Heat shock protein HSP 90-beta
Details
- Name
- Heat shock protein HSP 90-beta
- Synonyms
- Heat shock 84 kDa
- Heat shock protein family C member 3
- HSP 84
- HSP 90
- HSP84
- HSP90B
- HSPC2
- HSPC3
- HSPCB
- Gene Name
- HSP90AB1
- UniProtKB Entry
- P08238Swiss-Prot
- Organism
- Humans
- NCBI Taxonomy ID
- 9606
- Amino acid sequence
>lcl|BSEQ0003760|Heat shock protein HSP 90-beta MPEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLT DPSKLDSGKELKIDIIPNPQERTLTLVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAG ADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVRADHGEPIGRGTK VILHLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYLEKEREKEISDDEAEEEKGEKEEE DKDDEEKPKIEDVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNPDDITQEE YGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRAPFDLFENKKKKNNIKLYVRRV FIMDSCDELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNIVKKCLELFSELA EDKENYKKFYEAFSKNLKLGIHEDSTNRRRLSELLRYHTSQSGDEMTSLSEYVSRMKETQ KSIYYITGESKEQVANSAFVERVRKRGFEVVYMTEPIDEYCVQQLKEFDGKSLVSVTKEG LELPEDEEEKKKMEESKAKFENLCKLMKEILDKKVEKVTISNRLVSSPCCIVTSTYGWTA NMERIMKAQALRDNSTMGYMMAKKHLEINPDHPIVETLRQKAEADKNDKAVKDLVVLLFE TALLSSGFSLEDPQTHSNRIYRMIKLGLGIDEDEVAAEEPNAAVPDEIPPLEGDEDASRM EEVD
- Number of residues
- 724
- Molecular Weight
- 83263.475
- Theoretical pI
- 4.68
- GO Classification
- FunctionsATP binding / double-stranded RNA binding / kinase binding / MHC class II protein complex binding / nitric-oxide synthase regulator activity / TPR domain bindingProcessescellular response to heat / cellular response to interleukin-4 / negative regulation of proteasomal ubiquitin-dependent protein catabolic process / placenta development / positive regulation of nitric oxide biosynthetic process / protein folding / response to unfolded protein / virion attachment to host cellComponentscell surface / cytoplasm / cytosol / extracellular exosome / melanosome / membrane / mitochondrion / nucleoplasm
- 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 linked to its ATPase 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:16478993, PubMed:19696785). 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. 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). 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. They first alter the steady-state levels of certain transcription factors in response to various physiological cues. 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. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery (PubMed:18239673). Main chaperone involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription (PubMed:20353823). Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059)
- Specific Function
- ATP binding
- Pfam Domain Function
