoxic (By similarity). Involved also in the detoxification of lipid-derived aldehydes like acrolein (By similarity). Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs, including the anthracyclines doxorubicin (DOX) and daunorubicin (DAUN) (PubMed:11306097, PubMed:18276838). Also acts as an inhibitor of protein S-nitrosylation by mediating degradation of S-nitroso-coenzyme A (S-nitroso-CoA), a cofactor required to S-nitrosylate proteins (PubMed:30538128). S-nitroso-CoA reductase activity is involved in reprogramming intermediary metabolism in renal proximal tubules, notably by inhibiting protein S-nitrosylation of isoform 2 of PKM (PKM2) (By similarity). Also acts as a S-nitroso-glutathione reductase by catalyzing the NADPH-dependent reduction of S-nitrosoglutathione (PubMed:31649033). Displays no reductase activity towards retinoids (By similarity)
- Specific Function
- aldo-keto reductase (NADPH) activity
- Gene Name
- AKR1A1
- Uniprot ID
- P14550
- Uniprot Name
- Aldo-keto reductase family 1 member A1
- Molecular Weight
- 36572.71 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the reduction of two molecules of cytochrome b5 using NADH as the electron donor
- Specific Function
- ADP binding
- Gene Name
- CYB5R3
- Uniprot ID
- P00387
- Uniprot Name
- NADH-cytochrome b5 reductase 3
- Molecular Weight
- 34234.55 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Maintains high levels of reduced glutathione in the cytosol
- Specific Function
- electron transfer activity
- Gene Name
- GSR
- Uniprot ID
- P00390
- Uniprot Name
- Glutathione reductase, mitochondrial
- Molecular Weight
- 56256.565 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate
- Specific Function
- calcium ion binding
- Gene Name
- TKT
- Uniprot ID
- P29401
- Uniprot Name
- Transketolase
- Molecular Weight
- 67876.95 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2)
- Specific Function
- antioxidant activity
- Gene Name
- PRDX2
- Uniprot ID
- P32119
- Uniprot Name
- Peroxiredoxin-2
- Molecular Weight
- 21891.725 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (PubMed:10893423, PubMed:9497358). Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides (PubMed:10893423). Also has phospholipase activity, can therefore either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity) (PubMed:10893423, PubMed:26830860). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH (PubMed:10893423). Plays a role in cell protection against oxidative stress by detoxifying peroxides and in phospholipid homeostasis (PubMed:10893423). Exhibits acyl-CoA-dependent lysophospholipid acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (PubMed:26830860). Shows a clear preference for LPC as the lysophospholipid and for palmitoyl CoA as the fatty acyl substrate (PubMed:26830860)
- Specific Function
- 1-acylglycerophosphocholine O-acyltransferase activity
- Gene Name
- PRDX6
- Uniprot ID
- P30041
- Uniprot Name
- Peroxiredoxin-6
- Molecular Weight
- 25034.715 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (PubMed:2001362, PubMed:20676357, PubMed:21245143, PubMed:21593166, PubMed:25678563). Exerts a strong chemotactic effect on leukocytes partly through activation of one of its membrane receptors BSG/CD147, initiating a signaling cascade that culminates in MAPK/ERK activation (PubMed:11943775, PubMed:21245143). Activates endothelial cells (ECs) in a pro-inflammatory manner by stimulating activation of NF-kappa-B and ERK, JNK and p38 MAP-kinases and by inducing expression of adhesion molecules including SELE and VCAM1 (PubMed:15130913). Induces apoptosis in ECs by promoting the FOXO1-dependent expression of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis (PubMed:31063815). In response to oxidative stress, initiates proapoptotic and antiapoptotic signaling in ECs via activation of NF-kappa-B and AKT1 and up-regulation of antiapoptotic protein BCL2 (PubMed:23180369). Negatively regulates MAP3K5/ASK1 kinase activity, autophosphorylation and oxidative stress-induced apoptosis mediated by MAP3K5/ASK1 (PubMed:26095851). Necessary for the assembly of TARDBP in heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and regulates TARDBP binding to RNA UG repeats and TARDBP-dependent expression of HDAC6, ATG7 and VCP which are involved in clearance of protein aggregates (PubMed:25678563). Plays an important role in platelet activation and aggregation (By similarity). Regulates calcium mobilization and integrin ITGA2B:ITGB3 bidirectional signaling via increased ROS production as well as by facilitating the interaction between integrin and the cell cytoskeleton (By similarity). Binds heparan sulfate glycosaminoglycans (PubMed:11943775). Inhibits replication of influenza A virus (IAV) (PubMed:19207730). Inhibits ITCH/AIP4-mediated ubiquitination of matrix protein 1 (M1) of IAV by impairing the interaction of ITCH/AIP4 with M1, followed by the suppression of the nuclear export of M1, and finally reduction of the replication of IAV (PubMed:22347431, PubMed:30328013)
- Specific Function
- cyclosporin A binding
- Gene Name
- PPIA
- Uniprot ID
- P62937
- Uniprot Name
- Peptidyl-prolyl cis-trans isomerase A
- Molecular Weight
- 18012.42 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, chaperone-mediated autophagy, activation of proteolysis of misfolded proteins, formation and dissociation of protein complexes, and antigen presentation. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation (PubMed:21148293, PubMed:21150129, PubMed:23018488, PubMed:24732912, PubMed:27916661, PubMed:2799391, PubMed:36586411). This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones (PubMed:12526792, PubMed:21148293, PubMed:21150129, PubMed:23018488, PubMed:24732912, PubMed:27916661). The co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation (PubMed:12526792, PubMed:21148293, PubMed:21150129, PubMed:23018488, PubMed:24732912, PubMed:27916661). The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 (PubMed:24121476, PubMed:24318877, PubMed:26865365, PubMed:27474739). Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70 (PubMed:12526792). Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:10722728, PubMed:11276205). Substrate recognition component in chaperone-mediated autophagy (CMA), a selective protein degradation process that mediates degradation of proteins with a -KFERQ motif: HSPA8/HSC70 specifically recognizes and binds cytosolic proteins bearing a -KFERQ motif and promotes their recruitment to the surface of the lysosome where they bind to lysosomal protein LAMP2 (PubMed:11559757, PubMed:2799391, PubMed:36586411). KFERQ motif-containing proteins are eventually transported into the lysosomal lumen where they are degraded (PubMed:11559757, PubMed:2799391, PubMed:36586411). In conjunction with LAMP2, facilitates MHC class II presentation of cytoplasmic antigens by guiding antigens to the lysosomal membrane for interaction with LAMP2 which then elicits MHC class II presentation of peptides to the cell membrane (PubMed:15894275). Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1 (PubMed:23990462). It is recruited to clathrin-coated vesicles through its interaction with DNAJC6 leading to activation of HSPA8/HSC70 ATPase activity and therefore uncoating of clathrin-coated vesicles (By similarity)
- Specific Function
- A1 adenosine receptor binding
- Gene Name
- HSPA8
- Uniprot ID
- P11142
- Uniprot Name
- Heat shock cognate 71 kDa protein
- Molecular Weight
- 70897.565 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:11274138, PubMed:12526792, PubMed:15577939, PubMed:15937123, PubMed:27353360, PubMed:29127155). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself (PubMed:29127155). Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:26991466, PubMed:27295069). Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70 (PubMed:12526792). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels (PubMed:25973397). In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues (PubMed:25973397). Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment (PubMed:25973397). Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11276205). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Mediates the association of TOMM70 with IRF3 or TBK1 in mitochondrial outer membrane which promotes host antiviral response (PubMed:20628368, PubMed:25609812)
- Specific Function
- ATP binding
- Gene Name
- HSP90AA1
- Uniprot ID
- P07900
- Uniprot Name
- Heat shock protein HSP 90-alpha
- Molecular Weight
- 84659.015 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Cytosolic prostaglandin synthase that catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) (PubMed:10922363). Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes (PubMed:11274138, PubMed:12077419). Facilitates HIF alpha proteins hydroxylation via interaction with EGLN1/PHD2, leading to recruit EGLN1/PHD2 to the HSP90 pathway (PubMed:24711448)
- Specific Function
- DNA polymerase binding
- Gene Name
- PTGES3
- Uniprot ID
- Q15185
- Uniprot Name
- Prostaglandin E synthase 3
- Molecular Weight
- 18697.195 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Acts as a co-chaperone for HSP90AA1 (PubMed:27353360). Mediates the association of the molecular chaperones HSPA8/HSC70 and HSP90 (By similarity)
- Specific Function
- Hsp90 protein binding
- Gene Name
- STIP1
- Uniprot ID
- P31948
- Uniprot Name
- Stress-induced-phosphoprotein 1
- Molecular Weight
- 62638.7 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit to form the 80S initiation complex in the cytoplasm (PubMed:10085284, PubMed:14654845, PubMed:21536732, PubMed:32669547). Behaves as a stimulatory translation initiation factor downstream insulin/growth factors. Is also involved in ribosome biogenesis. Associates with pre-60S subunits in the nucleus and is involved in its nuclear export. Cytoplasmic release of TIF6 from 60S subunits and nuclear relocalization is promoted by a RACK1 (RACK1)-dependent protein kinase C activity (PubMed:10085284, PubMed:14654845, PubMed:21536732). In tissues responsive to insulin, controls fatty acid synthesis and glycolysis by exerting translational control of adipogenic transcription factors such as CEBPB, CEBPD and ATF4 that have G/C rich or uORF in their 5'UTR. Required for ROS-dependent megakaryocyte maturation and platelets formation, controls the expression of mitochondrial respiratory chain genes involved in reactive oxygen species (ROS) synthesis (By similarity). Involved in miRNA-mediated gene silencing by the RNA-induced silencing complex (RISC). Required for both miRNA-mediated translational repression and miRNA-mediated cleavage of complementary mRNAs by RISC (PubMed:17507929). Modulates cell cycle progression and global translation of pre-B cells, its activation seems to be rate-limiting in tumorigenesis and tumor growth (By similarity)
- Specific Function
- ribosomal large subunit binding
- Gene Name
- EIF6
- Uniprot ID
- P56537
- Uniprot Name
- Eukaryotic translation initiation factor 6
- Molecular Weight
- 26598.84 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon
- Specific Function
- ATP binding
- Gene Name
- EIF4A1
- Uniprot ID
- P60842
- Uniprot Name
- Eukaryotic initiation factor 4A-I
- Molecular Weight
- 46153.525 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- In the cytoplasm, catalyzes the conversion of glucose-6-phosphate to fructose-6-phosphate, the second step in glycolysis, and the reverse reaction during gluconeogenesis (PubMed:28803808). Besides it's role as a glycolytic enzyme, also acts as a secreted cytokine: acts as an angiogenic factor (AMF) that stimulates endothelial cell motility (PubMed:11437381). Acts as a neurotrophic factor, neuroleukin, for spinal and sensory neurons (PubMed:11004567, PubMed:3352745). It is secreted by lectin-stimulated T-cells and induces immunoglobulin secretion (PubMed:11004567, PubMed:3352745)
- Specific Function
- carbohydrate derivative binding
- Gene Name
- GPI
- Uniprot ID
- P06744
- Uniprot Name
- Glucose-6-phosphate isomerase
- Molecular Weight
- 63146.745 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Interconverts simultaneously and stereospecifically pyruvate and lactate with concomitant interconversion of NADH and NAD(+)
- Specific Function
- cadherin binding
- Gene Name
- LDHA
- Uniprot ID
- P00338
- Uniprot Name
- L-lactate dehydrogenase A chain
