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Protein

Low affinity immunoglobulin gamma Fc region receptor II-a

Gene

FCGR2A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds to the Fc region of immunoglobulins gamma. Low affinity receptor. By binding to IgG it initiates cellular responses against pathogens and soluble antigens. Promotes phagocytosis of opsonized antigens.1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Immunity

Keywords - Ligandi

IgG-binding protein

Enzyme and pathway databases

ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_160158. Role of phospholipids in phagocytosis.
REACT_160274. FCGR activation.

Names & Taxonomyi

Protein namesi
Recommended name:
Low affinity immunoglobulin gamma Fc region receptor II-a
Short name:
IgG Fc receptor II-a
Alternative name(s):
CDw32
Fc-gamma RII-a
Short name:
Fc-gamma-RIIa
Short name:
FcRII-a
CD_antigen: CD32
Gene namesi
Name:FCGR2A
Synonyms:CD32, FCG2, FCGR2A1, IGFR2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:3616. FCGR2A.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini34 – 217184ExtracellularSequence AnalysisAdd
BLAST
Transmembranei218 – 24023HelicalSequence AnalysisAdd
BLAST
Topological domaini241 – 31777CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28063.

Chemistry

DrugBankiDB00054. 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. Intravenous Immunoglobulin.
DB00075. Muromonab.
DB00108. Natalizumab.
DB00110. Palivizumab.
DB00073. Rituximab.
DB00081. Tositumomab.
DB00072. Trastuzumab.

Polymorphism and mutation databases

BioMutaiFCGR2A.
DMDMi160332371.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 33331 PublicationAdd
BLAST
Chaini34 – 317284Low affinity immunoglobulin gamma Fc region receptor II-aPRO_0000015145Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi62 ↔ 104
Glycosylationi97 – 971N-linked (GlcNAc...)1 Publication
Disulfide bondi143 ↔ 187
Glycosylationi178 – 1781N-linked (GlcNAc...)1 Publication
Modified residuei288 – 2881Phosphotyrosine; by SRC-type Tyr-kinases1 Publication
Modified residuei304 – 3041Phosphotyrosine; by SRC-type Tyr-kinases1 Publication

Post-translational modificationi

Phosphorylated by SRC-type Tyr-kinases such as LYN, BLK, FYN, HCK and SYK.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP12318.
PRIDEiP12318.

PTM databases

PhosphoSiteiP12318.

Expressioni

Tissue specificityi

Found on monocytes, neutrophils and eosinophil platelets.

Gene expression databases

BgeeiP12318.
CleanExiHS_FCGR2A.
ExpressionAtlasiP12318. baseline and differential.
GenevestigatoriP12318.

Organism-specific databases

HPAiHPA010718.
HPA014730.

Interactioni

Subunit structurei

Interacts with INPP5D/SHIP1 and INPPL1/SHIP2, regulating its function. Interacts with APCS and FGR. Interacts with HCK.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
UBQLN1Q9UMX03EBI-1395970,EBI-741480
UBQLN1Q9UMX0-23EBI-1395970,EBI-10173939

Protein-protein interaction databases

BioGridi108506. 25 interactions.
IntActiP12318. 3 interactions.
MINTiMINT-8013486.
STRINGi9606.ENSP00000271450.

Structurei

Secondary structure

1
317
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi42 – 476Combined sources
Beta strandi50 – 534Combined sources
Beta strandi57 – 648Combined sources
Beta strandi68 – 714Combined sources
Beta strandi73 – 775Combined sources
Beta strandi80 – 823Combined sources
Beta strandi87 – 937Combined sources
Helixi96 – 983Combined sources
Beta strandi100 – 1067Combined sources
Beta strandi107 – 1104Combined sources
Beta strandi115 – 1206Combined sources
Beta strandi123 – 1275Combined sources
Beta strandi131 – 1333Combined sources
Beta strandi139 – 1457Combined sources
Helixi146 – 1483Combined sources
Beta strandi151 – 1588Combined sources
Beta strandi161 – 1688Combined sources
Beta strandi171 – 1766Combined sources
Helixi179 – 1813Combined sources
Beta strandi183 – 1919Combined sources
Beta strandi194 – 1974Combined sources
Beta strandi201 – 2055Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FCGX-ray2.00A34-207[»]
1H9VX-ray3.00A37-208[»]
3D5OX-ray2.80F37-207[»]
3RY4X-ray1.50A37-206[»]
3RY5X-ray2.30A37-206[»]
3RY6X-ray3.80C40-206[»]
ProteinModelPortaliP12318.
SMRiP12318. Positions 37-207.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12318.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 11880Ig-like C2-type 1Add
BLAST
Domaini122 – 20483Ig-like C2-type 2Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG25177.
GeneTreeiENSGT00760000119130.
HOGENOMiHOG000251632.
HOVERGENiHBG051602.
InParanoidiP12318.
KOiK06472.
OMAiDLEPPWI.
OrthoDBiEOG708W0N.
PhylomeDBiP12318.
TreeFamiTF335097.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
SMARTiSM00409. IG. 2 hits.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P12318-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MTMETQMSQN VCPRNLWLLQ PLTVLLLLAS ADSQAAAPPK AVLKLEPPWI
60 70 80 90 100
NVLQEDSVTL TCQGARSPES DSIQWFHNGN LIPTHTQPSY RFKANNNDSG
110 120 130 140 150
EYTCQTGQTS LSDPVHLTVL SEWLVLQTPH LEFQEGETIM LRCHSWKDKP
160 170 180 190 200
LVKVTFFQNG KSQKFSHLDP TFSIPQANHS HSGDYHCTGN IGYTLFSSKP
210 220 230 240 250
VTITVQVPSM GSSSPMGIIV AVVIATAVAA IVAAVVALIY CRKKRISANS
260 270 280 290 300
TDPVKAAQFE PPGRQMIAIR KRQLEETNND YETADGGYMT LNPRAPTDDD
310
KNIYLTLPPN DHVNSNN
Length:317
Mass (Da):35,001
Last modified:November 13, 2007 - v4
Checksum:i07F73F3BB282DFF6
GO
Isoform 2 (identifier: P12318-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     35-35: Missing.

