ID IGHG1_HUMAN Reviewed; 399 AA. AC P01857; A0A0A0MS08; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 03-MAY-2023, sequence version 2. DT 02-SEP-2026, entry version 244. DE RecName: Full=Immunoglobulin heavy constant gamma 1 {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.14}; 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.14}; 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE IGHG1*01) (ISOFORM 1). 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 [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGHG1*05) RP (ISOFORMS 1 AND 2). 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 [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 329-399 (ISOFORM 2). RX PubMed=2026457; DOI=10.1016/0165-2478(91)90143-x; RA Kinoshita K., Shimizu A., Honjo T.; RT "The membrane exons of the pseudo-gamma-chain gene of the human RT immunoglobulin are apparently functional and highly homologous to those of RT the gamma 1 gene."; RL Immunol. Lett. 27:151-155(1991). RN [5] 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 [6] 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 [7] 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 [8] 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 [9] 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 [10] 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 [11] RP GLYCOSYLATION AT ASN-180, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=10818239; DOI=10.1016/s0014-5793(00)01557-x; RA Masuda K., Yamaguchi Y., Kato K., Takahashi N., Shimada I., Arata Y.; RT "Pairing of oligosaccharides in the Fc region of immunoglobulin G."; RL FEBS Lett. 473:349-357(2000). RN [12] RP GLYCOSYLATION AT ASN-180, AND DEGLYCOSYLATION (MICROBIAL INFECTION). RX PubMed=11406581; DOI=10.1093/emboj/20.12.3046; RA Collin M., Olsen A.; RT "EndoS, a novel secreted protein from Streptococcus pyogenes with RT endoglycosidase activity on human IgG."; RL EMBO J. 20:3046-3055(2001). RN [13] 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 [14] 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 [15] 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 [16] RP FUNCTION, AND PTM. RX PubMed=12427744; DOI=10.1074/jbc.m210665200; RA Shinkawa T., Nakamura K., Yamane N., Shoji-Hosaka E., Kanda Y., RA Sakurada M., Uchida K., Anazawa H., Satoh M., Yamasaki M., Hanai N., RA Shitara K.; RT "The absence of fucose but not the presence of galactose or bisecting N- RT acetylglucosamine of human IgG1 complex-type oligosaccharides shows the RT critical role of enhancing antibody-dependent cellular cytotoxicity."; RL J. Biol. Chem. 278:3466-3473(2003). RN [17] RP NOMENCLATURE, AND C-DOMAIN. RX PubMed=15572068; DOI=10.1016/j.dci.2004.07.003; RA Lefranc M.P., Pommie C., Kaas Q., Duprat E., Bosc N., Guiraudou D., RA Jean C., Ruiz M., Da Piedade I., Rouard M., Foulquier E., Thouvenin V., RA Lefranc G.; RT "IMGT unique numbering for immunoglobulin and T cell receptor constant RT domains and Ig superfamily C-like domains."; RL Dev. Comp. Immunol. 29:185-203(2005). RN [18] RP FUNCTION. RX PubMed=16219319; DOI=10.1016/j.jim.2005.08.009; RA Niwa R., Natsume A., Uehara A., Wakitani M., Iida S., Uchida K., Satoh M., RA Shitara K.; RT "IgG subclass-independent improvement of antibody-dependent cellular RT cytotoxicity by fucose removal from Asn297-linked oligosaccharides."; RL J. Immunol. Methods 306:151-160(2005). RN [19] 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 [20] RP FUNCTION, AND PTM. RX PubMed=18420934; DOI=10.1126/science.1154315; RA Anthony R.M., Nimmerjahn F., Ashline D.J., Reinhold V.N., Paulson J.C., RA Ravetch J.V.; RT "Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG RT Fc."; RL Science 320:373-376(2008). RN [21] 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 [22] 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 [23] 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 [24] RP GLYCOSYLATION AT ASN-180, AND DEGLYCOSYLATION (MICROBIAL INFECTION). RX PubMed=20357243; DOI=10.1182/blood-2009-08-239020; RA Allhorn M., Briceno J.G., Baudino L., Lood C., Olsson M.L., Izui S., RA Collin M.; RT "The IgG-specific endoglycosidase EndoS inhibits both cellular and RT complement-mediated autoimmune hemolysis."; RL Blood 115:5080-5088(2010). RN [25] 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 [26] 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 [27] RP GLYCOSYLATION AT ASN-180, IDENTIFICATION BY MASS SPECTROMETRY, AND PTM. RX PubMed=22184099; DOI=10.1074/mcp.m111.014563; RA Selman M.H., de Jong S.E., Soonawala D., Kroon F.P., Adegnika A.A., RA Deelder A.M., Hokke C.H., Yazdanbakhsh M., Wuhrer M.; RT "Changes in antigen-specific IgG1 Fc N-glycosylation upon influenza and RT tetanus vaccination."; RL Mol. Cell. Proteomics 11:M111.014563-M111.014563(2012). RN [28] 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 [29] RP DEGLYCOSYLATION (MICROBIAL INFECTION). RX PubMed=23865566; DOI=10.1042/bj20130126; RA Sjoegren J., Struwe W.B., Cosgrave E.F., Rudd P.M., Stervander M., RA Allhorn M., Hollands A., Nizet V., Collin M.; RT "EndoS2 is a unique and conserved enzyme of serotype M49 group A RT Streptococcus that hydrolyses N-linked glycans on IgG and alpha1-acid RT glycoprotein."; RL Biochem. J. 455:107-118(2013). RN [30] 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 [31] RP FUNCTION, GLYCOSYLATION AT ASN-180, IDENTIFICATION BY MASS SPECTROMETRY, RP AND PTM. RX PubMed=26140596; DOI=10.1016/j.cell.2015.06.026; RA Wang T.T., Maamary J., Tan G.S., Bournazos S., Davis C.W., Krammer F., RA Schlesinger S.J., Palese P., Ahmed R., Ravetch J.V.; RT "Anti-HA Glycoforms Drive B Cell Affinity Selection and Determine Influenza RT Vaccine Efficacy."; RL Cell 162:160-169(2015). RN [32] RP GLYCOSYLATION AT ASN-180, IDENTIFICATION BY MASS SPECTROMETRY, AND PTM. RX PubMed=25733881; DOI=10.1073/pnas.1422481112; RA Washburn N., Schwab I., Ortiz D., Bhatnagar N., Lansing J.C., Medeiros A., RA Tyler S., Mekala D., Cochran E., Sarvaiya H., Garofalo K., Meccariello R., RA Meador J.W. III, Rutitzky L., Schultes B.C., Ling L., Avery W., RA Nimmerjahn F., Manning A.M., Kaundinya G.V., Bosques C.J.; RT "Controlled tetra-Fc sialylation of IVIg results in a drug candidate with RT consistent enhanced anti-inflammatory activity."; RL Proc. Natl. Acad. Sci. U.S.A. 112:E1297-E1306(2015). RN [33] 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 [34] RP FUNCTION, INTERACTION WITH FCGR1A; FCGR2A; FCGR2B; FCGR3A AND FCGR3B, AND RP PTM. RX PubMed=28566370; DOI=10.4049/jimmunol.1700116; RA Bruggeman C.W., Dekkers G., Bentlage A.E.H., Treffers L.W., RA Nagelkerke S.Q., Lissenberg-Thunnissen S., Koeleman C.A.M., Wuhrer M., RA van den Berg T.K., Rispens T., Vidarsson G., Kuijpers T.W.; RT "Enhanced Effector Functions Due to Antibody Defucosylation Depend on the RT Effector Cell Fcgamma Receptor Profile."; RL J. Immunol. 199:204-211(2017). RN [35] RP GLYCOSYLATION AT ASN-180, IDENTIFICATION BY MASS SPECTROMETRY, AND PTM. RX PubMed=29133956; DOI=10.1038/s41467-017-01525-0; RA Benedetti E., Pucic-Bakovic M., Keser T., Wahl A., Hassinen A., Yang J.Y., RA Liu L., Trbojevic-Akmacic I., Razdorov G., Stambuk J., Klaric L., RA Ugrina I., Selman M.H.J., Wuhrer M., Rudan I., Polasek O., Hayward C., RA Grallert H., Strauch K., Peters A., Meitinger T., Gieger C., Vilaj M., RA Boons G.J., Moremen K.W., Ovchinnikova T., Bovin N., Kellokumpu S., RA Theis F.J., Lauc G., Krumsiek J.; RT "Network inference from glycoproteomics data reveals new reactions in the RT IgG glycosylation pathway."; RL Nat. Commun. 8:1483-1483(2017). RN [36] RP GLYCOSYLATION AT ASN-180, IDENTIFICATION BY MASS SPECTROMETRY, AND PTM. RX PubMed=29445378; DOI=10.3389/fimmu.2018.00129; RA Sonneveld M.E., Koeleman C.A.M., Plomp H.R., Wuhrer M., RA van der Schoot C.E., Vidarsson G.; RT "Fc-Glycosylation in Human IgG1 and IgG3 Is Similar for Both Total and RT Anti-Red-Blood Cell Anti-K Antibodies."; RL Front. Immunol. 9:129-129(2018). RN [37] RP FUNCTION, INTERACTION WITH FCGR3A, GLYCOSYLATION AT ASN-180, PTM, AND RP MUTAGENESIS OF ASN-180. RX PubMed=30061887; DOI=10.3389/fimmu.2018.01614; RA Goletz C., Lischke T., Harnack U., Schiele P., Danielczyk A., Ruehmann J., RA Goletz S.; RT "Glyco-Engineered Anti-Human Programmed Death-Ligand 1 Antibody Mediates RT Stronger CD8 T Cell Activation Than Its Normal Glycosylated and Non- RT Glycosylated Counterparts."; RL Front. Immunol. 