Immunoglobulin heavy constant gamma 1

Details

Name
Immunoglobulin heavy constant gamma 1
Kind
protein
Synonyms
  • Ig gamma-1 chain C region
  • Ig gamma-1 chain C region EU
  • Ig gamma-1 chain C region KOL
  • Ig gamma-1 chain C region NIE
Gene Name
IGHG1
UniProtKB Entry
P01857Swiss-Prot
Organism
Humans
NCBI Taxonomy ID
9606
Amino acid sequence
>lcl|BSEQ0055465|Immunoglobulin heavy constant gamma 1
ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSS
GLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGG
PSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYN
STYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDE
LTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRW
QQGNVFSCSVMHEALHNHYTQKSLSLSPELQLEESCAEAQDGELDGLWTTITIFITLFLL
SVCYSATVTFFKVKWIFSSVVDLKQTIIPDYRNMIGQGA
Number of residues
399
Molecular Weight
43911.6
Theoretical pI
8.31
GO Classification
Functions
Fc-gamma receptor I complex binding
Processes
adaptive immune response / antibacterial humoral response / antibody-dependent cellular cytotoxicity / complement-dependent cytotoxicity
Components
IgG immunoglobulin complex / plasma membrane
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
Pfam Domain Function
Signal Regions
Not Available
Transmembrane Regions
351-371
Cellular Location
Secreted
Gene sequence
Not Available
Chromosome Location
Not Available
Locus
14q32.33
External Identifiers
ResourceLink
UniProtKB IDP01857
UniProtKB Entry NameIGHG1_HUMAN
GeneCard IDIGHG1
GenAtlas IDIGHG1
HGNC IDHGNC:5525
PDB ID(s)1AJ7, 1AQK, 1AXS, 1BEY, 1D5B, 1D5I, 1D6V, 1DFB, 1DN2, 1E4K, 1FC1, 1FC2, 1FCC, 1GAF, 1H3T, 1H3U, 1H3V, 1H3W, 1H3X, 1H3Y, 1HKL, 1HZH, 1I7Z, 1L6X, 1N7M, 1OQO, 1OQX, 1PG7, 1T83, 1T89, 1VGE, 2DTS, 2GJ7, 2I5Y, 2IWG, 2J6E, 2JB5, 2JB6, 2O5X, 2O5Y, 2O5Z, 2OSL, 2QAD, 2QL1, 2QQK, 2QQL, 2QQN, 2QR0, 2R56, 2RCS, 2VXQ, 2WAH, 3AGV, 3AVE, 3AY4, 3B2U, 3B2V, 3BDY, 3BE1, 3BKY, 3BN9, 3BQU, 3C08, 3C09, 3C2S, 3CFJ, 3CFK, 3CSY, 3D0L, 3D0V, 3D6G, 3D85, 3DJ9, 3DNK, 3DO3, 3DRO, 3DRQ, 3DVG, 3DVN, 3EYF, 3EYO, 3EYQ, 3FJT, 3MCL, 3O11, 3RY6, 3S7G, 3SGJ, 3SGK, 3TV3, 3TWC, 3TYG, 3U0W, 3U7W, 3U7Y, 3V7M, 3V8C, 3V95, 3WJJ, 3WJL, 3WKN, 3WN5, 4ACP, 4B7I, 4BM7, 4BSV, 4BSW, 4BYH, 4CDH, 4D9Q, 4D9R, 4DAG, 4DZ8, 4EOW, 4HIX, 4J12, 4KU1, 4LLD, 4LLM, 4LLQ, 4N0U, 4NQS, 4NQT, 4NQU, 4NWT, 4NWU, 4O4Y, 4O51, 4Q6Y, 4Q74, 4Q7D, 4W4N, 4W4O, 4WI2, 4WI3, 4WI4, 4WI5, 4WI6, 4WI7, 4WI8, 4WI9, 4X4M, 4X98, 4X99, 4XMP, 4XNY, 4XNZ, 4XXD, 4ZNE, 5BW7, 5C7K, 5D4Q, 5D6D, 5DI8, 5DJ0, 5DJ2, 5DJ6, 5DJ8, 5DJA, 5DJC, 5DJD, 5DJX, 5DJY, 5DJZ, 5DK0, 5DK2, 5DVK, 5DVL, 5DVM, 5DVN, 5DVO, 5GSQ, 5HSF, 5HY9, 5HYE, 5HYF, 5HYI, 5IQ7, 5IQ9, 5IW3, 5IW6, 5JIH, 5JII, 5JIK, 5K33, 5K64, 5K65, 5K8D, 5KWG, 5M3V, 5TPS, 5U4Y, 5U52, 5U66, 5V43, 5V4E, 6DCV, 6DCW, 6DE7, 6F2Z, 6G1E, 6N35, 6YT7, 7KWO, 7LUR, 7Q15, 7Q3P, 7WSO, 8DIN, 8DIR, 8DJ7
