IGHG1_HUMAN
ID IGHG1_HUMAN Reviewed; 330 AA.
AC P01857;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=Immunoglobulin heavy constant gamma 1 {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.11};
DE AltName: Full=Ig gamma-1 chain C region {ECO:0000305};
DE AltName: Full=Ig gamma-1 chain C region EU {ECO:0000305|PubMed:5489771, ECO:0000305|PubMed:5530842};
DE AltName: Full=Ig gamma-1 chain C region KOL {ECO:0000305|PubMed:6884994};
DE AltName: Full=Ig gamma-1 chain C region NIE {ECO:0000305|PubMed:826475};
GN Name=IGHG1 {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.11};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=826475;
RA Ponstingl H., Hilschmann N.;
RT "The rule of antibody structure. The primary structure of a monoclonal IgG1
RT immunoglobulin (myeloma protein Nie). III. The chymotryptic peptides of the
RT H-chain, alignment of the tryptic peptides and discussion of the complete
RT structure.";
RL Hoppe-Seyler's Z. Physiol. Chem. 357:1571-1604(1976).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE IGHG1*01).
RX PubMed=6811139; DOI=10.1016/0092-8674(82)90183-0;
RA Takahashi N., Ueda S., Obata M., Nikaido T., Nakai S., Honjo T.;
RT "Structure of human immunoglobulin gamma genes: implications for evolution
RT of a gene family.";
RL Cell 29:671-679(1982).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6287432; DOI=10.1093/nar/10.13.4071;
RA Ellison J.W., Berson B.J., Hood L.E.;
RT "The nucleotide sequence of a human immunoglobulin C gamma1 gene.";
RL Nucleic Acids Res. 10:4071-4079(1982).
RN [4]
RP PROTEIN SEQUENCE (IMGT ALLELE IGHG1*03), DISULFIDE BONDS, AND VARIANTS
RP ARG-97; GLU-239 AND MET-241.
RX PubMed=6884994;
RA Schmidt W.E., Jung H.-D., Palm W., Hilschmann N.;
RT "Three-dimensional structure determination of antibodies. Primary structure
RT of crystallized monoclonal immunoglobulin IgG1 KOL, I.";
RL Hoppe-Seyler's Z. Physiol. Chem. 364:713-747(1983).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGHG1*05).
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [6]
RP PROTEIN SEQUENCE OF 1-135 (IMGT ALLELE IGHG1*03), AND VARIANT ARG-97.
RX PubMed=5489771; DOI=10.1021/bi00818a008;
RA Cunningham B.A., Rutishauser U., Gall W.E., Gottlieb P.D., Waxdal M.J.,
RA Edelman G.M.;
RT "The covalent structure of a human gamma G-immunoglobulin. VII. Amino acid
RT sequence of heavy-chain cyanogen bromide fragments H1-H4.";
RL Biochemistry 9:3161-3170(1970).
RN [7]
RP PROTEIN SEQUENCE OF 136-329 (IMGT ALLELE IGHG1*03), AND VARIANTS GLU-239
RP AND MET-241.
RX PubMed=5530842; DOI=10.1021/bi00818a009;
RA Rutishauser U., Cunningham B.A., Bennett C., Konigsberg W.H., Edelman G.M.;
RT "The covalent structure of a human gamma G-immunoglobulin. 8. Amino acid
RT sequence of heavy-chain cyanogen bromide fragments H5-H7.";
RL Biochemistry 9:3171-3181(1970).
RN [8]
RP DISULFIDE BONDS.
RX PubMed=4923144; DOI=10.1021/bi00818a011;
RA Gall W.E., Edelman G.M.;
RT "The covalent structure of a human gamma G-immunoglobulin. X. Intrachain
RT disulfide bonds.";
RL Biochemistry 9:3188-3196(1970).
RN [9]
RP DISULFIDE BONDS.
RX PubMed=1002129;
RA Dreker L., Schwarz J., Reichel W., Hilschmann N.;
RT "Rule of antibody structure. The primary structure of a monoclonal IgG1
RT immunoglobulin (myeloma protein Nie), I: purification and characterization
RT of the protein, the L- and H-chains, the cyanogen bromide cleavage
RT products, and the disulfide bridges.";
RL Hoppe-Seyler's Z. Physiol. Chem. 357:1515-1540(1976).
RN [10]
RP NOMENCLATURE.
RX PubMed=11340299; DOI=10.1159/000049189;
RA Lefranc M.P.;
RT "Nomenclature of the human immunoglobulin heavy (IGH) genes.";
RL Exp. Clin. Immunogenet. 18:100-116(2001).
RN [11]
RP NOMENCLATURE.
RA Lefranc M.P., Lefranc G.;
RT "The Immunoglobulin FactsBook.";
RL (In) Lefranc M.P., Lefranc G. (eds.);
RL The Immunoglobulin FactsBook., pp.1-458, Academic Press, London. (2001).
RN [12]
RP FUNCTION, INTERACTION WITH FCGR1A; FCGR2A AND FCGR3A, AND MUTAGENESIS OF
RP LEU-117; LEU-118; 117-LEU-LEU-118; GLY-120 AND LYS-205.
RX PubMed=11711607; DOI=10.1128/jvi.75.24.12161-12168.2001;
RA Hezareh M., Hessell A.J., Jensen R.C., van de Winkel J.G., Parren P.W.;
RT "Effector function activities of a panel of mutants of a broadly
RT neutralizing antibody against human immunodeficiency virus type 1.";
RL J. Virol. 75:12161-12168(2001).
RN [13]
RP REVIEW ON SOMATIC HYPERMUTATION.
RX PubMed=17576170; DOI=10.1146/annurev.genet.41.110306.130340;
RA Teng G., Papavasiliou F.N.;
RT "Immunoglobulin somatic hypermutation.";
RL Annu. Rev. Genet. 41:107-120(2007).
RN [14]
RP GLYCOSYLATION AT ASN-180.
RX PubMed=19358553; DOI=10.1021/ac900231w;
RA Thaysen-Andersen M., Mysling S., Hojrup P.;
RT "Site-specific glycoprofiling of N-linked glycopeptides using MALDI-TOF MS:
RT strong correlation between signal strength and glycoform quantities.";
RL Anal. Chem. 81:3933-3943(2009).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-180.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [16]
RP GLYCOSYLATION AT ASN-180.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [17]
RP REVIEW ON IMMUNOGLOBULINS.