- Molecular Weight
- 36688.465 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes one of the two ATP producing reactions in the glycolytic pathway via the reversible conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate (PubMed:30323285, PubMed:7391028). In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein) (PubMed:2324090). May play a role in sperm motility (PubMed:26677959)
- Specific Function
- ADP binding
- Gene Name
- PGK1
- Uniprot ID
- P00558
- Uniprot Name
- Phosphoglycerate kinase 1
- Molecular Weight
- 44614.36 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin
- Specific Function
- GTP binding
- Gene Name
- TUBB
- Uniprot ID
- P07437
- Uniprot Name
- Tubulin beta chain
- Molecular Weight
- 49670.515 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity (PubMed:11812157). In conjunction with the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions via regulation of actin dynamics (PubMed:15580268). Required for the centralization of the mitotic spindle and symmetric division of zygotes (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization in epithelial cells (PubMed:21834987). Required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation (PubMed:23633677). Required for neural tube morphogenesis and neural crest cell migration (By similarity)
- Specific Function
- actin filament binding
- Gene Name
- CFL1
- Uniprot ID
- P23528
- Uniprot Name
- Cofilin-1
- Molecular Weight
- 18502.315 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negative regulator of osteogenesis. Blocks the nuclear translocation of the phosphorylated form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on cyclin D1 expression resulting in blockage of neuronal apoptosis elicited by SRPK2. Negative regulator of signaling cascades that mediate activation of MAP kinases via AKAP13
- Specific Function
- cadherin binding
- Gene Name
- YWHAB
- Uniprot ID
- P31946
- Uniprot Name
- 14-3-3 protein beta/alpha
- Molecular Weight
- 28082.165 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Biosynthesis of L-glutamate from L-aspartate or L-cysteine (PubMed:21900944). Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involved in hepatic glucose synthesis during development and in adipocyte glyceroneogenesis. Using L-cysteine as substrate, regulates levels of mercaptopyruvate, an important source of hydrogen sulfide. Mercaptopyruvate is converted into H(2)S via the action of 3-mercaptopyruvate sulfurtransferase (3MST). Hydrogen sulfide is an important synaptic modulator and neuroprotectant in the brain. In addition, catalyzes (2S)-2-aminobutanoate, a by-product in the cysteine biosynthesis pathway (PubMed:27827456)
- Specific Function
- L-aspartate
- Gene Name
- GOT1
- Uniprot ID
- P17174
- Uniprot Name
- Aspartate aminotransferase, cytoplasmic
- Molecular Weight
- 46247.14 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the production of glutathione from gamma-glutamylcysteine and glycine in an ATP-dependent manner (PubMed:7646467, PubMed:9215686). Glutathione (gamma-glutamylcysteinylglycine, GSH) is the most abundant intracellular thiol in living aerobic cells and is required for numerous processes including the protection of cells against oxidative damage, amino acid transport, the detoxification of foreign compounds, the maintenance of protein sulfhydryl groups in a reduced state and acts as a cofactor for a number of enzymes (PubMed:10369661). Participates in ophthalmate biosynthesis in hepatocytes (By similarity)
- Specific Function
- ATP binding
- Gene Name
- GSS
- Uniprot ID
- P48637
- Uniprot Name
- Glutathione synthetase
- Molecular Weight
- 52384.325 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Acts as a transcriptional repressor (PubMed:17974029). Has mitogenic activity for fibroblasts (PubMed:11751870, PubMed:26845719). Heparin-binding protein (PubMed:15491618)
- Specific Function
- actin binding
- Gene Name
- HDGF
- Uniprot ID
- P51858
- Uniprot Name
- Hepatoma-derived growth factor
- Molecular Weight
- 26788.105 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalytic subunit of the enzyme which catalyzes the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers
- Specific Function
- isocitrate dehydrogenase (NAD+) activity
- Gene Name
- IDH3A
- Uniprot ID
- P50213
- Uniprot Name
- Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial
- Molecular Weight
- 39591.365 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- In the soluble state, catalyzes glutaredoxin-like thiol disulfide exchange reactions with reduced glutathione as electron donor. Reduces selenite and dehydroascorbate and may act as an antioxidant during oxidative stress response (PubMed:25581026, PubMed:37759794). Can insert into membranes and form voltage-dependent multi-ion conductive channels. Membrane insertion seems to be redox-regulated and may occur only under oxidizing conditions. Involved in regulation of the cell cycle
- Specific Function
- cadherin binding
- Gene Name
- CLIC1
- Uniprot ID
- O00299
- Uniprot Name
- Chloride intracellular channel protein 1
- Molecular Weight
- 26922.47 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Implicated in immunoproteasome assembly and required for efficient antigen processing. The PA28 activator complex enhances the generation of class I binding peptides by altering the cleavage pattern of the proteasome
- Specific Function
- endopeptidase activator activity
- Gene Name
- PSME1
- Uniprot ID
- Q06323
- Uniprot Name
- Proteasome activator complex subunit 1
- Molecular Weight
- 28722.9 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Binds ATP, opioids and phosphatidylethanolamine. Has lower affinity for phosphatidylinositol and phosphatidylcholine. Serine protease inhibitor which inhibits thrombin, neuropsin and chymotrypsin but not trypsin, tissue type plasminogen activator and elastase (By similarity). Inhibits the kinase activity of RAF1 by inhibiting its activation and by dissociating the RAF1/MEK complex and acting as a competitive inhibitor of MEK phosphorylation
- Specific Function
- ATP binding
- Gene Name
- PEBP1
- Uniprot ID
- P30086
- Uniprot Name
- Phosphatidylethanolamine-binding protein 1
- Molecular Weight
- 21056.65 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglyceratea crucial step in glycolysis, by using 2,3-bisphosphoglycerate (PubMed:23653202). Also catalyzes the interconversion of (2R)-2,3-bisphosphoglycerate and (2R)-3-phospho-glyceroyl phosphate (PubMed:23653202)
- Specific Function
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity
- Gene Name
- PGAM1
- Uniprot ID
- P18669
- Uniprot Name
- Phosphoglycerate mutase 1
- Molecular Weight
- 28803.675 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Plays a role in RAN-dependent nucleocytoplasmic transport. Alleviates the TNPO1-dependent inhibition of RAN GTPase activity and mediates the dissociation of RAN from proteins involved in transport into the nucleus (By similarity). Induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins (PubMed:20485264). Promotes the disassembly of the complex formed by RAN and importin beta. Promotes dissociation of RAN from a complex with KPNA2 and CSE1L (By similarity). Required for normal mitotic spindle assembly and normal progress through mitosis via its effect on RAN (PubMed:17671426). Does not increase the RAN GTPase activity by itself, but increases GTP hydrolysis mediated by RANGAP1 (PubMed:7882974). Inhibits RCC1-dependent exchange of RAN-bound GDP by GTP (PubMed:7616957, PubMed:7882974)
- Specific Function
- cadherin binding
- Gene Name
- RANBP1
- Uniprot ID
- P43487
- Uniprot Name
- Ran-specific GTPase-activating protein
- Molecular Weight
- 23309.92 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the formation of UDP-alpha-D-glucuronate, a constituent of complex glycosaminoglycans (PubMed:21502315, PubMed:21961565, PubMed:22123821, PubMed:23106432, PubMed:25478983, PubMed:27966912, PubMed:30420606, PubMed:30457329). Required for the biosynthesis of chondroitin sulfate and heparan sulfate. Required for embryonic development via its role in the biosynthesis of glycosaminoglycans (By similarity). Required for proper brain and neuronal development (PubMed:32001716)
- Specific Function
- identical protein binding
- Gene Name
- UGDH
- Uniprot ID
- O60701
- Uniprot Name
- UDP-glucose 6-dehydrogenase
- Molecular Weight
- 55023.545 Da
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system. Exogenously applied M.tuberculosis EsxA or EsxA-EsxB (or EsxA expressed in host) binds B2M and decreases its export to the cell surface (total protein levels do not change), probably leading to defects in class I antigen presentation (PubMed:25356553)
- Specific Function
- identical protein binding
- Gene Name
- B2M
- Uniprot ID
- P61769
- Uniprot Name
- Beta-2-microglobulin
- Molecular Weight
- 13714.43 Da
References
- Deng NJ, Yan L, Singh D, Cieplak P: Molecular basis for the Cu2+ binding-induced destabilization of beta2-microglobulin revealed by molecular dynamics simulation. Biophys J. 2006 Jun 1;90(11):3865-79. Epub 2006 Mar 2. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Copper metallochaperone essential for the maturation of cytochrome c oxidase subunit II (MT-CO2/COX2). Not required for the synthesis of MT-CO2/COX2 but plays a crucial role in stabilizing MT-CO2/COX2 during its subsequent maturation. Involved in transporting copper to the Cu(A) site on MT-CO2/COX2 (PubMed:15229189, PubMed:15659396, PubMed:16735468, PubMed:17189203, PubMed:19336478). Plays an important role in the regulation of copper homeostasis by controlling the abundance and cell membrane localization of copper transporter CTR1 (By similarity)
- Specific Function
- copper chaperone activity
- Gene Name
- SCO1
- Uniprot ID
- O75880
- Uniprot Name
- Protein SCO1 homolog, mitochondrial
- Molecular Weight
- 33813.69 Da
References
- Banci L, Bertini I, Calderone V, Ciofi-Baffoni S, Mangani S, Martinelli M, Palumaa P, Wang S: A hint for the function of human Sco1 from different structures. Proc Natl Acad Sci U S A. 2006 Jun 6;103(23):8595-600. Epub 2006 May 30. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Not Available
- Specific Function
- Not Available
- Gene Name
- PRNP
- Uniprot ID
- F7VJQ1
- Uniprot Name
- Alternative prion protein
- Molecular Weight
- 8690.77 Da
References
- Wells MA, Jackson GS, Jones S, Hosszu LL, Craven CJ, Clarke AR, Collinge J, Waltho JP: A reassessment of copper(II) binding in the full-length prion protein. Biochem J. 2006 Nov 1;399(3):435-44. [Article]
- Merle U, Stremmel W, Gessner R: Influence of homozygosity for methionine at codon 129 of the human prion gene on the onset of neurological and hepatic symptoms in Wilson disease. Arch Neurol. 2006 Jul;63(7):982-5. [Article]
- Shiraishi N, Utsunomiya H, Nishikimi M: Combination of NADPH and copper ions generates proteinase K-resistant aggregates from recombinant prion protein. J Biol Chem. 2006 Nov 17;281(46):34880-7. Epub 2006 Sep 21. [Article]
- Shearer J, Soh P: The copper(II) adduct of the unstructured region of the amyloidogenic fragment derived from the human prion protein is redox-active at physiological pH. Inorg Chem. 2007 Feb 5;46(3):710-9. [Article]
- Valensin G, Molteni E, Valensin D, Taraszkiewicz M, Kozlowski H: Molecular dynamics study of the Cu2+ binding-induced "structuring" of the N-terminal domain of human prion protein. J Phys Chem B. 2009 Mar 19;113(11):3277-9. doi: 10.1021/jp901030a. [Article]
- Pushie MJ, Vogel HJ: A potential mechanism for Cu2+ reduction, beta-cleavage, and beta-sheet initiation within the N-terminal domain of the prion protein: insights from density functional theory and molecular dynamics calculations. J Toxicol Environ Health A. 2009;72(17-18):1040-59. doi: 10.1080/15287390903084389. [Article]
