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UniProtKB/Swiss-Prot entry P31994


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FCG2B_HUMAN
Primary accession number P31994
Secondary accession numbers A6H8N3 O95649 Q53X85 Q5VXA9 Q8NIA1
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on May 30, 2000 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 112)
Name and origin of the protein
Protein name Low affinity immunoglobulin gamma Fc region receptor II-b [Precursor]
Synonyms IgG Fc receptor II-b
Fc-gamma RII-b
Fc-gamma-RIIb
FcRII-b
CDw32
CD32 antigen
Gene name
Name: FCGR2B
Synonyms: CD32, FCG2, IGFR2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS IIB1 AND IIB2).
TISSUE=Lymphocyte;
Ng S., Sinclair N.R.S., Anderson C., Bell D.A., Cairns E.;
"Fc-gamma-RIIb nucleotide sequences in SLE and non-SLE humans in vivo derived lymphocytes.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IIB2).
TISSUE=Placenta;
PubMed=2531080 [NCBI, ExPASy, EBI, Israel, Japan]
Stuart S.G., Simister N.E., Clarkson S.B., Kacinski B.M., Shapiro M., Mellman I.;
"Human IgG Fc receptor (hFcRII; CD32) exists as multiple isoforms in macrophages, lymphocytes and IgG-transporting placental epithelium.";
EMBO J. 8:3657-3666(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS IIB1; IIB2 AND IIB3), AND VARIANT PHE-205.
DOI=10.1084/jem.170.4.1369; PubMed=2529342 [NCBI, ExPASy, EBI, Israel, Japan]
Brooks D.G., Qiu W.Q., Luster A.D., Ravetch J.V.;
"Structure and expression of human IgG FcRII(CD32). Functional heterogeneity is encoded by the alternatively spliced products of multiple genes.";
J. Exp. Med. 170:1369-1385(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IIB2).
TISSUE=Placenta;
DOI=10.1002/eji.1830200624; PubMed=2142460 [NCBI, ExPASy, EBI, Israel, Japan]
Engelhardt W., Geerds C., Frey J.;
"Distribution, inducibility and biological function of the cloned and expressed human beta Fc receptor II.";
Eur. J. Immunol. 20:1367-1377(1990).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IIB2).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS IIB1 AND IIB2).
TISSUE=Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 132-253, AND VARIANT THR-232.
DOI=10.1002/art.10257; PubMed=12115230 [NCBI, ExPASy, EBI, Israel, Japan]
Kyogoku C., Dijstelbloem H.M., Tsuchiya N., Hatta Y., Kato H., Yamaguchi A., Fukazawa T., Jansen M.D., Hashimoto H., van de Winkel J.G.J., Kallenberg C.G.M., Tokunaga K.;
"Fc gamma receptor gene polymorphisms in Japanese patients with systemic lupus erythematosus: contribution of FCGR2B to genetic susceptibility.";
Arthritis Rheum. 46:1242-1254(2002).
[9]
INTERACTION WITH MEASLES VIRUS N PROTEIN.
DOI=10.1099/vir.0.80791-0; PubMed=15914856 [NCBI, ExPASy, EBI, Israel, Japan]
Laine D., Bourhis J.-M., Longhi S., Flacher M., Cassard L., Canard B., Sautes-Fridman C., Rabourdin-Combe C., Valentin H.;
"Measles virus nucleoprotein induces cell-proliferation arrest and apoptosis through NTAIL-NR and NCORE-FcgammaRIIB1 interactions, respectively.";
J. Gen. Virol. 86:1771-1784(2005).
[10]
X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 46-217, AND DISULFIDE BONDS.
DOI=10.1093/emboj/18.5.1095; PubMed=10064577 [NCBI, ExPASy, EBI, Israel, Japan]
Sondermann P., Huber R., Jacob U.;
"Crystal structure of the soluble form of the human fcgamma-receptor IIb: a new member of the immunoglobulin superfamily at 1.7 A resolution.";
EMBO J. 18:1095-1103(1999).
[11]
VARIANT ASP-258.
DOI=10.1093/intimm/5.3.239; PubMed=8466861 [NCBI, ExPASy, EBI, Israel, Japan]
Warmerdam P.A., van den Herik-Oudijk I.E., Parren P.W., Westerdaal N.A., van de Winkel J.G., Capel P.J.;
"Interaction of a human Fc gamma RIIb1 (CD32) isoform with murine and human IgG subclasses.";
Int. Immunol. 5:239-247(1993).
Comments
  • FUNCTION: Receptor for the Fc region of complexed or aggregated immunoglobulins gamma. Low affinity receptor. Involved in a variety of effector and regulatory functions such as phagocytosis of immune complexes and modulation of antibody production by B-cells. Binding to this receptor results in down-modulation of previous state of cell activation triggered via antigen receptors on B-cells (BCR), T-cells (TCR) or via another Fc receptor. Isoform IIB1 fails to mediate endocytosis or phagocytosis. Isoform IIB2 does not trigger phagocytosis.
  • SUBUNIT: Isoform IIB1 interacts with measles virus N protein. N protein is released in the blood following lysis of measles infected cells. This interaction presumably block inflammatory immune response. Interacts with INPP5D/SHIP1.
  • INTERACTION:
    P46108:CRK; NbExp=1; IntAct=EBI-724784, EBI-886;
    P06241:FYN; NbExp=1; IntAct=EBI-724784, EBI-515315;
