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P12319

- FCERA_HUMAN

UniProt

P12319 - FCERA_HUMAN

Protein

High affinity immunoglobulin epsilon receptor subunit alpha

Gene

FCER1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 1 (01 Oct 1989)
      Previous versions | rss
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    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

    GO - Biological processi

    1. activation of JUN kinase activity Source: Ensembl
    2. Fc-epsilon receptor signaling pathway Source: Reactome
    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

    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

    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

    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 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

    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

    1
    257
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12319.

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei206 – 22419HelicalSequence AnalysisAdd
    BLAST

    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.
    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 148 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