Reviewed, UniProtKB/Swiss-Prot P31994 (FCG2B_HUMAN)

Names and origin

Protein names

Recommended name:
    Low affinity immunoglobulin gamma Fc region receptor II-b
      Short name=IgG Fc receptor II-b
Alternative name(s):
    Fc-gamma RII-b
    Fc-gamma-RIIb
      Short name=FcRII-b
    CDw32
    CD_antigen=CD32

Gene names

Name:	FCGR2B
Synonyms:	CD32, FCG2, IGFR2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	310 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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 structure	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. Ref.9
Subcellular location	Cell membrane; Single-pass type I membrane protein.
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.
Involvement in 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.
Sequence similarities	Contains 2 Ig-like C2-type (immunoglobulin-like) domains.
Caution	Has sometimes been attributed to correspond to FcR-IIC.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene
Domain	Immunoglobulin domain Repeat Signal Transmembrane
Ligand	IgG-binding protein
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	immune response Ref.4 Traceable author statement. Source: ProtInc interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW signal transduction Ref.4 Traceable author statement. Source: ProtInc
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from Experiment. Source: Reactome
Molecular function	IgG binding Inferred from electronic annotation. Source: UniProtKB-KW receptor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CRK	P46108	1	EBI-724784,EBI-886
FYN	P06241	1	EBI-724784,EBI-515315
GRB2	P62993	1	EBI-724784,EBI-401755
IGHG1	P01857	2	EBI-724784,EBI-356114
NCK1	P16333	1	EBI-724784,EBI-389883
PLCG1	P19174	1	EBI-724784,EBI-79387
SRC	P12931	1	EBI-724784,EBI-621482

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform IIB1 (identifier: P31994-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform IIB2 (identifier: P31994-2)

The sequence of this isoform differs from the canonical sequence as follows:
     254-272: Missing.

Isoform IIB3 (identifier: P31994-3)

The sequence of this isoform differs from the canonical sequence as follows:
     39-45: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 42

42

Potential

Chain

43 – 310

268

Low affinity immunoglobulin gamma Fc region receptor II-b

PRO_0000015147

Regions

Topological domain

43 – 217

175

Extracellular Potential

Transmembrane

218 – 240

23

Potential

Topological domain

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

Amino acid modifications

Glycosylation

106

1

N-linked (GlcNAc...) Potential

Glycosylation

180

1

N-linked (GlcNAc...) Potential

Glycosylation

187

1

N-linked (GlcNAc...) Potential

Disulfide bond

71 ↔ 113

Ref.10

Disulfide bond

152 ↔ 196

Ref.10

Natural variations

Alternative sequence

39 – 45

7

Missing in isoform IIB3.

VSP_002642

Alternative sequence

254 – 272

19

Missing in isoform IIB2.

VSP_002643

Natural variant

205

1

Y → F: dbSNP rs1050499. Ref.3

VAR_027045

Natural variant

232

1

I → T Ref.8

VAR_015515

Natural variant

258

1

Y → D Ref.11

VAR_008798

Experimental info

Sequence conflict

46

1

Missing in AAD00637. Ref.1

Sequence conflict

46

1

Missing in AAD00638. Ref.1

Sequence conflict

46

1

Missing in AAD00639. Ref.1

Sequence conflict

46

1

Missing in AAD00644. Ref.1

Sequence conflict

178

1

D → I in CAA35644. Ref.2

Sequence conflict

178

1

D → I in CAA35645. Ref.2

Sequence conflict

230

1

T → I in CAA35644. Ref.2

Sequence conflict

230

1

T → I in CAA35645. Ref.2

Sequence conflict

242

1

V → G in CAA35644. Ref.2

Sequence conflict

242

1

V → G in CAA35645. Ref.2

Sequence conflict

275

1

P → S Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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.

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.

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.

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310

Helix Strand Turn

Details...

