Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P06734

- FCER2_HUMAN

UniProt

P06734 - FCER2_HUMAN

Protein

Low affinity immunoglobulin epsilon Fc receptor

Gene

FCER2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Low-affinity receptor for immunoglobulin E (IgE) and CR2/CD21. Has essential roles in the regulation of IgE production and in the differentiation of B-cells (it is a B-cell-specific antigen).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei149 – 1502Cleavage
    Metal bindingi249 – 2491Calcium1 Publication
    Metal bindingi251 – 2511Calcium1 Publication
    Metal bindingi269 – 2691Calcium1 Publication
    Metal bindingi270 – 2701Calcium1 Publication

    GO - Molecular functioni

    1. carbohydrate binding Source: InterPro
    2. integrin binding Source: ProtInc
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. Notch signaling pathway Source: Reactome
    2. positive regulation of humoral immune response mediated by circulating immunoglobulin Source: Ensembl
    3. positive regulation of killing of cells of other organism Source: BHF-UCL
    4. positive regulation of nitric-oxide synthase activity Source: BHF-UCL
    5. positive regulation of nitric-oxide synthase biosynthetic process Source: BHF-UCL

    Keywords - Molecular functioni

    Receptor

    Keywords - Ligandi

    Calcium, IgE-binding protein, Lectin, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_163910. NOTCH2 intracellular domain regulates transcription.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Low affinity immunoglobulin epsilon Fc receptor
    Alternative name(s):
    BLAST-2
    C-type lectin domain family 4 member J
    Fc-epsilon-RII
    Immunoglobulin E-binding factor
    Lymphocyte IgE receptor
    CD_antigen: CD23
    Cleaved into the following 2 chains:
    Gene namesi
    Name:FCER2
    Synonyms:CD23A, CLEC4J, FCE2, IGEBF
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:3612. FCER2.

    Subcellular locationi

    Cell membrane; Single-pass type II membrane protein. Cell membrane; Lipid-anchor. Secreted
    Note: Also exists as a soluble excreted form, sCD23.

    GO - Cellular componenti

    1. external side of plasma membrane Source: Ensembl
    2. extracellular vesicular exosome Source: UniProt
    3. integral component of plasma membrane Source: ProtInc
    4. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28058.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 321321Low affinity immunoglobulin epsilon Fc receptor membrane-bound formPRO_0000017391Add
    BLAST
    Chaini150 – 321172Low affinity immunoglobulin epsilon Fc receptor soluble formPRO_0000017392Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi17 – 171S-palmitoyl cysteine1 Publication
    Lipidationi18 – 181S-palmitoyl cysteine1 Publication
    Glycosylationi63 – 631N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi160 ↔ 288
    Disulfide bondi163 ↔ 174
    Disulfide bondi191 ↔ 282
    Disulfide bondi259 ↔ 273

    Post-translational modificationi

    N- and O-glycosylated.
    The secreted form sCD23 is produced by ADAM10-mediated ectodomain shedding.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

    Proteomic databases

    MaxQBiP06734.
    PaxDbiP06734.
    PRIDEiP06734.

    PTM databases

    PhosphoSiteiP06734.

    Miscellaneous databases

    PMAP-CutDBP06734.

    Expressioni

    Gene expression databases

    ArrayExpressiP06734.
    BgeeiP06734.
    CleanExiHS_FCER2.
    GenevestigatoriP06734.

    Organism-specific databases

    HPAiCAB002624.
    HPA008928.

    Interactioni

    Subunit structurei

    Homotrimer.2 Publications

    Protein-protein interaction databases

    BioGridi108502. 3 interactions.
    STRINGi9606.ENSP00000264072.

    Structurei

    Secondary structure

    1
    321
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi159 – 1624
    Beta strandi164 – 1663
    Beta strandi168 – 1703
    Beta strandi173 – 18210
    Helixi184 – 19310
    Beta strandi196 – 1983
    Helixi204 – 2118
    Beta strandi215 – 2173
    Beta strandi219 – 2268
    Turni227 – 2304
    Beta strandi231 – 2344
    Turni247 – 2526
    Beta strandi253 – 2564
    Beta strandi259 – 2624
    Turni264 – 2663
    Beta strandi268 – 2714
    Beta strandi277 – 2859
    Beta strandi287 – 2893
    Beta strandi291 – 2944