RX PubMed=20176268; DOI=10.1016/j.jaci.2009.09.046;
RA Schroeder H.W. Jr., Cavacini L.;
RT "Structure and function of immunoglobulins.";
RL J. Allergy Clin. Immunol. 125:S41-S52(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP REVIEW ON FUNCTION.
RX PubMed=22158414; DOI=10.1038/nri3128;
RA McHeyzer-Williams M., Okitsu S., Wang N., McHeyzer-Williams L.;
RT "Molecular programming of B cell memory.";
RL Nat. Rev. Immunol. 12:24-34(2012).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX PubMed=7236608; DOI=10.1021/bi00512a001;
RA Deisenhofer J.;
RT "Crystallographic refinement and atomic models of a human Fc fragment and
RT its complex with fragment B of protein A from Staphylococcus aureus at
RT 2.9- and 2.8-A resolution.";
RL Biochemistry 20:2361-2370(1981).
RN [23]
RP INVOLVEMENT IN MULTIPLE MYELOMA.
RX PubMed=8943038; DOI=10.1073/pnas.93.24.13931;
RA Bergsagel P.L., Chesi M., Nardini E., Brents L.A., Kirby S.L., Kuehl W.M.;
RT "Promiscuous translocations into immunoglobulin heavy chain switch regions
RT in multiple myeloma.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:13931-13936(1996).
RN [24]
RP INVOLVEMENT IN MULTIPLE MYELOMA.
RX PubMed=11972529; DOI=10.1046/j.1365-2141.2002.03438.x;
RA Harrison C.J., Mazzullo H., Ross F.M., Cheung K.L., Gerrard G.,
RA Harewood L., Mehta A., Lachmann H.J., Hawkins P.N., Orchard K.H.;
RT "Translocations of 14q32 and deletions of 13q14 are common chromosomal
RT abnormalities in systemic amyloidosis.";
RL Br. J. Haematol. 117:427-435(2002).
CC -!- FUNCTION: Constant region of immunoglobulin heavy chains.
CC Immunoglobulins, also known as antibodies, are membrane-bound or
CC secreted glycoproteins produced by B lymphocytes. In the recognition
CC phase of humoral immunity, the membrane-bound immunoglobulins serve as
CC receptors which, upon binding of a specific antigen, trigger the clonal
CC expansion and differentiation of B lymphocytes into immunoglobulins-
CC secreting plasma cells. Secreted immunoglobulins mediate the effector
CC phase of humoral immunity, which results in the elimination of bound
CC antigens (PubMed:22158414, PubMed:20176268). The antigen binding site
CC is formed by the variable domain of one heavy chain, together with that
CC of its associated light chain. Thus, each immunoglobulin has two
CC antigen binding sites with remarkable affinity for a particular
CC antigen. The variable domains are assembled by a process called V-(D)-J
CC rearrangement and can then be subjected to somatic hypermutations
CC which, after exposure to antigen and selection, allow affinity
CC maturation for a particular antigen (PubMed:17576170, PubMed:20176268).
CC Mediates IgG effector functions on monocytes triggering ADCC of virus-
CC infected cells. {ECO:0000269|PubMed:11711607,
CC ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268,
CC ECO:0000303|PubMed:22158414}.
CC -!- SUBUNIT: Immunoglobulins are composed of two identical heavy chains and
CC two identical light chains; disulfide-linked (PubMed:20176268).
CC Interacts with FCGR1A; this interaction mediates IgG effector functions
CC on monocytes. Interacts with FCGR2A and FCGR3A (PubMed:11711607).
CC {ECO:0000269|PubMed:11711607, ECO:0000303|PubMed:20176268}.
CC -!- INTERACTION:
CC P01857; P12314: FCGR1A; NbExp=2; IntAct=EBI-356114, EBI-2869867;
CC P01857; P31994: FCGR2B; NbExp=31; IntAct=EBI-356114, EBI-724784;
CC P01857; P04488: gE; Xeno; NbExp=2; IntAct=EBI-356114, EBI-15581257;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268,
CC ECO:0000303|PubMed:22158414}. Cell membrane
CC {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
CC -!- POLYMORPHISM: There are several alleles. The sequence shown is that of
CC IMGT allele IGHG1*05. {ECO:0000305}.
CC -!- DISEASE: Multiple myeloma (MM) [MIM:254500]: A malignant tumor of
CC plasma cells usually arising in the bone marrow and characterized by
CC diffuse involvement of the skeletal system, hyperglobulinemia, Bence-
CC Jones proteinuria and anemia. Complications of multiple myeloma are
CC bone pain, hypercalcemia, renal failure and spinal cord compression.
CC The aberrant antibodies that are produced lead to impaired humoral
CC immunity and patients have a high prevalence of infection. Amyloidosis
CC may develop in some patients. Multiple myeloma is part of a spectrum of
CC diseases ranging from monoclonal gammopathy of unknown significance
CC (MGUS) to plasma cell leukemia. {ECO:0000269|PubMed:11972529,
CC ECO:0000269|PubMed:8943038}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. A chromosomal aberration
CC involving IGHG1 is found in multiple myeloma. Translocation
CC t(11;14)(q13;q32) with the IgH locus. Translocation t(11;14)(q13;q32)
CC with CCND1; translocation t(4;14)(p16.3;q32.3) with FGFR3;
CC translocation t(6;14)(p25;q32) with IRF4.
CC -!- CAUTION: For an example of a full-length immunoglobulin gamma heavy
CC chain see AC P0DOX5. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC82527.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; J00228; AAC82527.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL122127; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A93433; GHHU.
DR PDB; 1AJ7; X-ray; 2.10 A; H=1-103.
DR PDB; 1AQK; X-ray; 1.84 A; H=1-103.
DR PDB; 1AXS; X-ray; 2.60 A; B/H=1-101.
DR PDB; 1BEY; X-ray; 3.25 A; H=1-98.
DR PDB; 1D5B; X-ray; 2.80 A; B/H=1-101.
DR PDB; 1D5I; X-ray; 2.00 A; H=1-101.
DR PDB; 1D6V; X-ray; 2.00 A; H=1-101.
