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P12319

- FCERA_HUMAN

UniProt

P12319 - FCERA_HUMAN

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Protein
High affinity immunoglobulin epsilon receptor subunit alpha
Gene
FCER1A, FCE1A
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 epsilon. High affinity receptor. Responsible for initiating the allergic response. Binding of allergen to receptor-bound IgE leads to cell activation and the release of mediators (such as histamine) responsible for the manifestations of allergy. The same receptor also induces the secretion of important lymphokines.

GO - Molecular functioni

  1. IgE receptor activity Source: Ensembl
Complete GO annotation...

GO - Biological processi

  1. Fc-epsilon receptor signaling pathway Source: Reactome
  2. activation of JUN kinase activity Source: Ensembl
  3. innate immune response Source: Reactome
  4. leukotriene biosynthetic process Source: Ensembl
  5. positive regulation of calcium-mediated signaling Source: Ensembl
  6. positive regulation of granulocyte macrophage colony-stimulating factor biosynthetic process Source: Ensembl
  7. positive regulation of interleukin-3 biosynthetic process Source: Ensembl
  8. positive regulation of mast cell degranulation Source: Ensembl
  9. positive regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
  10. positive regulation of type I hypersensitivity Source: Ensembl
  11. serotonin secretion Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

IgE-binding protein

Enzyme and pathway databases

ReactomeiREACT_163701. FCERI mediated MAPK activation.
REACT_163769. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_163834. FCERI mediated Ca+2 mobilization.
REACT_163936. Fc epsilon receptor (FCERI) signaling.
REACT_163994. FCERI mediated NF-kB activation.

Names & Taxonomyi

Protein namesi
Recommended name:
High affinity immunoglobulin epsilon receptor subunit alpha
Alternative name(s):
Fc-epsilon RI-alpha
Short name:
FcERI
IgE Fc receptor subunit alpha
Gene namesi
Name:FCER1A
Synonyms:FCE1A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3609. FCER1A.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 205180Extracellular Reviewed prediction
Add
BLAST
Transmembranei206 – 22419Helical; Reviewed prediction
Add
BLAST
Topological domaini225 – 25733Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. cell surface Source: UniProtKB
  2. external side of plasma membrane Source: Ensembl
  3. integral component of plasma membrane Source: ProtInc
  4. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28056.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 25251 Publication
Add
BLAST
Chaini26 – 257232High affinity immunoglobulin epsilon receptor subunit alpha
PRO_0000015161Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi46 – 461N-linked (GlcNAc...)2 Publications
Disulfide bondi51 ↔ 932 Publications
Glycosylationi67 – 671N-linked (GlcNAc...)2 Publications
Glycosylationi75 – 751N-linked (GlcNAc...) Reviewed prediction
Glycosylationi99 – 991N-linked (GlcNAc...)1 Publication
Disulfide bondi132 ↔ 1762 Publications
Glycosylationi160 – 1601N-linked (GlcNAc...) Reviewed prediction
Glycosylationi165 – 1651N-linked (GlcNAc...)1 Publication
Glycosylationi191 – 1911N-linked (GlcNAc...)2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP12319.
PRIDEiP12319.

PTM databases

PhosphoSiteiP12319.

Expressioni

Gene expression databases

ArrayExpressiP12319.
BgeeiP12319.
CleanExiHS_FCER1A.
GenevestigatoriP12319.

Organism-specific databases

HPAiCAB022102.

Interactioni

Subunit structurei

Tetramer of an alpha chain, a beta chain, and two disulfide linked gamma chains.