- Remelli M, Valensin D, Toso L, Gralka E, Guerrini R, Marzola E, Kozlowski H: Thermodynamic and spectroscopic investigation on the role of Met residues in Cu(II) binding to the non-octarepeat site of the human prion protein. Metallomics. 2012 Aug;4(8):794-806. doi: 10.1039/c2mt20060k. Epub 2012 Jul 13. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Glycine receptors are ligand-gated chloride channels (PubMed:23994010, PubMed:25730860). Channel opening is triggered by extracellular glycine (PubMed:14551753, PubMed:16144831, PubMed:2155780, PubMed:22715885, PubMed:22973015, PubMed:25973519, PubMed:7920629, PubMed:9009272). Channel opening is also triggered by taurine and beta-alanine (PubMed:16144831, PubMed:9009272). Channel characteristics depend on the subunit composition; heteropentameric channels are activated by lower glycine levels and display faster desensitization (PubMed:14551753). Plays an important role in the down-regulation of neuronal excitability (PubMed:8298642, PubMed:9009272). Contributes to the generation of inhibitory postsynaptic currents (PubMed:25445488). Channel activity is potentiated by ethanol (PubMed:25973519). Potentiation of channel activity by intoxicating levels of ethanol contribute to the sedative effects of ethanol (By similarity)
- Specific Function
- extracellularly glycine-gated chloride channel activity
- Gene Name
- GLRA1
- Uniprot ID
- P23415
- Uniprot Name
- Glycine receptor subunit alpha-1
- Molecular Weight
- 52623.35 Da
References
- Chen Z, Dillon GH, Huang R: Identification of residues critical for Cu2+-mediated inhibition of glycine alpha1 receptors. Neuropharmacology. 2006 Sep;51(4):701-8. Epub 2006 Jul 12. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- May play a role in microtubule-mediated transport or vesicle function
- Specific Function
- beta-tubulin binding
- Gene Name
- HTT
- Uniprot ID
- P42858
- Uniprot Name
- Huntingtin
- Molecular Weight
- 347599.665 Da
References
- Fox JH, Kama JA, Lieberman G, Chopra R, Dorsey K, Chopra V, Volitakis I, Cherny RA, Bush AI, Hersch S: Mechanisms of copper ion mediated Huntington's disease progression. PLoS One. 2007 Mar 28;2(3):e334. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as a DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, formamidopyrimidine (Fapy) and 5-hydroxyuracil. Has marginal activity towards 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. Has DNA glycosylase/lyase activity towards mismatched uracil and thymine, in particular in U:C and T:C mismatches. Specifically binds 5-hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of 5hmC
- Specific Function
- class I DNA-(apurinic or apyrimidinic site) endonuclease activity
- Gene Name
- NEIL1
- Uniprot ID
- Q96FI4
- Uniprot Name
- Endonuclease 8-like 1
- Molecular Weight
- 43683.625 Da
References
- Hegde ML, Hegde PM, Holthauzen LM, Hazra TK, Rao KS, Mitra S: Specific Inhibition of NEIL-initiated repair of oxidized base damage in human genome by copper and iron: potential etiological linkage to neurodegenerative diseases. J Biol Chem. 2010 Sep 10;285(37):28812-25. doi: 10.1074/jbc.M110.126664. Epub 2010 Jul 9. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Has DNA glycosylase activity towards 5-hydroxyuracil and other oxidized derivatives of cytosine with a preference for mismatched double-stranded DNA (DNA bubbles). Has low or no DNA glycosylase activity towards thymine glycol, 2-hydroxyadenine, hypoxanthine and 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates
- Specific Function
- class I DNA-(apurinic or apyrimidinic site) endonuclease activity
- Gene Name
- NEIL2
- Uniprot ID
- Q969S2
- Uniprot Name
- Endonuclease 8-like 2
- Molecular Weight
- 36826.285 Da
References
- Hegde ML, Hegde PM, Holthauzen LM, Hazra TK, Rao KS, Mitra S: Specific Inhibition of NEIL-initiated repair of oxidized base damage in human genome by copper and iron: potential etiological linkage to neurodegenerative diseases. J Biol Chem. 2010 Sep 10;285(37):28812-25. doi: 10.1074/jbc.M110.126664. Epub 2010 Jul 9. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Is a copper-binding glycoprotein with ferroxidase activity. It oxidizes Fe(2+) to Fe(3+) without releasing radical oxygen species (PubMed:31125343). May be involved in the regulation of intracellular iron content (PubMed:31125343)
- Specific Function
- copper ion binding
- Gene Name
- HEPHL1
- Uniprot ID
- Q6MZM0
- Uniprot Name
- Ferroxidase HEPHL1
- Molecular Weight
- 131601.67 Da
References
- Petrak J, Vyoral D: Hephaestin--a ferroxidase of cellular iron export. Int J Biochem Cell Biol. 2005 Jun;37(6):1173-8. Epub 2005 Jan 26. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Serine protease inhibitor. Inhibits TMPRSS7 (PubMed:15853774). Is a primary inhibitor of tissue-type plasminogen activator (PLAT) and urokinase-type plasminogen activator (PLAU). As PLAT inhibitor, it is required for fibrinolysis down-regulation and is responsible for the controlled degradation of blood clots (PubMed:17912461, PubMed:8481516, PubMed:9207454). As PLAU inhibitor, it is involved in the regulation of cell adhesion and spreading (PubMed:9175705). Acts as a regulator of cell migration, independently of its role as protease inhibitor (PubMed:15001579, PubMed:9168821). It is required for stimulation of keratinocyte migration during cutaneous injury repair (PubMed:18386027). It is involved in cellular and replicative senescence (PubMed:16862142). Plays a role in alveolar type 2 cells senescence in the lung (By similarity). Is involved in the regulation of cementogenic differentiation of periodontal ligament stem cells, and regulates odontoblast differentiation and dentin formation during odontogenesis (PubMed:25808697, PubMed:27046084)
- Specific Function
- protease binding
- Gene Name
- SERPINE1
- Uniprot ID
- P05121
- Uniprot Name
- Plasminogen activator inhibitor 1
- Molecular Weight
- 45059.695 Da
References
- Thompson LC, Goswami S, Peterson CB: Metals affect the structure and activity of human plasminogen activator inhibitor-1. II. Binding affinity and conformational changes. Protein Sci. 2011 Feb;20(2):366-78. doi: 10.1002/pro.567. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- May function as calcium sensor and modulator, contributing to cellular calcium signaling. May function by interacting with other proteins, such as TPR-containing proteins, and indirectly play a role in many physiological processes. May also play a role in suppressing tumor cell growth
- Specific Function
- calcium ion binding
- Gene Name
- S100A2
- Uniprot ID
- P29034
- Uniprot Name
- Protein S100-A2
- Molecular Weight
- 11116.695 Da
References
- Haase-Kohn C, Wolf S, Lenk J, Pietzsch J: Copper-mediated cross-linking of S100A4, but not of S100A2, results in proinflammatory effects in melanoma cells. Biochem Biophys Res Commun. 2011 Sep 30;413(3):494-8. doi: 10.1016/j.bbrc.2011.08.132. Epub 2011 Sep 6. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Calcium-binding protein that plays a role in various cellular processes including motility, angiogenesis, cell differentiation, apoptosis, and autophagy (PubMed:16707441, PubMed:23752197, PubMed:30713770). Increases cell motility and invasiveness by interacting with non-muscle myosin heavy chain (NMMHC) IIA/MYH9 (PubMed:16707441). Mechanistically, promotes filament depolymerization and increases the amount of soluble myosin-IIA, resulting in the formation of stable protrusions facilitating chemotaxis (By similarity). Modulates also the pro-apoptotic function of TP53 by binding to its C-terminal transactivation domain within the nucleus and reducing its protein levels (PubMed:23752197). Within the extracellular space, stimulates cytokine production including granulocyte colony-stimulating factor and CCL24 from T-lymphocytes (By similarity). In addition, stimulates T-lymphocyte chemotaxis by acting as a chemoattractant complex with PGLYRP1 that promotes lymphocyte migration via CCR5 and CXCR3 receptors (PubMed:26654597, PubMed:30713770)
- Specific Function
- actin binding
- Gene Name
- S100A4
- Uniprot ID
- P26447
- Uniprot Name
- Protein S100-A4
- Molecular Weight
- 11728.41 Da
References
- Haase-Kohn C, Wolf S, Lenk J, Pietzsch J: Copper-mediated cross-linking of S100A4, but not of S100A2, results in proinflammatory effects in melanoma cells. Biochem Biophys Res Commun. 2011 Sep 30;413(3):494-8. doi: 10.1016/j.bbrc.2011.08.132. Epub 2011 Sep 6. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release (PubMed:20798282, PubMed:26442590, PubMed:28288128, PubMed:30404828). Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores (PubMed:28288128, PubMed:30404828). Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis (PubMed:30404828). Acts also as a molecular chaperone in its multimeric membrane-bound state, assisting in the folding of synaptic fusion components called SNAREs (Soluble NSF Attachment Protein REceptors) at presynaptic plasma membrane in conjunction with cysteine string protein-alpha/DNAJC5 (PubMed:20798282). This chaperone activity is important to sustain normal SNARE-complex assembly during aging (PubMed:20798282). Also plays a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity (PubMed:26442590)
- Specific Function
- actin binding
- Gene Name
- SNCA
- Uniprot ID
- P37840
- Uniprot Name
- Alpha-synuclein
- Molecular Weight
- 14460.155 Da
References
- Rose F, Hodak M, Bernholc J: Mechanism of copper(II)-induced misfolding of Parkinson's disease protein. Sci Rep. 2011;1:11. doi: 10.1038/srep00011. Epub 2011 Jun 14. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Important signaling molecule that activates signaling cascades downstream of NTRK2 (PubMed:11152678). During development, promotes the survival and differentiation of selected neuronal populations of the peripheral and central nervous systems. Participates in axonal growth, pathfinding and in the modulation of dendritic growth and morphology. Major regulator of synaptic transmission and plasticity at adult synapses in many regions of the CNS. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (LTP), long-term depression (LTD), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability
- Specific Function
- growth factor activity
- Gene Name
- BDNF
- Uniprot ID
- P23560
- Uniprot Name
- Brain-derived neurotrophic factor
- Molecular Weight
- 27817.72 Da
References
- Travaglia A, La Mendola D, Magri A, Nicoletti VG, Pietropaolo A, Rizzarelli E: Copper, BDNF and Its N-terminal domain: inorganic features and biological perspectives. Chemistry. 2012 Dec 3;18(49):15618-31. doi: 10.1002/chem.201202775. Epub 2012 Nov 7. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Multifunctional protein with controversial molecular function which plays an important role in cell protection against oxidative stress and cell death acting as oxidative stress sensor and redox-sensitive chaperone and protease (PubMed:12796482, PubMed:17015834, PubMed:18711745, PubMed:19229105, PubMed:20304780, PubMed:25416785, PubMed:26995087, PubMed:28993701). It is involved in neuroprotective mechanisms like the stabilization of NFE2L2 and PINK1 proteins, male fertility as a positive regulator of androgen signaling pathway as well as cell growth and transformation through, for instance, the modulation of NF-kappa-B signaling pathway (PubMed:12612053, PubMed:14749723, PubMed:15502874, PubMed:17015834, PubMed:18711745, PubMed:21097510). Has been described as a protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals (PubMed:25416785, PubMed:28596309). But this function is rebuted by other works (PubMed:27903648, PubMed:31653696). As a protein deglycase, repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) that cause irreversible damage (PubMed:25416785, PubMed:26995087, PubMed:28013050). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair (PubMed:28596309). Protects histones from adduction by methylglyoxal, controls the levels of methylglyoxal-derived argininine modifications on chromatin (PubMed:30150385). Able to remove the glycations and restore histone 3, histone glycation disrupts both local and global chromatin architecture by altering histone-DNA interactions as well as histone acetylation and ubiquitination levels (PubMed:30150385, PubMed:30894531). Displays a very low glyoxalase activity that may reflect its deglycase activity (PubMed:22523093, PubMed:28993701, PubMed:31653696). Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death (PubMed:16390825). Required for correct mitochondrial morphology and function as well as for autophagy of dysfunctional mitochondria (PubMed:16632486, PubMed:19229105). Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking (PubMed:18711745). Regulates astrocyte inflammatory responses, may modulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells (PubMed:23847046). In pancreatic islets, involved in the maintenance of mitochondrial reactive oxygen species (ROS) levels and glucose homeostasis in an age- and diet dependent manner. Protects pancreatic beta cells from cell death induced by inflammatory and cytotoxic setting (By similarity). Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress (PubMed:18626009). Metal-binding protein able to bind copper as well as toxic mercury ions, enhances the cell protection mechanism against induced metal toxicity (PubMed:23792957). In macrophages, interacts with the NADPH oxidase subunit NCF1 to direct NADPH oxidase-dependent ROS production, and protects against sepsis (By similarity)