DR PDB; 1DFB; X-ray; 2.70 A; H=1-103.
DR PDB; 1DN2; X-ray; 2.70 A; A/B=120-326.
DR PDB; 1E4K; X-ray; 3.20 A; A/B=106-330.
DR PDB; 1FC1; X-ray; 2.90 A; A/B=106-329.
DR PDB; 1FC2; X-ray; 2.80 A; D=106-329.
DR PDB; 1FCC; X-ray; 3.20 A; A/B=121-326.
DR PDB; 1GAF; X-ray; 1.95 A; H=1-103.
DR PDB; 1H3T; X-ray; 2.40 A; A/B=108-330.
DR PDB; 1H3U; X-ray; 2.40 A; A/B=108-330.
DR PDB; 1H3V; X-ray; 3.10 A; A/B=108-330.
DR PDB; 1H3W; X-ray; 2.85 A; M=108-330.
DR PDB; 1H3X; X-ray; 2.44 A; A/B=108-330.
DR PDB; 1H3Y; X-ray; 4.10 A; A/B=108-330.
DR PDB; 1HKL; X-ray; 2.68 A; H=1-103.
DR PDB; 1HZH; X-ray; 2.70 A; H/K=1-330.
DR PDB; 1I7Z; X-ray; 2.30 A; B/D=1-103.
DR PDB; 1L6X; X-ray; 1.65 A; A=120-326.
DR PDB; 1N7M; X-ray; 1.80 A; L=2-102.
DR PDB; 1OQO; X-ray; 2.30 A; A/B=119-330.
DR PDB; 1OQX; X-ray; 2.60 A; A/B=119-330.
DR PDB; 1PG7; X-ray; 2.50 A; H/I=1-100.
DR PDB; 1T83; X-ray; 3.00 A; A/B=107-330.
DR PDB; 1T89; X-ray; 3.50 A; A/B=107-330.
DR PDB; 1VGE; X-ray; 2.00 A; H=1-103.
DR PDB; 2DTS; X-ray; 2.20 A; A/B=108-330.
DR PDB; 2GJ7; X-ray; 5.00 A; A/B=106-330.
DR PDB; 2I5Y; X-ray; 2.20 A; H=1-101.
DR PDB; 2IWG; X-ray; 2.35 A; A/D=120-326.
DR PDB; 2J6E; X-ray; 3.00 A; A/B=99-330.
DR PDB; 2JB5; X-ray; 2.80 A; H=1-102.
DR PDB; 2JB6; X-ray; 2.85 A; B/H=1-102.
DR PDB; 2O5X; X-ray; 2.05 A; H=1-108.
DR PDB; 2O5Y; X-ray; 2.85 A; H=1-108.
DR PDB; 2O5Z; X-ray; 2.40 A; H=1-108.
DR PDB; 2OSL; X-ray; 2.60 A; A/H=1-103.
DR PDB; 2QAD; X-ray; 3.30 A; D/H=1-101.
DR PDB; 2QL1; X-ray; 2.53 A; A=106-330.
DR PDB; 2QQK; X-ray; 2.75 A; H=1-107.
DR PDB; 2QQL; X-ray; 3.10 A; H=1-107.
DR PDB; 2QQN; X-ray; 2.20 A; H=1-107.
DR PDB; 2QR0; X-ray; 3.50 A; B/F/H/L/N/R/T/X=1-103.
DR PDB; 2R56; X-ray; 2.80 A; H/I=1-100.
DR PDB; 2RCS; X-ray; 2.10 A; H=1-103.
DR PDB; 2VXQ; X-ray; 1.90 A; H=1-100.
DR PDB; 2WAH; X-ray; 2.51 A; A/B=120-328.
DR PDB; 3AGV; X-ray; 2.15 A; A/B=120-330.
DR PDB; 3AVE; X-ray; 2.00 A; A/B=108-330.
DR PDB; 3AY4; X-ray; 2.20 A; A/B=108-330.
DR PDB; 3B2U; X-ray; 2.58 A; C/F/H/J/N/Q/T/W=1-102.
DR PDB; 3B2V; X-ray; 3.30 A; H=1-102.
DR PDB; 3BDY; X-ray; 2.60 A; H=1-107.
DR PDB; 3BE1; X-ray; 2.90 A; H=1-107.
DR PDB; 3BKY; X-ray; 2.61 A; H=1-104.
DR PDB; 3BN9; X-ray; 2.17 A; D/F=1-107.
DR PDB; 3BQU; X-ray; 3.00 A; B=2-103.
DR PDB; 3C08; X-ray; 2.15 A; H=1-102.
DR PDB; 3C09; X-ray; 3.20 A; C/H=1-102.
DR PDB; 3C2S; X-ray; 2.30 A; A=106-330.
DR PDB; 3CFJ; X-ray; 2.60 A; B/D/F/H=1-104.
DR PDB; 3CFK; X-ray; 2.60 A; B/D/F/H/I/K/N/P=1-104.
DR PDB; 3CSY; X-ray; 3.40 A; A/C/E/G=1-101.
DR PDB; 3D0L; X-ray; 2.35 A; B=2-105.
DR PDB; 3D0V; X-ray; 2.05 A; B=2-105.
DR PDB; 3D6G; X-ray; 2.30 A; A/B=119-328.
DR PDB; 3D85; X-ray; 1.90 A; B=1-108.
DR PDB; 3DJ9; X-ray; 1.75 A; A=119-225.
DR PDB; 3DNK; X-ray; 2.84 A; A/B=119-330.
DR PDB; 3DO3; X-ray; 2.50 A; A/B=119-330.
DR PDB; 3DRO; X-ray; 3.90 A; B=2-103.
DR PDB; 3DRQ; X-ray; 2.00 A; B=2-103.
DR PDB; 3DVG; X-ray; 2.60 A; B=1-107.
DR PDB; 3DVN; X-ray; 2.70 A; B/H=1-107.
DR PDB; 3EYF; X-ray; 2.30 A; B/D=1-108.
DR PDB; 3EYO; X-ray; 2.50 A; B/D=1-108.
DR PDB; 3EYQ; X-ray; 2.40 A; D=1-108.
DR PDB; 3FJT; X-ray; 2.50 A; A/B=119-327.