Beta strand

51 – 56

6

Beta strand

59 – 62

4

Beta strand

66 – 72

7

Beta strand

83 – 86

4

Beta strand

96 – 102

7

Helix

105 – 107

3

Beta strand

109 – 114

6

Beta strand

124 – 129

6

Beta strand

131 – 136

6

Beta strand

140 – 142

3

Beta strand

148 – 154

7

Helix

155 – 157

3

Beta strand

161 – 167

7

Beta strand

170 – 177

8

Beta strand

180 – 183

4

Helix

188 – 190

3

Beta strand

192 – 200

9

Beta strand

203 – 206

4

Beta strand

210 – 214

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform IIB1 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 2186F8538FF01F36	FASTA	310	34,044
	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
	Isoform IIB2. Checksum: 3B76609541B30962	FASTA	291	31,944
	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 VVALIYCRKK RISANPTNPD EADKVGAENT ITYSLLMHPD ALEEPDDQNR I
	Isoform IIB3. Checksum: B84833348A175687	FASTA	303	33,450
	10 20 30 40 50 60 MGILSFLPVL ATESDWADCK SPQPWGHMLL WTAVLFLAAP PKAVLKLEPQ WINVLQEDSV 70 80 90 100 110 120 TLTCRGTHSP ESDSIQWFHN GNLIPTHTQP SYRFKANNND SGEYTCQTGQ TSLSDPVHLT 130 140 150 160 170 180 VLSEWLVLQT PHLEFQEGET IVLRCHSWKD KPLVKVTFFQ NGKSKKFSRS DPNFSIPQAN 190 200 210 220 230 240 HSHSGDYHCT GNIGYTLYSS KPVTITVQAP SSSPMGIIVA VVTGIAVAAI VAAVVALIYC 250 260 270 280 290 300 RKKRISALPG YPECREMGET LPEKPANPTN PDEADKVGAE NTITYSLLMH PDALEEPDDQ NRI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Fc-gamma-RIIb nucleotide sequences in SLE and non-SLE humans in vivo derived lymphocytes." Ng S., Sinclair N.R.S., Anderson C., Bell D.A., Cairns E. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS IIB1 AND IIB2). Tissue: Lymphocyte.
[2]	"Human IgG Fc receptor (hFcRII; CD32) exists as multiple isoforms in macrophages, lymphocytes and IgG-transporting placental epithelium." Stuart S.G., Simister N.E., Clarkson S.B., Kacinski B.M., Shapiro M., Mellman I. EMBO J. 8:3657-3666(1989) [PubMed: 2531080] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IIB2). Tissue: Placenta.
[3]	"Structure and expression of human IgG FcRII(CD32). Functional heterogeneity is encoded by the alternatively spliced products of multiple genes." Brooks D.G., Qiu W.Q., Luster A.D., Ravetch J.V. J. Exp. Med. 170:1369-1385(1989) [PubMed: 2529342] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS IIB1; IIB2 AND IIB3), VARIANT PHE-205.
[4]	"Distribution, inducibility and biological function of the cloned and expressed human beta Fc receptor II." Engelhardt W., Geerds C., Frey J. Eur. J. Immunol. 20:1367-1377(1990) [PubMed: 2142460] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IIB2). Tissue: Placenta.
[5]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IIB2).
[6]	"The DNA sequence and biological annotation of human chromosome 1." 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. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS IIB1 AND IIB2). Tissue: Skin.
[8]	"Fc gamma receptor gene polymorphisms in Japanese patients with systemic lupus erythematosus: contribution of FCGR2B to genetic susceptibility." 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. Arthritis Rheum. 46:1242-1254(2002) [PubMed: 12115230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 132-253, VARIANT THR-232.
[9]	"Measles virus nucleoprotein induces cell-proliferation arrest and apoptosis through NTAIL-NR and NCORE-FcgammaRIIB1 interactions, respectively." Laine D., Bourhis J.-M., Longhi S., Flacher M., Cassard L., Canard B., Sautes-Fridman C., Rabourdin-Combe C., Valentin H. J. Gen. Virol. 86:1771-1784(2005) [PubMed: 15914856] [Abstract] Cited for: INTERACTION WITH MEASLES VIRUS N PROTEIN.
[10]	"Crystal structure of the soluble form of the human fcgamma-receptor IIb: a new member of the immunoglobulin superfamily at 1.7 A resolution." Sondermann P., Huber R., Jacob U. EMBO J. 18:1095-1103(1999) [PubMed: 10064577] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 46-217, DISULFIDE BONDS.
[11]	"Interaction of a human Fc gamma RIIb1 (CD32) isoform with murine and human IgG subclasses." Warmerdam P.A., van den Herik-Oudijk I.E., Parren P.W., Westerdaal N.A., van de Winkel J.G., Capel P.J. Int. Immunol. 5:239-247(1993) [PubMed: 8466861] [Abstract] Cited for: VARIANT ASP-258.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBLGenBankDDBJ

U87560 mRNA. Translation: AAD00627.1.
U87561 mRNA. Translation: AAD00628.1.
U87562 mRNA. Translation: AAD00629.1.
U87563 mRNA. Translation: AAD00630.1.
U87564 mRNA. Translation: AAD00631.1.
U87565 mRNA. Translation: AAD00632.1.
U87566 mRNA. Translation: AAD00633.1.
U87567 mRNA. Translation: AAD00634.1.
U87568 mRNA. Translation: AAD00635.1.
U87569 mRNA. Translation: AAD00636.1.
U87570 mRNA. Translation: AAD00637.1.
U87571 mRNA. Translation: AAD00638.1.
U87572 mRNA. Translation: AAD00639.1.
U87573 mRNA. Translation: AAD00640.1.
U87574 mRNA. Translation: AAD00641.1.
U87575 mRNA. Translation: AAD00642.1.
U87576 mRNA. Translation: AAD00643.1.
U87577 mRNA. Translation: AAD00644.1.
X17653 mRNA. Translation: CAA35644.1.
X17653 mRNA. Translation: CAA35645.1. Different initiation.
M31933 mRNA. Translation: AAA35841.1.
M31934 mRNA. Translation: AAA35842.1.
M31935 mRNA. Translation: AAA35843.1.
X52473 mRNA. Translation: CAA36713.1.
CR407635 mRNA. Translation: CAG28563.1.
AL359541 Genomic DNA. No translation available.
BC031992 mRNA. Translation: AAH31992.1.
BC146678 mRNA. Translation: AAI46679.1.
AB050934 mRNA. Translation: BAB92093.1.

IPI

IPI00013969.
IPI00434996.
IPI00479827.

PIR

JL0119.

RefSeq

NP_001002273.1.
NP_001002274.1.
NP_001002275.1.
NP_003992.3.

UniGene

Hs.654395

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FCB	X-ray	1.74	A	46-217	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P31994. 8 interactions.

PTM databases

PhosphoSite

P31994.

Proteomic databases

PRIDE

P31994.

Genome annotation databases

Ensembl

ENSG00000072694. Homo sapiens. [Contig view]

GeneID

2213.

KEGG

hsa:2213.

Organism-specific databases

GeneCards

GC01P159899.

H-InvDB

HIX0001249.

HGNC

HGNC:3618. FCGR2B.

HPA

CAB007796.

MIM

604590. gene.

PharmGKB

PA28064.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P31994.

HOVERGEN

P31994.

OMA

P31994. MHPDALE.

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.

Gene expression databases

ArrayExpress

P31994.

Bgee

P31994.

CleanEx

HS_FCGR2B.

GermOnline

ENSG00000072694. Homo sapiens.

Family and domain databases

InterPro

IPR013151. Ig.
IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view]

Gene3D

G3DSA:2.60.40.10. Ig-like_fold. 2 hits.

Pfam

PF00047. ig. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]

SMART

SM00409. IG. 2 hits.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 2 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

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

Search...

Entry information

Entry name

FCG2B_HUMAN

Accession

Primary (citable) accession number: P31994
Secondary accession number(s): A6H8N3 , O95649, Q53X85, Q5VXA9, Q8NIA1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	May 30, 2000
Last modified:	June 16, 2009
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)