- Specific Function
- cadherin binding
- Gene Name
- PARK7
- Uniprot ID
- Q99497
- Uniprot Name
- Parkinson disease protein 7
- Molecular Weight
- 19890.88 Da
References
- Bjorkblom B, Adilbayeva A, Maple-Grodem J, Piston D, Okvist M, Xu XM, Brede C, Larsen JP, Moller SG: Parkinson disease protein DJ-1 binds metals and protects against metal-induced cytotoxicity. J Biol Chem. 2013 Aug 2;288(31):22809-20. doi: 10.1074/jbc.M113.482091. Epub 2013 Jun 21. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Curator comments
- Copper-protein complex induces anti-aggregative and anti-apoptotic effects
- General Function
- Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism
- Specific Function
- amyloid-beta binding
- Gene Name
- IAPP
- Uniprot ID
- P10997
- Uniprot Name
- Islet amyloid polypeptide
- Molecular Weight
- 9806.35 Da
References
- Lee EC, Ha E, Singh S, Legesse L, Ahmad S, Karnaukhova E, Donaldson RP, Jeremic AM: Copper(II)-human amylin complex protects pancreatic cells from amylin toxicity. Phys Chem Chem Phys. 2013 Aug 14;15(30):12558-71. doi: 10.1039/c3cp44542a. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles (By similarity). Is a critical central regulator of gonadal function
- Specific Function
- signaling receptor binding
- Gene Name
- TAC3
- Uniprot ID
- Q9UHF0
- Uniprot Name
- Tachykinin-3
- Molecular Weight
- 13438.25 Da
References
- Russino D, McDonald E, Hejazi L, Hanson GR, Jones CE: The tachykinin peptide neurokinin B binds copper forming an unusual [CuII(NKB)2] complex and inhibits copper uptake into 1321N1 astrocytoma cells. ACS Chem Neurosci. 2013 Oct 16;4(10):1371-81. doi: 10.1021/cn4000988. Epub 2013 Aug 7. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Not Available
- Specific Function
- Not Available
- Gene Name
- A1BG
- Uniprot ID
- P04217
- Uniprot Name
- Alpha-1B-glycoprotein
- Molecular Weight
- 54253.0 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Functions as a carrier for hydrophobic molecules in body fluids (Probable). Essential for the solubility and activity of lipidated Wnt family members, including WNT1, WNT2B, WNT3, WNT3A, WNT5A, WNT7A, WNT7B, WNT8, WNT9A, WNT9B, WNT10A and WNT10B (PubMed:26902720). Binds vitamin E (PubMed:12463752, PubMed:15952736). May transport vitamin E in body fluids under conditions where the lipoprotein system is not sufficient (PubMed:15952736). May be involved in the transport of vitamin E across the blood-brain barrier (PubMed:19046407)
- Specific Function
- vitamin E binding
- Gene Name
- AFM
- Uniprot ID
- P43652
- Uniprot Name
- Afamin
- Molecular Weight
- 69068.47 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis
- Specific Function
- growth factor activity
- Gene Name
- AGT
- Uniprot ID
- P01019
- Uniprot Name
- Angiotensinogen
- Molecular Weight
- 52069.475 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Promotes endocytosis, possesses opsonic properties and influences the mineral phase of bone. Shows affinity for calcium and barium ions
- Specific Function
- cysteine-type endopeptidase inhibitor activity
- Gene Name
- AHSG
- Uniprot ID
- P02765
- Uniprot Name
- Alpha-2-HS-glycoprotein
- Molecular Weight
- 39340.41 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. May also function as a calcium-dependent lectin
- Specific Function
- calcium ion binding
- Gene Name
- APCS
- Uniprot ID
- P02743
- Uniprot Name
- Serum amyloid P-component
- Molecular Weight
- 25386.92 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility
- Specific Function
- amyloid-beta binding
- Gene Name
- APOA1
- Uniprot ID
- P02647
- Uniprot Name
- Apolipoprotein A-I
- Molecular Weight
- 30777.58 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism
- Specific Function
- apolipoprotein receptor binding
- Gene Name
- APOA2
- Uniprot ID
- P02652
- Uniprot Name
- Apolipoprotein A-II
- Molecular Weight
- 11174.925 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons
- Specific Function
- antioxidant activity
- Gene Name
- APOA4
- Uniprot ID
- P06727
- Uniprot Name
- Apolipoprotein A-IV
- Molecular Weight
- 45371.745 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Macrophage receptor that binds to the apolipoprotein B48 (APOB) of dietary triglyceride (TG)-rich lipoproteins (TRL) or to a like domain of APOB in hypertriglyceridemic very low density lipoprotein (HTG-VLDL). Binds and internalizes TRL when out of the context of the macrophage. May provide essential lipids to reticuloendothelial cells. Could also be involved in foam cell formation with elevated TRL and remnant lipoprotein (RLP). Mediates the rapid high-affinity uptake of chylomicrons (CM), HTG-VLDL, and trypsinized (tryp) VLDL devoid of APOE in vitro in macrophages
- Specific Function
- very-low-density lipoprotein particle receptor activity
- Gene Name
- APOBR
- Uniprot ID
- Q0VD83
- Uniprot Name
- Apolipoprotein B receptor
- Molecular Weight
- 115633.15 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase. Both proapolipoprotein C-II and apolipoprotein C-II can activate lipoprotein lipase. In normolipidemic individuals, it is mainly distributed in the HDL, whereas in hypertriglyceridemic individuals, predominantly found in the VLDL and LDL
- Specific Function
- lipase inhibitor activity
- Gene Name
- APOC2
- Uniprot ID
- P02655
- Uniprot Name
- Apolipoprotein C-II
- Molecular Weight
- 11283.78 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Component of triglyceride-rich very low density lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma (PubMed:18201179, PubMed:22510806). Plays a multifaceted role in triglyceride homeostasis (PubMed:18201179, PubMed:22510806). Intracellularly, promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and secretion; extracellularly, attenuates hydrolysis and clearance of triglyceride-rich lipoproteins (TRLs) (PubMed:18201179, PubMed:22510806). Impairs the lipolysis of TRLs by inhibiting lipoprotein lipase and the hepatic uptake of TRLs by remnant receptors (PubMed:18201179, PubMed:22510806). Formed of several curved helices connected via semiflexible hinges, so that it can wrap tightly around the curved micelle surface and easily adapt to the different diameters of its natural binding partners (PubMed:18408013)
- Specific Function
- cholesterol binding
- Gene Name
- APOC3
- Uniprot ID
- P02656
- Uniprot Name
- Apolipoprotein C-III
- Molecular Weight
- 10852.19 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- APOD occurs in the macromolecular complex with lecithin-cholesterol acyltransferase. It is probably involved in the transport and binding of bilin. Appears to be able to transport a variety of ligands in a number of different contexts
- Specific Function
- cholesterol binding
- Gene Name
- APOD
- Uniprot ID
- P05090
- Uniprot Name
- Apolipoprotein D
- Molecular Weight
- 21275.37 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids (PubMed:14754908, PubMed:1911868, PubMed:6860692). APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance (PubMed:14754908, PubMed:1911868, PubMed:1917954, PubMed:23620513, PubMed:2762297, PubMed:6860692, PubMed:9395455). Apolipoproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma (PubMed:2762297, PubMed:6860692, PubMed:9395455). As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL) (PubMed:1911868, PubMed:6860692). It also binds a wide range of cellular receptors including the LDL receptor/LDLR, the LDL receptor-related proteins LRP1, LRP2 and LRP8 and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles (PubMed:12950167, PubMed:1530612, PubMed:1917954, PubMed:20030366, PubMed:20303980, PubMed:2063194, PubMed:2762297, PubMed:7635945, PubMed:7768901, PubMed:8756331, PubMed:8939961). Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells (PubMed:23676495, PubMed:7635945, PubMed:9395455, PubMed:9488694). A main function of APOE is to mediate lipoprotein clearance through the uptake of chylomicrons, VLDLs, and HDLs by hepatocytes (PubMed:1911868, PubMed:1917954, PubMed:23676495, PubMed:29516132, PubMed:9395455). APOE is also involved in the biosynthesis by the liver of VLDLs as well as their uptake by peripheral tissues ensuring the delivery of triglycerides and energy storage in muscle, heart and adipose tissues (PubMed:2762297, PubMed:29516132). By participating in the lipoprotein-mediated distribution of lipids among tissues, APOE plays a critical role in plasma and tissues lipid homeostasis (PubMed:1917954, PubMed:2762297, PubMed:29516132). APOE is also involved in two steps of reverse cholesterol transport, the HDLs-mediated transport of cholesterol from peripheral tissues to the liver, and thereby plays an important role in cholesterol homeostasis (PubMed:14754908, PubMed:23620513, PubMed:9395455). First, it is functionally associated with ABCA1 in the biogenesis of HDLs in tissues (PubMed:14754908, PubMed:23620513). Second, it is enriched in circulating HDLs and mediates their uptake by hepatocytes (PubMed:9395455). APOE also plays an important role in lipid transport in the central nervous system, regulating neuron survival and sprouting (PubMed:25173806, PubMed:8939961). APOE is also involved in innate and adaptive immune responses, controlling for instance the survival of myeloid-derived suppressor cells (By similarity). Binds to the immune cell receptor LILRB4 (PubMed:30333625). APOE may also play a role in transcription regulation through a receptor-dependent and cholesterol-independent mechanism, that activates MAP3K12 and a non-canonical MAPK signal transduction pathway that results in enhanced AP-1-mediated transcription of APP (PubMed:28111074)
- Specific Function
- amyloid-beta binding
- Gene Name
- APOE
- Uniprot ID
- P02649
- Uniprot Name
- Apolipoprotein E
- Molecular Weight
- 36153.83 Da
References
- Xu H, Finkelstein DI, Adlard PA: Interactions of metals and Apolipoprotein E in Alzheimer's disease. Front Aging Neurosci. 2014 Jun 12;6:121. doi: 10.3389/fnagi.2014.00121. eCollection 2014. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells
- Specific Function
- heparin binding
- Gene Name
- APOH
- Uniprot ID
- P02749
- Uniprot Name
- Beta-2-glycoprotein 1
- Molecular Weight
- 38297.8 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Stimulates lipid degradation in adipocytes and causes the extensive fat losses associated with some advanced cancers. May bind polyunsaturated fatty acids
- Specific Function
- protein transmembrane transporter activity
- Gene Name
- AZGP1
- Uniprot ID
- P25311
- Uniprot Name
- Zinc-alpha-2-glycoprotein
- Molecular Weight
- 34258.525 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes
- Specific Function
- Not Available
- Gene Name
- C1QC
- Uniprot ID
- P02747
- Uniprot Name
- Complement C1q subcomponent subunit C
- Molecular Weight
- 25773.56 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- C1s B chain is a serine protease that combines with C1q and C1r to form C1, the first component of the classical pathway of the complement system. C1r activates C1s so that it can, in turn, activate C2 and C4. Cleaves also IGFBP5 and thereby inhibits the trophic effects of IGF1
- Specific Function
- calcium ion binding
- Gene Name
- C1S
- Uniprot ID
- P09871
- Uniprot Name
- Complement C1s subcomponent
- Molecular Weight
- 76683.905 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- C3 plays a central role in the activation of the complement system. Its processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates
- Specific Function
- C5L2 anaphylatoxin chemotactic receptor binding
- Gene Name
- C3
- Uniprot ID
- P01024
- Uniprot Name
- Complement C3
- Molecular Weight
