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P11912

- CD79A_HUMAN

UniProt

P11912 - CD79A_HUMAN

Protein

B-cell antigen receptor complex-associated protein alpha chain

Gene

CD79A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 2 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    Required in cooperation with CD79B for initiation of the signal transduction cascade activated by binding of antigen to the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Also required for BCR surface expression and for efficient differentiation of pro- and pre-B-cells. Stimulates SYK autophosphorylation and activation. Binds to BLNK, bringing BLNK into proximity with SYK and allowing SYK to phosphorylate BLNK. Also interacts with and increases activity of some Src-family tyrosine kinases. Represses BCR signaling during development of immature B-cells.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei210 – 2101Required for binding to BLNKBy similarity

    GO - Molecular functioni

    1. transmembrane signaling receptor activity Source: InterPro

    GO - Biological processi

    1. B cell activation Source: UniProtKB
    2. B cell differentiation Source: UniProtKB
    3. B cell proliferation Source: UniProtKB
    4. B cell receptor signaling pathway Source: UniProtKB

    Keywords - Biological processi

    Adaptive immunity, Immunity

    Enzyme and pathway databases

    ReactomeiREACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    SignaLinkiP11912.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    B-cell antigen receptor complex-associated protein alpha chain
    Alternative name(s):
    Ig-alpha
    MB-1 membrane glycoprotein
    Membrane-bound immunoglobulin-associated protein
    Surface IgM-associated protein
    CD_antigen: CD79a
    Gene namesi
    Name:CD79A
    Synonyms:IGA, MB1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:1698. CD79A.

    Subcellular locationi

    Cell membrane; Single-pass type I membrane protein
    Note: Following antigen binding, the BCR has been shown to translocate from detergent-soluble regions of the cell membrane to lipid rafts although signal transduction through the complex can also occur outside lipid rafts.By similarity

    GO - Cellular componenti

    1. B cell receptor complex Source: UniProtKB
    2. external side of plasma membrane Source: UniProtKB
    3. integral component of membrane Source: UniProtKB-KW
    4. membrane raft Source: UniProtKB
    5. multivesicular body Source: UniProtKB
    6. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Agammaglobulinemia 3, autosomal recessive (AGM3) [MIM:613501]: A primary immunodeficiency characterized by profoundly low or absent serum antibodies and low or absent circulating B-cells due to an early block of B-cell development. Affected individuals develop severe infections in the first years of life.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry. Two different mutations, one at the splice donor site of intron 2 and the other at the splice acceptor site for exon 3, have been identified. Both mutations give rise to a truncated protein.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi197 – 1971S → A: Increased phosphorylation of Y-188; when associated with A-203 and V-209. 1 Publication
    Mutagenesisi203 – 2031S → A: Increased phosphorylation of Y-188; when associated with A-197 and V-209. 1 Publication
    Mutagenesisi209 – 2091T → V: Increased phosphorylation of Y-188; when associated with A-197 and A-203. 1 Publication

    Organism-specific databases

    MIMi613501. phenotype.
    Orphaneti33110. Autosomal agammaglobulinemia.
    PharmGKBiPA26237.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 32321 PublicationAdd
    BLAST
    Chaini33 – 226194B-cell antigen receptor complex-associated protein alpha chainPRO_0000014558Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi54 ↔ 106PROSITE-ProRule annotation
    Glycosylationi57 – 571N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi63 – 631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi73 – 731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi88 – 881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi97 – 971N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi112 – 1121N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi119 – 119Interchain (with C-136 in beta chain)PROSITE-ProRule annotation
    Modified residuei188 – 1881Phosphotyrosine; by SRC-type Tyr-kinasesPROSITE-ProRule annotation
    Modified residuei199 – 1991Phosphotyrosine; by SRC-type Tyr-kinasesPROSITE-ProRule annotation
    Modified residuei204 – 2041Asymmetric dimethylarginine; by PRMT1By similarity
    Modified residuei210 – 2101Phosphotyrosine; by Tyr-kinasesPROSITE-ProRule annotation

    Post-translational modificationi

    Phosphorylated on tyrosine, serine and threonine residues upon B-cell activation. Phosphorylation of tyrosine residues by Src-family kinases is an early and essential feature of the BCR signaling cascade. The phosphorylated tyrosines serve as docking sites for SH2-domain containing kinases, leading to their activation which in turn leads to phosphorylation of downstream targets. Phosphorylated by LYN. Phosphorylation of serine and threonine residues may prevent subsequent tyrosine phosphorylation.2 Publications
    Arginine methylation in the ITAM domain may interfere with the binding of SYK. It promotes signals leading to B-cell differentiation By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP11912.
    PaxDbiP11912.
    PeptideAtlasiP11912.
    PRIDEiP11912.

