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P12314

- FCGR1_HUMAN

UniProt

P12314 - FCGR1_HUMAN

Protein

High affinity immunoglobulin gamma Fc receptor I

Gene

FCGR1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 2 (19 Jul 2004)
      Previous versions | rss
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    Functioni

    High affinity receptor for the Fc region of immunoglobulins gamma. Functions in both innate and adaptive immune responses.5 Publications

    GO - Molecular functioni

    1. protein binding Source: BHF-UCL
    2. receptor signaling protein activity Source: ProtInc

    GO - Biological processi

    1. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
    2. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
    3. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
    4. cytokine-mediated signaling pathway Source: Reactome
    5. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    6. immune response Source: ProtInc
    7. innate immune response Source: Reactome
    8. interferon-gamma-mediated signaling pathway Source: Reactome
    9. intracellular signal transduction Source: GOC
    10. phagocytosis, engulfment Source: ProtInc
    11. signal transduction Source: ProtInc

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Immunity, Innate immunity

    Keywords - Ligandi

    IgG-binding protein

    Enzyme and pathway databases

    ReactomeiREACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_160158. Role of phospholipids in phagocytosis.
    REACT_160274. FCGR activation.
    REACT_25078. Interferon gamma signaling.
    SignaLinkiP12314.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    High affinity immunoglobulin gamma Fc receptor I
    Short name:
    IgG Fc receptor I
    Alternative name(s):
    Fc-gamma RI
    Short name:
    FcRI
    Fc-gamma RIA
    Short name:
    FcgammaRIa
    CD_antigen: CD64
    Gene namesi
    Name:FCGR1A
    Synonyms:FCG1, FCGR1, IGFR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3613. FCGR1A.

    Subcellular locationi

    Cell membrane 2 Publications; Single-pass type I membrane protein 2 Publications
    Note: Stabilized at the cell membrane through interaction with FCER1G.

    GO - Cellular componenti

    1. clathrin-coated endocytic vesicle membrane Source: Reactome
    2. early endosome membrane Source: Reactome
    3. integral component of membrane Source: UniProtKB-KW
    4. plasma membrane Source: BHF-UCL

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi306 – 3061N → D: Decreases cell membrane expression by 50% in absence of FCER1G. 1 Publication
    Mutagenesisi306 – 3061N → G: Increases cell membrane expression in absence of FCER1G. 1 Publication

    Organism-specific databases

    PharmGKBiPA28060.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 15151 PublicationAdd
    BLAST
    Chaini16 – 374359High affinity immunoglobulin gamma Fc receptor IPRO_0000015139Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi43 ↔ 851 PublicationPROSITE-ProRule annotation
    Glycosylationi59 – 591N-linked (GlcNAc...)2 Publications
    Glycosylationi78 – 781N-linked (GlcNAc...)3 Publications
    Disulfide bondi124 ↔ 1681 PublicationPROSITE-ProRule annotation
    Glycosylationi152 – 1521N-linked (GlcNAc...)2 Publications
    Glycosylationi159 – 1591N-linked (GlcNAc...)2 Publications
    Glycosylationi163 – 1631N-linked (GlcNAc...)2 Publications
    Glycosylationi195 – 1951N-linked (GlcNAc...)2 Publications
    Disulfide bondi212 ↔ 2601 PublicationPROSITE-ProRule annotation
    Glycosylationi240 – 2401N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Phosphorylated on serine residues.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP12314.
    PRIDEiP12314.

    PTM databases

    PhosphoSiteiP12314.

    Expressioni

    Tissue specificityi

    Monocyte/macrophage specific.

    Gene expression databases

    BgeeiP12314.
    CleanExiHS_FCGR1A.
    GenevestigatoriP12314.

    Interactioni

    Subunit structurei

    Interacts with FCERG1; forms a functional signaling complex. Interacts with FLNA; prevents FCGR1A degradation. Interacts with EPB41L2, LAT and PPL. Interacts with HCK and LYN.7 Publications

    Protein-protein interaction databases

    BioGridi108503. 5 interactions.
    IntActiP12314. 3 interactions.
    MINTiMINT-1538623.
    STRINGi9606.ENSP00000358165.