9:1614-1614(2018). RN [38] RP FUNCTION, INTERACTION WITH SPA (MICROBIAL INFECTION), SUBUNIT, AND RP MUTAGENESIS OF GLU-228; GLU-313 AND SER-323. RX PubMed=33563762; DOI=10.1073/pnas.2016772118; RA Cruz A.R., Boer M.A.D., Strasser J., Zwarthoff S.A., Beurskens F.J., RA de Haas C.J.C., Aerts P.C., Wang G., de Jong R.N., Bagnoli F., RA van Strijp J.A.G., van Kessel K.P.M., Schuurman J., Preiner J., RA Heck A.J.R., Rooijakkers S.H.M.; RT "Staphylococcal protein A inhibits complement activation by interfering RT with IgG hexamer formation."; RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021). RN [39] RP INTERACTION WITH FCGR1A; FCGR2A; FCGR2B AND FCGR3A. RX PubMed=37421619; DOI=10.1016/j.celrep.2023.112734; RA Tan Z.C., Lux A., Biburger M., Varghese P., Lees S., Nimmerjahn F., RA Meyer A.S.; RT "Mixed IgG Fc immune complexes exhibit blended binding profiles and refine RT FcR affinity estimates."; RL Cell Rep. 42:112734-112734(2023). RN [40] RP GLYCOSYLATION AT ASN-180, IDENTIFICATION BY MASS SPECTROMETRY, AND PTM. RX PubMed=36529104; DOI=10.1016/j.ebiom.2022.104408; RG Fatebenefratelli-Sacco Infectious Diseases Physicians group; RG UMC COVID-19 S3/HCW study group; RA Van Coillie J., Pongracz T., Rahmoeller J., Chen H.J., Geyer C.E., RA van Vught L.A., Buhre J.S., Sustic T., van Osch T.L.J., Steenhuis M., RA Hoepel W., Wang W., Lixenfeld A.S., Nouta J., Keijzer S., Linty F., RA Visser R., Larsen M.D., Martin E.L., Kuensting I., Lehrian S., RA von Kopylow V., Kern C., Lunding H.B., de Winther M., van Mourik N., RA Rispens T., Graf T., Slim M.A., Minnaar R.P., Bomers M.K., Sikkens J.J., RA Vlaar A.P.J., van der Schoot C.E., den Dunnen J., Wuhrer M., Ehlers M., RA Vidarsson G.; RT "The BNT162b2 mRNA SARS-CoV-2 vaccine induces transient afucosylated IgG1 RT in naive but not in antigen-experienced vaccinees."; RL EBioMedicine 87:104408-104408(2023). RN [41] RP FUNCTION, PTM, AND MUTAGENESIS OF ASN-180. RX PubMed=36867679; DOI=10.1126/sciimmunol.add8005; RA Cohen Saban N., Yalin A., Landsberger T., Salomon R., Alva A., Feferman T., RA Amit I., Dahan R.; RT "Fc glycoengineering of a PD-L1 antibody harnesses Fcgamma receptors for RT increased antitumor efficacy."; RL Sci. Immunol. 8:eadd8005-eadd8005(2023). RN [42] RP REVIEW ON IMMUNOGLOBULIN FC REGION GLYCOSYLATION, AND NOMENCLATURE. RX PubMed=38383719; DOI=10.1038/s41596-024-00963-7; RA Falck D., Wuhrer M.; RT "GlYcoLISA: antigen-specific and subclass-specific IgG Fc glycosylation RT analysis based on an immunosorbent assay with an LC-MS readout."; RL Nat. Protoc. 19:1887-1909(2024). RN [43] RP GLYCOSYLATION AT ASN-180, IDENTIFICATION BY MASS SPECTROMETRY, AND PTM. RX PubMed=39983994; DOI=10.1016/j.mcpro.2025.100928; RA van Tol B.D.M., Wasynczuk A.M., Gijze S., Mayboroda O.A., Nouta J., RA Dolhain R.J.E.M., Wuhrer M., Falck D.; RT "Comprehensive Immunoglobulin G, A, and M Glycopeptide Profiling for Large- RT Scale Biomedical Research."; RL Mol. Cell. Proteomics 24:100928-100928(2025). RN [44] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), AND INTERACTION WITH SPA (MICROBIAL RP INFECTION). 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 [45] RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 106-328 IN COMPLEX WITH FCGR3B, RP DISULFIDE BONDS, GLYCOSYLATION AT ASN-180, DOMAIN, AND SUBUNIT. RX PubMed=10917521; DOI=10.1038/35018508; RA Sondermann P., Huber R., Oosthuizen V., Jacob U.; RT "The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII RT complex."; RL Nature 406:267-273(2000). RN [46] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 106-328 IN COMPLEX WITH FCGR3A, RP DISULFIDE BONDS, GLYCOSYLATION AT ASN-180, AND PTM. RX PubMed=21768335; DOI=10.1073/pnas.1108455108; RA Ferrara C., Grau S., Jager C., Sondermann P., Brunker P., Waldhauer I., RA Hennig M., Ruf A., Rufer A.C., Stihle M., Umana P., Benz J.; RT "Unique carbohydrate-carbohydrate interactions are required for high RT affinity binding between FcgammaRIII and antibodies lacking core fucose."; RL Proc. Natl. Acad. Sci. U.S.A. 108:12669-12674(2011). RN [47] RP X-RAY CRYSTALLOGRAPHY (3.48 ANGSTROMS) OF 112-328 IN COMPLEX WITH FCGR1A, RP DISULFIDE BONDS, GLYCOSYLATION AT ASN-180, PTM, FUNCTION, AND DOMAIN. RX PubMed=25561553; DOI=10.1073/pnas.1418812112; RA Lu J., Chu J., Zou Z., Hamacher N.B., Rixon M.W., Sun P.D.; RT "Structure of FcgammaRI in complex with Fc reveals the importance of glycan RT recognition for high-affinity IgG binding."; RL Proc. Natl. Acad. Sci. U.S.A. 112:833-838(2015). RN [48] 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 [49] 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 (Ig) heavy chains. Igs are CC membrane-bound or secreted glycoproteins produced by B lymphocytes. In CC the recognition phase of humoral immunity, the membrane-bound Igs serve CC as receptors, which upon binding to a specific antigen trigger the CC clonal expansion and differentiation of B lymphocytes into Ig-secreting CC plasma cells. Secreted Igs known as antibodies mediate the effector CC phase of humoral immunity by blocking the interaction of infectious CC antigens with cellular receptors (via the antigen-binding region) and CC eliciting effector mechanisms that lead to pathogen neutralization (via CC the constant region) (PubMed:17576170, PubMed:20176268, CC PubMed:22158414). The antigen-binding region is formed by the variable CC domain of one heavy chain paired with the variable domain of its CC associated light chain. Each Ig molecule has two antigen-binding sites CC with remarkable affinity for a particular antigen due to V-(D)-J CC rearrangement, somatic hypermutations and affinity maturation of the CC variable domains upon antigen exposure (PubMed:17576170, CC PubMed:20176268, PubMed:22158414). The constant region defines the Ig CC isotype that perform distinct sets of effector functions. B cells CC diversify and rearrange their Ig constant regions through class-switch CC recombination, a process by which the constant region is switched from CC one Ig isotype to another, namely from IgM and IgD to IgG, IgA and IgE CC (PubMed:17576170, PubMed:20176268, PubMed:22158414). The constant CC region of Ig gamma-1 (IgG1) isotype interacts (via the fragment CC crystallizable, Fc) with receptors on innate immune cells and the CC complement system to mediate humoral effector functions, including CC antibody-dependent cellular cytotoxicity or phagocytosis, complement- CC dependent cytotoxicity and inflammatory responses. CC {ECO:0000269|PubMed:11711607, ECO:0000269|PubMed:12427744, CC ECO:0000269|PubMed:16219319, ECO:0000269|PubMed:18420934, CC ECO:0000269|PubMed:25561553, ECO:0000269|PubMed:26140596, CC ECO:0000269|PubMed:28566370, ECO:0000269|PubMed:30061887, CC ECO:0000269|PubMed:33563762, ECO:0000269|PubMed:36867679, CC ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, CC ECO:0000303|PubMed:22158414}. CC -!- SUBUNIT: Immunoglobulins (Igs) are composed of two identical heavy CC chains and two identical light chains; disulfide-linked CC (PubMed:20176268). Ig-gamma 1 (IgG1) molecules oligomerize (via non- CC covalent Fc region interactions) to form hexameric rings that serve as CC platforms for binding of the C1 complex (PubMed:33563762). Interacts CC (via Fc region and its N-linked glycan) with Fc receptors (via D2 CC domain). Assembled in immune complexes interacts with FCGR1A, FCGR2A, CC FCGR2B, FCGR3A and FCGR3B; these interactions are impacted by the CC glycans attached on the Fc domain, with afucosylated glycans displaying CC up to 100-fold higher affinity for FCGR3A (PubMed:10917521, CC PubMed:11711607, PubMed:21768335, PubMed:25561553, PubMed:28566370, CC PubMed:30061887, PubMed:37421619). {ECO:0000269|PubMed:10917521, CC ECO:0000269|PubMed:11711607, ECO:0000269|PubMed:21768335, CC ECO:0000269|PubMed:25561553, ECO:0000269|PubMed:28566370, CC ECO:0000269|PubMed:30061887, ECO:0000269|PubMed:33563762, CC ECO:0000269|PubMed:37421619, ECO:0000303|PubMed:20176268}. CC -!- SUBUNIT: (Microbial infection) Interacts (via Fc region) with S. aureus CC spa/protein A (via B domain); spa interferes with the formation of CC IgG:C1q complexes preventing complement activation and protecting CC bacteria from phagocytic killing. {ECO:0000269|PubMed:33563762, CC ECO:0000269|PubMed:7236608}. CC -!- INTERACTION: CC P01857; P31994: FCGR2B; NbExp=31; IntAct=EBI-356114, EBI-724784; CC P01857-1; P12314: FCGR1A; NbExp=2; IntAct=EBI-42826219, EBI-2869867; CC P01857-1; P04488: gE; Xeno; NbExp=2; IntAct=EBI-42826219, EBI-15581257; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted CC {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane CC {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}; Single-pass CC membrane protein {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=2; Synonyms=Membrane-bound, mIgG1 {ECO:0000303|PubMed:2026457}; CC IsoId=P01857-2; Sequence=Displayed; CC Name=1; Synonyms=Secreted, sIgG1 {ECO:0000303|PubMed:6884994}; CC IsoId=P01857-1; Sequence=VSP_061818, VSP_061819; CC -!