    PTM databases

    PhosphoSiteiP11912.

    Expressioni

    Tissue specificityi

    B-cells.

    Gene expression databases

    ArrayExpressiP11912.
    BgeeiP11912.
    CleanExiHS_CD79A.
    GenevestigatoriP11912.

    Organism-specific databases

    HPAiCAB000019.
    HPA017748.

    Interactioni

    Subunit structurei

    Heterodimer of alpha and beta chains; disulfide-linked. Part of the B-cell antigen receptor complex where the alpha/beta chain heterodimer is non-covalently associated with an antigen-specific membrane-bound surface immunoglobulin of two heavy chains and two light chains. Interacts through its phosphorylated ITAM domain with the SH2 domains of SYK which stimulates SYK autophosphorylation and activation. Also interacts, when phosphorylated on Tyr-210, with the SH2 domain of BLNK/SLP65, bringing BLNK into proximity with SYK and allowing SYK to phosphorylate BLNK which is necessary for trafficking of the BCR to late endosomes. Interacts with Src-family tyrosine kinases including FYN and LYN, increasing their activity By similarity.By similarity

    Protein-protein interaction databases

    BioGridi107411. 11 interactions.
    IntActiP11912. 1 interaction.
    MINTiMINT-6491159.
    STRINGi9606.ENSP00000221972.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CV9NMR-A184-195[»]
    DisProtiDP00502.
    ProteinModelPortaliP11912.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11912.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini33 – 143111ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini166 – 22661CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei144 – 16522HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini33 – 11684Ig-like C2-typeAdd
    BLAST
    Domaini177 – 20529ITAMPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 ITAM domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG41728.
    HOGENOMiHOG000074307.
    HOVERGENiHBG050854.
    InParanoidiP11912.
    KOiK06506.
    OMAiRKRWQNE.
    OrthoDBiEOG7J70GM.
    PhylomeDBiP11912.
    TreeFamiTF336032.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003598. Ig_sub2.
    IPR013106. Ig_V-set.
    IPR003110. Phos_immunorcpt_sig_ITAM.
    [Graphical view]
    PfamiPF02189. ITAM. 1 hit.
    PF07686. V-set. 1 hit.
    [Graphical view]
    SMARTiSM00408. IGc2. 1 hit.
    SM00077. ITAM. 1 hit.
    [Graphical view]
    PROSITEiPS50835. IG_LIKE. 1 hit.
    PS51055. ITAM_1. 1 hit.
    [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: P11912-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    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

    MPGGPGVLQA LPATIFLLFL LSAVYLGPGC QALWMHKVPA SLMVSLGEDA    50
    HFQCPHNSSN NANVTWWRVL HGNYTWPPEF LGPGEDPNGT LIIQNVNKSH 100
    GGIYVCRVQE GNESYQQSCG TYLRVRQPPP RPFLDMGEGT KNRIITAEGI 150
    ILLFCAVVPG TLLLFRKRWQ NEKLGLDAGD EYEDENLYEG LNLDDCSMYE 200
    DISRGLQGTY QDVGSLNIGD VQLEKP 226
    Length:226
    Mass (Da):25,038
    Last modified:June 1, 1994 - v2
    Checksum:i6E5B837409969292
    GO
    Isoform 2 (identifier: P11912-2) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         89-127: GTLIIQNVNKSHGGIYVCRVQEGNESYQQSCGTYLRVRQ → E

    Show »
    Length:188
    Mass (Da):20,786
    Checksum:i176B170B710E6EEB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti47 – 471G → V in BAD97091. 1 PublicationCurated
    Sequence conflicti69 – 691V → I in AAA60270. (PubMed:1639443)Curated
    Sequence conflicti189 – 1891E → G in BAD97091. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei89 – 12739GTLII…LRVRQ → E in isoform 2. 2 PublicationsVSP_002476Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S46706 mRNA. Translation: AAB23558.1.
    M80462 mRNA. Translation: AAA59556.1.
    M74721 mRNA. Translation: AAA60270.1.
    S75217 mRNA. Translation: AAB20812.1.
    M86921 mRNA. Translation: AAA59557.1.
    U05259 Genomic DNA. Translation: AAA20495.1.
    S79248 mRNA. Translation: AAC60653.1.
    X83540 mRNA. Translation: CAA58523.1.
    AK223371 mRNA. Translation: BAD97091.1.
    X13451 mRNA. Translation: CAA31802.1. Sequence problems.
    CCDSiCCDS12589.1. [P11912-1]
    CCDS46088.1. [P11912-2]
    PIRiI54539. A46477.
    S12504.
    RefSeqiNP_001774.1. NM_001783.3. [P11912-1]
    NP_067612.1. NM_021601.3. [P11912-2]
    UniGeneiHs.631567.

