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P12314

- FCGR1_HUMAN

UniProt

P12314 - FCGR1_HUMAN

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Protein

High affinity immunoglobulin gamma Fc receptor I

Gene
FCGR1A, FCG1, FCGR1, IGFR1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini16 – 292277Extracellular Reviewed predictionAdd
BLAST
Transmembranei293 – 31321Helical; Reviewed predictionAdd
BLAST
Topological domaini314 – 37461Cytoplasmic Reviewed predictionAdd
BLAST

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
Complete GO annotation...

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 Publication
Glycosylationi59 – 591N-linked (GlcNAc...)1 Publication
Glycosylationi78 – 781N-linked (GlcNAc...)2 Publications
Disulfide bondi124 ↔ 1681 Publication
Glycosylationi152 – 1521N-linked (GlcNAc...)1 Publication
Glycosylationi159 – 1591N-linked (GlcNAc...)1 Publication
Glycosylationi163 – 1631N-linked (GlcNAc...)1 Publication
Glycosylationi195 – 1951N-linked (GlcNAc...)1 Publication
Disulfide bondi212 ↔ 2601 Publication
Glycosylationi240 – 2401N-linked (GlcNAc...) Reviewed prediction

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. 1 interaction.
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.

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

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. VSP_002637Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251T → S in CAA32537. 1 Publication
Sequence conflicti115 – 1151T → M in AAA58414. 1 Publication
Sequence conflicti183 – 1831V → QY in AAA58414. 1 Publication
Sequence conflicti284 – 2841Q → R in AAA58414. 1 Publication
Sequence conflicti324 – 3241D → N in AAA58414. 1 Publication
Sequence conflicti338 – 3381I → T1 Publication
Sequence conflicti338 – 3381I → T1 Publication

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]
ENST00000580698; ENSP00000462402; ENSG00000266332. [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. 1 interaction.
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 ]
ENST00000580698 ; ENSP00000462402 ; ENSG00000266332 . [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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 156 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

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