DR PDB; 3MCL; X-ray; 1.70 A; H=1-107.
DR PDB; 3O11; X-ray; 2.80 A; B/H=1-103.
DR PDB; 3RY6; X-ray; 3.80 A; A/B=114-327.
DR PDB; 3S7G; X-ray; 3.13 A; A/B/C/D=104-330.
DR PDB; 3SGJ; X-ray; 2.20 A; A/B=106-330.
DR PDB; 3SGK; X-ray; 2.40 A; A/B=106-330.
DR PDB; 3TV3; X-ray; 1.29 A; H=1-104.
DR PDB; 3TWC; X-ray; 1.65 A; H=1-104.
DR PDB; 3TYG; X-ray; 3.25 A; H=1-104.
DR PDB; 3U0W; X-ray; 2.00 A; H=1-103.
DR PDB; 3U7W; X-ray; 2.60 A; H=1-104.
DR PDB; 3U7Y; X-ray; 2.45 A; H=1-104.
DR PDB; 3V7M; X-ray; 2.02 A; A=119-327.
DR PDB; 3V8C; X-ray; 2.77 A; A/B=119-330.
DR PDB; 3V95; X-ray; 2.70 A; A/B=119-330.
DR PDB; 3WJJ; X-ray; 2.60 A; A/B=99-328.
DR PDB; 3WJL; X-ray; 2.86 A; A/B=99-328.
DR PDB; 3WKN; X-ray; 2.90 A; A/B/C/D/I/J/M/N=119-330.
DR PDB; 3WN5; X-ray; 2.78 A; A/B/D/E=99-328.
DR PDB; 4ACP; X-ray; 2.49 A; A/B=101-329.
DR PDB; 4B7I; X-ray; 2.36 A; A/B=120-329.
DR PDB; 4BM7; X-ray; 1.95 A; A/B=106-329.
DR PDB; 4BSV; X-ray; 1.75 A; A/B=106-330.
DR PDB; 4BSW; X-ray; 2.15 A; A/B=106-330.
DR PDB; 4BYH; X-ray; 2.30 A; A/B=106-329.
DR PDB; 4CDH; X-ray; 2.30 A; A/B=101-330.
DR PDB; 4D9Q; X-ray; 2.28 A; E/H=2-102.
DR PDB; 4D9R; X-ray; 2.42 A; E/H=2-103.
DR PDB; 4DAG; X-ray; 3.39 A; H=2-98.
DR PDB; 4DZ8; X-ray; 1.91 A; A/B=108-330.
DR PDB; 4EOW; X-ray; 1.97 A; H=1-101.
DR PDB; 4HIX; X-ray; 2.20 A; H=1-107.
DR PDB; 4J12; X-ray; 1.90 A; A=119-327.
DR PDB; 4KU1; X-ray; 1.90 A; A/B=120-327.
DR PDB; 4LLD; X-ray; 1.19 A; A=1-103.
DR PDB; 4LLM; X-ray; 1.75 A; A=1-103.
DR PDB; 4LLQ; X-ray; 1.42 A; A=1-103.
DR PDB; 4N0U; X-ray; 3.80 A; E=119-327.
DR PDB; 4NQS; X-ray; 2.64 A; A/B/G/H=118-330.
DR PDB; 4NQT; X-ray; 2.10 A; A=118-330.
DR PDB; 4NQU; X-ray; 2.50 A; A=118-330.
DR PDB; 4NWT; X-ray; 1.75 A; H=6-95.
DR PDB; 4NWU; X-ray; 1.60 A; H=6-105.
DR PDB; 4O4Y; X-ray; 1.85 A; A=106-119.
DR PDB; 4O51; X-ray; 2.20 A; M/N/O/P=106-119.
DR PDB; 4Q6Y; X-ray; 3.00 A; A/B/C/D=109-329.
DR PDB; 4Q74; X-ray; 2.19 A; A/B=108-329.
DR PDB; 4Q7D; X-ray; 2.35 A; A/B=109-329.
DR PDB; 4W4N; X-ray; 1.80 A; A/B=107-329.
DR PDB; 4W4O; X-ray; 1.80 A; A/B=107-330.
DR PDB; 4WI2; X-ray; 1.90 A; A/B=120-327.
DR PDB; 4WI3; X-ray; 2.70 A; A/B=120-327.
DR PDB; 4WI4; X-ray; 2.80 A; A/B=121-327.
DR PDB; 4WI5; X-ray; 2.80 A; A/B=120-327.
DR PDB; 4WI6; X-ray; 2.20 A; A/B=120-327.
DR PDB; 4WI7; X-ray; 1.90 A; A/B=120-327.
DR PDB; 4WI8; X-ray; 2.80 A; A/B=120-327.
DR PDB; 4WI9; X-ray; 2.65 A; A/B=120-327.
DR PDB; 4X4M; X-ray; 3.48 A; A/B/C/D=112-330.
DR PDB; 4X98; X-ray; 2.50 A; A=108-327, B=121-327.
DR PDB; 4X99; X-ray; 2.50 A; A/B=108-330.
DR PDB; 4XMP; X-ray; 1.78 A; H=1-103.
DR PDB; 4XNY; X-ray; 2.30 A; H=1-103.
DR PDB; 4XNZ; X-ray; 3.39 A; B/E/H=1-103.
DR PDB; 4XXD; X-ray; 2.41 A; B/E=1-107.
DR PDB; 4ZNE; X-ray; 2.42 A; E/J=104-330.
DR PDB; 5BW7; X-ray; 3.00 A; A/B=108-330.
DR PDB; 5C7K; X-ray; 4.60 A; E=1-106.
DR PDB; 5D4Q; X-ray; 2.39 A; A/B=109-329.
DR PDB; 5D6D; X-ray; 3.13 A; A/B=108-329.
DR PDB; 5DI8; X-ray; 1.90 A; A/B=104-330.
DR PDB; 5DJ0; X-ray; 2.28 A; A/B=104-330.
DR PDB; 5DJ2; X-ray; 2.56 A; A/B=104-330.
DR PDB; 5DJ6; X-ray; 2.00 A; A/B=104-330.
DR PDB; 5DJ8; X-ray; 2.40 A; A/B=104-330.
DR PDB; 5DJA; X-ray; 2.90 A; A/B=104-330.