- 187146.73 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Non-enzymatic component of the C3 and C5 convertases and thus essential for the propagation of the classical complement pathway. Covalently binds to immunoglobulins and immune complexes and enhances the solubilization of immune aggregates and the clearance of IC through CR1 on erythrocytes. C4A isotype is responsible for effective binding to form amide bonds with immune aggregates or protein antigens, while C4B isotype catalyzes the transacylation of the thioester carbonyl group to form ester bonds with carbohydrate antigens
- Specific Function
- carbohydrate binding
- Gene Name
- C4B
- Uniprot ID
- P0C0L5
- Uniprot Name
- Complement C4-B
- Molecular Weight
- 192749.785 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Controls the classical pathway of complement activation. It binds as a cofactor to C3b/C4b inactivator (C3bINA), which then hydrolyzes the complement fragment C4b. It also accelerates the degradation of the C4bC2a complex (C3 convertase) by dissociating the complement fragment C2a. Alpha chain binds C4b. It interacts also with anticoagulant protein S and with serum amyloid P component
- Specific Function
- RNA binding
- Gene Name
- C4BPA
- Uniprot ID
- P04003
- Uniprot Name
- C4b-binding protein alpha chain
- Molecular Weight
- 67032.63 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Activation of C5 by a C5 convertase initiates the spontaneous assembly of the late complement components, C5-C9, into the membrane attack complex. C5b has a transient binding site for C6. The C5b-C6 complex is the foundation upon which the lytic complex is assembled
- Specific Function
- chemokine activity
- Gene Name
- C5
- Uniprot ID
- P01031
- Uniprot Name
- Complement C5
- Molecular Weight
- 188303.705 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells
- Specific Function
- protein-containing complex binding
- Gene Name
- C8B
- Uniprot ID
- P07358
- Uniprot Name
- Complement component C8 beta chain
- Molecular Weight
- 66947.22 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells (PubMed:26841934, PubMed:9212048, PubMed:9634479). C9 is the pore-forming subunit of the MAC (PubMed:26841934, PubMed:30111885, PubMed:4055801)
- Specific Function
- Not Available
- Gene Name
- C9
- Uniprot ID
- P02748
- Uniprot Name
- Complement component C9
- Molecular Weight
- 63172.72 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Glycoprotein that plays an essential role in maintaining a well-balanced immune response by modulating complement activation. Acts as a soluble inhibitor of complement, where its binding to self markers such as glycan structures prevents complement activation and amplification on cell surfaces (PubMed:21285368, PubMed:25402769). Accelerates the decay of the complement alternative pathway (AP) C3 convertase C3bBb, thus preventing local formation of more C3b, the central player of the complement amplification loop (PubMed:19503104, PubMed:26700768). As a cofactor of the serine protease factor I, CFH also regulates proteolytic degradation of already-deposited C3b (PubMed:18252712, PubMed:23332154, PubMed:28671664). In addition, mediates several cellular responses through interaction with specific receptors. For example, interacts with CR3/ITGAM receptor and thereby mediates the adhesion of human neutrophils to different pathogens. In turn, these pathogens are phagocytosed and destroyed (PubMed:20008295, PubMed:9558116)
- Specific Function
- complement component C3b binding
- Gene Name
- CFH
- Uniprot ID
- P08603
- Uniprot Name
- Complement factor H
- Molecular Weight
- 139095.31 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Trypsin-like serine protease that plays an essential role in regulating the immune response by controlling all complement pathways. Inhibits these pathways by cleaving three peptide bonds in the alpha-chain of C3b and two bonds in the alpha-chain of C4b thereby inactivating these proteins (PubMed:17320177, PubMed:7360115). Essential cofactors for these reactions include factor H and C4BP in the fluid phase and membrane cofactor protein/CD46 and CR1 on cell surfaces (PubMed:12055245, PubMed:2141838, PubMed:9605165). The presence of these cofactors on healthy cells allows degradation of deposited C3b by CFI in order to prevent undesired complement activation, while in apoptotic cells or microbes, the absence of such cofactors leads to C3b-mediated complement activation and subsequent opsonization (PubMed:28671664)
- Specific Function
- metal ion binding
- Gene Name
- CFI
- Uniprot ID
- P05156
- Uniprot Name
- Complement factor I
- Molecular Weight
- 65749.78 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Tetranectin binds to plasminogen and to isolated kringle 4. May be involved in the packaging of molecules destined for exocytosis. Plays a role in retinal function (PubMed:35331648)
- Specific Function
- calcium ion binding
- Gene Name
- CLEC3B
- Uniprot ID
- P05452
- Uniprot Name
- Tetranectin
- Molecular Weight
- 22536.665 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Functions as extracellular chaperone that prevents aggregation of non native proteins (PubMed:11123922, PubMed:19535339). Prevents stress-induced aggregation of blood plasma proteins (PubMed:11123922, PubMed:12176985, PubMed:17260971, PubMed:19996109). Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro) (PubMed:12047389, PubMed:17407782, PubMed:17412999). Does not require ATP (PubMed:11123922). Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70 (PubMed:11123922). Does not refold proteins by itself (PubMed:11123922). Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation (PubMed:21505792). Protects cells against apoptosis and against cytolysis by complement (PubMed:2780565). Intracellular forms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:20068069). Promotes proteasomal degradation of COMMD1 and IKBKB (PubMed:20068069). Modulates NF-kappa-B transcriptional activity (PubMed:12882985). A mitochondrial form suppresses BAX-dependent release of cytochrome c into the cytoplasm and inhibit apoptosis (PubMed:16113678, PubMed:17689225). Plays a role in the regulation of cell proliferation (PubMed:19137541). An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5 (PubMed:22689054). Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (PubMed:24073260). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity)
- Specific Function
- amyloid-beta binding
- Gene Name
- CLU
- Uniprot ID
- P10909
- Uniprot Name
- Clusterin
- Molecular Weight
- 52494.22 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing. Thrombin triggers the production of pro-inflammatory cytokines, such as MCP-1/CCL2 and IL8/CXCL8, in endothelial cells (PubMed:30568593, PubMed:9780208)
- Specific Function
- calcium ion binding
- Gene Name
- F2
- Uniprot ID
- P00734
- Uniprot Name
- Prothrombin
- Molecular Weight
- 70036.295 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Multifunctional and multicompartmental protein involved in inflammation and infection processes, ribosome biogenesis, protein synthesis in mitochondria, regulation of apoptosis, transcriptional regulation and pre-mRNA splicing (PubMed:10022843, PubMed:10479529, PubMed:10722602, PubMed:11086025, PubMed:11859136, PubMed:15243141, PubMed:16140380, PubMed:16177118, PubMed:17881511, PubMed:18676636, PubMed:19004836, PubMed:19164550, PubMed:20810993, PubMed:21536856, PubMed:21544310, PubMed:22700724, PubMed:28942965, PubMed:8662673, PubMed:8710908, PubMed:9461517). At the cell surface is thought to act as an endothelial receptor for plasma proteins of the complement and kallikrein-kinin cascades (PubMed:10479529, PubMed:11859136, PubMed:8662673, PubMed:8710908). Putative receptor for C1q; specifically binds to the globular 'heads' of C1q thus inhibiting C1; may perform the receptor function through a complex with C1qR/CD93 (PubMed:20810993, PubMed:8195709). In complex with cytokeratin-1/KRT1 is a high affinity receptor for kininogen-1/HMWK (PubMed:21544310). Can also bind other plasma proteins, such as coagulation factor XII leading to its autoactivation. May function to bind initially fluid kininogen-1 to the cell membrane. The secreted form may enhance both extrinsic and intrinsic coagulation pathways. It is postulated that the cell surface form requires docking with transmembrane proteins for downstream signaling which might be specific for a cell-type or response. By acting as C1q receptor is involved in chemotaxis of immature dendritic cells and neutrophils and is proposed to signal through CD209/DC-SIGN on immature dendritic cells, through integrin alpha-4/beta-1 during trophoblast invasion of the decidua, and through integrin beta-1 during endothelial cell adhesion and spreading (PubMed:16140380, PubMed:22700724, PubMed:9461517). Signaling involved in inhibition of innate immune response is implicating the PI3K-AKT/PKB pathway (PubMed:16177118). Required for protein synthesis in mitochondria (PubMed:28942965). In mitochondrial translation may be involved in formation of functional 55S mitoribosomes; the function seems to involve its RNA-binding activity (By similarity). May be involved in the nucleolar ribosome maturation process; the function may involve the exchange of FBL for RRP1 in the association with pre-ribosome particles (By similarity). Involved in regulation of RNA splicing by inhibiting the RNA-binding capacity of SRSF1 and its phosphorylation (PubMed:10022843, PubMed:21536856). Is required for the nuclear translocation of splicing factor U2AF1L4 (By similarity). Involved in regulation of CDKN2A- and HRK-mediated apoptosis. Stabilizes mitochondrial CDKN2A isoform smARF (PubMed:17486078). May be involved in regulation of FOXC1 transcriptional activity and NFY/CCAAT-binding factor complex-mediated transcription (PubMed:15243141, PubMed:18676636). May play a role in antibacterial defense as it can bind to cell surface hyaluronan and inhibit Streptococcus pneumoniae hyaluronate lyase (PubMed:19004836). May be involved in modulation of the immune response; ligation by HCV core protein is resulting in suppression of interleukin-12 production in monocyte-derived dendritic cells (PubMed:11086025, PubMed:17881511). Involved in regulation of antiviral response by inhibiting RIGI- and IFIH1-mediated signaling pathways probably involving its association with MAVS after viral infection (PubMed:19164550). Acts as a regulator of DNA repair via homologous recombination by inhibiting the activity of MRE11: interacts with unphosphorylated MRE11 and RAD50 in absence of DNA damage, preventing formation and activity of the MRN complex. Following DNA damage, dissociates from phosphorylated MRE11, allowing formation of the MRN complex (PubMed:31353207)
- Specific Function
- adrenergic receptor binding
- Gene Name
- C1QBP
- Uniprot ID
- Q07021
- Uniprot Name
- Complement component 1 Q subcomponent-binding protein, mitochondrial
- Molecular Weight
- 31361.935 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed (PubMed:19666512). Plays a role in ciliogenesis (PubMed:20393563)
- Specific Function
- actin binding
- Gene Name
- GSN
- Uniprot ID
- P06396
- Uniprot Name
- Gelsolin
- Molecular Weight
- 85696.935 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Involved in oxygen transport from the lung to the various peripheral tissues
- Specific Function
- heme binding
- Gene Name
- HBA1
- Uniprot ID
- P69905
- Uniprot Name
- Hemoglobin subunit alpha
- Molecular Weight
- 15257.405 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Involved in oxygen transport from the lung to the various peripheral tissues
- Specific Function
- heme binding
- Gene Name
- HBB
- Uniprot ID
- P68871
- Uniprot Name
- Hemoglobin subunit beta
- Molecular Weight
- 15998.34 Da
References
- Winterbourn CC, Carrell RW: Oxidation of human haemoglobin by copper. Mechanism and suggested role of the thiol group of residue beta-93. Biochem J. 1977 Jul 1;165(1):141-8. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Component of heterochromatin that recognizes and binds histone H3 tails methylated at 'Lys-9' (H3K9me), leading to epigenetic repression. In contrast, it is excluded from chromatin when 'Tyr-41' of histone H3 is phosphorylated (H3Y41ph). Can interact with lamin-B receptor (LBR). This interaction can contribute to the association of the heterochromatin with the inner nuclear membrane. Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins
- Specific Function
- chromatin binding
- Gene Name
- CBX5
- Uniprot ID