Protein-protein interaction databases

BioGridi108499. 3 interactions.
DIPiDIP-6166N.
IntActiP12319. 1 interaction.
STRINGi9606.ENSP00000315719.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi33 – 375
Beta strandi39 – 424
Beta strandi47 – 504
Beta strandi53 – 553
Beta strandi63 – 664
Beta strandi69 – 724
Beta strandi75 – 806
Helixi85 – 873
Beta strandi89 – 946
Beta strandi96 – 994
Beta strandi104 – 1096
Beta strandi111 – 1188
Beta strandi120 – 1234
Beta strandi128 – 1347
Helixi135 – 1373
Beta strandi140 – 1478
Beta strandi150 – 1578
Beta strandi158 – 1658
Helixi168 – 1703
Beta strandi172 – 1809
Beta strandi183 – 1864
Beta strandi190 – 1956

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ALSmodel-A26-197[»]
1ALTmodel-A26-197[»]
1F2QX-ray2.40A26-201[»]
1F6AX-ray3.50A26-201[»]
1J86X-ray3.20A/B26-201[»]
1J87X-ray3.20A26-197[»]
1J88X-ray3.20A/B/C/D/E26-197[»]
1J89X-ray4.10A/B/C/D/E26-197[»]
1RPQX-ray3.00A/B/C/D26-201[»]
2Y7QX-ray3.40A26-201[»]
ProteinModelPortaliP12319.
SMRiP12319. Positions 26-199.

Miscellaneous databases

EvolutionaryTraceiP12319.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 11081Ig-like 1
Add
BLAST
Domaini111 – 19383Ig-like 2
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG27903.
HOGENOMiHOG000251632.
HOVERGENiHBG051602.
InParanoidiP12319.
KOiK08089.
OMAiYENHNIS.
OrthoDBiEOG72NRRC.
PhylomeDBiP12319.
TreeFamiTF335097.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P12319-1 [UniParc]FASTAAdd to Basket

« Hide

MAPAMESPTL LCVALLFFAP DGVLAVPQKP KVSLNPPWNR IFKGENVTLT    50
CNGNNFFEVS STKWFHNGSL SEETNSSLNI VNAKFEDSGE YKCQHQQVNE 100
SEPVYLEVFS DWLLLQASAE VVMEGQPLFL RCHGWRNWDV YKVIYYKDGE 150
ALKYWYENHN ISITNATVED SGTYYCTGKV WQLDYESEPL NITVIKAPRE 200
KYWLQFFIPL LVVILFAVDT GLFISTQQQV TFLLKIKRTR KGFRLLNPHP 250
KPNPKNN 257
Length:257
Mass (Da):29,596
Last modified:October 1, 1989 - v1
Checksum:iF183BB2357DDAD58
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti84 – 841K → R.
Corresponds to variant rs2298804 [ dbSNP | Ensembl ].
VAR_020091
Natural varianti101 – 1011S → N.
Corresponds to variant rs2298805 [ dbSNP | Ensembl ].
VAR_020092

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X06948 mRNA. Translation: CAA30025.1.
J03605 mRNA. Translation: AAA36204.1.
BC005912 mRNA. Translation: AAH05912.1.
CCDSiCCDS1184.1.
PIRiS00682.
RefSeqiNP_001992.1. NM_002001.3.
UniGeneiHs.897.

Genome annotation databases

EnsembliENST00000368115; ENSP00000357097; ENSG00000179639.
GeneIDi2205.
KEGGihsa:2205.
UCSCiuc001ftq.3. human.

Polymorphism databases

DMDMi119865.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X06948 mRNA. Translation: CAA30025.1 .
J03605 mRNA. Translation: AAA36204.1 .
BC005912 mRNA. Translation: AAH05912.1 .
CCDSi CCDS1184.1.
PIRi S00682.
RefSeqi NP_001992.1. NM_002001.3.
UniGenei Hs.897.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ALS model - A 26-197 [» ]
1ALT model - A 26-197 [» ]
1F2Q X-ray 2.40 A 26-201 [» ]
1F6A X-ray 3.50 A 26-201 [» ]
1J86 X-ray 3.20 A/B 26-201 [» ]
1J87 X-ray 3.20 A 26-197 [» ]
1J88 X-ray 3.20 A/B/C/D/E 26-197 [» ]
1J89 X-ray 4.10 A/B/C/D/E 26-197 [» ]
1RPQ X-ray 3.00 A/B/C/D 26-201 [» ]
2Y7Q X-ray 3.40 A 26-201 [» ]
ProteinModelPortali P12319.
SMRi P12319. Positions 26-199.
ModBasei Search...