DR PDB; 5DJC; X-ray; 2.10 A; A/B/D/E=104-330.
DR PDB; 5DJD; X-ray; 2.30 A; A/B=104-330.
DR PDB; 5DJX; X-ray; 2.25 A; A/B/D/E=104-330.
DR PDB; 5DJY; X-ray; 2.15 A; A/B=104-330.
DR PDB; 5DJZ; X-ray; 1.90 A; A/B=104-330.
DR PDB; 5DK0; X-ray; 2.30 A; A/B=104-330.
DR PDB; 5DK2; X-ray; 2.60 A; A/B/D/E=104-330.
DR PDB; 5DVK; X-ray; 2.60 A; A=104-330.
DR PDB; 5DVL; X-ray; 1.90 A; A=104-330.
DR PDB; 5DVM; X-ray; 2.95 A; A=104-330.
DR PDB; 5DVN; X-ray; 2.50 A; A=104-330.
DR PDB; 5DVO; X-ray; 2.50 A; A/B=104-330.
DR PDB; 5GSQ; X-ray; 1.85 A; A/B/C/D=106-330.
DR PDB; 5HSF; X-ray; 1.52 A; A/B=221-330.
DR PDB; 5HY9; X-ray; 2.70 A; A/B=104-330.
DR PDB; 5HYE; X-ray; 1.89 A; A/C=104-330.
DR PDB; 5HYF; X-ray; 1.80 A; A=104-330.
DR PDB; 5HYI; X-ray; 2.90 A; A/B/C/D=104-330.
DR PDB; 5IQ7; X-ray; 3.29 A; H=1-102.
DR PDB; 5IQ9; X-ray; 2.40 A; A/H=1-101.
DR PDB; 5IW3; X-ray; 2.05 A; A=119-326.
DR PDB; 5IW6; X-ray; 2.34 A; A=119-327, B=122-326.
DR PDB; 5JIH; X-ray; 1.66 A; A/B=108-329.
DR PDB; 5JII; X-ray; 1.79 A; A/B=108-329.
DR PDB; 5JIK; X-ray; 1.82 A; A/B=108-329.
DR PDB; 5K33; X-ray; 3.30 A; A=108-329.
DR PDB; 5K64; X-ray; 2.44 A; A/B=108-330.
DR PDB; 5K65; X-ray; 2.50 A; A/B=108-330.
DR PDB; 5K8D; X-ray; 4.19 A; B=104-329.
DR PDB; 5KWG; X-ray; 4.30 A; A=108-330.
DR PDB; 5M3V; X-ray; 1.97 A; A/B=104-330.
DR PDB; 5TPS; X-ray; 2.70 A; A/B=104-330.
DR PDB; 5U4Y; X-ray; 2.50 A; A/B=118-329.
DR PDB; 5U52; X-ray; 1.94 A; A/B=119-326.
DR PDB; 5U66; X-ray; 1.70 A; A=120-326.
DR PDB; 5V43; X-ray; 2.32 A; A/B=104-329.
DR PDB; 5V4E; X-ray; 3.22 A; A/B/C/D/E/F/G/H=104-329.
DR PDB; 6DCV; X-ray; 1.90 A; B/H=1-107.
DR PDB; 6DCW; X-ray; 2.00 A; H=1-107.
DR PDB; 6DE7; X-ray; 4.12 A; D=1-105, H=1-103.
DR PDB; 6F2Z; X-ray; 2.30 A; A/B=104-330.
DR PDB; 6G1E; X-ray; 1.88 A; A=104-156.
DR PDB; 6N35; X-ray; 1.75 A; H/M=1-102.
DR PDB; 6YT7; X-ray; 1.55 A; B=104-330.
DR PDB; 7KWO; EM; 2.90 A; V=12-329.
DR PDB; 7LUR; X-ray; 1.95 A; A/B=104-330.
DR PDBsum; 1AJ7; -.
DR PDBsum; 1AQK; -.
DR PDBsum; 1AXS; -.
DR PDBsum; 1BEY; -.
DR PDBsum; 1D5B; -.
DR PDBsum; 1D5I; -.
DR PDBsum; 1D6V; -.
DR PDBsum; 1DFB; -.
DR PDBsum; 1DN2; -.
DR PDBsum; 1E4K; -.
DR PDBsum; 1FC1; -.
DR PDBsum; 1FC2; -.
DR PDBsum; 1FCC; -.
DR PDBsum; 1GAF; -.
DR PDBsum; 1H3T; -.
DR PDBsum; 1H3U; -.
DR PDBsum; 1H3V; -.
DR PDBsum; 1H3W; -.
DR PDBsum; 1H3X; -.
DR PDBsum; 1H3Y; -.
DR PDBsum; 1HKL; -.
DR PDBsum; 1HZH; -.
DR PDBsum; 1I7Z; -.
DR PDBsum; 1L6X; -.
DR PDBsum; 1N7M; -.
DR PDBsum; 1OQO; -.
DR PDBsum; 1OQX; -.
DR PDBsum; 1PG7; -.
DR PDBsum; 1T83; -.
DR PDBsum; 1T89; -.
DR PDBsum; 1VGE; -.
DR PDBsum; 2DTS; -.
DR PDBsum; 2GJ7; -.
DR PDBsum; 2I5Y; -.
DR PDBsum; 2IWG; -.
DR PDBsum; 2J6E; -.
DR PDBsum; 2JB5; -.
DR PDBsum; 2JB6; -.
DR PDBsum; 2O5X; -.
DR PDBsum; 2O5Y; -.
DR PDBsum; 2O5Z; -.
DR PDBsum; 2OSL; -.
DR PDBsum; 2QAD; -.
DR PDBsum; 2QL1; -.
DR PDBsum; 2QQK; -.
DR PDBsum; 2QQL; -.
DR PDBsum; 2QQN; -.
DR PDBsum; 2QR0; -.
DR PDBsum; 2R56; -.
DR PDBsum; 2RCS; -.
DR PDBsum; 2VXQ; -.
DR PDBsum; 2WAH; -.
DR PDBsum; 3AGV; -.
DR PDBsum; 3AVE; -.
DR PDBsum; 3AY4; -.
DR PDBsum; 3B2U; -.
DR PDBsum; 3B2V; -.