    Genome annotation databases

    EnsembliENST00000221972; ENSP00000221972; ENSG00000105369. [P11912-1]
    ENST00000444740; ENSP00000400605; ENSG00000105369. [P11912-2]
    GeneIDi973.
    KEGGihsa:973.
    UCSCiuc002oru.3. human. [P11912-2]
    uc002orv.3. human. [P11912-1]

    Polymorphism databases

    DMDMi547896.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    CD79Abase

    CD79A mutation db

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S46706 mRNA. Translation: AAB23558.1 .
    M80462 mRNA. Translation: AAA59556.1 .
    M74721 mRNA. Translation: AAA60270.1 .
    S75217 mRNA. Translation: AAB20812.1 .
    M86921 mRNA. Translation: AAA59557.1 .
    U05259 Genomic DNA. Translation: AAA20495.1 .
    S79248 mRNA. Translation: AAC60653.1 .
    X83540 mRNA. Translation: CAA58523.1 .
    AK223371 mRNA. Translation: BAD97091.1 .
    X13451 mRNA. Translation: CAA31802.1 . Sequence problems.
    CCDSi CCDS12589.1. [P11912-1 ]
    CCDS46088.1. [P11912-2 ]
    PIRi I54539. A46477.
    S12504.
    RefSeqi NP_001774.1. NM_001783.3. [P11912-1 ]
    NP_067612.1. NM_021601.3. [P11912-2 ]
    UniGenei Hs.631567.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CV9 NMR - A 184-195 [» ]
    DisProti DP00502.
    ProteinModelPortali P11912.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107411. 11 interactions.
    IntActi P11912. 1 interaction.
    MINTi MINT-6491159.
    STRINGi 9606.ENSP00000221972.

    PTM databases

    PhosphoSitei P11912.

    Polymorphism databases

    DMDMi 547896.

    Proteomic databases

    MaxQBi P11912.
    PaxDbi P11912.
    PeptideAtlasi P11912.
    PRIDEi P11912.

    Protocols and materials databases

    DNASUi 973.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000221972 ; ENSP00000221972 ; ENSG00000105369 . [P11912-1 ]
    ENST00000444740 ; ENSP00000400605 ; ENSG00000105369 . [P11912-2 ]
    GeneIDi 973.
    KEGGi hsa:973.
    UCSCi uc002oru.3. human. [P11912-2 ]
    uc002orv.3. human. [P11912-1 ]

    Organism-specific databases

    CTDi 973.
    GeneCardsi GC19P042381.
    HGNCi HGNC:1698. CD79A.
    HPAi CAB000019.
    HPA017748.
    MIMi 112205. gene.
    613501. phenotype.
    neXtProti NX_P11912.
    Orphaneti 33110. Autosomal agammaglobulinemia.
    PharmGKBi PA26237.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG41728.
    HOGENOMi HOG000074307.
    HOVERGENi HBG050854.
    InParanoidi P11912.
    KOi K06506.
    OMAi RKRWQNE.
    OrthoDBi EOG7J70GM.
    PhylomeDBi P11912.
    TreeFami TF336032.

    Enzyme and pathway databases

    Reactomei REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    SignaLinki P11912.