- P45973
- Uniprot Name
- Chromobox protein homolog 5
- Molecular Weight
- 22224.81 Da
References
- Bryan SE, Simons SJ, Vizard DL, Hardy KJ: Interactions of mercury and copper with constitutive heterochromatin and euchromatin in vivo and in vitro. Biochemistry. 1976 Apr 20;15(8):1667-76. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Primate-specific plasma protein associated with apolipoprotein L-I (apoL-I)-containing high-density lipoprotein (HDL). This HDL particle, termed trypanosome lytic factor-1 (TLF-1), mediates human innate immune protection against many species of African trypanosomes. Binds hemoglobin with high affinity and may contribute to the clearance of cell-free hemoglobin to allow hepatic recycling of heme iron
- Specific Function
- hemoglobin binding
- Gene Name
- HPR
- Uniprot ID
- P00739
- Uniprot Name
- Haptoglobin-related protein
- Molecular Weight
- 39029.345 Da
References
- Muranjan M, Nussenzweig V, Tomlinson S: Characterization of the human serum trypanosome toxin, haptoglobin-related protein. J Biol Chem. 1998 Feb 13;273(7):3884-7. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Involved in protein-protein interactions that result in protein complexes, receptor-ligand binding or cell adhesion
- Specific Function
- insulin-like growth factor binding
- Gene Name
- IGFALS
- Uniprot ID
- P35858
- Uniprot Name
- Insulin-like growth factor-binding protein complex acid labile subunit
- Molecular Weight
- 66034.13 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). Mediates IgG effector functions on monocytes triggering ADCC of virus-infected cells
- Specific Function
- antigen binding
- Gene Name
- IGHG1
- Uniprot ID
- P01857
- Uniprot Name
- Immunoglobulin heavy constant gamma 1
- Molecular Weight
- 43911.6 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268)
- Specific Function
- antigen binding
- Gene Name
- IGHG4
- Uniprot ID
- P01861
- Uniprot Name
- Immunoglobulin heavy constant gamma 4
- Molecular Weight
- 43831.355 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268)
- Specific Function
- antigen binding
- Gene Name
- IGKV3-20
- Uniprot ID
- P01619
- Uniprot Name
- Immunoglobulin kappa variable 3-20
- Molecular Weight
- 12556.955 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Critical for B-cell development
- Specific Function
- antigen binding
- Gene Name
- IGLL1
- Uniprot ID
- P15814
- Uniprot Name
- Immunoglobulin lambda-like polypeptide 1
- Molecular Weight
- 22962.89 Da
References
- Baker BL, Hultquist DE: A copper-binding immunoglobulin from a myeloma patient. Purification, identification, and physical characterization. J Biol Chem. 1978 Feb 25;253(4):1195-200. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- May act as a carrier of hyaluronan in serum or as a binding protein between hyaluronan and other matrix protein, including those on cell surfaces in tissues to regulate the localization, synthesis and degradation of hyaluronan which are essential to cells undergoing biological processes
- Specific Function
- endopeptidase inhibitor activity
- Gene Name
- ITIH2
- Uniprot ID
- P19823
- Uniprot Name
- Inter-alpha-trypsin inhibitor heavy chain H2
- Molecular Weight
- 106462.725 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Kininogens are inhibitors of thiol proteases. HMW-kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII; HMW-kininogen inhibits the thrombin- and plasmin-induced aggregation of thrombocytes. LMW-kininogen inhibits the aggregation of thrombocytes. LMW-kininogen is in contrast to HMW-kininogen not involved in blood clotting
- Specific Function
- cysteine-type endopeptidase inhibitor activity
- Gene Name
- KNG1
- Uniprot ID
- P01042
- Uniprot Name
- Kininogen-1
- Molecular Weight
- 71956.965 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- May regulate the activity of kinases such as PKC and SRC via binding to integrin beta-1 (ITB1) and the receptor of activated protein C kinase 1 (RACK1). In complex with C1QBP is a high affinity receptor for kininogen-1/HMWK
- Specific Function
- carbohydrate binding
- Gene Name
- KRT1
- Uniprot ID
- P04264
- Uniprot Name
- Keratin, type II cytoskeletal 1
- Molecular Weight
- 66038.505 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Plays a role in the establishment of the epidermal barrier on plantar skin (By similarity). Involved in the maintenance of cell layer development and keratin filament bundles in suprabasal cells of the epithelium (By similarity)
- Specific Function
- protein heterodimerization activity
- Gene Name
- KRT10
- Uniprot ID
- P13645
- Uniprot Name
- Keratin, type I cytoskeletal 10
- Molecular Weight
- 58826.915 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Probably contributes to terminal cornification (PubMed:1380918). Associated with keratinocyte activation, proliferation and keratinization (PubMed:12598329). Required for maintenance of corneocytes and keratin filaments in suprabasal keratinocytes in the epidermis of the ear, potentially via moderation of expression and localization of keratins and their partner proteins (By similarity). Plays a role in the establishment of the epidermal barrier on plantar skin (By similarity)
- Specific Function
- cytoskeletal protein binding
- Gene Name
- KRT2
- Uniprot ID
- P35908
- Uniprot Name
- Keratin, type II cytoskeletal 2 epidermal
- Molecular Weight
- 65432.65 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- May serve an important special function either in the mature palmar and plantar skin tissue or in the morphogenetic program of the formation of these tissues. Plays a role in keratin filament assembly
- Specific Function
- structural constituent of cytoskeleton
- Gene Name
- KRT9
- Uniprot ID
- P35527
- Uniprot Name
- Keratin, type I cytoskeletal 9
- Molecular Weight
- 62064.29 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Not Available
- Specific Function
- type I transforming growth factor beta receptor binding
- Gene Name
- LRG1
- Uniprot ID
- P02750
- Uniprot Name
- Leucine-rich alpha-2-glycoprotein
- Molecular Weight
- 38177.49 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Not Available
- Specific Function
- collagen binding
- Gene Name
- LUM
- Uniprot ID
- P51884
- Uniprot Name
- Lumican
- Molecular Weight
- 38428.585 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- May play a scavenger role by digesting biologically active peptidoglycan (PGN) into biologically inactive fragments. Has no direct bacteriolytic activity
- Specific Function
- N-acetylmuramoyl-L-alanine amidase activity
- Gene Name
- PGLYRP2
- Uniprot ID
- Q96PD5
- Uniprot Name
- N-acetylmuramoyl-L-alanine amidase
- Molecular Weight
- 62216.365 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells
- Specific Function
- apolipoprotein binding
- Gene Name
- PLG
- Uniprot ID
- P00747
- Uniprot Name
- Plasminogen
- Molecular Weight
- 90568.415 Da
References
- Lind SE, McDonagh JR, Smith CJ: Oxidative inactivation of plasmin and other serine proteases by copper and ascorbate. Blood. 1993 Sep 1;82(5):1522-31. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Hydrolyzes the toxic metabolites of a variety of organophosphorus insecticides. Capable of hydrolyzing a broad spectrum of organophosphate substrates and lactones, and a number of aromatic carboxylic acid esters. Mediates an enzymatic protection of low density lipoproteins against oxidative modification and the consequent series of events leading to atheroma formation
- Specific Function
- acyl-L-homoserine-lactone lactonohydrolase activity
- Gene Name
- PON1
- Uniprot ID
- P27169
- Uniprot Name
- Serum paraoxonase/arylesterase 1
- Molecular Weight
- 39730.99 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- LA-PF4 stimulates DNA synthesis, mitosis, glycolysis, intracellular cAMP accumulation, prostaglandin E2 secretion, and synthesis of hyaluronic acid and sulfated glycosaminoglycan. It also stimulates the formation and secretion of plasminogen activator by human synovial cells. NAP-2 is a ligand for CXCR1 and CXCR2, and NAP-2, NAP-2(73), NAP-2(74), NAP-2(1-66), and most potent NAP-2(1-63) are chemoattractants and activators for neutrophils. TC-1 and TC-2 are antibacterial proteins, in vitro released from activated platelet alpha-granules. CTAP-III(1-81) is more potent than CTAP-III desensitize chemokine-induced neutrophil activation
- Specific Function
- chemokine activity
- Gene Name
- PPBP
- Uniprot ID
- P02775
- Uniprot Name
- Platelet basic protein
- Molecular Weight
- 13894.035 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin
- Specific Function
- identical protein binding
- Gene Name
- SERPINA1
- Uniprot ID
- P01009
- Uniprot Name
- Alpha-1-antitrypsin
- Molecular Weight
- 46736.195 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Inhibits human amidolytic and kininogenase activities of tissue kallikrein. Inhibition is achieved by formation of an equimolar, heat- and SDS-stable complex between the inhibitor and the enzyme, and generation of a small C-terminal fragment of the inhibitor due to cleavage at the reactive site by tissue kallikrein
- Specific Function
- serine-type endopeptidase inhibitor activity
- Gene Name
- SERPINA4
- Uniprot ID
- P29622
- Uniprot Name
- Kallistatin
- Molecular Weight
- 48541.51 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Major transport protein for glucocorticoids and progestins in the blood of almost all vertebrate species
- Specific Function
- serine-type endopeptidase inhibitor activity
- Gene Name
- SERPINA6
- Uniprot ID
- P08185
- Uniprot Name
- Corticosteroid-binding globulin
- Molecular Weight
- 45140.49 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Major thyroid hormone transport protein in serum
- Specific Function
- serine-type endopeptidase inhibitor activity
- Gene Name
- SERPINA7
- Uniprot ID
- P05543
- Uniprot Name
- Thyroxine-binding globulin
- Molecular Weight
- 46324.12 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade (PubMed:15140129, PubMed:15853774). AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa (PubMed:15140129). Its inhibitory activity is greatly enhanced in the presence of heparin
- Specific Function
- heparin binding
- Gene Name
- SERPINC1
- Uniprot ID
- P01008
- Uniprot Name
- Antithrombin-III
- Molecular Weight
- 52601.935 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Thrombin inhibitor activated by the glycosaminoglycans, heparin or dermatan sulfate. In the presence of the latter, HC-II becomes the predominant thrombin inhibitor in place of antithrombin III (AT-III). Also inhibits chymotrypsin, but in a glycosaminoglycan-independent manner
- Specific Function
- endopeptidase inhibitor activity
- Gene Name
- SERPIND1
- Uniprot ID
- P05546
- Uniprot Name
- Heparin cofactor 2
- Molecular Weight
- 57070.16 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Neurotrophic protein; induces extensive neuronal differentiation in retinoblastoma cells. Potent inhibitor of angiogenesis. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, it exhibits no serine protease inhibitory activity
- Specific Function
- serine-type endopeptidase inhibitor activity
- Gene Name
- SERPINF1
- Uniprot ID
- P36955
- Uniprot Name
- Pigment epithelium-derived factor
- Molecular Weight
- 46311.685 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Serine protease inhibitor. The major targets of this inhibitor are plasmin and trypsin, but it also inactivates matriptase-3/TMPRSS7 and chymotrypsin
- Specific Function
- endopeptidase inhibitor activity
- Gene Name
- SERPINF2
- Uniprot ID
- P08697
- Uniprot Name
- Alpha-2-antiplasmin
- Molecular Weight
- 54565.32 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Activation of the C1 complex is under control of the C1-inhibitor. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases. May play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. Very efficient inhibitor of FXIIa. Inhibits chymotrypsin and kallikrein
- Specific Function
- serine-type endopeptidase inhibitor activity
- Gene Name
- SERPING1
- Uniprot ID
- P05155
- Uniprot Name
- Plasma protease C1 inhibitor
- Molecular Weight
- 55153.645 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain
- Specific Function
- hormone activity
- Gene Name
- TTR
- Uniprot ID
- P02766
- Uniprot Name
- Transthyretin
- Molecular Weight
- 15886.88 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway
- Specific Function
- collagen binding
- Gene Name
- VTN
- Uniprot ID
- P04004
- Uniprot Name
- Vitronectin
- Molecular Weight
- 54305.135 Da
References
- Wang F, Chmil C, Pierce F, Ganapathy K, Gump BB, MacKenzie JA, Metchref Y, Bendinskas K: Immobilized metal affinity chromatography and human serum proteomics. J Chromatogr B Analyt Technol Biomed Life Sci. 2013 Sep 1;934:26-33. doi: 10.1016/j.jchromb.2013.06.032. Epub 2013 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- May play a role in postsynaptic function. The C-terminal gamma-secretase processed fragment, ALID1, activates transcription activation through APBB1 (Fe65) binding (By similarity). Couples to JIP signal transduction through C-terminal binding. May interact with cellular G-protein signaling pathways. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I
- Specific Function
- alpha-2A adrenergic receptor binding
- Gene Name
- APLP1
- Uniprot ID
- P51693
- Uniprot Name
- Amyloid beta precursor like protein 1
- Molecular Weight
- 72175.825 Da
References
- Mayer MC, Kaden D, Schauenburg L, Hancock MA, Voigt P, Roeser D, Barucker C, Than ME, Schaefer M, Multhaup G: Novel zinc-binding site in the E2 domain regulates amyloid precursor-like protein 1 (APLP1) oligomerization. J Biol Chem. 2014 Jul 4;289(27):19019-30. doi: 10.1074/jbc.M114.570382. Epub 2014 May 22. [Article]
- Kind
- Protein group
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin
- Specific Function
- GTP binding
Components:
Name | UniProt ID |
---|---|
Tubulin alpha-3C chain | P0DPH7 |
Tubulin alpha-3D chain | P0DPH8 |
References
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
Enzymes
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Destroys radicals which are normally produced within the cells and which are toxic to biological systems
- Specific Function
- copper ion binding
- Gene Name
- SOD1
- Uniprot ID
- P00441
- Uniprot Name
- Superoxide dismutase [Cu-Zn]
- Molecular Weight
- 15935.685 Da
References
- Bost M, Houdart S, Oberli M, Kalonji E, Huneau JF, Margaritis I: Dietary copper and human health: Current evidence and unresolved issues. J Trace Elem Med Biol. 2016 May;35:107-15. doi: 10.1016/j.jtemb.2016.02.006. Epub 2016 Mar 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Catalyzes the oxidative deamination of primary amines to the corresponding aldehydes with the concomitant production of hydrogen peroxide and ammonia (PubMed:12072962, PubMed:19764817, PubMed:239684, PubMed:8144586). Its preferred substrates are the diamines histamine and 1-methylhistamine and it could therefore play a role in allergic and immune responses (PubMed:12072962). Has a broad specificity for diamines and can also act on cadaverine and putrescine, two products of amino acid catabolism (PubMed:12072962). It could also act on polyamines, like spermidine and spermine though less efficiently, and regulate various biological processes (PubMed:12072962, PubMed:239684)
- Specific Function
- calcium ion binding
- Gene Name
- AOC1
- Uniprot ID
- P19801
- Uniprot Name
- Diamine oxidase [copper-containing]
- Molecular Weight
- 85377.1 Da
References
- Bost M, Houdart S, Oberli M, Kalonji E, Huneau JF, Margaritis I: Dietary copper and human health: Current evidence and unresolved issues. J Trace Elem Med Biol. 2016 May;35:107-15. doi: 10.1016/j.jtemb.2016.02.006. Epub 2016 Mar 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin (PubMed:26838787). Regulator of Ras expression. May play a role in tumor suppression. Plays a role in the aortic wall architecture (By similarity)
- Specific Function
- collagen binding
- Gene Name
- LOX
- Uniprot ID
- P28300
- Uniprot Name
- Protein-lysine 6-oxidase
- Molecular Weight
- 46943.67 Da
References
- Bost M, Houdart S, Oberli M, Kalonji E, Huneau JF, Margaritis I: Dietary copper and human health: Current evidence and unresolved issues. J Trace Elem Med Biol. 2016 May;35:107-15. doi: 10.1016/j.jtemb.2016.02.006. Epub 2016 Mar 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix
- Specific Function
- cytochrome-c oxidase activity
- Gene Name
- MT-CO1
- Uniprot ID
- P00395
- Uniprot Name
- Cytochrome c oxidase subunit 1
- Molecular Weight
- 57040.91 Da
References
- Tapiero H, Townsend DM, Tew KD: Trace elements in human physiology and pathology. Copper. Biomed Pharmacother. 2003 Nov;57(9):386-98. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the initial and rate limiting step in the cascade of reactions leading to melanin production from tyrosine (By similarity). In addition to hydroxylating tyrosine to DOPA (3,4-dihydroxyphenylalanine), also catalyzes the oxidation of DOPA to DOPA-quinone, and possibly the oxidation of DHI (5,6-dihydroxyindole) to indole-5,6 quinone (PubMed:28661582)
- Specific Function
- copper ion binding
- Gene Name
- TYR
- Uniprot ID
- P14679
- Uniprot Name
- Tyrosinase
- Molecular Weight
- 60392.69 Da
References
- Tapiero H, Townsend DM, Tew KD: Trace elements in human physiology and pathology. Copper. Biomed Pharmacother. 2003 Nov;57(9):386-98. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Catalyzes the hydroxylation of dopamine to noradrenaline (also known as norepinephrine), and is thus vital for regulation of these neurotransmitters
- Specific Function
- catalytic activity
- Gene Name
- DBH
- Uniprot ID
- P09172
- Uniprot Name
- Dopamine beta-hydroxylase
- Molecular Weight
- 69064.45 Da
References
- Tapiero H, Townsend DM, Tew KD: Trace elements in human physiology and pathology. Copper. Biomed Pharmacother. 2003 Nov;57(9):386-98. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Bifunctional enzyme that catalyzes the post-translational modification of inactive peptidylglycine precursors to the corresponding bioactive alpha-amidated peptides, a terminal modification in biosynthesis of many neural and endocrine peptides (PubMed:12699694). Alpha-amidation involves two sequential reactions, both of which are catalyzed by separate catalytic domains of the enzyme. The first step, catalyzed by peptidyl alpha-hydroxylating monooxygenase (PHM) domain, is the copper-, ascorbate-, and O2- dependent stereospecific hydroxylation (with S stereochemistry) at the alpha-carbon (C-alpha) of the C-terminal glycine of the peptidylglycine substrate (PubMed:12699694). The second step, catalyzed by the peptidylglycine amidoglycolate lyase (PAL) domain, is the zinc-dependent cleavage of the N-C-alpha bond, producing the alpha-amidated peptide and glyoxylate (PubMed:12699694). Similarly, catalyzes the two-step conversion of an N-fatty acylglycine to a primary fatty acid amide and glyoxylate (By similarity)
- Specific Function
- calcium ion binding
- Gene Name
- PAM
- Uniprot ID
- P19021
- Uniprot Name
- Peptidyl-glycine alpha-amidating monooxygenase
- Molecular Weight
- 108331.35 Da
References
- Tapiero H, Townsend DM, Tew KD: Trace elements in human physiology and pathology. Copper. Biomed Pharmacother. 2003 Nov;57(9):386-98. [Article]
- Kind
- Protein group
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Catalyzes the oxidative deamination of primary and some secondary amine such as neurotransmitters, with concomitant reduction of oxygen to hydrogen peroxide and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues (PubMed:18391214, PubMed:20493079, PubMed:24169519, PubMed:8316221). Preferentially oxidizes serotonin (PubMed:20493079, PubMed:24169519). Also catalyzes the oxidative deamination of kynuramine to 3-(2-aminophenyl)-3-oxopropanal that can spontaneously condense to 4-hydroxyquinoline (By similarity)
- Specific Function
- aliphatic amine oxidase activity
Components:
References
- Tapiero H, Townsend DM, Tew KD: Trace elements in human physiology and pathology. Copper. Biomed Pharmacother. 2003 Nov;57(9):386-98. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Ribonuclease that cleaves tRNA within anticodon loops to produce tRNA-derived stress-induced fragments (tiRNAs) which inhibit protein synthesis and triggers the assembly of stress granules (SGs) (PubMed:1400510, PubMed:21855800). Binds to actin on the surface of endothelial cells; once bound, angiogenin is endocytosed and translocated to the nucleus (PubMed:8127865). Stimulates ribosomal RNA synthesis including that containing the initiation site sequences of 45S rRNA (PubMed:12051708). Angiogenin induces vascularization of normal and malignant tissues (PubMed:19354288). Angiogenic activity is regulated by interaction with RNH1 in vivo (PubMed:19354288)
- Specific Function
- actin binding
- Gene Name
- ANG
- Uniprot ID
- P03950
- Uniprot Name
- Angiogenin
- Molecular Weight
- 16549.95 Da
References
- Tapiero H, Townsend DM, Tew KD: Trace elements in human physiology and pathology. Copper. Biomed Pharmacother. 2003 Nov;57(9):386-98. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Its primary physiological function is unclear. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May promote myelin homeostasis through acting as an agonist for ADGRG6 receptor. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro) (By similarity). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or Zn(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity)
- Specific Function
- amyloid-beta binding
- Gene Name
- PRNP
- Uniprot ID
- P04156
- Uniprot Name
- Major prion protein
- Molecular Weight
- 27661.21 Da
References
- Tapiero H, Townsend DM, Tew KD: Trace elements in human physiology and pathology. Copper. Biomed Pharmacother. 2003 Nov;57(9):386-98. [Article]
Carriers
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- No
- Actions
- Binder
- General Function
- Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs (Probable). Its main function is the regulation of the colloidal osmotic pressure of blood (Probable). Major zinc transporter in plasma, typically binds about 80% of all plasma zinc (PubMed:19021548). Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (By similarity). The shared binding site between zinc and calcium at residue Asp-273 suggests a crosstalk between zinc and calcium transport in the blood (By similarity). The rank order of affinity is zinc > calcium > magnesium (By similarity). Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli (PubMed:6234017). Does not prevent iron uptake by the bacterial siderophore aerobactin (PubMed:6234017)
- Specific Function
- antioxidant activity
- Gene Name
- ALB
- Uniprot ID
- P02768
- Uniprot Name
- Albumin
- Molecular Weight
- 69365.94 Da
References
- Tapiero H, Townsend DM, Tew KD: Trace elements in human physiology and pathology. Copper. Biomed Pharmacother. 2003 Nov;57(9):386-98. [Article]
- Bar-Or D, Rael LT, Lau EP, Rao NK, Thomas GW, Winkler JV, Yukl RL, Kingston RG, Curtis CG: An analog of the human albumin N-terminus (Asp-Ala-His-Lys) prevents formation of copper-induced reactive oxygen species. Biochem Biophys Res Commun. 2001 Jun 15;284(3):856-62. [Article]
- Sakata N, Moh A, Takebayashi S: Contribution of superoxide to reduced antioxidant activity of glycoxidative serum albumin. Heart Vessels. 2002 Nov;17(1):22-9. [Article]
- She YM, Narindrasorasak S, Yang S, Spitale N, Roberts EA, Sarkar B: Identification of metal-binding proteins in human hepatoma lines by immobilized metal affinity chromatography and mass spectrometry. Mol Cell Proteomics. 2003 Dec;2(12):1306-18. Epub 2003 Oct 7. [Article]
- Smith SD, She YM, Roberts EA, Sarkar B: Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J Proteome Res. 2004 Jul-Aug;3(4):834-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- No
- Actions
- Binder
- General Function
- Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region, a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase
- Specific Function
- brain-derived neurotrophic factor binding
- Gene Name
- A2M
- Uniprot ID
- P01023
- Uniprot Name
- Alpha-2-macroglobulin
- Molecular Weight
- 163289.945 Da
References
- Liu N, Lo LS, Askary SH, Jones L, Kidane TZ, Trang T, Nguyen M, Goforth J, Chu YH, Vivas E, Tsai M, Westbrook T, Linder MC: Transcuprein is a macroglobulin regulated by copper and iron availability. J Nutr Biochem. 2007 Sep;18(9):597-608. Epub 2007 Mar 23. [Article]
- Tapiero H, Townsend DM, Tew KD: Trace elements in human physiology and pathology. Copper. Biomed Pharmacother. 2003 Nov;57(9):386-98. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- No
- Actions
- Binder
- General Function