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0016602|Heat shock protein HSP 90-beta (HSP90AB1) ATGCCTGAGGAAGTGCACCATGGAGAGGAGGAGGTGGAGACTTTTGCCTTTCAGGCAGAA ATTGCCCAACTCATGTCCCTCATCATCAATACCTTCTATTCCAACAAGGAGATTTTCCTT CGGGAGTTGATCTCTAATGCTTCTGATGCCTTGGACAAGATTCGCTATGAGAGCCTGACA GACCCTTCGAAGTTGGACAGTGGTAAAGAGCTGAAAATTGACATCATCCCCAACCCTCAG GAACGTACCCTGACTTTGGTAGACACAGGCATTGGCATGACCAAAGCTGATCTCATAAAT AATTTGGGAACCATTGCCAAGTCTGGTACTAAAGCATTCATGGAGGCTCTTCAGGCTGGT GCAGACATCTCCATGATTGGGCAGTTTGGTGTTGGCTTTTATTCTGCCTACTTGGTGGCA GAGAAAGTGGTTGTGATCACAAAGCACAACGATGATGAACAGTATGCTTGGGAGTCTTCT GCTGGAGGTTCCTTCACTGTGCGTGCTGACCATGGTGAGCCCATTGGCAGGGGTACCAAA GTGATCCTCCATCTTAAAGAAGATCAGACAGAGTACCTAGAAGAGAGGCGGGTCAAAGAA GTAGTGAAGAAGCATTCTCAGTTCATAGGCTATCCCATCACCCTTTATTTGGAGAAGGAA CGAGAGAAGGAAATTAGTGATGATGAGGCAGAGGAAGAGAAAGGTGAGAAAGAAGAGGAA GATAAAGATGATGAAGAAAAACCCAAGATCGAAGATGTGGGTTCAGATGAGGAGGATGAC AGCGGTAAGGATAAGAAGAAGAAAACTAAGAAGATCAAAGAGAAATACATTGATCAGGAA GAACTAAACAAGACCAAGCCTATTTGGACCAGAAACCCTGATGACATCACCCAAGAGGAG TATGGAGAATTCTACAAGAGCCTCACTAATGACTGGGAAGACCACTTGGCAGTCAAGCAC TTTTCTGTAGAAGGTCAGTTGGAATTCAGGGCATTGCTATTTATTCCTCGTCGGGCTCCC TTTGACCTTTTTGAGAACAAGAAGAAAAAGAACAACATCAAACTCTATGTCCGCCGTGTG TTCATCATGGACAGCTGTGATGAGTTGATACCAGAGTATCTCAATTTTATCCGTGGTGTG GTTGACTCTGAGGATCTGCCCCTGAACATCTCCCGAGAAATGCTCCAGCAGAGCAAAATC TTGAAAGTCATTCGCAAAAACATTGTTAAGAAGTGCCTTGAGCTCTTCTCTGAGCTGGCA GAAGACAAGGAGAATTACAAGAAATTCTATGAGGCATTCTCTAAAAATCTCAAGCTTGGA ATCCACGAAGACTCCACTAACCGCCGCCGCCTGTCTGAGCTGCTGCGCTATCATACCTCC CAGTCTGGAGATGAGATGACATCTCTGTCAGAGTATGTTTCTCGCATGAAGGAGACACAG AAGTCCATCTATTACATCACTGGTGAGAGCAAAGAGCAGGTGGCCAACTCAGCTTTTGTG GAGCGAGTGCGGAAACGGGGCTTCGAGGTGGTATATATGACCGAGCCCATTGACGAGTAC TGTGTGCAGCAGCTCAAGGAATTTGATGGGAAGAGCCTGGTCTCAGTTACCAAGGAGGGT CTGGAGCTGCCTGAGGATGAGGAGGAGAAGAAGAAGATGGAAGAGAGCAAGGCAAAGTTT GAGAACCTCTGCAAGCTCATGAAAGAAATCTTAGATAAGAAGGTTGAGAAGGTGACAATC TCCAATAGACTTGTGTCTTCACCTTGCTGCATTGTGACCAGCACCTACGGCTGGACAGCC AATATGGAGCGGATCATGAAAGCCCAGGCACTTCGGGACAACTCCACCATGGGCTATATG ATGGCCAAAAAGCACCTGGAGATCAACCCTGACCACCCCATTGTGGAGACGCTGCGGCAG AAGGCTGAGGCCGACAAGAATGATAAGGCAGTTAAGGACCTGGTGGTGCTGCTGTTTGAA ACCGCCCTGCTATCTTCTGGCTTTTCCCTTGAGGATCCCCAGACCCACTCCAACCGCATC TATCGCATGATCAAGCTAGGTCTAGGTATTGATGAAGATGAAGTGGCAGCAGAGGAACCC AATGCTGCAGTTCCTGATGAGATCCCCCCTCTCGAGGGCGATGAGGATGCGTCTCGCATG GAAGAAGTCGATTAG
- Chromosome Location
- 6
- Locus
- 6p21.1
- External Identifiers
Resource Link UniProtKB ID P08238 UniProtKB Entry Name HS90B_HUMAN GenBank Protein ID 306891 GenBank Gene ID M16660 GeneCard ID HSP90AB1 GenAtlas ID HSP90AB1 HGNC ID HGNC:5258 PDB ID(s) 1QZ2, 1UYM, 2L6J, 3FWV, 3NMQ, 3PRY, 3UQ3, 5FWK, 5FWL, 5FWM, 5FWP, 5UC4, 5UCH, 5UCI, 5UCJ, 6N8W, 6N8Y, 7ULJ, 7Z37, 7Z38, 7ZR0, 7ZR5, 7ZR6, 7ZUB, 8EOA, 8EOB, 8GAE, 8GFT, 8QMO KEGG ID hsa:3326 IUPHAR/Guide To Pharmacology ID 2907 NCBI Gene ID 3326 - General References
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Associated Data
- Bio-Entities
Bio-Entity Type Heat shock protein HSP 90-beta (Humans) protein primary- Drug Relations