- DOMAIN: The Fc region of an IgG molecule represents the disulfide- CC linked C-terminal part of the heavy chain containing the CH2 and CH3 CC domains. Can be isolated by proteolysis such as papain digestion of CC IgG. {ECO:0000269|PubMed:10917521}. CC -!- PTM: N-glycosylated. Carries predominantly biantennary complex-type CC glycans attached at Asn-180 residue on the Fc region of each heavy CC chain. Unique Fc glycan profiles found in secreted IgGs are induced in CC an antigen-specific way, likely programmed during B cell priming to CC mount an appropriate Ig effector response (PubMed:10818239, CC PubMed:10917521, PubMed:21768335, PubMed:22184099, PubMed:25561553, CC PubMed:29133956, PubMed:29445378). The core glycan is composed of two CC sequential N-acetylglucosamine (GlcNAc) moieties followed by a central CC mannose (Man) from which two additional Man residues branch out CC (alpha1,3 and alpha1,6 antennae) each capped with a GlcNAc. Additional CC sugar molecules can be added to generate over 30 possible glycans. Such CC sugar modifications include the addition of one fucose at the initial CC GlcNAc, galactose (Gal) and sialic acid (Neu5Ac) residues at antennary CC GlcNAc or a bisecting GlcNAc to the core Man (PubMed:10818239, CC PubMed:22184099, PubMed:29133956, PubMed:38383719). Variable addition CC of sugars account for different IgG functional states associated with CC antibody-dependent cellular cytotoxicity or phagocytosis and CC inflammatory responses such as complement activation and cytokine CC secretion. Fc N-glycan diversity is further enhanced by asymmetric CC glycan pairing on the heavy chains (PubMed:10818239, PubMed:20357243, CC PubMed:22184099, PubMed:29133956). Fc N-glycan sialylation is linked to CC anti-inflammatory effects. It regulates Fc effector functions through CC conformational changes leading to preferential interaction with type II CC Fc receptors while reducing binding to type I Fc receptors. During CC plasmablast response, sialylated Fc domains within immune complexes CC signal via FCER2/CD23 and drive the selection of B cells with high CC affinity for antigen (PubMed:18420934, PubMed:22184099, CC PubMed:25733881, PubMed:26140596). Fc Igs carrying afucosylated N- CC glycans preferentially activate FCGR3A, antigen-dependent cellular CC cytotoxicity and antitumor immunity (PubMed:12427744, PubMed:21768335, CC PubMed:28566370, PubMed:30061887, PubMed:36867679). CC {ECO:0000269|PubMed:10818239, ECO:0000269|PubMed:10917521, CC ECO:0000269|PubMed:12427744, ECO:0000269|PubMed:18420934, CC ECO:0000269|PubMed:20357243, ECO:0000269|PubMed:21768335, CC ECO:0000269|PubMed:22184099, ECO:0000269|PubMed:25561553, CC ECO:0000269|PubMed:25733881, ECO:0000269|PubMed:26140596, CC ECO:0000269|PubMed:28566370, ECO:0000269|PubMed:29133956, CC ECO:0000269|PubMed:29445378, ECO:0000269|PubMed:30061887, CC ECO:0000269|PubMed:36867679, ECO:0000303|PubMed:38383719}. CC -!- PTM: (Microbial infection) Deglycosylation on Asn-180 by S. pyogenes CC EndoS or Endos2 endoglucosidases prevents interaction between CC immunoglobulin-gamma (IgG) and Fc receptors, impairing ability to CC activate the complement pathway. {ECO:0000269|PubMed:11406581, CC ECO:0000269|PubMed:20357243, ECO:0000269|PubMed:23865566}. 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=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J00228; AAC82527.1; ALT_INIT; Genomic_DNA. DR EMBL; AL122127; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X52847; -; NOT_ANNOTATED_CDS; mRNA. 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=106-328. DR PDB; 1FC1; X-ray; 2.90 A; A/B=106-328. DR PDB; 1FC2; X-ray; 2.80 A; D=106-328. 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=108-328. DR PDB; 1H3U; X-ray; 2.40 A; A/B=108-328. DR PDB; 1H3V; X-ray; 3.10 A; A/B=108-328. DR PDB; 1H3W; X-ray; 2.85 A; M=108-328. DR PDB; 1H3X; X-ray; 2.44 A; A/B=108-328. DR PDB; 1H3Y; X-ray; 4.10 A; A/B=108-328. DR PDB; 1HKL; X-ray; 2.68 A; H=1-103. DR PDB; 1HZH; X-ray; 2.70 A; H/K=1-328. 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=1-102. DR PDB; 1OQO; X-ray; 2.30 A; A/B=119-328. DR PDB; 1OQX; X-ray; 2.60 A; A/B=119-328. DR PDB; 1PG7; X-ray; 2.50 A; H/I=1-100. DR PDB; 1T83; X-ray; 3.00 A; A/B=107-328. DR PDB; 1T89; X-ray; 3.50 A; A/B=107-328. DR PDB; 1VGE; X-ray; 2.00 A; H=1-103. DR PDB; 2DTS; X-ray; 2.20 A; A/B=108-328. DR PDB; 2GJ7; X-ray; 5.00 A; A/B=106-328. DR PDB; 2I5Y; X-ray; 2.20 A; H/R=1-101. DR PDB; 2IWG; X-ray; 2.35 A; A/D=120-326. DR PDB; 2J6E; X-ray; 3.00 A; A/B=99-328. 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=106-328. 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=120-328. DR PDB; 3AVE; X-ray; 2.00 A; A/B=108-328. DR PDB; 3AY4; X-ray; 2.20 A; A/B=108-328. 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=1-103. 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=106-328. 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=1-105. DR PDB; 3D0V; X-ray; 2.05 A; B=1-105. 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=119-328. DR PDB; 3DO3; X-ray; 2.50 A; A/B=119-328. DR PDB; 3DRO; X-ray; 3.90 A; B=1-103. DR PDB; 3DRQ; X-ray; 2.00 A; B=1-103. 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=104-328. DR PDB; 3SGJ; X-ray; 2.20 A; A/B=106-328. DR PDB; 3SGK; X-ray; 2.40 A; A/B=106-328. 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=119-328. DR PDB; 3V95; X-ray; 2.70 A; A/B=119-328. 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=119-328. 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=106-328. DR PDB; 4BSW; X-ray; 2.15 A; A/B=106-328. DR PDB; 4BYH; X-ray; 2.30 A; A/B=106-329. DR PDB; 4CDH; X-ray; 2.30 A; A/B=101-328. DR PDB; 4D9Q; X-ray; 2.28 A; E/H=1-102. DR PDB; 4D9R; X-ray; 2.42 A; E/H=1-103. DR PDB; 4DAG; X-ray; 3.39 A; H=1-98. DR PDB; 4DZ8; X-ray; 1.91 A; A/B=108-328. 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=118-328. DR PDB; 4NQT; X-ray; 2.10 A; A=118-328. DR PDB; 4NQU; X-ray; 2.50 A; A=118-328. DR PDB; 4NWT; X-ray; 1.75 A; H=1-105. DR PDB; 4NWU; X-ray; 1.60 A; H=1-105. 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=109-328. DR PDB; 4Q74; X-ray; 2.19 A; A/B=108-328. DR PDB; 4Q7D; X-ray; 2.35 A; A/B=109-328. DR PDB; 4W4N; X-ray; 1.80 A; A/B=107-328. DR PDB; 4W4O; X-ray; 1.80 A; A/B=107-328. 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=112-328. DR PDB; 4X98; X-ray; 2.50 A; A=108-327, B=121-327. DR PDB; 4X99; X-ray; 2.50 A; A/B=108-328. 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=104-328. DR PDB; 5BW7; X-ray; 3.00 A; A/B=108-328. DR PDB; 5C7K; X-ray; 4.60 A; E=1-106. DR PDB; 5D4Q; X-ray; 2.39 A; A/B=109-328. DR PDB; 5D6D; X-ray; 3.13 A; A/B=108-328. DR PDB; 5DI8; X-ray; 1.90 A; A/B=104-328. DR PDB; 5DJ0; X-ray; 2.28 A; A/B=104-328. DR PDB; 5DJ2; X-ray; 2.56 A; A/B=104-328. DR PDB; 5DJ6; X-ray; 2.00 A; A/B=104-328. DR PDB; 5DJ8; X-ray; 2.40 A; A/B=104-328. DR PDB; 5DJA; X-ray; 2.90 A; A/B=104-328. DR PDB; 5DJC; X-ray; 2.10 A; A/B/D/E=104-328. DR PDB; 5DJD; X-ray; 2.30 A; A/B=104-328. DR PDB; 5DJX; X-ray; 2.25 A; A/B/D/E=104-328. DR PDB; 5DJY; X-ray; 2.15 A; A/B=104-328. DR PDB; 5DJZ; X-ray; 1.90 A; A/B=104-328. DR PDB; 5DK0; X-ray; 2.30 A; A/B=104-328. DR PDB; 5DK2; X-ray; 2.60 A; A/B/D/E=104-328. DR PDB; 5DVK; X-ray; 2.60 A; A=104-328. DR PDB; 5DVL; X-ray; 1.90 A; A=104-328. DR PDB; 5DVM; X-ray; 2.95 A; A=104-328. DR PDB; 5DVN; X-ray; 2.50 A; A=104-328. DR PDB; 5DVO; X-ray; 2.50 A; A/B=104-328. DR PDB; 5GSQ; X-ray; 1.85 A; A/B/C/D=106-328. DR PDB; 5HSF; X-ray; 1.52 A; A/B=221-343. DR PDB; 5HY9; X-ray; 2.70 A; A/B=104-328. DR PDB; 5HYE; X-ray; 1.89 A; A/C=104-328. DR PDB; 5HYF; X-ray; 1.80 A; A=104-328. DR PDB; 5HYI; X-ray; 2.90 A; A/B/C/D=104-328. 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=108-328. DR PDB; 5JII; X-ray; 1.79 A; A/B=108-328. DR PDB; 5JIK; X-ray; 1.82 A; A/B=108-328. DR PDB; 5K33; X-ray; 3.30 A; A=108-328. DR PDB; 5K64; X-ray; 2.44 A; A/B=108-328. DR PDB; 5K65; X-ray; 2.50 A; A/B=108-328. DR PDB; 5K8D; X-ray; 4.19 A; B=104-328. DR PDB; 5KWG; X-ray; 4.30 A; A=108-328. DR PDB; 5M3V; X-ray; 1.97 A; A=104-238, B=104-328. DR PDB; 5TPS; X-ray; 2.70 A; A/B=104-328. DR PDB; 5U4Y; X-ray; 2.50 A; A/B=118-328. 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=104-328. DR PDB; 5V4E; X-ray; 3.22 A; A/B/C/D/E/F/G/H=104-328. 