    P62993:GRB2; NbExp=1; IntAct=EBI-724784, EBI-401755;
    P01857:IGHG1; NbExp=2; IntAct=EBI-724784, EBI-356114;
    P16333:NCK1; NbExp=1; IntAct=EBI-724784, EBI-389883;
    P19174:PLCG1; NbExp=1; IntAct=EBI-724784, EBI-79387;
    P12931:SRC; NbExp=1; IntAct=EBI-724784, EBI-621482;
  • SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.
  • ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.
    NameIIB1
    Isoform IDP31994-1
    This is the isoform sequence displayed in this entry.
    NameIIB2
    Isoform IDP31994-2
    Features which should be applied to build the isoform sequence: VSP_002643.
    NameIIB3
    Isoform IDP31994-3
    Features which should be applied to build the isoform sequence: VSP_002642.
  • TISSUE SPECIFICITY: Is the most broadly distributed Fc-gamma-receptor. Expressed in monocyte, neutrophils, macrophages, basophils, eosinophils, Langerhans cells, B-cells, platelets cells and placenta (endothelial cells). Not detected in natural killer cells.
  • DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases.
  • DISEASE: A chromosomal aberration involving FCGR2B is found in a follicular lymphoma. Translocation t(1;22)(q22;q11). The translocation leads to the hyperexpression of the receptor. This may play a role in the tumor progression.
  • SIMILARITY: Contains 2 Ig-like C2-type (immunoglobulin-like) domains.
  • CAUTION: Has sometimes been attributed to correspond to FcR-IIC.
  • WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/FCGR2BID397.html";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U87560; AAD00627.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U87561; AAD00628.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U87562; AAD00629.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U87563; AAD00630.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U87564; AAD00631.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U87565; AAD00632.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U87566; AAD00633.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U87567; AAD00634.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U87568; AAD00635.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U87569; AAD00636.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U87570; AAD00637.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U87571; AAD00638.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U87572; AAD00639.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U87573; AAD00640.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U87574; AAD00641.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U87575; AAD00642.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U87576; AAD00643.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U87577; AAD00644.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X17653; CAA35644.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X17653; CAA35645.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M31933; AAA35841.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M31934; AAA35842.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M31935; AAA35843.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X52473; CAA36713.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR407635; CAG28563.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL359541; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
BC031992; AAH31992.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC146678; AAI46679.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB050934; BAB92093.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00013969; -.
IPI00434996; -.
IPI00479827; -.
PIR JL0119; JL0119.
RefSeq NP_001002273.1; -.
NP_001002274.1; -.
NP_001002275.1; -.
NP_003992.3; -.
UniGene Hs.654395
3D structure databases
PDB
2FCB; X-ray; 1.74 A; A=46-217.[ExPASy / RCSB / EBI]
PDBsum 2FCB; -.
ModBase P31994.
Protein-protein interaction databases
IntAct P31994; 8.
PTM databases
PhosphoSite P31994; -.
Enzyme and pathway databases
Pathway_Interaction_DB bcr_5pathway; BCR signaling pathway.
fcer1pathway; Fc-epsilon receptor I signaling in mast cells.
Reactome REACT_6900; Signaling in Immune system.
Organism-specific databases
GeneCards GC01P159899; -.
H-InvDB HIX0001249; -.
HGNC HGNC:3618; FCGR2B.
GenAtlas FCGR2B.
HPA CAB007796; -.
MIM 604590; gene. [NCBI / EBI]
PharmGKB PA28064; -.
Gene expression databases
ArrayExpress P31994; -.
Bgee P31994; -.
CleanEx HS_FCGR2B; -.
GermOnline ENSG00000072694; Homo sapiens.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886; Cellular component: plasma membrane (inferred from experiment from Reactome).
