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FCGRB_HUMAN
ID   FCGRB_HUMAN             Reviewed;         280 AA.
AC   Q92637; Q7KZ13; Q92638;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=Putative high affinity immunoglobulin gamma Fc receptor IB;
DE            Short=IgG Fc receptor IB;
DE   AltName: Full=Fc gamma receptor IB pseudogene {ECO:0000312|HGNC:HGNC:3614};
DE   AltName: Full=Fc-gamma RIB;
DE            Short=FcRIB;
DE            Short=hFcgammaRIB;
DE   Flags: Precursor;
GN   Name=FCGR1BP {ECO:0000312|HGNC:HGNC:3614}; Synonyms=FCGR1B, IGFRB;
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 [MRNA] (ISOFORMS 1 AND 3), FUNCTION, SUBCELLULAR
RP   LOCATION, AND INDUCTION BY IFNG.
RC   TISSUE=Blood;
RX   PubMed=1430234; DOI=10.1172/jci116094;
RA   Porges A.J., Redecha P.B., Doebele R., Pan L.C., Salmon J.E.,
RA   Kimberly R.P.;
RT   "Novel Fc gamma receptor I family gene products in human mononuclear
RT   cells.";
RL   J. Clin. Invest. 90:2102-2109(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION BY IFNG.
RX   PubMed=1402657; DOI=10.1084/jem.176.4.1115;
RA   Benech P.D., Sastry K.N., Iyer R.R., Eichbaum Q.G., Raveh D.P.,
RA   Ezekowitz R.A.;
RT   "Definition of interferon gamma-response elements in a novel human Fc gamma
RT   receptor gene (Fc gamma RIb) and characterization of the gene structure.";
RL   J. Exp. Med. 176:1115-1123(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   IDENTIFICATION.
RX   PubMed=8697799; DOI=10.1159/000134330;
RA   Maresco D.L., Chang E., Theil K.S., Francke U., Anderson C.L.;
RT   "The three genes of the human FCGR1 gene family encoding Fc gamma RI flank
RT   the centromere of chromosome 1 at 1p12 and 1q21.";
RL   Cytogenet. Cell Genet. 73:157-163(1996).
RN   [5]
RP   FUNCTION, AND ALTERNATIVE SPLICING.
RX   PubMed=9881690; DOI=10.1016/s0161-5890(98)00079-0;
RA   Ernst L.K., Duchemin A.-M., Miller K.L., Anderson C.L.;
RT   "Molecular characterization of six variant Fcgamma receptor class I (CD64)
RT   transcripts.";
RL   Mol. Immunol. 35:943-954(1998).
CC   -!- FUNCTION: May bind to the Fc region of immunoglobulins gamma with a low
CC       affinity compared to FCGR1A. May function in the humoral immune
CC       response. {ECO:0000269|PubMed:1430234, ECO:0000269|PubMed:9881690}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1430234};
CC       Single-pass type I membrane protein {ECO:0000269|PubMed:1430234}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=b2;
CC         IsoId=Q92637-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q92637-2; Sequence=VSP_033216, VSP_033217;
CC       Name=3; Synonyms=b3;
CC         IsoId=Q92637-3; Sequence=VSP_033215;
CC   -!- INDUCTION: Up-regulated by IFNG/IFN-gamma. {ECO:0000269|PubMed:1402657,
CC       ECO:0000269|PubMed:1430234}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. FCGR1 family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
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DR   EMBL; L03419; AAA35825.1; -; mRNA.
DR   EMBL; L03420; AAA35826.1; -; mRNA.
DR   EMBL; S45709; AAD13842.1; -; Genomic_DNA.
DR   EMBL; S45704; AAD13842.1; JOINED; Genomic_DNA.
DR   EMBL; S45705; AAD13842.1; JOINED; Genomic_DNA.
DR   EMBL; S45707; AAD13842.1; JOINED; Genomic_DNA.
DR   EMBL; S45708; AAD13842.1; JOINED; Genomic_DNA.
DR   EMBL; AL357493; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; I55577; I55577.
DR   RefSeq; NP_001004340.2; NM_001004340.3.
DR   RefSeq; NP_001017986.1; NM_001017986.3.
DR   RefSeq; NP_001231839.1; NM_001244910.1.
DR   AlphaFoldDB; Q92637; -.
DR   SMR; Q92637; -.
DR   BioGRID; 108504; 2.
DR   STRING; 9606.ENSP00000358391; -.
DR   DrugBank; DB00028; Human immunoglobulin G.
DR   GlyGen; Q92637; 3 sites.
DR   iPTMnet; Q92637; -.
DR   PhosphoSitePlus; Q92637; -.