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=104-328. DR PDB; 6G1E; X-ray; 1.88 A; A=104-156. DR PDB; 6N35; X-ray; 1.75 A; H/M=1-101. DR PDB; 6YT7; X-ray; 1.55 A; B=104-328. DR PDB; 7KWO; EM; 2.90 A; V=12-328. DR PDB; 7LUR; X-ray; 1.95 A; A/B=104-328. DR PDB; 7Q15; X-ray; 3.30 A; E/F=104-328. DR PDB; 7Q3P; X-ray; 2.10 A; A/B/C=104-328. DR PDB; 7WSO; EM; 3.03 A; B/K=120-371. DR PDB; 8DIN; X-ray; 2.50 A; A/B=112-328. DR PDB; 8DIR; X-ray; 2.30 A; A/B=112-328. DR PDB; 8DJ7; X-ray; 2.39 A; A/B=112-328. DR PDB; 8YP1; X-ray; 2.79 A; A/B/C/D=104-328. DR PDB; 9HIZ; X-ray; 2.90 A; A/B/C/D=119-327. DR PDB; 9JMJ; EM; 3.40 A; A/B/C=99-328. DR PDB; 9JMM; EM; 2.80 A; B=99-328. DR PDB; 9MVX; X-ray; 1.84 A; A/B=108-328. DR AlphaFoldDB; P01857; -. DR EMDB; EMD-0235; -. DR EMDB; EMD-0236; -. DR EMDB; EMD-0433; -. DR EMDB; EMD-0434; -. DR EMDB; EMD-10118; -. DR EMDB; EMD-10123; -. DR EMDB; EMD-10124; -. DR EMDB; EMD-10732; -. DR EMDB; EMD-10734; -. DR EMDB; EMD-10863; -. DR EMDB; EMD-11061; -. DR EMDB; EMD-11062; -. DR EMDB; EMD-11173; -. DR EMDB; EMD-11174; -. DR EMDB; EMD-11184; -. DR EMDB; EMD-11647; -. DR EMDB; EMD-11648; -. DR EMDB; EMD-12271; -. DR EMDB; EMD-12272; -. DR EMDB; EMD-12274; -. DR EMDB; EMD-12275; -. DR EMDB; EMD-12276; -. DR EMDB; EMD-12277; -. DR EMDB; EMD-12278; -. DR EMDB; EMD-12279; -. DR EMDB; EMD-12280; -. DR EMDB; EMD-12281; -. DR EMDB; EMD-12282; -. DR EMDB; EMD-12283; -. DR EMDB; EMD-12284; -. DR EMDB; EMD-12365; -. DR EMDB; EMD-12366; -. DR EMDB; EMD-12367; -. DR EMDB; EMD-12890; -. DR EMDB; EMD-12891; -. DR EMDB; EMD-13190; -. DR EMDB; EMD-13316; -. DR EMDB; EMD-13857; -. DR EMDB; EMD-13868; -. DR EMDB; EMD-13870; -. DR EMDB; EMD-13871; -. DR EMDB; EMD-13872; -. DR EMDB; EMD-13873; -. DR EMDB; EMD-13875; -. DR EMDB; EMD-14141; -. DR EMDB; EMD-14142; -. DR EMDB; EMD-14143; -. DR EMDB; EMD-14250; -. DR EMDB; EMD-14591; -. DR EMDB; EMD-14750; -. DR EMDB; EMD-15971; -. DR EMDB; EMD-16024; -. DR EMDB; EMD-16026; -. DR EMDB; EMD-16113; -. DR EMDB; EMD-16397; -. DR EMDB; EMD-16460; -. DR EMDB; EMD-16473; -. DR EMDB; EMD-16493; -. DR EMDB; EMD-16676; -. DR EMDB; EMD-16678; -. DR EMDB; EMD-16680; -. DR EMDB; EMD-16805; -. DR EMDB; EMD-16807; -. DR EMDB; EMD-17362; -. DR EMDB; EMD-17655; -. DR EMDB; EMD-17677; -. DR EMDB; EMD-17993; -. DR EMDB; EMD-18188; -. DR EMDB; EMD-18189; -. DR EMDB; EMD-18190; -. DR EMDB; EMD-18560; -. DR EMDB; EMD-18571; -. DR EMDB; EMD-19002; -. DR EMDB; EMD-19016; -. DR EMDB; EMD-19017; -. DR EMDB; EMD-19440; -. DR EMDB; EMD-19665; -. DR EMDB; EMD-20118; -. DR EMDB; EMD-20151; -. DR EMDB; EMD-20152; -. DR EMDB; EMD-20153; -. DR EMDB; EMD-20175; -. DR EMDB; EMD-20189; -. DR EMDB; EMD-20191; -. DR EMDB; EMD-20224; -. DR EMDB; EMD-20301; -. DR EMDB; EMD-20511; -. DR EMDB; EMD-20538; -. DR EMDB; EMD-20540; -. DR EMDB; EMD-20541; -. DR EMDB; EMD-20594; -. DR EMDB; EMD-20605; -. DR EMDB; EMD-20608; -. DR EMDB; EMD-20735; -. DR EMDB; EMD-20806; -. DR EMDB; EMD-20813; -. DR EMDB; EMD-20817; -. DR EMDB; EMD-20818; -. DR EMDB; EMD-20819; -. DR EMDB; EMD-20863; -. DR EMDB; EMD-21042; -. DR EMDB; EMD-21043; -. DR EMDB; EMD-21208; -. DR EMDB; EMD-21212; -. DR EMDB; EMD-21258; -. DR EMDB; EMD-21383; -. DR EMDB; EMD-21456; -. DR EMDB; EMD-21927; -. DR EMDB; EMD-21928; -. DR EMDB; EMD-22048; -. DR EMDB; EMD-22127; -. DR EMDB; EMD-22128; -. DR EMDB; EMD-22137; -. DR EMDB; EMD-22506; -. DR EMDB; EMD-22512; -. DR EMDB; EMD-22652; -. DR EMDB; EMD-22653; -. DR EMDB; EMD-22654; -. DR EMDB; EMD-22655; -. DR EMDB; EMD-22729; -. DR EMDB; EMD-22730; -. DR EMDB; EMD-22731; -. DR EMDB; EMD-22732; -. DR EMDB; EMD-22733; -. DR EMDB; EMD-22734; -. DR EMDB; EMD-22735; -. DR EMDB; EMD-22736; -. DR EMDB; EMD-22737; -. DR EMDB; EMD-22738; -. DR EMDB; EMD-22739; -. DR EMDB; EMD-22740; -. DR EMDB; EMD-22741; -. DR EMDB; EMD-22788; -. DR EMDB; EMD-22804; -. DR EMDB; EMD-22819; -. DR EMDB; EMD-22820; -. DR EMDB; EMD-22839; -. DR EMDB; EMD-22841; -. DR EMDB; EMD-22842; -. DR EMDB; EMD-22847; -. DR EMDB; EMD-22848; -. DR EMDB; EMD-22851; -. DR EMDB; EMD-22852; -. DR EMDB; EMD-22853; -. DR EMDB; EMD-22925; -. DR EMDB; EMD-22926; -. DR EMDB; EMD-23003; -. DR EMDB; EMD-23016; -. DR EMDB; EMD-23033; -. DR EMDB; EMD-23064; -. DR EMDB; EMD-23065; -. DR EMDB; EMD-23092; -. DR EMDB; EMD-23093; -. DR EMDB; EMD-23098; -. DR EMDB; EMD-23125; -. DR EMDB; EMD-23126; -. DR EMDB; EMD-23127; -. DR EMDB; EMD-23246; -. DR EMDB; EMD-23248; -. DR EMDB; EMD-23252; -. DR EMDB; EMD-23253; -. DR EMDB; EMD-23254; -. DR EMDB; EMD-23277; -. DR EMDB; EMD-23279; -. DR EMDB; EMD-23312; -. DR EMDB; EMD-23411; -. DR EMDB; EMD-23412; -. DR EMDB; EMD-23424; -. DR EMDB; EMD-23462; -. DR EMDB; EMD-23463; -. DR EMDB; EMD-23464; -. DR EMDB; EMD-23465; -. DR EMDB; EMD-23490; -. DR EMDB; EMD-23498; -. DR EMDB; EMD-23499; -. DR EMDB; EMD-23506; -. DR EMDB; EMD-23521; -. DR EMDB; EMD-23564; -. DR EMDB; EMD-23565; -. DR EMDB; EMD-23571; -. DR EMDB; EMD-23572; -. DR EMDB; EMD-23589; -. DR EMDB; EMD-23603; -. DR EMDB; EMD-23625; -. DR EMDB; EMD-23640; -. DR EMDB; EMD-23662; -. DR EMDB; EMD-23693; -. DR EMDB; EMD-23694; -. DR EMDB; EMD-23695; -. DR EMDB; EMD-23696; -. DR EMDB; EMD-23697; -. DR EMDB; EMD-23708; -. DR EMDB; EMD-23710; -. DR EMDB; EMD-23711; -. DR EMDB; EMD-23712; -. DR EMDB; EMD-23713; -. DR EMDB; EMD-23715; -. DR EMDB; EMD-23719; -. DR EMDB; EMD-23914; -. DR EMDB; EMD-23915; -. DR EMDB; EMD-23918; -. DR EMDB; EMD-23933; -. DR EMDB; EMD-23979; -. DR EMDB; EMD-23980; -. DR EMDB; EMD-24060; -. DR EMDB; EMD-24061; -. DR EMDB; EMD-24062; -. DR EMDB; EMD-24063; -. DR EMDB; EMD-24064; -. DR EMDB; EMD-24071; -. DR EMDB; EMD-24072; -. DR EMDB; EMD-24128; -. DR EMDB; EMD-24192; -. DR EMDB; EMD-24193; -. DR EMDB; EMD-24318; -. DR EMDB; EMD-24319; -. DR EMDB; EMD-24320; -. DR EMDB; EMD-24362; -. DR EMDB; EMD-24504; -. DR EMDB; EMD-24623; -. DR EMDB; EMD-24628; -. DR EMDB; EMD-24675; -. DR EMDB; EMD-24676; -. DR EMDB; EMD-24708; -. DR EMDB; EMD-24786; -. DR EMDB; EMD-24787; -. DR EMDB; EMD-24788; -. DR EMDB; EMD-24868; -. DR EMDB; EMD-24875; -. DR EMDB; EMD-25008; -. DR EMDB; EMD-25045; -. DR EMDB; EMD-25103; -. DR EMDB; EMD-25105; -. DR EMDB; EMD-25163; -. DR EMDB; EMD-25171; -. DR EMDB; EMD-25172; -. DR EMDB; EMD-25173; -. DR EMDB; EMD-25174; -. DR EMDB; EMD-25175; -. DR EMDB; EMD-25176; -. DR EMDB; EMD-25177; -. DR EMDB; EMD-25200; -. DR EMDB; EMD-25209; -. DR EMDB; EMD-25210; -. DR EMDB; EMD-25427; -. DR EMDB; EMD-25476; -. DR EMDB; EMD-25477; -. DR EMDB; EMD-25478; -. DR EMDB; EMD-25583; -. DR EMDB; EMD-25585; -. DR EMDB; EMD-25685; -. DR EMDB; EMD-25686; -. DR EMDB; EMD-25687; -. DR EMDB; EMD-25688; -. DR EMDB; EMD-25699; -. DR EMDB; EMD-25730; -. DR EMDB; EMD-25732; -. DR EMDB; EMD-25735; -. DR EMDB; EMD-25736; -. DR EMDB; EMD-25763; -. DR EMDB; EMD-25767; -. DR EMDB; EMD-25797; -. DR EMDB; EMD-25806; -. DR EMDB; EMD-25807; -. DR EMDB; EMD-25814; -. DR EMDB; EMD-25815; -. DR EMDB; EMD-25834; -. DR EMDB; EMD-25835; -. DR EMDB; EMD-25836; -. DR EMDB; EMD-25929; -. DR EMDB; EMD-25982; -. DR EMDB; EMD-26054; -. DR EMDB; EMD-26057; -. DR EMDB; EMD-26135; -. DR EMDB; EMD-26195; -. DR EMDB; EMD-26256; -. DR EMDB; EMD-26397; -. DR EMDB; EMD-26398; -. DR EMDB; EMD-26399; -. DR EMDB; EMD-26400; -. DR EMDB; EMD-26429; -. DR EMDB; EMD-26430; -. DR EMDB; EMD-26431; -. DR EMDB; EMD-26443; -. DR EMDB; EMD-26458; -. DR EMDB; EMD-26594; -. DR EMDB; EMD-26608; -. DR EMDB; EMD-26648; -. DR EMDB; EMD-26704; -. DR EMDB; EMD-26738; -. DR EMDB; EMD-27024; -. DR EMDB; EMD-27103; -. DR EMDB; EMD-27177; -. DR EMDB; EMD-27194; -. DR EMDB; EMD-27195; -. DR EMDB; EMD-27202; -. DR EMDB; EMD-27222; -. DR EMDB; EMD-27254; -. DR EMDB; EMD-27255; -. DR EMDB; EMD-27440; -. DR EMDB; EMD-27441; -. DR EMDB; EMD-27443; -. DR EMDB; EMD-27511; -. DR EMDB; EMD-27512; -. DR EMDB; EMD-27513; -. DR EMDB; EMD-27514; -. DR EMDB; EMD-27518; -. DR EMDB; EMD-27525; -. DR EMDB; EMD-27526; -. DR EMDB; EMD-27538; -. DR EMDB; EMD-27596; -. DR EMDB; EMD-27735; -. DR EMDB; EMD-27749; -. DR EMDB; EMD-27750; -. DR EMDB; EMD-27775; -. DR EMDB; EMD-27785; -. DR EMDB; EMD-27786; -. DR EMDB; EMD-27787; -. DR EMDB; EMD-27788; -. DR EMDB; EMD-27789; -. DR EMDB; EMD-27808; -. DR EMDB; EMD-27846; -. DR EMDB; EMD-27920; -. DR EMDB; EMD-27921; -. DR EMDB; EMD-27939; -. DR EMDB; EMD-27995; -. DR EMDB; EMD-28135; -. DR EMDB; EMD-28192; -. DR EMDB; EMD-28196; -. DR EMDB; EMD-28228; -. DR EMDB; EMD-28555; -. DR EMDB; EMD-28617; -. DR EMDB; EMD-28618; -. DR EMDB; EMD-28619; -. DR EMDB; EMD-28833; -. DR EMDB; EMD-28881; -. DR EMDB; EMD-28882; -. DR EMDB; EMD-28883; -. DR EMDB; EMD-28884; -. DR EMDB; EMD-28885; -. DR EMDB; EMD-29077; -. DR EMDB; EMD-29209; -. DR EMDB; EMD-29264; -. DR EMDB; EMD-29288; -. DR EMDB; EMD-29419; -. DR EMDB; EMD-29686; -. DR EMDB; EMD-29704; -. DR EMDB; EMD-29705; -. DR EMDB; EMD-29706; -. DR EMDB; EMD-29707; -. DR EMDB; EMD-29708; -. DR EMDB; EMD-29709; -. DR EMDB; EMD-29710; -. DR EMDB; EMD-29711; -. DR EMDB; EMD-29712; -. DR EMDB; EMD-29725; -. DR EMDB; EMD-29731; -. DR EMDB; EMD-29738; -. DR EMDB; EMD-29783; -. DR EMDB; EMD-29907; -. DR EMDB; EMD-29908; -. DR EMDB; EMD-29909; -. DR EMDB; EMD-29950; -. DR EMDB; EMD-30326; -. DR EMDB; EMD-30331; -. DR EMDB; EMD-30332; -. DR EMDB; EMD-30333; -. DR