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HLImodel-A173-285[»]
    1KJEmodel-A173-285[»]
    1T8CNMR-A156-298[»]
    1T8DNMR-A156-298[»]
    2H2RX-ray1.50A/B150-321[»]
    2H2TX-ray1.30B150-321[»]
    4EZMX-ray3.10G/H/I/J/K/L156-298[»]
    4G96X-ray2.25A/B/C/D156-298[»]
    4G9AX-ray2.00A/B/C/D156-298[»]
    4GI0X-ray2.27A/B/C156-298[»]
    4GJ0X-ray1.95A/B/C/D156-298[»]
    4GJXX-ray2.80A/B/C/D/E/F/G/H156-298[»]
    4GK1X-ray2.24A/B/C/D/E/F/G156-298[»]
    4GKOX-ray3.30G/H/I/J/K/L156-298[»]
    4J6JX-ray1.90A/B/C/D156-298[»]
    4J6KX-ray2.30A/B/C/D/E/F/G/H156-298[»]
    4J6LX-ray3.15A/B/C/D/E/F/G/H156-298[»]
    4J6MX-ray2.48A/B/C/D/E/F/G/H156-298[»]
    4J6NX-ray2.85A/B156-298[»]
    4J6PX-ray1.90A/B/C/D156-298[»]
    4J6QX-ray2.54A156-298[»]
    4KI1X-ray3.20E/F/G/H156-298[»]
    ProteinModelPortaliP06734.
    SMRiP06734. Positions 134-291.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06734.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2121CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini48 – 321274ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei22 – 4726Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati69 – 8921Add
    BLAST
    Repeati90 – 11021Add
    BLAST
    Repeati111 – 13121Add
    BLAST
    Domaini162 – 284123C-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 C-type lectin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG235454.
    HOGENOMiHOG000089951.
    HOVERGENiHBG051599.
    InParanoidiP06734.
    KOiK06468.
    OMAiKCYYFGE.
    OrthoDBiEOG7FV3QQ.
    PhylomeDBiP06734.
    TreeFamiTF333341.

    Family and domain databases

    Gene3Di3.10.100.10. 1 hit.
    InterProiIPR001304. C-type_lectin.
    IPR016186. C-type_lectin-like.
    IPR018378. C-type_lectin_CS.
    IPR016187. C-type_lectin_fold.
    [Graphical view]
    PfamiPF00059. Lectin_C. 1 hit.
    [Graphical view]
    SMARTiSM00034. CLECT. 1 hit.
    [Graphical view]
    SUPFAMiSSF56436. SSF56436. 1 hit.
    PROSITEiPS00615. C_TYPE_LECTIN_1. 1 hit.
    PS50041. C_TYPE_LECTIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P06734-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEEGQYSEIE ELPRRRCCRR GTQIVLLGLV TAALWAGLLT LLLLWHWDTT    50
    QSLKQLEERA ARNVSQVSKN LESHHGDQMA QKSQSTQISQ ELEELRAEQQ 100
    RLKSQDLELS WNLNGLQADL SSFKSQELNE RNEASDLLER LREEVTKLRM 150
    ELQVSSGFVC NTCPEKWINF QRKCYYFGKG TKQWVHARYA CDDMEGQLVS 200
    IHSPEEQDFL TKHASHTGSW IGLRNLDLKG EFIWVDGSHV DYSNWAPGEP 250
    TSRSQGEDCV MMRGSGRWND AFCDRKLGAW VCDRLATCTP PASEGSAESM 300
    GPDSRPDPDG RLPTPSAPLH S 321
    Length:321
    Mass (Da):36,469
    Last modified:January 1, 1988 - v1
    Checksum:iF86708C0E6515B87
    GO

    Sequence cautioni

    The sequence AAA52433.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti269 – 2691N → T in CAA28465. (PubMed:3034567)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti62 – 621R → W.
    Corresponds to variant rs2228137 [ dbSNP | Ensembl ].
    VAR_035387
    Natural varianti284 – 2841R → Q.
    Corresponds to variant rs8102872 [ dbSNP | Ensembl ].
    VAR_035388
    Natural varianti316 – 3161S → F.1 Publication
    VAR_069800

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15059 mRNA. Translation: AAA52434.1.
    M14766 mRNA. Translation: AAA52435.1.
    X04772 mRNA. Translation: CAA28465.1.
    AC008763 Genomic DNA. No translation available.
    BC014108 mRNA. Translation: AAH14108.1.
    BC062591 mRNA. Translation: AAH62591.1.
    M23562 Genomic DNA. Translation: AAA52433.1. Sequence problems.
    CCDSiCCDS12184.1.
    PIRiA26067. LNHUER.
    RefSeqiNP_001193948.2. NM_001207019.2.
    NP_001207429.1. NM_001220500.1.
    NP_001993.2. NM_002002.4.
    XP_005272519.1. XM_005272462.2.
    XP_006722750.1. XM_006722687.1.
    UniGeneiHs.465778.