DR   BioMuta; FCGR1B; -.
DR   DMDM; 74760649; -.
DR   jPOST; Q92637; -.
DR   MassIVE; Q92637; -.
DR   PaxDb; Q92637; -.
DR   PeptideAtlas; Q92637; -.
DR   PRIDE; Q92637; -.
DR   ProteomicsDB; 75392; -. [Q92637-1]
DR   ProteomicsDB; 75393; -. [Q92637-2]
DR   ProteomicsDB; 75394; -. [Q92637-3]
DR   Antibodypedia; 53772; 71 antibodies from 14 providers.
DR   DNASU; 2210; -.
DR   Ensembl; ENST00000369383.8; ENSP00000358390.4; ENSG00000198019.13. [Q92637-3]
DR   UCSC; uc031upv.2; human. [Q92637-1]
DR   DisGeNET; 2210; -.
DR   GeneCards; FCGR1B; -.
DR   HGNC; HGNC:3614; FCGR1BP.
DR   HPA; ENSG00000198019; Tissue enhanced (epididymis, lymphoid tissue).
DR   MIM; 601502; gene.
DR   neXtProt; NX_Q92637; -.
DR   OpenTargets; ENSG00000198019; -.
DR   VEuPathDB; HostDB:ENSG00000198019; -.
DR   eggNOG; ENOG502S1XR; Eukaryota.
DR   GeneTree; ENSGT01050000244808; -.
DR   HOGENOM; CLU_124507_0_0_1; -.
DR   InParanoid; Q92637; -.
DR   OrthoDB; 866496at2759; -.
DR   PhylomeDB; Q92637; -.
DR   TreeFam; TF335097; -.
DR   PathwayCommons; Q92637; -.
DR   Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR   Reactome; R-HSA-877300; Interferon gamma signaling.
DR   BioGRID-ORCS; 2210; 267 hits in 991 CRISPR screens.
DR   GenomeRNAi; 2210; -.
DR   Pharos; Q92637; Tbio.
DR   PRO; PR:Q92637; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q92637; protein.
DR   Bgee; ENSG00000198019; Expressed in monocyte and 100 other tissues.
DR   ExpressionAtlas; Q92637; baseline and differential.
DR   Genevisible; Q92637; HS.
DR   GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR   GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0019864; F:IgG binding; IEA:UniProtKB-KW.
DR   GO; GO:0019763; F:immunoglobulin receptor activity; NAS:UniProtKB.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0006955; P:immune response; NAS:UniProtKB.
DR   GO; GO:0050776; P:regulation of immune response; IBA:GO_Central.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   Pfam; PF13895; Ig_2; 1.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 2.
DR   SUPFAM; SSF48726; SSF48726; 2.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   5: Uncertain;
KW   Adaptive immunity; Alternative splicing; Cell membrane; Disulfide bond;
KW   Glycoprotein; IgG-binding protein; Immunity; Immunoglobulin domain;
KW   Membrane; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..280
FT                   /note="Putative high affinity immunoglobulin gamma Fc
FT                   receptor IB"
FT                   /id="PRO_0000331462"
FT   TOPO_DOM        16..198
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        220..280
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          22..101
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          95..184
FT                   /note="Ig-like C2-type 2"
FT   REGION          258..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..272
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        152
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        43..85
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        124..168
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VAR_SEQ         11..102
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:1430234"
FT                   /id="VSP_033215"
FT   VAR_SEQ         188..223
FT                   /note="GLQLPTPVWFHVLFYLAVGIMFLVNTVLWVTIRKEL -> ELFPAPVLNASV
FT                   TSPLLEGNLVTLSCETKLLLQRPGL (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_033216"
FT   VAR_SEQ         224..280
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_033217"
FT   CONFLICT        154
FT                   /note="T -> A (in Ref. 1; AAA35826)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   280 AA;  32232 MW;  C6C6C45AE3D345C6 CRC64;
     MWFLTTLLLW VPVDGQVDTT KAVITLQPPW VSVFQEETVT LHCEVLHLPG SSSTQWFLNG
     TATQTSTPSY RITSASVNDS GEYRCQRGLS GRSDPIQLEI HRGWLLLQVS SRVFMEGEPL
     ALRCHAWKDK LVYNVLYYRN GKAFKFFHWN SNLTILKTNI SHNGTYHCSG MGKHRYTSAG
     ISQYTVKGLQ LPTPVWFHVL FYLAVGIMFL VNTVLWVTIR KELKRKKKWN LEISLDSGHE
     KKVISSLQED RHLEEELKCQ EQKEEQLQEG VHRKEPQGAT
 
 
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