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P12318

- FCG2A_HUMAN

UniProt

P12318 - FCG2A_HUMAN

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Protein
Low affinity immunoglobulin gamma Fc region receptor II-a
Gene
FCGR2A, CD32, FCG2, FCGR2A1, IGFR2
Organism
Homo sapiens (Human)
Status
Reviewed - 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

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

Organism-specific databases

HGNCiHGNC:3616. FCGR2A.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini34 – 217184Extracellular Reviewed prediction
Add
BLAST
Transmembranei218 – 24023Helical; Reviewed prediction
Add
BLAST
Topological domaini241 – 31777Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

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

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 Publication
Add
BLAST
Chaini34 – 317284Low affinity immunoglobulin gamma Fc region receptor II-a
PRO_0000015145Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi62 ↔ 1042 Publications
Glycosylationi97 – 971N-linked (GlcNAc...)1 Publication
Disulfide bondi143 ↔ 1872 Publications
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

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.3 Publications

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP12318.

Family & Domainsi

Domains and Repeats

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

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.
VSP_036865

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21T → A in AAA35827. 1 Publication

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...

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

« 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: September 3, 2014
This is version 166 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

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