EMDB; EMD-30337; -. DR EMDB; EMD-30374; -. DR EMDB; EMD-30484; -. DR EMDB; EMD-30529; -. DR EMDB; EMD-30530; -. DR EMDB; EMD-30531; -. DR EMDB; EMD-30982; -. DR EMDB; EMD-30983; -. DR EMDB; EMD-30993; -. DR EMDB; EMD-30994; -. DR EMDB; EMD-31014; -. DR EMDB; EMD-31017; -. DR EMDB; EMD-31033; -. DR EMDB; EMD-31034; -. DR EMDB; EMD-31035; -. DR EMDB; EMD-31036; -. DR EMDB; EMD-31209; -. DR EMDB; EMD-31210; -. DR EMDB; EMD-31374; -. DR EMDB; EMD-31376; -. DR EMDB; EMD-31377; -. DR EMDB; EMD-31378; -. DR EMDB; EMD-31380; -. DR EMDB; EMD-31390; -. DR EMDB; EMD-31391; -. DR EMDB; EMD-31434; -. DR EMDB; EMD-31444; -. DR EMDB; EMD-31625; -. DR EMDB; EMD-31637; -. DR EMDB; EMD-31639; -. DR EMDB; EMD-31681; -. DR EMDB; EMD-31683; -. DR EMDB; EMD-31725; -. DR EMDB; EMD-31726; -. DR EMDB; EMD-31743; -. DR EMDB; EMD-31744; -. DR EMDB; EMD-32421; -. DR EMDB; EMD-32422; -. DR EMDB; EMD-32423; -. DR EMDB; EMD-32427; -. DR EMDB; EMD-32429; -. DR EMDB; EMD-32497; -. DR EMDB; EMD-32498; -. DR EMDB; EMD-32499; -. DR EMDB; EMD-32552; -. DR EMDB; EMD-32553; -. DR EMDB; EMD-32554; -. DR EMDB; EMD-32594; -. DR EMDB; EMD-32595; -. DR EMDB; EMD-32596; -. DR EMDB; EMD-32638; -. DR EMDB; EMD-32639; -. DR EMDB; EMD-32641; -. DR EMDB; EMD-32646; -. DR EMDB; EMD-32647; -. DR EMDB; EMD-32648; -. DR EMDB; EMD-32651; -. DR EMDB; EMD-32718; -. DR EMDB; EMD-32719; -. DR EMDB; EMD-32728; -. DR EMDB; EMD-32762; -. DR EMDB; EMD-32832; -. DR EMDB; EMD-32944; -. DR EMDB; EMD-32958; -. DR EMDB; EMD-32959; -. DR EMDB; EMD-32961; -. DR EMDB; EMD-32962; -. DR EMDB; EMD-32963; -. DR EMDB; EMD-33023; -. DR EMDB; EMD-33024; -. DR EMDB; EMD-33045; -. DR EMDB; EMD-33059; -. DR EMDB; EMD-33060; -. DR EMDB; EMD-33062; -. DR EMDB; EMD-33064; -. DR EMDB; EMD-33065; -. DR EMDB; EMD-33066; -. DR EMDB; EMD-33067; -. DR EMDB; EMD-33068; -. DR EMDB; EMD-33123; -. DR EMDB; EMD-33124; -. DR EMDB; EMD-33125; -. DR EMDB; EMD-33130; -. DR EMDB; EMD-33140; -. DR EMDB; EMD-33150; -. DR EMDB; EMD-33151; -. DR EMDB; EMD-33191; -. DR EMDB; EMD-33345; -. DR EMDB; EMD-33506; -. DR EMDB; EMD-33643; -. DR EMDB; EMD-33644; -. DR EMDB; EMD-33650; -. DR EMDB; EMD-33651; -. DR EMDB; EMD-33718; -. DR EMDB; EMD-33743; -. DR EMDB; EMD-33744; -. DR EMDB; EMD-33748; -. DR EMDB; EMD-33760; -. DR EMDB; EMD-33764; -. DR EMDB; EMD-33766; -. DR EMDB; EMD-33772; -. DR EMDB; EMD-33821; -. DR EMDB; EMD-33823; -. DR EMDB; EMD-33824; -. DR EMDB; EMD-33825; -. DR EMDB; EMD-33826; -. DR EMDB; EMD-33827; -. DR EMDB; EMD-33828; -. DR EMDB; EMD-33829; -. DR EMDB; EMD-33830; -. DR EMDB; EMD-34063; -. DR EMDB; EMD-34164; -. DR EMDB; EMD-34190; -. DR EMDB; EMD-34192; -. DR EMDB; EMD-34193; -. DR EMDB; EMD-34194; -. DR EMDB; EMD-34649; -. DR EMDB; EMD-34650; -. DR EMDB; EMD-34651; -. DR EMDB; EMD-34652; -. DR EMDB; EMD-34653; -. DR EMDB; EMD-34655; -. DR EMDB; EMD-34656; -. DR EMDB; EMD-34657; -. DR EMDB; EMD-34658; -. DR EMDB; EMD-34741; -. DR EMDB; EMD-34742; -. DR EMDB; EMD-34806; -. DR EMDB; EMD-34807; -. DR EMDB; EMD-34808; -. DR EMDB; EMD-34817; -. DR EMDB; EMD-34818; -. DR EMDB; EMD-34819; -. DR EMDB; EMD-34871; -. DR EMDB; EMD-34872; -. DR EMDB; EMD-34874; -. DR EMDB; EMD-34928; -. DR EMDB; EMD-34931; -. DR EMDB; EMD-34940; -. DR EMDB; EMD-34944; -. DR EMDB; EMD-34945; -. DR EMDB; EMD-34946; -. DR EMDB; EMD-35063; -. DR EMDB; EMD-35064; -. DR EMDB; EMD-35155; -. DR EMDB; EMD-35171; -. DR EMDB; EMD-35172; -. DR EMDB; EMD-35526; -. DR EMDB; EMD-35627; -. DR EMDB; EMD-35930; -. DR EMDB; EMD-35945; -. DR EMDB; EMD-36003; -. DR EMDB; EMD-36258; -. DR EMDB; EMD-36262; -. DR EMDB; EMD-36335; -. DR EMDB; EMD-36336; -. DR EMDB; EMD-36337; -. DR EMDB; EMD-36338; -. DR EMDB; EMD-36641; -. DR EMDB; EMD-36649; -. DR EMDB; EMD-36849; -. DR EMDB; EMD-36905; -. DR EMDB; EMD-36906; -. DR EMDB; EMD-37203; -. DR EMDB; EMD-37210; -. DR EMDB; EMD-37471; -. DR EMDB; EMD-37670; -. DR EMDB; EMD-37673; -. DR EMDB; EMD-37678; -. DR EMDB; EMD-37725; -. DR EMDB; EMD-37726; -. DR EMDB; EMD-37756; -. DR EMDB; EMD-37849; -. DR EMDB; EMD-38372; -. DR EMDB; EMD-38613; -. DR EMDB; EMD-38617; -. DR EMDB; EMD-38620; -. DR EMDB; EMD-38621; -. DR EMDB; EMD-38706; -. DR EMDB; EMD-38707; -. DR EMDB; EMD-38708; -. DR EMDB; EMD-38983; -. DR EMDB; EMD-39553; -. DR EMDB; EMD-39645; -. DR EMDB; EMD-39670; -. DR EMDB; EMD-39762; -. DR EMDB; EMD-39805; -. DR EMDB; EMD-39806; -. DR EMDB; EMD-39900; -. DR EMDB; EMD-39916; -. DR EMDB; EMD-39917; -. DR EMDB; EMD-39918; -. DR EMDB; EMD-39919; -. DR EMDB; EMD-39920; -. DR EMDB; EMD-39921; -. DR EMDB; EMD-39922; -. DR EMDB; EMD-39924; -. DR EMDB; EMD-40088; -. DR EMDB; EMD-40240; -. DR EMDB; EMD-40274; -. DR EMDB; EMD-40589; -. DR EMDB; EMD-40590; -. DR EMDB; EMD-40591; -. DR EMDB; EMD-40594; -. DR EMDB; EMD-40598; -. DR EMDB; EMD-40825; -. DR EMDB; EMD-41072; -. DR EMDB; EMD-41156; -. DR EMDB; EMD-41179; -. DR EMDB; EMD-41245; -. DR EMDB; EMD-41247; -. DR EMDB; EMD-41255; -. DR EMDB; EMD-41275; -. DR EMDB; EMD-41305; -. DR EMDB; EMD-41306; -. DR EMDB; EMD-41383; -. DR EMDB; EMD-41384; -. DR EMDB; EMD-41385; -. DR EMDB; EMD-41386; -. DR EMDB; EMD-41387; -. DR EMDB; EMD-41388; -. DR EMDB; EMD-41389; -. DR EMDB; EMD-41390; -. DR EMDB; EMD-41391; -. DR EMDB; EMD-41392; -. DR EMDB; EMD-41393; -. DR EMDB; EMD-41394; -. DR EMDB; EMD-41395; -. DR EMDB; EMD-41396; -. DR EMDB; EMD-41398; -. DR EMDB; EMD-41417; -. DR EMDB; EMD-41418; -. DR EMDB; EMD-41461; -. DR EMDB; EMD-41495; -. DR EMDB; EMD-41496; -. DR EMDB; EMD-41505; -. DR EMDB; EMD-41506; -. DR EMDB; EMD-41613; -. DR EMDB; EMD-41703; -. DR EMDB; EMD-41774; -. DR EMDB; EMD-41821; -. DR EMDB; EMD-41822; -. DR EMDB; EMD-41845; -. DR EMDB; EMD-41874; -. DR EMDB; EMD-41899; -. DR EMDB; EMD-42041; -. DR EMDB; EMD-42149; -. DR EMDB; EMD-42151; -. DR EMDB; EMD-42363; -. DR EMDB; EMD-42364; -. DR EMDB; EMD-42365; -. DR EMDB; EMD-42366; -. DR EMDB; EMD-42377; -. DR EMDB; EMD-42839; -. DR EMDB; EMD-43047; -. DR EMDB; EMD-43071; -. DR EMDB; EMD-43139; -. DR EMDB; EMD-43148; -. DR EMDB; EMD-43169; -. DR EMDB; EMD-43170; -. DR EMDB; EMD-43171; -. DR EMDB; EMD-43172; -. DR EMDB; EMD-43200; -. DR EMDB; EMD-43201; -. DR EMDB; EMD-43202; -. DR EMDB; EMD-43203; -. DR EMDB; EMD-43212; -. DR EMDB; EMD-43213; -. DR EMDB; EMD-43214; -. DR EMDB; EMD-43215; -. DR EMDB; EMD-43216; -. DR EMDB; EMD-43217; -. DR EMDB; EMD-43218; -. DR EMDB; EMD-43219; -. DR EMDB; EMD-43220; -. DR EMDB; EMD-43221; -. DR EMDB; EMD-43231; -. DR EMDB; EMD-43232; -. DR EMDB; EMD-43255; -. DR EMDB; EMD-43315; -. DR EMDB; EMD-43407; -. DR EMDB; EMD-43439; -. DR EMDB; EMD-43478; -. DR EMDB; EMD-43479; -. DR EMDB; EMD-43480; -. DR EMDB; EMD-43499; -. DR EMDB; EMD-43507; -. DR EMDB; EMD-43529; -. DR EMDB; EMD-43534; -. DR EMDB; EMD-43536; -. DR EMDB; EMD-43538; -. DR EMDB; EMD-43539; -. DR EMDB; EMD-43540; -. DR EMDB; EMD-43541; -. DR EMDB; EMD-43545; -. DR EMDB; EMD-43551; -. DR EMDB; EMD-43552; -. DR EMDB; EMD-43553; -. DR EMDB; EMD-43604; -. DR EMDB; EMD-43667; -. DR EMDB; EMD-43672; -. DR EMDB; EMD-43842; -. DR EMDB; EMD-43879; -. DR EMDB; EMD-43880; -. DR EMDB; EMD-43881; -. DR EMDB; EMD-43980; -. DR EMDB; EMD-44064; -. DR EMDB; EMD-44143; -. DR EMDB; EMD-44246; -. DR EMDB; EMD-44305; -. DR EMDB; EMD-44451; -. DR EMDB; EMD-44452; -. DR EMDB; EMD-44484; -. DR EMDB; EMD-44595; -. DR EMDB; EMD-44627; -. DR EMDB; EMD-44628; -. DR EMDB; EMD-44629; -. DR EMDB; EMD-44734; -. DR EMDB; EMD-4520; -. DR EMDB; EMD-4521; -. DR EMDB; EMD-45412; -. DR EMDB; EMD-45443; -. DR EMDB; EMD-45444; -. DR EMDB; EMD-45530; -. DR EMDB; EMD-45624; -. DR EMDB; EMD-45728; -. DR EMDB; EMD-45749; -. DR EMDB; EMD-46041; -. DR EMDB; EMD-46042; -. DR EMDB; EMD-46044; -. DR EMDB; EMD-46045; -. DR EMDB; EMD-46046; -. DR EMDB; EMD-46478; -. DR EMDB; EMD-46532; -. DR EMDB; EMD-46533; -. DR EMDB; EMD-46534; -. DR EMDB; EMD-46602; -. DR EMDB; EMD-46605; -. DR EMDB; EMD-46606; -. DR EMDB; EMD-46613; -. DR EMDB; EMD-46614; -. DR EMDB; EMD-46653; -. DR EMDB; EMD-46655; -. DR EMDB; EMD-46670; -. DR EMDB; EMD-46760; -. DR EMDB; EMD-46884; -. DR EMDB; EMD-46914; -. DR EMDB; EMD-47007; -. DR EMDB; EMD-47008; -. DR EMDB; EMD-47009; -. DR EMDB; EMD-47013; -. DR EMDB; EMD-47014; -. DR EMDB; EMD-47015; -. DR EMDB; EMD-47017; -. DR EMDB; EMD-47040; -. DR EMDB; EMD-47042; -. DR EMDB; EMD-47104; -. DR EMDB; EMD-47134; -. DR EMDB; EMD-47153; -. DR EMDB; EMD-47324; -. DR EMDB; EMD-47333; -. DR EMDB; EMD-47487; -. DR EMDB; EMD-47571; -. DR EMDB; EMD-47928; -. DR EMDB; EMD-47950; -. DR EMDB; EMD-48120; -. DR EMDB; EMD-48221; -. DR EMDB; EMD-48275; -. DR EMDB; EMD-48284; -. DR EMDB; EMD-48303; -. DR EMDB; EMD-48306; -. DR EMDB; EMD-48331; -. DR EMDB; EMD-48344; -. DR EMDB; EMD-48345; -. DR EMDB; EMD-48346; -. DR EMDB; EMD-48393; -. DR EMDB; EMD-48404; -. DR EMDB; EMD-48419; -. DR EMDB; EMD-48507; -. DR