DR PDBsum; 3BDY; -.
DR PDBsum; 3BE1; -.
DR PDBsum; 3BKY; -.
DR PDBsum; 3BN9; -.
DR PDBsum; 3BQU; -.
DR PDBsum; 3C08; -.
DR PDBsum; 3C09; -.
DR PDBsum; 3C2S; -.
DR PDBsum; 3CFJ; -.
DR PDBsum; 3CFK; -.
DR PDBsum; 3CSY; -.
DR PDBsum; 3D0L; -.
DR PDBsum; 3D0V; -.
DR PDBsum; 3D6G; -.
DR PDBsum; 3D85; -.
DR PDBsum; 3DJ9; -.
DR PDBsum; 3DNK; -.
DR PDBsum; 3DO3; -.
DR PDBsum; 3DRO; -.
DR PDBsum; 3DRQ; -.
DR PDBsum; 3DVG; -.
DR PDBsum; 3DVN; -.
DR PDBsum; 3EYF; -.
DR PDBsum; 3EYO; -.
DR PDBsum; 3EYQ; -.
DR PDBsum; 3FJT; -.
DR PDBsum; 3MCL; -.
DR PDBsum; 3O11; -.
DR PDBsum; 3RY6; -.
DR PDBsum; 3S7G; -.
DR PDBsum; 3SGJ; -.
DR PDBsum; 3SGK; -.
DR PDBsum; 3TV3; -.
DR PDBsum; 3TWC; -.
DR PDBsum; 3TYG; -.
DR PDBsum; 3U0W; -.
DR PDBsum; 3U7W; -.
DR PDBsum; 3U7Y; -.
DR PDBsum; 3V7M; -.
DR PDBsum; 3V8C; -.
DR PDBsum; 3V95; -.
DR PDBsum; 3WJJ; -.
DR PDBsum; 3WJL; -.
DR PDBsum; 3WKN; -.
DR PDBsum; 3WN5; -.
DR PDBsum; 4ACP; -.
DR PDBsum; 4B7I; -.
DR PDBsum; 4BM7; -.
DR PDBsum; 4BSV; -.
DR PDBsum; 4BSW; -.
DR PDBsum; 4BYH; -.
DR PDBsum; 4CDH; -.
DR PDBsum; 4D9Q; -.
DR PDBsum; 4D9R; -.
DR PDBsum; 4DAG; -.
DR PDBsum; 4DZ8; -.
DR PDBsum; 4EOW; -.
DR PDBsum; 4HIX; -.
DR PDBsum; 4J12; -.
DR PDBsum; 4KU1; -.
DR PDBsum; 4LLD; -.
DR PDBsum; 4LLM; -.
DR PDBsum; 4LLQ; -.
DR PDBsum; 4N0U; -.
DR PDBsum; 4NQS; -.
DR PDBsum; 4NQT; -.
DR PDBsum; 4NQU; -.
DR PDBsum; 4NWT; -.
DR PDBsum; 4NWU; -.
DR PDBsum; 4O4Y; -.
DR PDBsum; 4O51; -.
DR PDBsum; 4Q6Y; -.
DR PDBsum; 4Q74; -.
DR PDBsum; 4Q7D; -.
DR PDBsum; 4W4N; -.
DR PDBsum; 4W4O; -.
DR PDBsum; 4WI2; -.
DR PDBsum; 4WI3; -.
DR PDBsum; 4WI4; -.
DR PDBsum; 4WI5; -.
DR PDBsum; 4WI6; -.
DR PDBsum; 4WI7; -.
DR PDBsum; 4WI8; -.
DR PDBsum; 4WI9; -.
DR PDBsum; 4X4M; -.
DR PDBsum; 4X98; -.
DR PDBsum; 4X99; -.
DR PDBsum; 4XMP; -.
DR PDBsum; 4XNY; -.
DR PDBsum; 4XNZ; -.
DR PDBsum; 4XXD; -.
DR PDBsum; 4ZNE; -.
DR PDBsum; 5BW7; -.
DR PDBsum; 5C7K; -.
DR PDBsum; 5D4Q; -.
DR PDBsum; 5D6D; -.
DR PDBsum; 5DI8; -.
DR PDBsum; 5DJ0; -.
DR PDBsum; 5DJ2; -.
DR PDBsum; 5DJ6; -.
DR PDBsum; 5DJ8; -.
DR PDBsum; 5DJA; -.
DR PDBsum; 5DJC; -.
DR PDBsum; 5DJD; -.
DR PDBsum; 5DJX; -.
DR PDBsum; 5DJY; -.
DR PDBsum; 5DJZ; -.
DR PDBsum; 5DK0; -.
DR PDBsum; 5DK2; -.
DR PDBsum; 5DVK; -.
DR PDBsum; 5DVL; -.
DR PDBsum; 5DVM; -.
DR PDBsum; 5DVN; -.
DR PDBsum; 5DVO; -.
DR PDBsum; 5GSQ; -.
DR PDBsum; 5HSF; -.
DR PDBsum; 5HY9; -.
DR PDBsum; 5HYE; -.
DR PDBsum; 5HYF; -.
DR PDBsum; 5HYI; -.
DR PDBsum; 5IQ7; -.
DR PDBsum; 5IQ9; -.
DR PDBsum; 5IW3; -.
DR PDBsum; 5IW6; -.
DR PDBsum; 5JIH; -.
DR PDBsum; 5JII; -.
DR PDBsum; 5JIK; -.
DR PDBsum; 5K33; -.
DR PDBsum; 5K64; -.
DR PDBsum; 5K65; -.
DR PDBsum; 5K8D; -.
DR PDBsum; 5KWG; -.
DR PDBsum; 5M3V; -.
DR PDBsum; 5TPS; -.
DR PDBsum; 5U4Y; -.
DR PDBsum; 5U52; -.
DR PDBsum; 5U66; -.
DR PDBsum; 5V43; -.
DR PDBsum; 5V4E; -.
DR PDBsum; 6DCV; -.
DR PDBsum; 6DCW; -.
DR PDBsum; 6DE7; -.
DR PDBsum; 6F2Z; -.
DR PDBsum; 6G1E; -.
DR PDBsum; 6N35; -.
DR PDBsum; 6YT7; -.