General References
  1. Ellison JW, Berson BJ, Hood LE: The nucleotide sequence of a human immunoglobulin C gamma1 gene. Nucleic Acids Res. 1982 Jul 10;10(13):4071-9. [Article]
  2. Cunningham BA, Rutishauser U, Gall WE, Gottlieb PD, Waxdal MJ, Edelman GM: The covalent structure of a human gamma G-immunoglobulin. VII. Amino acid sequence of heavy-chain cyanogen bromide fragments H1-H4. Biochemistry. 1970 Aug 4;9(16):3161-70. [Article]
  3. Rutishauser U, Cunningham BA, Bennett C, Konigsberg WH, Edelman GM: The covalent structure of a human gamma G-immunoglobulin. 8. Amino acid sequence of heavy-chain cyanogen bromide fragments H5-H7. Biochemistry. 1970 Aug 4;9(16):3171-81. [Article]
  4. Ponstingl H, Hilschmann N: [The rule of antibody structure. The primary structure of a monoclonal IgG1 immunoglobulin (myeloma protein Nie). III. The chymotryptic peptides of the H-chain, alignment of the tryptic peptides and discussion of the complete structure]. Hoppe Seylers Z Physiol Chem. 1976 Nov;357(11):1571-604. [Article]
  5. Schmidt WE, Jung HD, Palm W, Hilschmann N: [Three-dimensional structure determination of antibodies. Primary structure of crystallized monoclonal immunoglobulin IgG1 KOL, I]. Hoppe Seylers Z Physiol Chem. 1983 Jun;364(6):713-47. [Article]
  6. Gall WE, Edelman GM: The covalent structure of a human gamma G-immunoglobulin. X. Intrachain disulfide bonds. Biochemistry. 1970 Aug 4;9(16):3188-96. [Article]
  7. Dreker L, Schwarz J, Reichel W, Hilschmann N: [Rule of antibody structure. the primary structure of a monoclonal IgG1 immunoglobulin (myeloma protein Nie), I: Purification and characterization of the protein, the L- and H-chains, the cyanogenbromide cleavage products, and the disulfide bridges (author's transl)]. Hoppe Seylers Z Physiol Chem. 1976 Nov;357(11):1515-40. [Article]
  8. Thaysen-Andersen M, Mysling S, Hojrup P: Site-specific glycoprofiling of N-linked glycopeptides using MALDI-TOF MS: strong correlation between signal strength and glycoform quantities. Anal Chem. 2009 May 15;81(10):3933-43. doi: 10.1021/ac900231w. [Article]
  9. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. doi: 10.1021/pr8008012. [Article]
  10. Jia W, Lu Z, Fu Y, Wang HP, Wang LH, Chi H, Yuan ZF, Zheng ZB, Song LN, Han HH, Liang YM, Wang JL, Cai Y, Zhang YK, Deng YL, Ying WT, He SM, Qian XH: A strategy for precise and large scale identification of core fucosylated glycoproteins. Mol Cell Proteomics. 2009 May;8(5):913-23. doi: 10.1074/mcp.M800504-MCP200. Epub 2009 Jan 12. [Article]