    Genome annotation databases

    EnsembliENST00000346664; ENSP00000264072; ENSG00000104921.
    ENST00000597921; ENSP00000471974; ENSG00000104921.
    GeneIDi2208.
    KEGGihsa:2208.
    UCSCiuc002mhm.2. human.

    Polymorphism databases

    DMDMi119862.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - Glycan Binding

    CD23

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15059 mRNA. Translation: AAA52434.1 .
    M14766 mRNA. Translation: AAA52435.1 .
    X04772 mRNA. Translation: CAA28465.1 .
    AC008763 Genomic DNA. No translation available.
    BC014108 mRNA. Translation: AAH14108.1 .
    BC062591 mRNA. Translation: AAH62591.1 .
    M23562 Genomic DNA. Translation: AAA52433.1 . Sequence problems.
    CCDSi CCDS12184.1.
    PIRi A26067. LNHUER.
    RefSeqi NP_001193948.2. NM_001207019.2.
    NP_001207429.1. NM_001220500.1.
    NP_001993.2. NM_002002.4.
    XP_005272519.1. XM_005272462.2.
    XP_006722750.1. XM_006722687.1.
    UniGenei Hs.465778.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HLI model - A 173-285 [» ]
    1KJE model - A 173-285 [» ]
    1T8C NMR - A 156-298 [» ]
    1T8D NMR - A 156-298 [» ]
    2H2R X-ray 1.50 A/B 150-321 [» ]
    2H2T X-ray 1.30 B 150-321 [» ]
    4EZM X-ray 3.10 G/H/I/J/K/L 156-298 [» ]
    4G96 X-ray 2.25 A/B/C/D 156-298 [» ]
    4G9A X-ray 2.00 A/B/C/D 156-298 [» ]
    4GI0 X-ray 2.27 A/B/C 156-298 [» ]
    4GJ0 X-ray 1.95 A/B/C/D 156-298 [» ]
    4GJX X-ray 2.80 A/B/C/D/E/F/G/H 156-298 [» ]
    4GK1 X-ray 2.24 A/B/C/D/E/F/G 156-298 [» ]
    4GKO X-ray 3.30 G/H/I/J/K/L 156-298 [» ]
    4J6J X-ray 1.90 A/B/C/D 156-298 [» ]
    4J6K X-ray 2.30 A/B/C/D/E/F/G/H 156-298 [» ]
    4J6L X-ray 3.15 A/B/C/D/E/F/G/H 156-298 [» ]
    4J6M X-ray 2.48 A/B/C/D/E/F/G/H 156-298 [» ]
    4J6N X-ray 2.85 A/B 156-298 [» ]
    4J6P X-ray 1.90 A/B/C/D 156-298 [» ]
    4J6Q X-ray 2.54 A 156-298 [» ]
    4KI1 X-ray 3.20 E/F/G/H 156-298 [» ]
    ProteinModelPortali P06734.
    SMRi P06734. Positions 134-291.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108502. 3 interactions.
    STRINGi 9606.ENSP00000264072.

    Chemistry

    BindingDBi P06734.
    ChEMBLi CHEMBL2940.

    PTM databases

    PhosphoSitei P06734.

    Polymorphism databases

    DMDMi 119862.

    Proteomic databases

    MaxQBi P06734.
    PaxDbi P06734.
    PRIDEi P06734.

    Protocols and materials databases

    DNASUi 2208.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000346664 ; ENSP00000264072 ; ENSG00000104921 .
    ENST00000597921 ; ENSP00000471974 ; ENSG00000104921 .
    GeneIDi 2208.
    KEGGi hsa:2208.
    UCSCi uc002mhm.2. human.

    Organism-specific databases

    CTDi 2208.
    GeneCardsi GC19M007754.
    HGNCi HGNC:3612. FCER2.
    HPAi CAB002624.
    HPA008928.
    MIMi 151445. gene.
    neXtProti NX_P06734.
    PharmGKBi PA28058.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG235454.
    HOGENOMi HOG000089951.
    HOVERGENi HBG051599.
    InParanoidi P06734.
    KOi K06468.
    OMAi KCYYFGE.
    OrthoDBi EOG7FV3QQ.
    PhylomeDBi P06734.
    TreeFami TF333341.