    Structurei

    Secondary structure

    1
    374
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi23 – 286
    Beta strandi31 – 344
    Beta strandi39 – 446
    Beta strandi54 – 585
    Beta strandi67 – 748
    Helixi77 – 793
    Beta strandi81 – 9010
    Beta strandi96 – 1016
    Beta strandi103 – 1108
    Beta strandi112 – 1154
    Beta strandi120 – 1267
    Helixi127 – 1293
    Beta strandi133 – 1397
    Beta strandi142 – 1498
    Beta strandi153 – 1575
    Helixi160 – 1623
    Beta strandi164 – 17916
    Beta strandi181 – 1866
    Beta strandi193 – 1986
    Beta strandi200 – 2034
    Beta strandi208 – 2136
    Beta strandi225 – 2317
    Beta strandi234 – 2418
    Beta strandi244 – 2496
    Helixi252 – 2543
    Beta strandi256 – 2649
    Beta strandi270 – 2723
    Beta strandi276 – 2783

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3RJDX-ray2.65A21-282[»]
    ProteinModelPortaliP12314.
    SMRiP12314. Positions 21-282.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini16 – 292277ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini314 – 37461CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei293 – 31321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 10180Ig-like C2-type 1Add
    BLAST
    Domaini95 – 18490Ig-like C2-type 2Add
    BLAST
    Domaini190 – 27788Ig-like C2-type 3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni312 – 33221Interaction with EPB41L2Add
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG277652.
    HOGENOMiHOG000251632.
    HOVERGENiHBG051602.
    InParanoidiP12314.
    KOiK06498.
    OMAiRNSEFTI.
    PhylomeDBiP12314.
    TreeFamiTF335097.

    Family and domain databases

    Gene3Di2.60.40.10. 3 hits.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    IPR013151. Immunoglobulin.
    [Graphical view]
    PfamiPF00047. ig. 1 hit.
    [Graphical view]
    SMARTiSM00409. IG. 2 hits.
    SM00408. IGc2. 1 hit.
    [Graphical view]
    PROSITEiPS50835. IG_LIKE. 3 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: P12314-1) [UniParc]FASTAAdd to Basket

    Also known as: A

    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

    MWFLTTLLLW VPVDGQVDTT KAVITLQPPW VSVFQEETVT LHCEVLHLPG    50
    SSSTQWFLNG TATQTSTPSY RITSASVNDS GEYRCQRGLS GRSDPIQLEI 100
    HRGWLLLQVS SRVFTEGEPL ALRCHAWKDK LVYNVLYYRN GKAFKFFHWN 150
    SNLTILKTNI SHNGTYHCSG MGKHRYTSAG ISVTVKELFP APVLNASVTS 200
    PLLEGNLVTL SCETKLLLQR PGLQLYFSFY MGSKTLRGRN TSSEYQILTA 250
    RREDSGLYWC EAATEDGNVL KRSPELELQV LGLQLPTPVW FHVLFYLAVG 300
    IMFLVNTVLW VTIRKELKRK KKWDLEISLD SGHEKKVISS LQEDRHLEEE 350
    LKCQEQKEEQ LQEGVHRKEP QGAT 374
    Length:374
    Mass (Da):42,632
    Last modified:July 19, 2004 - v2
    Checksum:iD33D59398CEEA699
    GO
    Isoform 2 (identifier: P12314-2) [UniParc]FASTAAdd to Basket

    Also known as: B

    The sequence of this isoform differs from the canonical sequence as follows:
         333-374: HEKKVISSLQEDRHLEEELKCQEQKEEQLQEGVHRKEPQGAT → GQALEAPTQGCA

    Show »
    Length:344
    Mass (Da):38,795
    Checksum:iDDBE5DE64A66F6B8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251T → S in CAA32537. (PubMed:2974947)Curated
    Sequence conflicti115 – 1151T → M in AAA58414. (PubMed:1402657)Curated
    Sequence conflicti183 – 1831V → QY in AAA58414. (PubMed:1402657)Curated
    Sequence conflicti284 – 2841Q → R in AAA58414. (PubMed:1402657)Curated
    Sequence conflicti324 – 3241D → N in AAA58414. (PubMed:1402657)Curated
    Sequence conflicti338 – 3381I → T(PubMed:2974947)Curated
    Sequence conflicti338 – 3381I → T(PubMed:2911749)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti105 – 1051L → P.
    Corresponds to variant rs619322 [ dbSNP | Ensembl ].
    VAR_019522

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei333 – 37442HEKKV…PQGAT → GQALEAPTQGCA in isoform 2. 1 PublicationVSP_002637Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14356 mRNA. Translation: CAA32537.1.
    X14355 mRNA. Translation: CAA32536.1.
    L03418 mRNA. Translation: AAA36049.1.
    M91555
    , M91550, M91551, M91552, M91553, M91554 Genomic DNA. Translation: AAA58414.1.
    AL591493 Genomic DNA. Translation: CAI12557.1.
    CCDSiCCDS933.1. [P12314-1]
    PIRiA39878.
    A41357.
    RefSeqiNP_000557.1. NM_000566.3. [P12314-1]
    UniGeneiHs.77424.