Protein-protein interaction databases

BioGridi 108499. 3 interactions.
DIPi DIP-6166N.
IntActi P12319. 1 interaction.
STRINGi 9606.ENSP00000315719.

Chemistry

BindingDBi P12319.
ChEMBLi CHEMBL2248.
DrugBanki DB00895. Benzylpenicilloyl Polylysine.
DB00043. Omalizumab.

PTM databases

PhosphoSitei P12319.

Polymorphism databases

DMDMi 119865.

Proteomic databases

PaxDbi P12319.
PRIDEi P12319.

Protocols and materials databases

DNASUi 2205.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000368115 ; ENSP00000357097 ; ENSG00000179639 .
GeneIDi 2205.
KEGGi hsa:2205.
UCSCi uc001ftq.3. human.

Organism-specific databases

CTDi 2205.
GeneCardsi GC01P159259.
HGNCi HGNC:3609. FCER1A.
HPAi CAB022102.
MIMi 147140. gene.
neXtProti NX_P12319.
PharmGKBi PA28056.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG27903.
HOGENOMi HOG000251632.
HOVERGENi HBG051602.
InParanoidi P12319.
KOi K08089.
OMAi YENHNIS.
OrthoDBi EOG72NRRC.
PhylomeDBi P12319.
TreeFami TF335097.

Enzyme and pathway databases

Reactomei REACT_163701. FCERI mediated MAPK activation.
REACT_163769. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_163834. FCERI mediated Ca+2 mobilization.
REACT_163936. Fc epsilon receptor (FCERI) signaling.
REACT_163994. FCERI mediated NF-kB activation.

Miscellaneous databases

EvolutionaryTracei P12319.
GeneWikii FCER1A.
GenomeRNAii 2205.
NextBioi 8931.
PROi P12319.
SOURCEi Search...

Gene expression databases

ArrayExpressi P12319.
Bgeei P12319.
CleanExi HS_FCER1A.
Genevestigatori P12319.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of the gene coding for the alpha subunit of the human high affinity IgE receptor."
    Kochan J., Pettine L.F., Hakimi J., Kishi K., Kinet J.-P.
    Nucleic Acids Res. 16:3584-3584(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Human and rat mast cell high-affinity immunoglobulin E receptors: characterization of putative alpha-chain gene products."
    Shimizu A., Tepler I., Benfey P.N., Berenstein E.H., Siraganian R.P., Leder P.
    Proc. Natl. Acad. Sci. U.S.A. 85:1907-1911(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Mast cell.
  3. "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].
    Tissue: Prostate.
  4. "High-level expression of the truncated alpha chain of human high-affinity receptor for IgE as a soluble form by baculovirus-infected insect cells. Biochemical characterization of the recombinant product."
    Yagi S., Yanagida M., Tanida I., Hasegawa A., Okumura K., Ra C.
    Eur. J. Biochem. 220:593-598(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 26-197.
  5. "A modeling study of the alpha-subunit of human high-affinity receptor for immunoglobulin-E."
    Padlan E.A., Helm B.A.
    Receptor 2:129-144(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF 26-197.
  6. "Crystal structure of the human high-affinity IgE receptor."
    Garman S.C., Kinet J.P., Jardetzky T.S.
    Cell 95:951-961(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 26-201, GLYCOSYLATION AT ASN-46; ASN-67 AND ASN-191, DISULFIDE BONDS.
  7. "The analysis of the human high affinity IgE receptor Fc epsilon Ri alpha from multiple crystal forms."
    Garman S.C., Sechi S., Kinet J.P., Jardetzky T.S.
    J. Mol. Biol. 311:1049-1062(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 26-201, GLYCOSYLATION AT ASN-46; ASN-67; ASN-99; ASN-165 AND ASN-191, DISULFIDE BONDS.

Entry informationi

Entry nameiFCERA_HUMAN
AccessioniPrimary (citable) accession number: P12319
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: September 3, 2014
This is version 147 of the entry and version 1 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 chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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