    Miscellaneous databases

    EvolutionaryTracei P11912.
    GeneWikii CD79A.
    GenomeRNAii 973.
    NextBioi 4076.
    PROi P11912.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11912.
    Bgeei P11912.
    CleanExi HS_CD79A.
    Genevestigatori P11912.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003598. Ig_sub2.
    IPR013106. Ig_V-set.
    IPR003110. Phos_immunorcpt_sig_ITAM.
    [Graphical view ]
    Pfami PF02189. ITAM. 1 hit.
    PF07686. V-set. 1 hit.
    [Graphical view ]
    SMARTi SM00408. IGc2. 1 hit.
    SM00077. ITAM. 1 hit.
    [Graphical view ]
    PROSITEi PS50835. IG_LIKE. 1 hit.
    PS51055. ITAM_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure and expression of the mb-1 transcript in human lymphoid cells."
      Leduc I., Preud'Homme J.L., Cogne M.
      Clin. Exp. Immunol. 90:141-146(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Cloning and sequencing of the cDNA encoding the human homologue of the murine immunoglobulin-associated protein B29."
      Mueller B.S., Cooper L., Terhorst C.
      Eur. J. Immunol. 22:1621-1625(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Tonsil.
    3. "Molecular cloning of the Ig-alpha subunit of the human B-cell antigen receptor complex."
      Flaswinkel H., Reth M.
      Immunogenetics 36:266-269(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Human mb-1 gene: complete cDNA sequence and its expression in B cells bearing membrane Ig of various isotypes."
      Yu L.M., Chang T.W.
      J. Immunol. 148:633-637(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    5. "Molecular cloning and expression pattern of a human gene homologous to the murine mb-1 gene."
      Ha H.J., Kubagawa H., Burrows P.D.
      J. Immunol. 148:1526-1531(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
    6. "Chromosomal localization, genomic structure, and allelic polymorphism of the human CD79 alpha (Ig-alpha/mb-1) gene."
      Hashimoto S., Mohrenweiser H.W., Gregersen P.K., Chiorazzi N.
      Immunogenetics 40:287-295(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    7. "Structure, chromosomal localization, and methylation pattern of the human mb-1 gene."
      Ha H., Barnoski B.L., Sun L., Emanuel B.S., Burrows P.D.
      J. Immunol. 152:5749-5757(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    8. "Alternative splicing of CD79a (Ig-alpha/mb-1) and CD79b (Ig-beta/B29) RNA transcripts in human B cells."
      Hashimoto S., Chiorazzi N., Gregersen P.K.
      Mol. Immunol. 32:651-659(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    9. Koyama M., Nakamura T.
      Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    10. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Small intestine.
    11. "Isolation and chemical characterization of the human B29 and mb-1 proteins of the B cell antigen receptor complex."
      Vasile S., Coligan J.E., Yoshida M., Seon B.K.
      Mol. Immunol. 31:419-427(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 33-52.
    12. "B lymphocyte lineage-restricted expression of mb-1, a gene with CD3-like structural properties."
      Sakaguchi N., Kashiwamura S., Kimoto M., Thalmann P., Melchers F.
      EMBO J. 7:3457-3464(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 190-226 (ISOFORM 1).
    13. "Cooperativity and segregation of function within the Ig-alpha/beta heterodimer of the B cell antigen receptor complex."
      Luisiri P., Lee Y.J., Eisfelder B.J., Clark M.R.
      J. Biol. Chem. 271:5158-5163(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "B-cell antigen receptor-induced apoptosis requires both Ig alpha and Ig beta."
      Tseng J., Eisfelder B.J., Clark M.R.
      Blood 89:1513-1520(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Mutations in Igalpha (CD79a) result in a complete block in B-cell development."
      Minegishi Y., Coustan-Smith E., Rapalus L., Ersoy F., Campana D., Conley M.E.
      J. Clin. Invest. 104:1115-1121(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN AGM3.
    16. "The serine and threonine residues in the Ig-alpha cytoplasmic tail negatively regulate immunoreceptor tyrosine-based activation motif-mediated signal transduction."
      Mueller R., Wienands J., Reth M.
      Proc. Natl. Acad. Sci. U.S.A. 97:8451-8454(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, MUTAGENESIS OF SER-197; SER-203 AND THR-209.
    17. "Novel Igalpha (CD79a) gene mutation in a Turkish patient with B cell-deficient agammaglobulinemia."
      Wang Y., Kanegane H., Sanal O., Tezcan I., Ersoy F., Futatani T., Miyawaki T.
      Am. J. Med. Genet. 108:333-336(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN AGM3.
    18. "Substrate recognition by the Lyn protein-tyrosine kinase. NMR structure of the immunoreceptor tyrosine-based activation motif signaling region of the B cell antigen receptor."
      Gaul B.S., Harrison M.L., Geahlen R.L., Burton R.A., Post C.B.
      J. Biol. Chem. 275:16174-16182(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 184-195, PHOSPHORYLATION, INTERACTION WITH LYN.

    Entry informationi

    Entry nameiCD79A_HUMAN
    AccessioniPrimary (citable) accession number: P11912
    Secondary accession number(s): A0N775, Q53FB8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 146 of the entry and version 2 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 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    3. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3