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Protein

High affinity immunoglobulin epsilon receptor subunit alpha

Gene

FCER1A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

GO - Biological processi

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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:3609. FCER1A.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 205180ExtracellularSequence AnalysisAdd
BLAST
Transmembranei206 – 22419HelicalSequence AnalysisAdd
BLAST
Topological domaini225 – 25733CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • external side of plasma membrane Source: Ensembl
  • integral component of plasma membrane Source: ProtInc
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28056.

Chemistry

DrugBankiDB00895. Benzylpenicilloyl Polylysine.
DB00043. Omalizumab.

Polymorphism and mutation databases

BioMutaiFCER1A.
DMDMi119865.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 25251 PublicationAdd
BLAST
Chaini26 – 257232High affinity immunoglobulin epsilon receptor subunit alphaPRO_0000015161Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi46 – 461N-linked (GlcNAc...)2 Publications
Disulfide bondi51 ↔ 93
Glycosylationi67 – 671N-linked (GlcNAc...)2 Publications
Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi99 – 991N-linked (GlcNAc...)1 Publication
Disulfide bondi132 ↔ 176
Glycosylationi160 – 1601N-linked (GlcNAc...)Sequence Analysis
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

BgeeiP12319.
CleanExiHS_FCER1A.
ExpressionAtlasiP12319. baseline and differential.
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

1
257
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi33 – 375Combined sources
Beta strandi39 – 424Combined sources
Beta strandi47 – 504Combined sources
Beta strandi53 – 553Combined sources
Beta strandi63 – 664Combined sources
Beta strandi69 – 724Combined sources
Beta strandi75 – 806Combined sources
Helixi85 – 873Combined sources
Beta strandi89 – 946Combined sources
Beta strandi96 – 994Combined sources
Beta strandi104 – 1096Combined sources
Beta strandi111 – 1188Combined sources
Beta strandi120 – 1234Combined sources
Beta strandi128 – 1347Combined sources
Helixi135 – 1373Combined sources
Beta strandi140 – 1478Combined sources
Beta strandi150 – 1578Combined sources
Beta strandi158 – 1658Combined sources
Helixi168 – 1703Combined sources
Beta strandi172 – 1809Combined sources
Beta strandi183 – 1864Combined sources
Beta strandi190 – 1956Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12319.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG27903.
GeneTreeiENSGT00760000119130.
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

        10         20         30         40         50
MAPAMESPTL LCVALLFFAP DGVLAVPQKP KVSLNPPWNR IFKGENVTLT
60 70 80 90 100
CNGNNFFEVS STKWFHNGSL SEETNSSLNI VNAKFEDSGE YKCQHQQVNE
110 120 130 140 150
SEPVYLEVFS DWLLLQASAE VVMEGQPLFL RCHGWRNWDV YKVIYYKDGE
160 170 180 190 200
ALKYWYENHN ISITNATVED SGTYYCTGKV WQLDYESEPL NITVIKAPRE
210 220 230 240 250
KYWLQFFIPL LVVILFAVDT GLFISTQQQV TFLLKIKRTR KGFRLLNPHP

KPNPKNN
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:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

BindingDBiP12319.
ChEMBLiCHEMBL2248.
DrugBankiDB00895. Benzylpenicilloyl Polylysine.
DB00043. Omalizumab.

PTM databases

PhosphoSiteiP12319.

Polymorphism and mutation databases

BioMutaiFCER1A.
DMDMi119865.

Proteomic databases

PaxDbiP12319.
PRIDEiP12319.

Protocols and materials databases

DNASUi2205.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2205.
GeneCardsiGC01P159259.
HGNCiHGNC:3609. FCER1A.
HPAiCAB022102.
MIMi147140. gene.
neXtProtiNX_P12319.
PharmGKBiPA28056.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG27903.
GeneTreeiENSGT00760000119130.
HOGENOMiHOG000251632.
HOVERGENiHBG051602.
InParanoidiP12319.
KOiK08089.
OMAiYENHNIS.
OrthoDBiEOG72NRRC.
PhylomeDBiP12319.
TreeFamiTF335097.

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.

Miscellaneous databases

EvolutionaryTraceiP12319.
GeneWikiiFCER1A.
GenomeRNAii2205.
NextBioi8931.
PROiP12319.
SOURCEiSearch...

Gene expression databases

BgeeiP12319.
CleanExiHS_FCER1A.
ExpressionAtlasiP12319. baseline and differential.
GenevestigatoriP12319.

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]
ProtoNetiSearch...

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: April 29, 2015
This is version 152 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.