EMDB; EMD-48537; -. DR EMDB; EMD-48575; -. DR EMDB; EMD-48591; -. DR EMDB; EMD-48921; -. DR EMDB; EMD-48922; -. DR EMDB; EMD-49043; -. DR EMDB; EMD-49059; -. DR EMDB; EMD-49127; -. DR EMDB; EMD-49130; -. DR EMDB; EMD-49236; -. DR EMDB; EMD-49238; -. DR EMDB; EMD-49239; -. DR EMDB; EMD-49240; -. DR EMDB; EMD-49241; -. DR EMDB; EMD-49242; -. DR EMDB; EMD-49361; -. DR EMDB; EMD-49362; -. DR EMDB; EMD-49463; -. DR EMDB; EMD-49475; -. DR EMDB; EMD-49476; -. DR EMDB; EMD-49477; -. DR EMDB; EMD-49799; -. DR EMDB; EMD-49835; -. DR EMDB; EMD-49896; -. DR EMDB; EMD-50020; -. DR EMDB; EMD-50092; -. DR EMDB; EMD-50609; -. DR EMDB; EMD-50610; -. DR EMDB; EMD-50643; -. DR EMDB; EMD-50742; -. DR EMDB; EMD-51554; -. DR EMDB; EMD-51901; -. DR EMDB; EMD-51988; -. DR EMDB; EMD-52012; -. DR EMDB; EMD-53299; -. DR EMDB; EMD-53300; -. DR EMDB; EMD-53474; -. DR EMDB; EMD-53994; -. DR EMDB; EMD-53995; -. DR EMDB; EMD-53996; -. DR EMDB; EMD-53997; -. DR EMDB; EMD-53998; -. DR EMDB; EMD-53999; -. DR EMDB; EMD-54000; -. DR EMDB; EMD-54001; -. DR EMDB; EMD-54002; -. DR EMDB; EMD-54003; -. DR EMDB; EMD-54004; -. DR EMDB; EMD-54005; -. DR EMDB; EMD-55517; -. DR EMDB; EMD-55518; -. DR EMDB; EMD-55620; -. DR EMDB; EMD-60046; -. DR EMDB; EMD-60099; -. DR EMDB; EMD-60100; -. DR EMDB; EMD-60101; -. DR EMDB; EMD-60103; -. DR EMDB; EMD-60104; -. DR EMDB; EMD-60105; -. DR EMDB; EMD-60106; -. DR EMDB; EMD-60107; -. DR EMDB; EMD-60108; -. DR EMDB; EMD-60109; -. DR EMDB; EMD-60110; -. DR EMDB; EMD-60111; -. DR EMDB; EMD-60112; -. DR EMDB; EMD-60525; -. DR EMDB; EMD-60578; -. DR EMDB; EMD-60579; -. DR EMDB; EMD-60583; -. DR EMDB; EMD-60821; -. DR EMDB; EMD-60929; -. DR EMDB; EMD-60966; -. DR EMDB; EMD-60978; -. DR EMDB; EMD-60993; -. DR EMDB; EMD-60997; -. DR EMDB; EMD-61004; -. DR EMDB; EMD-61026; -. DR EMDB; EMD-61049; -. DR EMDB; EMD-61167; -. DR EMDB; EMD-61285; -. DR EMDB; EMD-61446; -. DR EMDB; EMD-61447; -. DR EMDB; EMD-61569; -. DR EMDB; EMD-61604; -. DR EMDB; EMD-61606; -. DR EMDB; EMD-61766; -. DR EMDB; EMD-61788; -. DR EMDB; EMD-61939; -. DR EMDB; EMD-62608; -. DR EMDB; EMD-62622; -. DR EMDB; EMD-62750; -. DR EMDB; EMD-62751; -. DR EMDB; EMD-62752; -. DR EMDB; EMD-62753; -. DR EMDB; EMD-62911; -. DR EMDB; EMD-63000; -. DR EMDB; EMD-63002; -. DR EMDB; EMD-63198; -. DR EMDB; EMD-63219; -. DR EMDB; EMD-63220; -. DR EMDB; EMD-63246; -. DR EMDB; EMD-63247; -. DR EMDB; EMD-63248; -. DR EMDB; EMD-63352; -. DR EMDB; EMD-63418; -. DR EMDB; EMD-63488; -. DR EMDB; EMD-63489; -. DR EMDB; EMD-63500; -. DR EMDB; EMD-63502; -. DR EMDB; EMD-63503; -. DR EMDB; EMD-63505; -. DR EMDB; EMD-63513; -. DR EMDB; EMD-63514; -. DR EMDB; EMD-63543; -. DR EMDB; EMD-63745; -. DR EMDB; EMD-63748; -. DR EMDB; EMD-63762; -. DR EMDB; EMD-63764; -. DR EMDB; EMD-63948; -. DR EMDB; EMD-63949; -. DR EMDB; EMD-63960; -. DR EMDB; EMD-63997; -. DR EMDB; EMD-63999; -. DR EMDB; EMD-64014; -. DR EMDB; EMD-64142; -. DR EMDB; EMD-64581; -. DR EMDB; EMD-64582; -. DR EMDB; EMD-64753; -. DR EMDB; EMD-64805; -. DR EMDB; EMD-65166; -. DR EMDB; EMD-65168; -. DR EMDB; EMD-66420; -. DR EMDB; EMD-66435; -. DR EMDB; EMD-66460; -. DR EMDB; EMD-68593; -. DR EMDB; EMD-70019; -. DR EMDB; EMD-70020; -. DR EMDB; EMD-70021; -. DR EMDB; EMD-70123; -. DR EMDB; EMD-70127; -. DR EMDB; EMD-70440; -. DR EMDB; EMD-70441; -. DR EMDB; EMD-70442; -. DR EMDB; EMD-70469; -. DR EMDB; EMD-70471; -. DR EMDB; EMD-70475; -. DR EMDB; EMD-70476; -. DR EMDB; EMD-70507; -. DR EMDB; EMD-70508; -. DR EMDB; EMD-70677; -. DR EMDB; EMD-70931; -. DR EMDB; EMD-7107; -. DR EMDB; EMD-7108; -. DR EMDB; EMD-71445; -. DR EMDB; EMD-71446; -. DR EMDB; EMD-71497; -. DR EMDB; EMD-71531; -. DR EMDB; EMD-71532; -. DR EMDB; EMD-71559; -. DR EMDB; EMD-71728; -. DR EMDB; EMD-71899; -. DR EMDB; EMD-72322; -. DR EMDB; EMD-72906; -. DR EMDB; EMD-73228; -. DR EMDB; EMD-73245; -. DR EMDB; EMD-73260; -. DR EMDB; EMD-73292; -. DR EMDB; EMD-73306; -. DR EMDB; EMD-73342; -. DR EMDB; EMD-7344; -. DR EMDB; EMD-73949; -. DR EMDB; EMD-7459; -. DR EMDB; EMD-7460; -. DR EMDB; EMD-74739; -. DR EMDB; EMD-74907; -. DR EMDB; EMD-75151; -. DR EMDB; EMD-7516; -. DR EMDB; EMD-7568; -. DR EMDB; EMD-75887; -. DR EMDB; EMD-75889; -. DR EMDB; EMD-75891; -. DR EMDB; EMD-75892; -. DR EMDB; EMD-75893; -. DR EMDB; EMD-76027; -. DR EMDB; EMD-76031; -. DR EMDB; EMD-76032; -. DR EMDB; EMD-76035; -. DR EMDB; EMD-76037; -. DR EMDB; EMD-76038; -. DR EMDB; EMD-7859; -. DR EMDB; EMD-7860; -. DR EMDB; EMD-7861; -. DR EMDB; EMD-7875; -. DR EMDB; EMD-7876; -. DR EMDB; EMD-8181; -. DR EMDB; EMD-8182; -. DR EMDB; EMD-8302; -. DR EMDB; EMD-8407; -. DR EMDB; EMD-8573; -. DR EMDB; EMD-8643; -. DR EMDB; EMD-8644; -. DR EMDB; EMD-8713; -. DR EMDB; EMD-8716; -. DR EMDB; EMD-8717; -. DR EMDB; EMD-8956; -. DR EMDB; EMD-8977; -. DR EMDB; EMD-8981; -. DR EMDB; EMD-9030; -. DR EMDB; EMD-9038; -. DR EMDB; EMD-9062; -. DR EMDB; EMD-9135; -. DR EMDB; EMD-9139; -. DR EMDB; EMD-9189; -. DR EMDB; EMD-9359; -. DR EMDB; EMD-9542; -. DR EMDB; EMD-9811; -. DR EMDB; EMD-9812; -. DR MDposit; P01857; -. DR MDRepo; 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 CORUM; P01857; -. DR DIP; DIP-29187N; -. DR FunCoup; P01857; 479. DR IntAct; P01857; 209. DR MINT; P01857; -. DR NDEx; IQUERY-CP-IGHG1; 4 NDEx IQuery Curated Pathways. DR BindingDB; 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 DrugCentral; P01857; -. DR IMGT_GENE-DB; IGHG1; -. DR CarbonylDB; P01857; -. DR GlyConnect; P01857; 115 N-Linked glycans (2 sites). DR GlyCosmos; P01857; 1 site, 170 glycans. DR GlyGen; P01857; 2 sites, 219 N-linked glycans (2 sites), 1 N-linked;o-linked glycan (1 site), 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 REPRODUCTION-2DPAGE; P01857; -. DR CPTAC; CPTAC-669; -. DR jPOST; P01857; -. DR MassIVE; P01857; -. DR PRIDE; P01857; -. DR ProteomicsDB; 51494; -. DR Pumba; P01857; -. DR ABCD; P01857; 7 sequenced antibodies. DR Ensembl; ENST00000390548.6; ENSP00000374990.2; ENSG00000211896.7. [P01857-2] DR Ensembl; ENST00000390549.6; ENSP00000374991.2; ENSG00000211896.7. [P01857-1] DR Ensembl; ENST00000631466.1; ENSP00000488387.1; ENSG00000277633.5. [P01857-1] DR Ensembl; ENST00000631539.1; ENSP00000487867.1; ENSG00000277633.5. [P01857-2] DR UCSC; uc059gdc.1; human. [P01857-2] DR AGR; HGNC:5525; -. 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 OpenTargets; ENSG00000211896; -. DR Orphanet; 67038; B-cell chronic lymphocytic leukemia. DR Orphanet; 536; Systemic lupus erythematosus. DR VEuPathDB; HostDB:ENSG00000211896; -. DR GeneTree; ENSGT00940000162793; -. DR HOGENOM; CLU_030625_0_0_1; -. DR InParanoid; P01857; -. DR OMA; DENCAEA; -. DR OrthoDB; 8694217at2759; -. DR PAN-GO; P01857; 5 GO annotations based on evolutionary models. 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 Agora; ENSG00000211896; -. 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 cell types or tissues. DR ExpressionAtlas; P01857; baseline and differential. DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; 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; NAS:UniProtKB. 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:0019731; P:antibacterial humoral response; IBA:GO_Central. DR GO; GO:0001788; P:antibody-dependent cellular cytotoxicity; IDA:UniProtKB. DR GO; GO:0050853; P:B cell receptor signaling pathway; NAS:ComplexPortal. DR GO; GO:0006958; P:complement activation, classical pathway; IBA:GO_Central. DR GO; GO:0097278; P:complement-dependent cytotoxicity; IDA:UniProtKB. DR CDD; cd21817; IgC1_CH1_IgEG; 1. DR CDD; cd05768; IgC1_CH3_IgAGD_CH4_IgAEM; 1. DR FunFam; 2.60.40.10:FF:000463; Immunoglobulin heavy constant gamma 1; 1. DR FunFam; 2.60.40.10:FF:001129; Immunoglobulin heavy constant gamma 1; 1. DR FunFam; 2.60.40.10:FF:001540; Immunoglobulin heavy constant gamma 1; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 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 InterPro; IPR050380; Immune_Resp_Modulators. DR PANTHER; PTHR23411; TAPASIN; 1. DR Pfam; PF07654; C1-set; 3. DR SMART; SM00407; IGc1; 3. DR SUPFAM; SSF48726; Immunoglobulin; 3. DR PROSITE; PS50835; IG_LIKE; 3. DR PROSITE; PS00290; IG_MHC; 2. 