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P12318

- FCG2A_HUMAN

UniProt

P12318 - FCG2A_HUMAN

Protein

Low affinity immunoglobulin gamma Fc region receptor II-a

Gene

FCGR2A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 4 (13 Nov 2007)
      Previous versions | rss
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    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

    1. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    2. innate immune response Source: Reactome

    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: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3616. FCGR2A.

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. integral component of membrane Source: UniProtKB-KW
    3. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28063.

    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-kinases2 Publications
    Modified residuei304 – 3041Phosphotyrosine; by SRC-type Tyr-kinases2 Publications

    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

    ArrayExpressiP12318.
    BgeeiP12318.
    CleanExiHS_FCGR2A.
    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

    Protein-protein interaction databases

    BioGridi108506. 10 interactions.
    IntActiP12318. 2 interactions.
    MINTiMINT-8013486.
    STRINGi9606.ENSP00000271450.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei218 – 24023HelicalSequence AnalysisAdd
    BLAST

    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.
    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. Align

    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

    MTMETQMSQN VCPRNLWLLQ PLTVLLLLAS ADSQAAAPPK AVLKLEPPWI    50
    NVLQEDSVTL TCQGARSPES DSIQWFHNGN LIPTHTQPSY RFKANNNDSG 100
    EYTCQTGQTS LSDPVHLTVL SEWLVLQTPH LEFQEGETIM LRCHSWKDKP 150
    LVKVTFFQNG KSQKFSHLDP TFSIPQANHS HSGDYHCTGN IGYTLFSSKP 200
    VTITVQVPSM GSSSPMGIIV AVVIATAVAA IVAAVVALIY CRKKRISANS 250
    TDPVKAAQFE PPGRQMIAIR KRQLEETNND YETADGGYMT LNPRAPTDDD 300
    KNIYLTLPPN DHVNSNN 317
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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]

    Polymorphism databases

    DMDMi160332371.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS30922.1. [P12318-2 ]
    CCDS44264.1. [P12318-1 ]
    PIRi JL0118.
    RefSeqi NP_001129691.1. NM_001136219.1. [P12318-1 ]
    NP_067674.2. NM_021642.3. [P12318-2 ]
    UniGenei Hs.352642.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FCG X-ray 2.00 A 34-207 [» ]
    1H9V X-ray 3.00 A 37-208 [» ]
    3D5O X-ray 2.80 F 37-207 [» ]
    3RY4 X-ray 1.50 A 37-206 [» ]
    3RY5 X-ray 2.30 A 37-206 [» ]
    3RY6 X-ray 3.80 C 40-206 [» ]
    ProteinModelPortali P12318.
    SMRi P12318. Positions 37-207.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108506. 10 interactions.
    IntActi P12318. 2 interactions.
    MINTi MINT-8013486.
    STRINGi 9606.ENSP00000271450.

    Chemistry

    BindingDBi P12318.
    ChEMBLi CHEMBL5841.
    DrugBanki 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.

    PTM databases

    PhosphoSitei P12318.

    Polymorphism databases

    DMDMi 160332371.

    Proteomic databases

    PaxDbi P12318.
    PRIDEi P12318.

    Protocols and materials databases

    DNASUi 2212.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000271450 ; ENSP00000271450 ; ENSG00000143226 . [P12318-1 ]
    ENST00000367972 ; ENSP00000356949 ; ENSG00000143226 . [P12318-2 ]
    GeneIDi 2212.
    KEGGi hsa:2212.
    UCSCi uc001gam.3. human. [P12318-2 ]
    uc001gan.3. human. [P12318-1 ]

    Organism-specific databases

    CTDi 2212.
    GeneCardsi GC01P161475.
    H-InvDB HIX0018571.
    HGNCi HGNC:3616. FCGR2A.
    HPAi HPA010718.
    HPA014730.
    MIMi 146790. gene.
    neXtProti NX_P12318.
    PharmGKBi PA28063.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG25177.
    HOGENOMi HOG000251632.
    HOVERGENi HBG051602.
    InParanoidi P12318.
    KOi K06472.
    OMAi DLEPPWI.
    OrthoDBi EOG708W0N.
    PhylomeDBi P12318.
    TreeFami TF335097.

    Enzyme and pathway databases

    Reactomei REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_160158. Role of phospholipids in phagocytosis.
    REACT_160274. FCGR activation.

    Miscellaneous databases

    ChiTaRSi FCGR2A. human.
    EvolutionaryTracei P12318.
    GeneWikii FCGR2A.
    GenomeRNAii 2212.
    NextBioi 8961.
    PROi P12318.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P12318.
    Bgeei P12318.
    CleanExi HS_FCGR2A.
    Genevestigatori P12318.

    Family and domain databases

    Gene3Di 2.60.40.10. 2 hits.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    [Graphical view ]
    SMARTi SM00409. IG. 2 hits.
    [Graphical view ]
    PROSITEi PS50835. IG_LIKE. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 167 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

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