    Enzyme and pathway databases

    Reactomei REACT_163910. NOTCH2 intracellular domain regulates transcription.

    Miscellaneous databases

    EvolutionaryTracei P06734.
    GeneWikii CD23.
    GenomeRNAii 2208.
    NextBioi 8943.
    PMAP-CutDB P06734.
    PROi P06734.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P06734.
    Bgeei P06734.
    CleanExi HS_FCER2.
    Genevestigatori P06734.

    Family and domain databases

    Gene3Di 3.10.100.10. 1 hit.
    InterProi IPR001304. C-type_lectin.
    IPR016186. C-type_lectin-like.
    IPR018378. C-type_lectin_CS.
    IPR016187. C-type_lectin_fold.
    [Graphical view ]
    Pfami PF00059. Lectin_C. 1 hit.
    [Graphical view ]
    SMARTi SM00034. CLECT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56436. SSF56436. 1 hit.
    PROSITEi PS00615. C_TYPE_LECTIN_1. 1 hit.
    PS50041. C_TYPE_LECTIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human lymphocyte Fc receptor for IgE: sequence homology of its cloned cDNA with animal lectins."
      Ikuta K., Takami M., Kim C.W., Honjo T., Miyoshi T., Tagaya Y., Kawabe T., Yodoi J.
      Proc. Natl. Acad. Sci. U.S.A. 84:819-823(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Cloning and expression of the cDNA coding for a human lymphocyte IgE receptor."
      Luedin C., Hofstetter H., Sarfati M., Levy C.A., Suter U., Alaimo D., Kilchherr E., Frost H., Delespesse G.
      EMBO J. 6:109-114(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: B-cell and Blood.
    6. "Two species of human Fc epsilon receptor II (Fc epsilon RII/CD23): tissue-specific and IL-4-specific regulation of gene expression."
      Yokota A., Kikutani H., Tanaka T., Sato R., Barsumian E.L., Suemura M., Kishimoto T.
      Cell 55:611-618(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. "Partial characterization of natural and recombinant human soluble CD23."
      Rose K., Turcatti G., Graber P., Pochon S., Regamey P.-O., Jansen K.U., Magnenat E., Aubonney N., Bonnefoy J.-Y.
      Biochem. J. 286:819-824(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS.
    8. "The low affinity IgE receptor (CD23) is cleaved by the metalloproteinase ADAM10."
      Lemieux G.A., Blumenkron F., Yeung N., Zhou P., Williams J., Grammer A.C., Petrovich R., Lipsky P.E., Moss M.L., Werb Z.
      J. Biol. Chem. 282:14836-14844(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE BY ADAM10.
    9. "Proteomic analysis of S-acylated proteins in human B cells reveals palmitoylation of the immune regulators CD20 and CD23."
      Ivaldi C., Martin B.R., Kieffer-Jaquinod S., Chapel A., Levade T., Garin J., Journet A.
      PLoS ONE 7:E37187-E37187(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-17 AND CYS-18, SUBCELLULAR LOCATION.
      Tissue: B-cell.
    10. "Modeling of the lectin-homology domains of the human and murine low-affinity Fc epsilon receptor (Fc epsilon RII/CD23)."
      Padlan E.A., Helm B.A.
      Receptor 3:325-341(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF LECTIN DOMAIN.
    11. "Structure-based modeling of the ligand binding domain of the human cell surface receptor CD23 and comparison of two independently derived molecular models."
      Bajorath J., Aruffo A.
      Protein Sci. 5:240-247(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF 173-285.
    12. Cited for: STRUCTURE BY NMR OF 156-298, DISULFIDE BONDS, SUBUNIT.
    13. "Structural changes in the lectin domain of CD23, the low-affinity IgE receptor, upon calcium binding."
      Wurzburg B.A., Tarchevskaya S.S., Jardetzky T.S.
      Structure 14:1049-1058(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 150-321 ALONE AND IN COMPLEX WITH CALCIUM, DISULFIDE BONDS.
    14. Cited for: VARIANT PHE-316.

    Entry informationi

    Entry nameiFCER2_HUMAN
    AccessioniPrimary (citable) accession number: P06734
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 1, 1988
    Last modified: October 1, 2014
    This is version 163 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

    Miscellaneous

    There are two kinds of Fc receptors for IgE, which differ in both structure and function: high affinity receptors on basophils and mast cells and low affinity receptors on lymphocytes and monocytes.

    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 19
      Human chromosome 19: 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