DR PDBsum; 7KWO; -.
DR PDBsum; 7LUR; -.
DR AlphaFoldDB; P01857; -.
DR SASBDB; P01857; -.
DR SMR; P01857; -.
DR ComplexPortal; CPX-6929; IgG1 - Ig kappa immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6931; IgG1 - Ig lambda 1 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6932; IgG1 - Ig lambda 2 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6933; IgG1 - Ig lambda 3 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6934; IgG1 - Ig lambda 6 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6935; IgG1 - Ig lambda 7 immunoglobulin complex, constant regions.
DR DIP; DIP-29187N; -.
DR IntAct; P01857; 121.
DR MINT; P01857; -.
DR DrugBank; DB07909; (1S,2S,5S)2-(4-GLUTARIDYLBENZYL)-5-PHENYL-1-CYCLOHEXANOL.
DR DrugBank; DB07883; (2-AMINO-3-PHENYL-BICYCLO[2.2.1]HEPT-2-YL)-PHENYL-METHANONE.
DR DrugBank; DB08294; 2-(4-HYDROXY-3-NITROPHENYL)ACETIC ACID.
DR DrugBank; DB07371; 3-(10-methyl-9-anthryl)propanoic acid.
DR DrugBank; DB07441; 3-{[(9-CYANO-9,10-DIHYDRO-10-METHYLACRIDIN-9-YL)CARBONYL]AMINO}PROPANOIC ACID.
DR DrugBank; DB08562; 4-(4-STYRYL-PHENYLCARBAMOYL)-BUTYRIC ACID.
DR DrugBank; DB08409; 4-NITRO-BENZYLPHOSPHONOBUTANOYL-GLYCINE.
DR DrugBank; DB08296; 5-(PARA-NITROPHENYL PHOSPHONATE)-PENTANOIC ACID.
DR DrugBank; DB08412; 6-{4-[HYDROXY-(4-NITRO-PHENOXY)-PHOSPHORYL]-BUTYRYLAMINO}-HEXANOIC ACID.
DR DrugBank; DB08332; 9-(2-carboxyethyl)-10-methylanthracene endoperoxide.
DR DrugBank; DB04473; alpha-L-fucose.
DR DrugBank; DB04639; Biphenylalanine.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB07375; Etiocholanedione.
DR DrugBank; DB07764; Fluorescin.
DR DrugBank; DB15258; Imlifidase.
DR DrugBank; DB01631; Methyl nonanoate.
DR DrugBank; DB07816; N-(P-CYANOPHENYL)-N'-DIPHENYLMETHYL-GUANIDINE-ACETIC ACID.
DR DrugBank; DB08377; N-[4-(4-nitrophenylphospho)butanoyl]-D-alanine.
DR DrugBank; DB08411; N-[4-(4-nitrophenylphospho)butanoyl]-L-alanine.
DR DrugBank; DB03740; N-acetyl-alpha-D-glucosamine.
DR DrugBank; DB07881; N-{[2-({[1-(4-CARBOXYBUTANOYL)AMINO]-2-PHENYLETHYL}-HYDROXYPHOSPHINYL)OXY]ACETYL}-2-PHENYLETHYLAMINE.
DR DrugBank; DB08410; PARA-NITROBENZYL GLUTARYL GLYCINIC ACID.
DR DrugBank; DB08394; PARA-NITROPHENYLPHOSPHONOBUTANOYL-GLYCINE.
DR DrugBank; DB07672; TRANS-2-(DIMETHYLPHENYLSILYL)-PIPERIDINE-N-OXIDE.
DR IMGT_GENE-DB; IGHG1; -.
DR CarbonylDB; P01857; -.
DR GlyConnect; 233; 111 N-Linked glycans.
DR GlyConnect; 671; 108 N-Linked glycans (2 sites).
DR GlyGen; P01857; 2 sites, 169 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P01857; -.
DR MetOSite; P01857; -.
DR PhosphoSitePlus; P01857; -.
DR SwissPalm; P01857; -.
DR BioMuta; IGHG1; -.
DR DMDM; 121039; -.
DR DOSAC-COBS-2DPAGE; P01857; -.
DR REPRODUCTION-2DPAGE; P01857; -.
DR UCD-2DPAGE; P01857; -.
DR CPTAC; CPTAC-669; -.
DR jPOST; P01857; -.
DR MassIVE; P01857; -.
DR MaxQB; P01857; -.
DR PeptideAtlas; P01857; -.
DR PRIDE; P01857; -.
DR ProteomicsDB; 51494; -.
DR ABCD; P01857; 7 sequenced antibodies.
DR Ensembl; ENST00000390549.6; ENSP00000374991.2; ENSG00000211896.7.
DR Ensembl; ENST00000631466.1; ENSP00000488387.1; ENSG00000277633.5.
DR UCSC; uc059gdc.1; human.
DR GeneCards; IGHG1; -.
DR HGNC; HGNC:5525; IGHG1.
DR HPA; ENSG00000211896; Group enriched (lymphoid tissue, urinary bladder).
DR MalaCards; IGHG1; -.
DR MIM; 147100; gene.
DR MIM; 254500; phenotype.
DR neXtProt; NX_P01857; -.
DR OpenTargets; ENSG00000211896; -.
DR Orphanet; 67038; B-cell chronic lymphocytic leukemia.
DR Orphanet; 536; Systemic lupus erythematosus.
DR VEuPathDB; HostDB:ENSG00000211896; -.
DR GeneTree; ENSGT00940000162793; -.
DR InParanoid; P01857; -.
DR PhylomeDB; P01857; -.
DR PathwayCommons; P01857; -.
DR Reactome; R-HSA-166663; Initial triggering of complement.
DR Reactome; R-HSA-173623; Classical antibody-mediated complement activation.
DR Reactome; R-HSA-2029481; FCGR activation.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-9664323; FCGR3A-mediated IL10 synthesis.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR Reactome; R-HSA-977606; Regulation of Complement cascade.
DR SignaLink; P01857; -.
DR ChiTaRS; IGHG1; human.
DR EvolutionaryTrace; P01857; -.
DR Pharos; P01857; Tclin.
DR PRO; PR:P01857; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P01857; protein.
DR Bgee; ENSG00000211896; Expressed in spleen and 94 other tissues.