    Genome annotation databases

    EnsembliENST00000369168; ENSP00000358165; ENSG00000150337. [P12314-1]
    GeneIDi2209.
    KEGGihsa:2209.
    UCSCiuc001esp.4. human. [P12314-1]

    Polymorphism databases

    DMDMi50403717.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    FCGR1Abase

    FCGR1A mutation db

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14356 mRNA. Translation: CAA32537.1 .
    X14355 mRNA. Translation: CAA32536.1 .
    L03418 mRNA. Translation: AAA36049.1 .
    M91555
    , M91550 , M91551 , M91552 , M91553 , M91554 Genomic DNA. Translation: AAA58414.1 .
    AL591493 Genomic DNA. Translation: CAI12557.1 .
    CCDSi CCDS933.1. [P12314-1 ]
    PIRi A39878.
    A41357.
    RefSeqi NP_000557.1. NM_000566.3. [P12314-1 ]
    UniGenei Hs.77424.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3RJD X-ray 2.65 A 21-282 [» ]
    ProteinModelPortali P12314.
    SMRi P12314. Positions 21-282.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108503. 5 interactions.
    IntActi P12314. 3 interactions.
    MINTi MINT-1538623.
    STRINGi 9606.ENSP00000358165.

    Chemistry

    BindingDBi P12314.
    ChEMBLi CHEMBL5349.
    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.
    DB00992. Methyl aminolevulinate.
    DB00075. Muromonab.
    DB00108. Natalizumab.
    DB00110. Palivizumab.
    DB00707. Porfimer.
    DB00073. Rituximab.
    DB00081. Tositumomab.
    DB00072. Trastuzumab.

    PTM databases

    PhosphoSitei P12314.

    Polymorphism databases

    DMDMi 50403717.

    Proteomic databases

    PaxDbi P12314.
    PRIDEi P12314.

    Protocols and materials databases

    DNASUi 2209.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369168 ; ENSP00000358165 ; ENSG00000150337 . [P12314-1 ]
    GeneIDi 2209.
    KEGGi hsa:2209.
    UCSCi uc001esp.4. human. [P12314-1 ]

    Organism-specific databases

    CTDi 2209.
    GeneCardsi GC01P149754.
    H-InvDB HIX0000999.
    HGNCi HGNC:3613. FCGR1A.
    MIMi 146760. gene.
    neXtProti NX_P12314.
    PharmGKBi PA28060.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG277652.
    HOGENOMi HOG000251632.
    HOVERGENi HBG051602.
    InParanoidi P12314.
    KOi K06498.
    OMAi RNSEFTI.
    PhylomeDBi P12314.
    TreeFami TF335097.

    Enzyme and pathway databases

    Reactomei REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_160158. Role of phospholipids in phagocytosis.
    REACT_160274. FCGR activation.
    REACT_25078. Interferon gamma signaling.
    SignaLinki P12314.

    Miscellaneous databases

    GeneWikii FCGR1A.
    GenomeRNAii 2209.
    NextBioi 8947.
    PROi P12314.
    SOURCEi Search...

    Gene expression databases

    Bgeei P12314.
    CleanExi HS_FCGR1A.
    Genevestigatori P12314.