GO:0019864; Molecular function: IgG binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004872; Molecular function: receptor activity (inferred from electronic annotation from UniProtKB-KW).
GO:0006955; Biological process: immune response (traceable author statement from ProtInc).
GO:0044419; Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0007165; Biological process: signal transduction (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR013151; Ig.
IPR007110; Ig-like.
IPR013783; Ig-like_fold.
IPR003599; Ig_sub.
IPR013106; Ig_V-set.
Graphical view of domain structure.
Gene3D G3DSA:2.60.40.10; Ig-like_fold; 2.
Pfam PF00047; ig; 1.
PF07686; V-set; 1.
Pfam graphical view of domain structure.
SMART SM00409; IG; 2.
SMART graphical view of domain structure.
PROSITE PS50835; IG_LIKE; 2.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P31994; -.
Genome annotation databases
Ensembl ENSG00000072694; Homo sapiens. [Contig view]
GeneID 2213; -.
KEGG hsa:2213; -.
Phylogenomic databases
HOGENOM P31994; -.
HOVERGEN P31994; -.
OMA P31994; MHPDALE.
Other
DrugBank DB00054; Abciximab.
DB00051; Adalimumab.
DB00092; Alefacept.
DB00087; Alemtuzumab.
DB00074; Basiliximab.
DB00112; Bevacizumab.
DB00002; Cetuximab.
DB00111; Daclizumab.
DB00095; Efalizumab.
DB00005; Etanercept.
DB00056; Gemtuzumab ozogamicin.
DB00078; Ibritumomab.
DB00028; Immune globulin.
DB00075; Muromonab.
DB00108; Natalizumab.
DB00110; Palivizumab.
DB00073; Rituximab.
DB00081; Tositumomab.
DB00072; Trastuzumab.
NextBio 8967; -.
SOURCE FCGR2B; Homo sapiens.
ProtoNet P31994.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Cell membrane; Chromosomal rearrangement; Disulfide bond; Glycoprotein; Host-virus interaction; IgG-binding protein; Immunoglobulin domain; Membrane; Polymorphism; Proto-oncogene; Receptor; Repeat; Signal; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    42  42     Potential. 
CHAIN   43   310  268     Low affinity immunoglobulin gamma Fc region receptor II-b. PRO_0000015147
TOPO_DOM   43   217  175     Extracellular (Potential). 
TRANSMEM   218   240  23     Potential. 
TOPO_DOM   241   310  70     Cytoplasmic (Potential). 
DOMAIN   48   127  80     Ig-like C2-type 1. 
DOMAIN   131   213  83     Ig-like C2-type 2. 
MOTIF   290   295  6     ITIM motif. 
CARBOHYD   106   106        N-linked (GlcNAc...) (Potential). 
CARBOHYD   180   180        N-linked (GlcNAc...) (Potential). 
CARBOHYD   187   187        N-linked (GlcNAc...) (Potential). 
DISULFID   71   113         
DISULFID   152   196         
VAR_SEQ   39    45        Missing (in isoform IIB3). VSP_002642
VAR_SEQ   254   272        Missing (in isoform IIB2). VSP_002643
VARIANT   205   205  1     Y -> F (in dbSNP:rs1050499 [NCBI]). VAR_027045 [3D]
VARIANT   232   232  1     I -> T. VAR_015515 
VARIANT   258   258  1     Y -> D. VAR_008798 
CONFLICT   46    46        Missing (in Ref. 1; AAD00637/AAD00638/AAD00639/AAD00644). 
CONFLICT   178   178        D -> I (in Ref. 2; CAA35644/CAA35645). 
CONFLICT   230   230        T -> I (in Ref. 2; CAA35644/CAA35645). 
CONFLICT   242   242        V -> G (in Ref. 2; CAA35644/CAA35645). 
CONFLICT   275   275        P -> S (in Ref. 2). 
STRAND   51    56  6      
STRAND   59    62  4      
STRAND   66    72  7      
STRAND   83    86  4      
STRAND   96   102  7      
HELIX   105   107  3      
STRAND   109   114  6      
STRAND   124   129  6      
STRAND   131   136  6      
STRAND   140   142  3      
STRAND   148   154  7      
HELIX   155   157  3      
STRAND   161   167  7      
STRAND   170   177  8      
STRAND   180   183  4      
HELIX   188   190  3      
STRAND   192   200  9      
STRAND   203   206  4      
STRAND   210   214  5      
Sequence information
Length: 310 AA [This is the length of the unprocessed precursor] Molecular weight: 34044 Da [This is the MW of the unprocessed precursor] CRC64: 2186F8538FF01F36 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGILSFLPVL ATESDWADCK SPQPWGHMLL WTAVLFLAPV AGTPAAPPKA VLKLEPQWIN 

        70         80         90        100        110        120 
VLQEDSVTLT CRGTHSPESD SIQWFHNGNL IPTHTQPSYR FKANNNDSGE YTCQTGQTSL 

       130        140        150        160        170        180 
SDPVHLTVLS EWLVLQTPHL EFQEGETIVL RCHSWKDKPL VKVTFFQNGK SKKFSRSDPN 

       190        200        210        220        230        240 
FSIPQANHSH SGDYHCTGNI GYTLYSSKPV TITVQAPSSS PMGIIVAVVT GIAVAAIVAA 

       250        260        270        280        290        300 
VVALIYCRKK RISALPGYPE CREMGETLPE KPANPTNPDE ADKVGAENTI TYSLLMHPDA 

       310 
LEEPDDQNRI 

P31994 in FASTA format

View entry in raw text format (no links)
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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