Show »
Length:316
Mass (Da):34,930
Checksum:i3B4B813ECF6DCFCD
GO

Sequence cautioni

The sequence AAA35932.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21T → A in AAA35827 (PubMed:2529342).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti63 – 631Q → R.
Corresponds to variant rs9427398 [ dbSNP | Ensembl ].
VAR_054857
Natural varianti140 – 1401M → V.
Corresponds to variant rs4986941 [ dbSNP | Ensembl ].
VAR_054858
Natural varianti167 – 1671H → R May be associated with susceptibility to lupus nephritis; does not efficiently recognize IgG2. 6 Publications
Corresponds to variant rs1801274 [ dbSNP | Ensembl ].
VAR_003955
Natural varianti218 – 2181I → V.1 Publication
Corresponds to variant rs17851834 [ dbSNP | Ensembl ].
VAR_054859

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei35 – 351Missing in isoform 2. 1 PublicationVSP_036865

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00644 mRNA. Translation: CAA68672.1.
M31932 mRNA. Translation: AAA35827.1.
AL590385 Genomic DNA. No translation available.
BC019931 mRNA. Translation: AAH19931.1.
BC020823 mRNA. Translation: AAH20823.1.
J03619 mRNA. Translation: AAA35932.1. Different initiation.
CCDSiCCDS30922.1. [P12318-2]
CCDS44264.1. [P12318-1]
PIRiJL0118.
RefSeqiNP_001129691.1. NM_001136219.1. [P12318-1]
NP_067674.2. NM_021642.3. [P12318-2]
UniGeneiHs.352642.

Genome annotation databases

EnsembliENST00000271450; ENSP00000271450; ENSG00000143226. [P12318-1]
ENST00000367972; ENSP00000356949; ENSG00000143226. [P12318-2]
GeneIDi2212.
KEGGihsa:2212.
UCSCiuc001gam.3. human. [P12318-2]
uc001gan.3. human. [P12318-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00644 mRNA. Translation: CAA68672.1.
M31932 mRNA. Translation: AAA35827.1.
AL590385 Genomic DNA. No translation available.
BC019931 mRNA. Translation: AAH19931.1.
BC020823 mRNA. Translation: AAH20823.1.
J03619 mRNA. Translation: AAA35932.1. Different initiation.
CCDSiCCDS30922.1. [P12318-2]
CCDS44264.1. [P12318-1]
PIRiJL0118.
RefSeqiNP_001129691.1. NM_001136219.1. [P12318-1]
NP_067674.2. NM_021642.3. [P12318-2]
UniGeneiHs.352642.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FCGX-ray2.00A34-207[»]
1H9VX-ray3.00A37-208[»]
3D5OX-ray2.80F37-207[»]
3RY4X-ray1.50A37-206[»]
3RY5X-ray2.30A37-206[»]
3RY6X-ray3.80C40-206[»]
ProteinModelPortaliP12318.
SMRiP12318. Positions 37-207.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108506. 25 interactions.
IntActiP12318. 3 interactions.
MINTiMINT-8013486.
STRINGi9606.ENSP00000271450.

Chemistry

BindingDBiP12318.
ChEMBLiCHEMBL5841.
DrugBankiDB00054. 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. Intravenous Immunoglobulin.
DB00075. Muromonab.
DB00108. Natalizumab.
DB00110. Palivizumab.
DB00073. Rituximab.
DB00081. Tositumomab.
DB00072. Trastuzumab.

PTM databases

PhosphoSiteiP12318.

Polymorphism and mutation databases

BioMutaiFCGR2A.
DMDMi160332371.

Proteomic databases

PaxDbiP12318.
PRIDEiP12318.