    Family and domain databases

    Gene3Di 2.60.40.10. 3 hits.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    IPR013151. Immunoglobulin.
    [Graphical view ]
    Pfami PF00047. ig. 1 hit.
    [Graphical view ]
    SMARTi SM00409. IG. 2 hits.
    SM00408. IGc2. 1 hit.
    [Graphical view ]
    PROSITEi PS50835. IG_LIKE. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of three cDNAs for the human high affinity Fc receptor (FcRI)."
      Allen J.M., Seed B.
      Nucleic Acids Res. 16:11824-11824(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    2. "Isolation and expression of functional high-affinity Fc receptor complementary DNAs."
      Allen J.M., Seed B.
      Science 243:378-381(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Novel Fc gamma receptor I family gene products in human mononuclear cells."
      Porges A.J., Redecha P.B., Doebele R., Pan L.C., Salmon J.E., Kimberly R.P.
      J. Clin. Invest. 90:2102-2109(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Blood.
    4. "Definition of interferon gamma-response elements in a novel human Fc gamma receptor gene (Fc gamma RIb) and characterization of the gene structure."
      Benech P.D., Sastry K.N., Iyer R.R., Eichbaum Q.G., Raveh D.P., Ezekowitz R.A.
      J. Exp. Med. 176:1115-1123(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Blood.
    5. "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].
    6. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 16-30.
    7. "Three genes for the human high affinity Fc receptor for IgG (Fc gamma RI) encode four distinct transcription products."
      Ernst L.K., van de Winkel J.G., Chiu I.M., Anderson C.L.
      J. Biol. Chem. 267:15692-15700(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING.
    8. "Physical and functional association of the high affinity immunoglobulin G receptor (Fc gamma RI) with the kinases Hck and Lyn."
      Wang A.V., Scholl P.R., Geha R.S.
      J. Exp. Med. 180:1165-1170(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HCK AND LYN.
    9. "FcR gamma-chain is essential for both surface expression and function of human Fc gamma RI (CD64) in vivo."
      van Vugt M.J., Heijnen I.A.F.M., Capel P.J.A., Park S.Y., Ra C., Saito T., Verbeek J.S., van de Winkel J.G.J.
      Blood 87:3593-3599(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FCER1G, SUBCELLULAR LOCATION.
    10. "Molecular characterization of six variant Fcgamma receptor class I (CD64) transcripts."
      Ernst L.K., Duchemin A.-M., Miller K.L., Anderson C.L.
      Mol. Immunol. 35:943-954(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ALTERNATIVE SPLICING, GLYCOSYLATION.
    11. "The FcgammaRIa (CD64) ligand binding chain triggers major histocompatibility complex class II antigen presentation independently of its associated FcR gamma-chain."
      van Vugt M.J., Kleijmeer M.J., Keler T., Zeelenberg I., van Dijk M.A., Leusen J.H.W., Geuze H.J., van de Winkel J.G.J.
      Blood 94:808-817(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "The cytoplasmic domain of human FcgammaRIa alters the functional properties of the FcgammaRI.gamma-chain receptor complex."
      Edberg J.C., Yee A.M., Rakshit D.S., Chang D.J., Gokhale J.A., Indik Z.K., Schreiber A.D., Kimberly R.P.
      J. Biol. Chem. 274:30328-30333(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FCER1G.
    13. "The adapter protein LAT enhances fcgamma receptor-mediated signal transduction in myeloid cells."
      Tridandapani S., Lyden T.W., Smith J.L., Carter J.E., Coggeshall K.M., Anderson C.L.
      J. Biol. Chem. 275:20480-20487(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LAT.
    14. "Fcgamma receptor transmembrane domains: role in cell surface expression, gamma chain interaction, and phagocytosis."
      Kim M.-K., Huang Z.-Y., Hwang P.-H., Jones B.A., Sato N., Hunter S., Kim-Han T.-H., Worth R.G., Indik Z.K., Schreiber A.D.
      Blood 101:4479-4484(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASN-306, SUBCELLULAR LOCATION.
    15. "Direct interaction between FcgammaRI (CD64) and periplakin controls receptor endocytosis and ligand binding capacity."
      Beekman J.M., Bakema J.E., van de Winkel J.G.J., Leusen J.H.W.
      Proc. Natl. Acad. Sci. U.S.A. 101:10392-10397(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPL.
    16. Cited for: INTERACTION WITH FLNA.
    17. Cited for: INTERACTION WITH EPB41L2.
    18. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78.
      Tissue: Liver.
    19. "Crystal structure of Fcgamma receptor I and its implication in high affinity gamma-immunoglobulin binding."
      Lu J., Ellsworth J.L., Hamacher N., Oak S.W., Sun P.D.
      J. Biol. Chem. 286:40608-40613(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 21-282, FUNCTION, DISULFIDE BONDS, GLYCOSYLATION AT ASN-59; ASN-78; ASN-152; ASN-159; ASN-163 AND ASN-195.

    Entry informationi

    Entry nameiFCGR1_HUMAN
    AccessioniPrimary (citable) accession number: P12314
    Secondary accession number(s): P12315
    , Q5QNW7, Q92495, Q92663
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 157 of the entry and version 2 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