  11. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  12. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
  13. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. [Article]
  14. Deisenhofer J: Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution. Biochemistry. 1981 Apr 28;20(9):2361-70. [Article]
  15. Bergsagel PL, Chesi M, Nardini E, Brents LA, Kirby SL, Kuehl WM: Promiscuous translocations into immunoglobulin heavy chain switch regions in multiple myeloma. Proc Natl Acad Sci U S A. 1996 Nov 26;93(24):13931-6. [Article]
  16. Harrison CJ, Mazzullo H, Ross FM, Cheung KL, Gerrard G, Harewood L, Mehta A, Lachmann HJ, Hawkins PN, Orchard KH: Translocations of 14q32 and deletions of 13q14 are common chromosomal abnormalities in systemic amyloidosis. Br J Haematol. 2002 May;117(2):427-35. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
N-acetyl-alpha-D-glucosamineexperimentalunknowntargetDetails
alpha-L-fucoseexperimentalunknowntargetDetails
3-(10-methyl-9-anthryl)propanoic acidexperimentalunknowntargetDetails
EtiocholanedioneexperimentalunknowntargetDetails
3-{[(9-CYANO-9,10-DIHYDRO-10-METHYLACRIDIN-9-YL)CARBONYL]AMINO}PROPANOIC ACIDexperimentalunknowntargetDetails
BiphenylalanineexperimentalunknowntargetDetails
TRANS-2-(DIMETHYLPHENYLSILYL)-PIPERIDINE-N-OXIDEexperimentalunknowntargetDetails
FluorescinexperimentalunknowntargetDetails
N-(P-CYANOPHENYL)-N'-DIPHENYLMETHYL-GUANIDINE-ACETIC ACIDexperimentalunknowntargetDetails
N-{[2-({[1-(4-CARBOXYBUTANOYL)AMINO]-2-PHENYLETHYL}-HYDROXYPHOSPHINYL)OXY]ACETYL}-2-PHENYLETHYLAMINEexperimentalunknowntargetDetails
(2-AMINO-3-PHENYL-BICYCLO[2.2.1]HEPT-2-YL)-PHENYL-METHANONEexperimentalunknowntargetDetails
(1S,2S,5S)2-(4-GLUTARIDYLBENZYL)-5-PHENYL-1-CYCLOHEXANOLexperimentalunknowntargetDetails
Methyl nonanoateexperimentalunknowntargetDetails
2-(4-HYDROXY-3-NITROPHENYL)ACETIC ACIDexperimentalunknowntargetDetails
5-(PARA-NITROPHENYL PHOSPHONATE)-PENTANOIC ACIDexperimentalunknowntargetDetails
9-(2-carboxyethyl)-10-methylanthracene endoperoxideexperimentalunknowntargetDetails
N-[4-(4-nitrophenylphospho)butanoyl]-D-alanineexperimentalunknowntargetDetails
PARA-NITROPHENYLPHOSPHONOBUTANOYL-GLYCINEexperimentalunknowntargetDetails
4-NITRO-BENZYLPHOSPHONOBUTANOYL-GLYCINEexperimentalunknowntargetDetails
PARA-NITROBENZYL GLUTARYL GLYCINIC ACIDexperimentalunknowntargetDetails
N-[4-(4-nitrophenylphospho)butanoyl]-L-alanineexperimentalunknowntargetDetails
6-{4-[HYDROXY-(4-NITRO-PHENOXY)-PHOSPHORYL]-BUTYRYLAMINO}-HEXANOIC ACIDexperimentalunknowntargetDetails
4-(4-STYRYL-PHENYLCARBAMOYL)-BUTYRIC ACIDexperimentalunknowntargetDetails
Copperapproved, investigationalunknowntargetDetails