Protocols and materials databases

DNASUi2212.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000271450; ENSP00000271450; ENSG00000143226. [P12318-1]
ENST00000367972; ENSP00000356949; ENSG00000143226. [P12318-2]
GeneIDi2212.
KEGGihsa:2212.
UCSCiuc001gam.3. human. [P12318-2]
uc001gan.3. human. [P12318-1]

Organism-specific databases

CTDi2212.
GeneCardsiGC01P161475.
H-InvDBHIX0018571.
HGNCiHGNC:3616. FCGR2A.
HPAiHPA010718.
HPA014730.
MIMi146790. gene.
neXtProtiNX_P12318.
PharmGKBiPA28063.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG25177.
GeneTreeiENSGT00760000119130.
HOGENOMiHOG000251632.
HOVERGENiHBG051602.
InParanoidiP12318.
KOiK06472.
OMAiDLEPPWI.
OrthoDBiEOG708W0N.
PhylomeDBiP12318.
TreeFamiTF335097.

Enzyme and pathway databases

ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_160158. Role of phospholipids in phagocytosis.
REACT_160274. FCGR activation.

Miscellaneous databases

ChiTaRSiFCGR2A. human.
EvolutionaryTraceiP12318.
GeneWikiiFCGR2A.
GenomeRNAii2212.
NextBioi8961.
PROiP12318.
SOURCEiSearch...

Gene expression databases

BgeeiP12318.
CleanExiHS_FCGR2A.
ExpressionAtlasiP12318. baseline and differential.
GenevestigatoriP12318.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
SMARTiSM00409. IG. 2 hits.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and expression of cDNA clones encoding a human receptor for IgG (Fc gamma RII)."
    Stuart S.G., Trounstine M.L., Vaux D.J.T., Koch T., Martens C.L., Moore K.W.
    J. Exp. Med. 166:1668-1684(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-167.
  2. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-167.
  3. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS ARG-167 AND VAL-218.
    Tissue: Lung and Testis.
  5. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-317 (ISOFORM 1), VARIANT ARG-167.
  6. "Isolation of cDNAs for two distinct human Fc receptors by ligand affinity cloning."
    Stengelin S., Stamenkovic I., Seed B.
    EMBO J. 7:1053-1059(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-317 (ISOFORM 1), VARIANT ARG-167.
  7. "Identification of multiple isoforms of the low-affinity human IgG Fc receptor."
    Seki T.
    Immunogenetics 30:5-12(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-317 (ISOFORM 1).
  8. "Biochemical analysis and crystallisation of Fc gamma RIIa, the low affinity receptor for IgG."
    Powell M.S., Barton P.A., Emmanouilidis D., Wines B.D., Neumann G.M., Peitersz G.A., Maxwell K.F., Garrett T.P., Hogarth P.M.
    Immunol. Lett. 68:17-23(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF N-TERMINUS, GLYCOSYLATION AT ASN-97 AND ASN-178, CRYSTALLIZATION.
  9. "Association of immunoglobulin G Fc receptor II with Src-like protein-tyrosine kinase Fgr in neutrophils."
    Hamada F., Aoki M., Akiyama T., Toyoshima K.
    Proc. Natl. Acad. Sci. U.S.A. 90:6305-6309(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FGR.
  10. "Physical and functional association of Src-related protein tyrosine kinases with Fc gamma RII in monocytic THP-1 cells."
    Ghazizadeh S., Bolen J.B., Fleit H.B.
    J. Biol. Chem. 269:8878-8884(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HCK, PHOSPHORYLATION.
  11. "In vivo and in vitro specificity of protein tyrosine kinases for immunoglobulin G receptor (FcgammaRII) phosphorylation."
    Bewarder N., Weinrich V., Budde P., Hartmann D., Flaswinkel H., Reth M., Frey J.
    Mol. Cell. Biol. 16:4735-4743(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-288 AND TYR-304.
  12. "SHIP-2 inositol phosphatase is inducibly expressed in human monocytes and serves to regulate Fcgamma receptor-mediated signaling."
    Pengal R.A., Ganesan L.P., Fang H., Marsh C.B., Anderson C.L., Tridandapani S.
    J. Biol. Chem. 278:22657-22663(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INPPL1.
  13. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 37-207.
  14. "Molecular basis for immune complex recognition: a comparison of Fc-receptor structures."
    Sondermann P., Kaiser J., Jacob U.
    J. Mol. Biol. 309:737-749(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 37-208, DISULFIDE BONDS.
  15. "Structural recognition and functional activation of FcgammaR by innate pentraxins."
    Lu J., Marnell L.L., Marjon K.D., Mold C., Du Clos T.W., Sun P.D.
    Nature 456:989-992(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 37-207 IN COMPLEX WITH APCS, SUBCELLULAR LOCATION, FUNCTION, DISULFIDE BONDS.
  16. "Fc gamma RIIA alleles are heritable risk factors for lupus nephritis in African Americans."
    Salmon J.E., Millard S., Schachter L.A., Arnett F.C., Ginzler E.M., Gourley M.F., Ramsey-Goldman R., Peterson M.G.E., Kimberly R.P.
    J. Clin. Invest. 97:1348-1354(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ARG-167.

Entry informationi

Entry nameiFCG2A_HUMAN
AccessioniPrimary (citable) accession number: P12318
Secondary accession number(s): Q8WUN1, Q8WW64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 13, 2007
Last modified: May 27, 2015
This is version 173 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.