DR ExpressionAtlas; P01857; baseline and differential.
DR Genevisible; P01857; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0071735; C:IgG immunoglobulin complex; IPI:ComplexPortal.
DR GO; GO:0042571; C:immunoglobulin complex, circulating; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
DR GO; GO:0003823; F:antigen binding; IBA:GO_Central.
DR GO; GO:0034988; F:Fc-gamma receptor I complex binding; IDA:UniProtKB.
DR GO; GO:0034987; F:immunoglobulin receptor binding; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IDA:ComplexPortal.
DR GO; GO:0001788; P:antibody-dependent cellular cytotoxicity; IDA:UniProtKB.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006958; P:complement activation, classical pathway; IBA:GO_Central.
DR GO; GO:0097278; P:complement-dependent cytotoxicity; IDA:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0006911; P:phagocytosis, engulfment; IBA:GO_Central.
DR GO; GO:0006910; P:phagocytosis, recognition; IBA:GO_Central.
DR GO; GO:0050871; P:positive regulation of B cell activation; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003006; Ig/MHC_CS.
DR InterPro; IPR003597; Ig_C1-set.
DR Pfam; PF07654; C1-set; 3.
DR SMART; SM00407; IGc1; 3.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS00290; IG_MHC; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Cell membrane; Chromosomal rearrangement;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin; Immunoglobulin domain; Membrane; Reference proteome;
KW Secreted.
FT CHAIN <1..330
FT /note="Immunoglobulin heavy constant gamma 1"
FT /id="PRO_0000153578"
FT DOMAIN 6..99
FT /note="Ig-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 121..220
FT /note="Ig-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 229..325
FT /note="Ig-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 1..98
FT /note="CH1"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..110
FT /note="Hinge"
FT REGION 111..223
FT /note="CH2"
FT REGION 224..330
FT /note="CH3"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:19139490,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19358553"
FT DISULFID 27..83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 103
FT /note="Interchain (with light chain)"
FT DISULFID 109
FT /note="Interchain (with heavy chain)"
FT DISULFID 112
FT /note="Interchain (with heavy chain)"
FT DISULFID 144..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 250..308
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 97
FT /note="K -> R (in IMGT allele IGHG1*03)"
FT /id="VAR_003886"
FT VARIANT 239
FT /note="D -> E (in IMGT allele IGHG1*03)"
FT /id="VAR_003887"
FT VARIANT 241
FT /note="L -> M (in IMGT allele IGHG1*03)"
FT /id="VAR_003888"
FT MUTAGEN 117..118
FT /note="LL->AA: Abolishes binding to FCGR1A, FCGR2A and
FT FCGR3A. Impairs ADCC of virus-infected cells by monocytes."
FT /evidence="ECO:0000269|PubMed:11711607"
FT MUTAGEN 117
FT /note="L->A: Reduces the affinity for FCGR1A about 5-fold.
FT Abolishes binding to FCGR2A and FCGR3A. Impairs ADCC of
FT virus-infected cells by monocytes. Impairs binding to
FT complement component C1q. Impairs complement-dependent
FT cytotoxicity."
FT /evidence="ECO:0000269|PubMed:11711607"
FT MUTAGEN 118
FT /note="L->E: Reduces the affinity for FCGR1A about 40-fold.
FT Abolishes binding to FCGR2A and FCGR3A. Impairs ADCC of
FT virus-infected cells by monocytes. Impairs binding to
FT complement component C1q. Impairs complement-dependent
FT cytotoxicity."
FT MUTAGEN 120
FT /note="G->A: Reduces the affinity for FCGR1A about 40-fold.
FT Abolishes binding to FCGR2A and FCGR3A. Impairs ADCC of
FT virus-infected cells by monocytes. Decreases binding to
FT complement component C1q. Decreases complement-dependent
FT cytotoxicity."
FT /evidence="ECO:0000269|PubMed:11711607"
FT MUTAGEN 205
FT /note="K->A: Does not affect binding to FCGR1A. Only
FT slightly affects binding to FCGR2A and FCGR3A. Impairs
FT binding to complement component C1q. Impairs complement-
FT dependent cytotoxicity."
FT /evidence="ECO:0000269|PubMed:11711607"
FT NON_TER 1
FT STRAND 7..14
FT /evidence="ECO:0007829|PDB:4LLD"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:4LLD"
FT STRAND 22..35
FT /evidence="ECO:0007829|PDB:4LLD"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:4LLD"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:4LLD"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:4LLD"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:5IQ7"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:5IQ7"
FT STRAND 63..72
FT /evidence="ECO:0007829|PDB:4LLD"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:4LLD"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:4LLD"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:4LLD"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:4LLD"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:4LLD"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:3SGJ"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:1HZH"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:1L6X"
FT HELIX 130..134
FT /evidence="ECO:0007829|PDB:1L6X"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:5IW3"
FT STRAND 141..149
FT /evidence="ECO:0007829|PDB:1L6X"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:1L6X"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:1L6X"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:1L6X"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:5M3V"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:5DI8"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:5GSQ"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:1L6X"
FT HELIX 193..197
FT /evidence="ECO:0007829|PDB:1L6X"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:1L6X"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:1L6X"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:1L6X"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:5HSF"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:5HSF"
FT STRAND 243..258
FT /evidence="ECO:0007829|PDB:5HSF"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:5HSF"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:1L6X"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:5HSF"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:3V8C"
FT STRAND 287..296
FT /evidence="ECO:0007829|PDB:5HSF"
FT HELIX 297..301
FT /evidence="ECO:0007829|PDB:5HSF"
FT STRAND 306..311
FT /evidence="ECO:0007829|PDB:5HSF"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:1FCC"
FT STRAND 318..324
FT /evidence="ECO:0007829|PDB:5HSF"
SQ SEQUENCE 330 AA; 36106 MW; 3770EE106C2FA33D CRC64;
ASTKGPSVFP LAPSSKSTSG GTAALGCLVK DYFPEPVTVS WNSGALTSGV HTFPAVLQSS
GLYSLSSVVT VPSSSLGTQT YICNVNHKPS NTKVDKKVEP KSCDKTHTCP PCPAPELLGG
PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN
STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE
LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW
QQGNVFSCSV MHEALHNHYT QKSLSLSPGK