- Multifunctional blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane (PubMed:16150804). Copper ions provide a large number of enzymatic activites. Oxidizes highly toxic ferrous ions to the ferric state for further incorporation onto apo-transferrins, catalyzes Cu(+) oxidation and promotes the oxidation of biogenic amines such as norepinephrin and serotonin (PubMed:14623105, PubMed:4643313, PubMed:5912351). Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1 (By similarity). Has glutathione peroxidase-like activity, can remove both hydrogen peroxide and lipid hydroperoxide in the presence of thiols (PubMed:10481051). Also shows NO-oxidase and NO2 synthase activities that determine endocrine NO homeostasis (PubMed:16906150)
- Specific Function
- copper ion binding
- Gene Name
- CP
- Uniprot ID
- P00450
- Uniprot Name
- Ceruloplasmin
- Molecular Weight
- 122218.48 Da
References
- Tapiero H, Townsend DM, Tew KD: Trace elements in human physiology and pathology. Copper. Biomed Pharmacother. 2003 Nov;57(9):386-98. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- No
- Actions
- Binder
- General Function
- Binds and deliver cytosolic copper to the copper ATPase proteins. May be important in cellular antioxidant defense
- Specific Function
- copper chaperone activity
- Gene Name
- ATOX1
- Uniprot ID
- O00244
- Uniprot Name
- Copper transport protein ATOX1
- Molecular Weight
- 7401.575 Da
References
- Tapiero H, Townsend DM, Tew KD: Trace elements in human physiology and pathology. Copper. Biomed Pharmacother. 2003 Nov;57(9):386-98. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- No
- Actions
- Binder
- General Function
- Delivers copper to copper zinc superoxide dismutase (SOD1)
- Specific Function
- cadherin binding
- Gene Name
- CCS
- Uniprot ID
- O14618
- Uniprot Name
- Copper chaperone for superoxide dismutase
- Molecular Weight
- 29040.445 Da
References
- Tapiero H, Townsend DM, Tew KD: Trace elements in human physiology and pathology. Copper. Biomed Pharmacother. 2003 Nov;57(9):386-98. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- No
- Actions
- Binder
- General Function
- Copper metallochaperone essential for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. Binds two copper ions and delivers them to the metallochaperone SCO1 which transports the copper ions to the Cu(A) site on the cytochrome c oxidase subunit II (MT-CO2/COX2)
- Specific Function
- copper chaperone activity
- Gene Name
- COX17
- Uniprot ID
- Q14061
- Uniprot Name
- Cytochrome c oxidase copper chaperone
- Molecular Weight
- 6915.03 Da
References
- Tapiero H, Townsend DM, Tew KD: Trace elements in human physiology and pathology. Copper. Biomed Pharmacother. 2003 Nov;57(9):386-98. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- No
- Actions
- Binder
- General Function
- Plasma membrane ferroxidase that mediates the extracellular conversion of ferrous/Fe(2+) iron into its ferric/Fe(3+) form. Couples ferroportin which specifically exports ferrous/Fe(2+) iron from cells to transferrin that only binds and shuttles extracellular ferric/Fe(3+) iron throughout the body (PubMed:22961397, PubMed:37277838). By helping iron transfer from cells to blood mainly contributes to dietary iron absorption by the intestinal epithelium and more generally regulates iron levels in the body (By similarity)
- Specific Function
- copper ion binding
- Gene Name
- HEPH
- Uniprot ID
- Q9BQS7
- Uniprot Name
- Hephaestin
- Molecular Weight
- 130447.755 Da
References
- Tapiero H, Townsend DM, Tew KD: Trace elements in human physiology and pathology. Copper. Biomed Pharmacother. 2003 Nov;57(9):386-98. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- No
- Actions
- Binder
- General Function
- Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin
- Specific Function
- copper ion binding
- Gene Name
- F5
- Uniprot ID
- P12259
- Uniprot Name
- Coagulation factor V
- Molecular Weight
- 251701.245 Da
References
- Tapiero H, Townsend DM, Tew KD: Trace elements in human physiology and pathology. Copper. Biomed Pharmacother. 2003 Nov;57(9):386-98. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- No
- Actions
- Binder
- General Function
- Factor VIII, along with calcium and phospholipid, acts as a cofactor for F9/factor IXa when it converts F10/factor X to the activated form, factor Xa
- Specific Function
- copper ion binding
- Gene Name
- F8
- Uniprot ID
- P00451
- Uniprot Name
- Coagulation factor VIII
- Molecular Weight
- 267007.42 Da
References
- Tapiero H, Townsend DM, Tew KD: Trace elements in human physiology and pathology. Copper. Biomed Pharmacother. 2003 Nov;57(9):386-98. [Article]
- Kind
- Protein group
- Organism
- Humans
- Pharmacological action
- No
- Actions
- Binder
- General Function
- Zinc-dependent transcriptional regulator of cellular adaption to conditions of exposure to heavy metals (PubMed:8065932). Binds to metal responsive elements (MRE) in promoters and activates the transcription of metallothionein genes like metallothionein-2/MT2A (PubMed:8065932). Also regulates the expression of metalloproteases in response to intracellular zinc and functions as a catabolic regulator of cartilages (By similarity)
- Specific Function
- cis-regulatory region sequence-specific DNA binding
Components:
References
- Tapiero H, Townsend DM, Tew KD: Trace elements in human physiology and pathology. Copper. Biomed Pharmacother. 2003 Nov;57(9):386-98. [Article]
Transporters
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- No
- Actions
- Substrate
- General Function
- Uniporter that mediates the transport of copper(1+) from the extracellular space to the cytoplasm, across the plasma membrane (PubMed:11734551, PubMed:16135512, PubMed:17525160, PubMed:19740744, PubMed:20451502, PubMed:20569931, PubMed:23658018) and delivers directly copper(1+) to specific chaperone such as ATOX1, via a copper(1+)- mediated transient interaction between the C-terminal domain and a copper(1+) chaperone, thus controlling intracellular copper(1+) levels (PubMed:11734551, PubMed:16135512, PubMed:17525160, PubMed:19740744, PubMed:20451502, PubMed:20569931, PubMed:23658018, PubMed:26745413). May function in copper(1+) import from the apical membrane thus may drive intestinal copper absorption (By similarity). The copper(1+) transport mechanism is sodium-independent, saturable and of high-affinity (PubMed:11734551). Also mediates the uptake of silver(1+) (PubMed:20569931). May function in the influx of the platinum-containing chemotherapeutic agents (PubMed:20451502, PubMed:20569931). The platinum-containing chemotherapeutic agents uptake is saturable (By similarity). In vitro, mediates the transport of cadmium(2+) into cells (PubMed:33294387). Also participates in the first step of copper(2+) acquisition by cells through a direct transfer of copper(2+) from copper(2+) carriers in blood, such as ALB to the N-terminal domain of SLC31A1, leading to copper(2+) reduction and probably followed by copper(1+) stabilization (PubMed:30489586). In addition, functions as a redox sensor to promote angiogenesis in endothelial cells, in a copper(1+) transport independent manner, by transmitting the VEGF-induced ROS signal through a sulfenylation at Cys-189 leadin g to a subsequent disulfide bond formation between SLC31A1 and KDR (PubMed:35027734). The SLC31A1-KDR complex is then co-internalized to early endosomes, driving a sustained VEGFR2 signaling (PubMed:35027734)
- Specific Function
- copper ion binding
- Gene Name
- SLC31A1
- Uniprot ID
- O15431
- Uniprot Name
- High affinity copper uptake protein 1
- Molecular Weight
- 21090.545 Da
References
- Tapiero H, Townsend DM, Tew KD: Trace elements in human physiology and pathology. Copper. Biomed Pharmacother. 2003 Nov;57(9):386-98. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- No
- Actions
- Substrate
- General Function
- Proton-coupled metal ion symporter operating with a proton to metal ion stoichiometry of 1:1 (PubMed:17109629, PubMed:17293870, PubMed:22736759, PubMed:25326704, PubMed:25491917). Selectively transports various divalent metal cations, in decreasing affinity: Cd(2+) > Fe(2+) > Co(2+), Mn(2+) >> Zn(2+), Ni(2+), VO(2+) (PubMed:17109629, PubMed:17293870, PubMed:22736759, PubMed:25326704, PubMed:25491917). Essential for maintenance of iron homeostasis by modulating intestinal absorption of dietary Fe(2+) and TF-associated endosomal Fe(2+) transport in erythroid precursors and other cells (By similarity). Enables Fe(2+) and Mn(2+) ion entry into mitochondria, and is thus expected to promote mitochondrial heme synthesis, iron-sulfur cluster biogenesis and antioxidant defense (By similarity) (PubMed:24448823). Can mediate uncoupled fluxes of either protons or metal ions
- Specific Function
- cadmium ion binding
- Gene Name
- SLC11A2
- Uniprot ID
- P49281
- Uniprot Name
- Natural resistance-associated macrophage protein 2
- Molecular Weight
- 62265.195 Da
References
- Tapiero H, Townsend DM, Tew KD: Trace elements in human physiology and pathology. Copper. Biomed Pharmacother. 2003 Nov;57(9):386-98. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- No
- Actions
- Substrate
- General Function
- ATP-driven copper (Cu(+)) ion pump that plays an important role in intracellular copper ion homeostasis (PubMed:10419525, PubMed:11092760, PubMed:28389643). Within a catalytic cycle, acquires Cu(+) ion from donor protein on the cytoplasmic side of the membrane and delivers it to acceptor protein on the lumenal side. The transfer of Cu(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing to outward-facing state (PubMed:10419525, PubMed:19453293, PubMed:19917612, PubMed:28389643, PubMed:31283225). Under physiological conditions, at low cytosolic copper concentration, it is localized at the trans-Golgi network (TGN) where it transfers Cu(+) ions to cuproenzymes of the secretory pathway (PubMed:11092760, PubMed:28389643). Upon elevated cytosolic copper concentrations, it relocalizes to the plasma membrane where it is responsible for the export of excess Cu(+) ions (PubMed:10419525, PubMed:28389643). May play a dual role in neuron function and survival by regulating cooper efflux and neuronal transmission at the synapse as well as by supplying Cu(+) ions to enzymes such as PAM, TYR and SOD3 (By similarity) (PubMed:28389643). In the melanosomes of pigmented cells, provides copper cofactor to TYR to form an active TYR holoenzyme for melanin biosynthesis (By similarity)
- Specific Function
- ATP binding
- Gene Name
- ATP7A
- Uniprot ID
- Q04656
- Uniprot Name
- Copper-transporting ATPase 1
- Molecular Weight
- 163371.335 Da
References
- Tapiero H, Townsend DM, Tew KD: Trace elements in human physiology and pathology. Copper. Biomed Pharmacother. 2003 Nov;57(9):386-98. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- No
- Actions
- Substrate
- General Function
- Copper ion transmembrane transporter involved in the export of copper out of the cells. It is involved in copper homeostasis in the liver, where it ensures the efflux of copper from hepatocytes into the bile in response to copper overload
- Specific Function
- ATP binding
- Gene Name
- ATP7B
- Uniprot ID
- P35670
- Uniprot Name
- Copper-transporting ATPase 2
- Molecular Weight
- 157261.34 Da
References
- Tapiero H, Townsend DM, Tew KD: Trace elements in human physiology and pathology. Copper. Biomed Pharmacother. 2003 Nov;57(9):386-98. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Does not function as a copper(1+) importer in vivo (By similarity). However, in vitro functions as a low-affinity copper(1+) importer (PubMed:17617060, PubMed:17944601). Regulator of SLC31A1 which facilitates the cleavage of the SLC31A1 ecto-domain or which stabilizes the truncated form of SLC31A1 (Truncated CTR1 form), thereby drives the SLC31A1 truncated form-dependent endosomal copper export and modulates the copper and cisplatin accumulation via SLC31A1 (By similarity)
- Specific Function
- copper ion transmembrane transporter activity
- Gene Name
- SLC31A2
- Uniprot ID
- O15432
- Uniprot Name
- Protein SLC31A2
- Molecular Weight
- 15681.29 Da
References
- van den Berghe PV, Klomp LW: New developments in the regulation of intestinal copper absorption. Nutr Rev. 2009 Nov;67(11):658-72. doi: 10.1111/j.1753-4887.2009.00250.x. [Article]
Drug created at September 29, 2015 17:21 / Updated at October 29, 2024 18:06