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 PDBsum; 7Q15; -. DR PDBsum; 7Q3P; -. DR PDBsum; 7WSO; -. DR PDBsum; 8DIN; -. DR PDBsum; 8DIR; -. DR PDBsum; 8DJ7; -. DR PDBsum; 8YP1; -. DR PDBsum; 9HIZ; -. DR PDBsum; 9JMJ; -. DR PDBsum; 9JMM; -. DR PDBsum; 9MVX; -. PE 1: Evidence at protein level; KW 3D-structure; Adaptive immunity; Alternative splicing; Cell membrane; KW Chromosomal rearrangement; Direct protein sequencing; Disulfide bond; KW Glycoprotein; Immunity; Immunoglobulin; Immunoglobulin domain; Membrane; KW Proteomics identification; Reference proteome; Secreted; Transmembrane; KW Transmembrane helix. FT CHAIN <1..399 FT /note="Immunoglobulin heavy constant gamma 1" FT /id="PRO_0000153578" FT TOPO_DOM 1..350 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 351..371 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 372..399 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" 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 /evidence="ECO:0000305|PubMed:15572068" FT REGION 1..21 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 99..110 FT /note="Hinge" FT REGION 115..224 FT /note="CH2; part of fragment crystallizable (Fc); Fc FT receptor binding" FT /evidence="ECO:0000269|PubMed:10917521, FT ECO:0000269|PubMed:25561553, ECO:0000305|PubMed:15572068" FT REGION 225..328 FT /note="CH3; part of fragment crystallizable (Fc)" FT /evidence="ECO:0000305|PubMed:15572068" FT CARBOHYD 180 FT /note="N-linked ([alpha-Neu5Ac-(2->6)-beta-D-Gal-(1->4)- FT beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)]-[beta-D-Gal- FT (1->4)-beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man- FT (1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc) (complex) FT asparagine" FT /evidence="ECO:0000305|PubMed:29133956, FT ECO:0000305|PubMed:29445378, ECO:0000305|PubMed:36529104, FT ECO:0000305|PubMed:39983994" FT CARBOHYD 180 FT /note="N-linked ([beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)- FT alpha-D-Man-(1->3)]-[beta-D-Gal-(1->4)-beta-D-GlcNAc- FT (1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc- FT (1->4)-beta-D-GlcNAc) (complex) asparagine" FT /evidence="ECO:0000269|PubMed:22184099, FT ECO:0000269|PubMed:26140596, ECO:0000269|PubMed:29133956, FT ECO:0000269|PubMed:29445378, ECO:0000269|PubMed:36529104, FT ECO:0000269|PubMed:39983994" FT CARBOHYD 180 FT /note="N-linked (alpha-Neu5Ac-(2->6)-beta-D-Gal-(1->4)- FT beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-Neu5Ac- FT (2->6)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)-alpha-D-Man- FT (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[alpha-L- FT Fuc-(1->6)]-beta-D-GlcNAc) (complex) asparagine" FT /evidence="ECO:0000269|PubMed:25733881, FT ECO:0000269|PubMed:29445378, ECO:0000269|PubMed:36529104" FT CARBOHYD 180 FT /note="N-linked (alpha-Neu5Ac-(2->6)-beta-D-Gal-(1->4)- FT beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-Neu5Ac- FT (2->6)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)-alpha-D-Man- FT (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D- FT GlcNAc) (complex) asparagine" FT /evidence="ECO:0000269|PubMed:29445378" FT CARBOHYD 180 FT /note="N-linked (alpha-Neu5Ac-(2->6)-beta-D-Gal-(1->4)- FT beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-Gal-(1->4)- FT beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)- FT beta-D-GlcNAc-(1->4)-[alpha-L-Fuc-(1->6)]-beta-D-GlcNAc) FT (complex) asparagine" FT /evidence="ECO:0000269|PubMed:10818239, FT ECO:0000305|PubMed:22184099, ECO:0000305|PubMed:26140596, FT ECO:0000305|PubMed:29133956, ECO:0000305|PubMed:29445378, FT ECO:0000305|PubMed:36529104, ECO:0000305|PubMed:39983994" FT CARBOHYD 180 FT /note="N-linked (alpha-Neu5Ac-(2->6)-beta-D-Gal-(1->4)- FT beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc- FT (1->4)]-[beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)-alpha-D- FT Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[alpha- FT L-Fuc-(1->6)]-beta-D-GlcNAc) (complex) asparagine" FT /evidence="ECO:0000305|PubMed:22184099, FT ECO:0000305|PubMed:29133956, ECO:0000305|PubMed:29445378, FT ECO:0000305|PubMed:36529104" FT CARBOHYD 180 FT /note="N-linked (alpha-Neu5Ac-(2->6)-beta-D-Gal-(1->4)- FT beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc- FT (1->4)]-[beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)-alpha-D- FT Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D- FT GlcNAc) (complex) asparagine" FT /evidence="ECO:0000305|PubMed:29133956, FT ECO:0000305|PubMed:39983994" FT CARBOHYD 180 FT /note="N-linked (alpha-Neu5Ac-(2->6)-beta-D-Gal-(1->4)- FT beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc- FT (1->4)]-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D- FT Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc) (complex) FT asparagine" FT /evidence="ECO:0000305|PubMed:29133956, FT ECO:0000305|PubMed:29445378" FT CARBOHYD 180 FT /note="N-linked (beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)- FT alpha-D-Man-(1->3)-[alpha-Neu5Ac-(2->6)-beta-D-Gal-(1->4)- FT beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)- FT beta-D-GlcNAc-(1->4)-[alpha-L-Fuc-(1->6)]-beta-D-GlcNAc) FT (complex) asparagine" FT /evidence="ECO:0000305|PubMed:22184099, FT ECO:0000305|PubMed:26140596, ECO:0000305|PubMed:29133956, FT ECO:0000305|PubMed:29445378, ECO:0000305|PubMed:36529104, FT ECO:0000305|PubMed:39983994" FT CARBOHYD 180 FT /note="N-linked (beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)- FT alpha-D-Man-(1->3)-[beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)- FT alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)- FT [alpha-L-Fuc-(1->6)]-beta-D-GlcNAc) (complex) asparagine" FT /evidence="ECO:0000269|PubMed:10818239, FT ECO:0000269|PubMed:22184099, ECO:0000269|PubMed:25733881, FT ECO:0000269|PubMed:26140596, ECO:0000269|PubMed:29133956, FT ECO:0000269|PubMed:29445378, ECO:0000269|PubMed:36529104, FT ECO:0000269|PubMed:39983994" FT CARBOHYD 180 FT /note="N-linked (beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)- FT alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man- FT (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[alpha-L- FT Fuc-(1->6)]-beta-D-GlcNAc) (complex) asparagine" FT /evidence="ECO:0000269|PubMed:29133956, FT ECO:0000305|PubMed:10818239, ECO:0000305|PubMed:22184099, FT ECO:0000305|PubMed:25733881, ECO:0000305|PubMed:26140596, FT ECO:0000305|PubMed:29445378, ECO:0000305|PubMed:36529104, FT ECO:0000305|PubMed:39983994" FT CARBOHYD 180 FT /note="N-linked (beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)- FT alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man- FT (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D- FT GlcNAc) (complex) asparagine" FT /evidence="ECO:0000305|PubMed:22184099, FT ECO:0000305|PubMed:26140596, ECO:0000305|PubMed:29133956, FT ECO:0000305|PubMed:29445378, ECO:0000305|PubMed:36529104, FT ECO:0000305|PubMed:39983994" FT CARBOHYD 180 FT /note="N-linked (beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)- FT alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->4)]-[alpha-Neu5Ac- FT (2->6)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)-alpha-D-Man- FT (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[alpha-L- FT Fuc-(1->6)]-beta-D-GlcNAc) (complex) asparagine" FT /evidence="ECO:0000305|PubMed:22184099, FT ECO:0000305|PubMed:29133956, ECO:0000305|PubMed:29445378, FT ECO:0000305|PubMed:36529104" FT CARBOHYD 180 FT /note="N-linked (beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)- FT alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->4)]-[alpha-Neu5Ac- FT (2->6)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)-alpha-D-Man- FT (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D- FT GlcNAc) (complex) asparagine" FT /evidence="ECO:0000305|PubMed:29133956, FT ECO:0000305|PubMed:39983994" FT CARBOHYD 180 FT /note="N-linked (beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)- FT alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->4)]-[beta-D-Gal- FT (1->4)-beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man- FT (1->4)-beta-D-GlcNAc-(1->4)-[alpha-L-Fuc-(1->6)]-beta-D- FT GlcNAc) (complex) asparagine" FT /evidence="ECO:0000269|PubMed:22184099, FT ECO:0000269|PubMed:26140596, ECO:0000269|PubMed:29133956, FT ECO:0000269|PubMed:29445378, ECO:0000269|PubMed:36529104, FT ECO:0000269|PubMed:39983994" FT CARBOHYD 180 FT /note="N-linked (beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)- FT alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->4)]-[beta-D-Gal- FT (1->4)-beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man- FT (1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc) (complex) FT asparagine" FT /evidence="ECO:0000269|PubMed:22184099, FT ECO:0000269|PubMed:29133956, ECO:0000269|PubMed:29445378, FT ECO:0000269|PubMed:39983994" FT CARBOHYD 180 FT /note="N-linked (beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)- FT alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->4)]-[beta-D-GlcNAc- FT (1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc- FT (1->4)-[alpha-L-Fuc-(1->6)]-beta-D-GlcNAc) (complex) FT asparagine" FT /evidence="ECO:0000269|PubMed:29133956, FT ECO:0000305|PubMed:22184099, ECO:0000305|PubMed:26140596, FT ECO:0000305|PubMed:29445378, ECO:0000305|PubMed:36529104, FT ECO:0000305|PubMed:39983994" FT CARBOHYD 180 FT /note="N-linked (beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)- FT alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->4)]-[beta-D-GlcNAc- FT (1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc- FT (1->4)-beta-D-GlcNAc) (complex) asparagine" FT /evidence="ECO:0000305|PubMed:22184099, FT ECO:0000305|PubMed:29133956, ECO:0000305|PubMed:29445378, FT ECO:0000305|PubMed:39983994" FT CARBOHYD 180 FT /note="N-linked (beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)- FT [beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)-alpha-D-Man- FT (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[alpha-L- FT Fuc-(1->6)]-beta-D-GlcNAc) (complex) asparagine" FT /evidence="ECO:0000269|PubMed:10818239, FT ECO:0000269|PubMed:10917521, ECO:0000269|PubMed:29133956, FT ECO:0000305|PubMed:22184099, ECO:0000305|PubMed:25733881, FT ECO:0000305|PubMed:26140596, ECO:0000305|PubMed:29445378, FT ECO:0000305|PubMed:36529104, ECO:0000305|PubMed:39983994, FT ECO:0000312|PDB:1E4K" FT CARBOHYD 180 FT /note="N-linked (beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)- FT [beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)-alpha-D-Man- FT (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D- FT GlcNAc) (complex) asparagine" FT /evidence="ECO:0000269|PubMed:29133956, FT ECO:0000305|PubMed:22184099, ECO:0000305|PubMed:26140596, FT ECO:0000305|PubMed:29445378, ECO:0000305|PubMed:36529104, FT ECO:0000305|PubMed:39983994" FT CARBOHYD 180 FT /note="N-linked (beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)- FT [beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man- FT (1->4)-beta-D-GlcNAc-(1->4)-[alpha-L-Fuc-(1->6)]-beta-D- FT GlcNAc) (complex) asparagine" FT /evidence="ECO:0000269|PubMed:10818239, FT ECO:0000269|PubMed:21768335, ECO:0000269|PubMed:22184099, FT ECO:0000269|PubMed:25561553, ECO:0000269|PubMed:25733881, FT ECO:0000269|PubMed:26140596, ECO:0000269|PubMed:29133956, FT ECO:0000269|PubMed:29445378, ECO:0000269|PubMed:36529104, FT ECO:0000269|PubMed:39983994, ECO:0000312|PDB:3SGJ, FT ECO:0000312|PDB:4X4M" FT CARBOHYD 180 FT /note="N-linked (beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)- FT [beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man- FT (1->4)-beta-D-GlcNAcl-(1->4)-beta-D-GlcNAc) (complex) FT asparagine" FT /evidence="ECO:0000269|PubMed:22184099, FT ECO:0000269|PubMed:26140596, ECO:0000269|PubMed:29133956, FT ECO:0000269|PubMed:29445378, ECO:0000269|PubMed:39983994" FT CARBOHYD 180 FT /note="N-linked (beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)- FT [beta-D-GlcNAc-(1->4)]-[alpha-Neu5Ac-(2->6)-beta-D-Gal- FT (1->4)-beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man- FT (1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc) (complex) FT asparagine" FT /evidence="ECO:0000305|PubMed:29133956, FT ECO:0000305|PubMed:29445378" FT CARBOHYD 180 FT /note="N-linked (beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)- FT [beta-D-GlcNAc-(1->4)]-[beta-D-Gal-(1->4)-beta-D-GlcNAc- FT (1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc- FT (1->4)-[alpha-L-Fuc-(1->6)]-beta-D-GlcNAc) (complex) FT asparagine" FT /evidence="ECO:0000269|PubMed:29133956, FT ECO:0000305|PubMed:22184099, ECO:0000305|PubMed:26140596, FT ECO:0000305|PubMed:29445378, ECO:0000305|PubMed:36529104, FT ECO:0000305|PubMed:39983994" FT CARBOHYD 180 FT /note="N-linked (beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)- FT [beta-D-GlcNAc-(1->4)]-[beta-D-Gal-(1->4)-beta-D-GlcNAc- FT (1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc- FT (1->4)-beta-D-GlcNAc) (complex) asparagine" FT /evidence="ECO:0000305|PubMed:22184099, FT ECO:0000305|PubMed:29133956, ECO:0000305|PubMed:29445378, FT ECO:0000305|PubMed:39983994" FT CARBOHYD 180 FT /note="N-linked (beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)- FT [beta-D-GlcNAc-(1->4)]-[beta-D-GlcNAc-(1->2)-alpha-D-Man- FT (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[alpha-L- FT Fuc-(1->6)]-beta-D-GlcNAc) (complex) asparagine" FT /evidence="ECO:0000269|PubMed:22184099, FT ECO:0000269|PubMed:26140596, ECO:0000269|PubMed:29133956, FT ECO:0000269|PubMed:29445378, ECO:0000269|PubMed:39983994" FT CARBOHYD 180 FT /note="N-linked (beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)- FT [beta-D-GlcNAc-(1->4)]-[beta-D-GlcNAc-(1->2)-alpha-D-Man- FT (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D- FT GlcNAc) (complex) asparagine" FT /evidence="ECO:0000269|PubMed:21768335, FT ECO:0000269|PubMed:22184099, ECO:0000269|PubMed:29133956, FT ECO:0000269|PubMed:29445378, ECO:0000269|PubMed:39983994, FT ECO:0000312|PDB:3SGK" FT CARBOHYD 180 FT /note="N-linked (GlcNAc...) (complex) asparagine" FT /evidence="ECO:0000269|PubMed:11406581, FT ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:19358553, ECO:0000269|PubMed:20357243" 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 /evidence="ECO:0000269|PubMed:10917521, FT ECO:0000269|PubMed:21768335, ECO:0000269|PubMed:25561553, FT ECO:0000312|PDB:1E4K, ECO:0000312|PDB:3SGJ, FT ECO:0000312|PDB:4X4M" FT DISULFID 144..204 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 144..204 FT /note="Intrachain" FT /evidence="ECO:0000269|PubMed:10917521, FT ECO:0000269|PubMed:21768335, ECO:0000269|PubMed:25561553, FT ECO:0000312|PDB:1E4K, ECO:0000312|PDB:3SGJ, FT ECO:0000312|PDB:4X4M" FT DISULFID 250..308 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 250..308 FT /note="Intrachain" FT /evidence="ECO:0000269|PubMed:10917521, FT ECO:0000269|PubMed:21768335, ECO:0000269|PubMed:25561553, FT ECO:0000312|PDB:1E4K, ECO:0000312|PDB:3SGJ, FT ECO:0000312|PDB:4X4M" FT VAR_SEQ 329..330 FT /note="EL -> GK (in isoform 1)" FT /id="VSP_061818" FT VAR_SEQ 331..399 FT /note="Missing (in isoform 1)" FT /id="VSP_061819" 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 180 FT /note="N->A: Loss of N-glycosylation. Abolishes binding to FT FCGR3A, FCGR3B and FCGR2BFc receptors. Decreases FCGR1A FT receptor binding." FT /evidence="ECO:0000269|PubMed:30061887, FT ECO:0000269|PubMed:36867679" 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 FT complement-dependent cytotoxicity." FT /evidence="ECO:0000269|PubMed:11711607" FT MUTAGEN 228 FT /note="E->R: Spontaneously forms hexameric Ig structures in FT solution in the absence of antigen; when associated with FT R-313 and Y-323." FT /evidence="ECO:0000269|PubMed:33563762" FT MUTAGEN 313 FT /note="E->R: Spontaneously forms hexameric Ig structures in FT solution in the absence of antigen; when associated with FT R-228 and Y-323." FT /evidence="ECO:0000269|PubMed:33563762" FT MUTAGEN 323 FT /note="S->Y: Spontaneously forms hexameric Ig structures in FT solution in the absence of antigen; when associated with FT R-228 and R-313." FT /evidence="ECO:0000269|PubMed:33563762" FT NON_TER 1 FT HELIX 1..3 FT /evidence="ECO:0007829|PDB:3TV3" FT STRAND 7..14 FT /evidence="ECO:0007829|PDB:4LLD" FT STRAND 16..18 FT /evidence="ECO:0007829|PDB:4LLD" FT STRAND 19..21 FT /evidence="ECO:0007829|PDB:2QAD" 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 47..49 FT /evidence="ECO:0007829|PDB:2QAD" FT STRAND 50..52 FT /evidence="ECO:0007829|PDB:4LLD" FT HELIX 53..55 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 99..101 FT /evidence="ECO:0007829|PDB:3MCL" FT HELIX 110..114 FT /evidence="ECO:0007829|PDB:3SGJ" 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:6YT7" FT HELIX 127..129 FT /evidence="ECO:0007829|PDB:6YT7" FT HELIX 130..134 FT /evidence="ECO:0007829|PDB:6YT7" FT STRAND 136..138 FT /evidence="ECO:0007829|PDB:5IW3" FT STRAND 141..149 FT /evidence="ECO:0007829|PDB:6YT7" FT STRAND 151..153 FT /evidence="ECO:0007829|PDB:6YT7" FT STRAND 157..162 FT /evidence="ECO:0007829|PDB:6YT7" FT STRAND 165..167 FT /evidence="ECO:0007829|PDB:6YT7" FT STRAND 170..172 FT /evidence="ECO:0007829|PDB:4WI6" FT HELIX 173..175 FT /evidence="ECO:0007829|PDB:6YT7" 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:6YT7" FT HELIX 193..197 FT /evidence="ECO:0007829|PDB:6YT7" FT STRAND 202..207 FT /evidence="ECO:0007829|PDB:6YT7" FT STRAND 211..213 FT /evidence="ECO:0007829|PDB:6YT7" FT STRAND 215..219 FT /evidence="ECO:0007829|PDB:6YT7" FT HELIX 221..223 FT /evidence="ECO:0007829|PDB:6YT7" FT STRAND 230..234 FT /evidence="ECO:0007829|PDB:5HSF" FT HELIX 235..237 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 HELIX 277..279 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" FT HELIX 326..328 FT /evidence="ECO:0007829|PDB:4W4O" FT STRAND 343..346 FT /evidence="ECO:0007829|PDB:7WSO" FT HELIX 349..370 FT /evidence="ECO:0007829|PDB:7WSO" SQ SEQUENCE 399 AA; 43912 MW; F87DF649F78907C9 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 QKSLSLSPEL QLEESCAEAQ DGELDGLWTT ITIFITLFLL SVCYSATVTF FKVKWIFSSV VDLKQTIIPD YRNMIGQGA //