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P11911

- CD79A_MOUSE

UniProt

P11911 - CD79A_MOUSE

Protein

B-cell antigen receptor complex-associated protein alpha chain

Gene

Cd79a

Organism
Mus musculus (Mouse)
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 (24 Jul 2007)
      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.11 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei204 – 2041Required for binding to BLNK

    GO - Molecular functioni

    1. protein binding Source: MGI
    2. 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: MGI

    Keywords - Biological processi

    Adaptive immunity, Immunity

    Enzyme and pathway databases

    ReactomeiREACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

    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, Mb-1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:101774. Cd79a.

    Subcellular locationi

    Cell membrane 3 Publications; Single-pass type I membrane protein 3 Publications
    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.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice display impaired B-cell development which does not progress pass the progenitor stage.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi176 – 1761Y → F: Increases tyrosine phosphorylation. Inhibits phosphorylation of BLNK. Impaired antigen presentation; when associated with F-204. 5 Publications
    Mutagenesisi182 – 1821Y → F: Strongly reduces tyrosine phosphorylation and pre-B-cell differentiation; when associated with F-193. Abolishes constitutive internalization of BCR. 4 Publications
    Mutagenesisi193 – 1931Y → F: Strongly reduces tyrosine phosphorylation and pre-B-cell differentiation; when associated with F-182. No effect on constitutive internalization of BCR. 4 Publications
    Mutagenesisi198 – 1981R → K: Associates more strongly with SYK. Increases calcium response upon BCR ligation. 1 Publication
    Mutagenesisi204 – 2041Y → F: Has little effect on tyrosine phosphorylation. Reduces pre-B-cell differentiation. Abolishes binding to BLNK. Inhibits phosphorylation of BLNK. No effect on cap formation or BCR internalization. Impaired antigen presentation; when associated with F-176. 5 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 28282 PublicationsAdd
    BLAST
    Chaini29 – 220192B-cell antigen receptor complex-associated protein alpha chainPRO_0000014559Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi50 ↔ 101PROSITE-ProRule annotation
    Glycosylationi58 – 581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi68 – 681N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi113 – 113Interchain (with C-135 in beta chain)PROSITE-ProRule annotation
    Modified residuei182 – 1821Phosphotyrosine; by SRC-type Tyr-kinases3 PublicationsPROSITE-ProRule annotation
    Modified residuei193 – 1931Phosphotyrosine; by SRC-type Tyr-kinases2 PublicationsPROSITE-ProRule annotation
    Modified residuei198 – 1981Asymmetric dimethylarginine; by PRMT11 Publication
    Modified residuei204 – 2041Phosphotyrosine; by Tyr-kinases2 PublicationsPROSITE-ProRule annotation

    Post-translational modificationi

    Phosphorylated on tyrosine, serine and threonine residues upon B-cell activation. Phosphorylation of tyrosine residues by Src-family kinases, including LYN, 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. Phosphorylation of serine and threonine residues may prevent subsequent tyrosine phosphorylation.4 Publications
    Arginine methylation in the ITAM domain may interfere with the binding of SYK. It promotes signals leading to B-cell differentiation.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Methylation, Phosphoprotein

    Proteomic databases

    PaxDbiP11911.
    PRIDEiP11911.

    PTM databases

    PhosphoSiteiP11911.

    Expressioni

    Tissue specificityi

    B-cells.

    Gene expression databases

    BgeeiP11911.
    CleanExiMM_CD79A.
    GenevestigatoriP11911.

    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-204, 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.8 Publications

    Protein-protein interaction databases

    BioGridi198611. 3 interactions.
    STRINGi10090.ENSMUSP00000003469.

    Structurei

    3D structure databases

    ProteinModelPortaliP11911.
    SMRiP11911. Positions 28-120.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini29 – 137109ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini160 – 22061CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei138 – 15922HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini29 – 11789Ig-like C2-typeAdd
    BLAST
    Domaini171 – 19929ITAMPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 ITAM domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG41728.
    GeneTreeiENSGT00510000049127.
    HOGENOMiHOG000074307.
    HOVERGENiHBG050854.
    InParanoidiP11911.
    KOiK06506.
    OMAiRKRWQNE.
    OrthoDBiEOG7J70GM.
    PhylomeDBiP11911.
    TreeFamiTF336032.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR013151. Immunoglobulin.
    IPR003110. Phos_immunorcpt_sig_ITAM.
    [Graphical view]
    PfamiPF00047. ig. 1 hit.
    PF02189. ITAM. 1 hit.
    [Graphical view]
    SMARTiSM00409. IG. 1 hit.
    SM00077. ITAM. 1 hit.
    [Graphical view]
    PROSITEiPS50835. IG_LIKE. 1 hit.
    PS51055. ITAM_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P11911-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPGGLEALRA LPLLLFLSYA CLGPGCQALR VEGGPPSLTV NLGEEARLTC    50
    ENNGRNPNIT WWFSLQSNIT WPPVPLGPGQ GTTGQLFFPE VNKNHRGLYW 100
    CQVIENNILK RSCGTYLRVR NPVPRPFLDM GEGTKNRIIT AEGIILLFCA 150
    VVPGTLLLFR KRWQNEKFGV DMPDDYEDEN LYEGLNLDDC SMYEDISRGL 200
    QGTYQDVGNL HIGDAQLEKP 220
    Length:220
    Mass (Da):24,583
    Last modified:July 24, 2007 - v2
    Checksum:iA4C648C2BE6D3E38
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti95 – 1006HRGLYW → TGACTG in CAA31801. (PubMed:2463161)Curated
    Sequence conflicti95 – 1006HRGLYW → TGACTG in AAA39494. (PubMed:2358676)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13450 mRNA. Translation: CAA31801.1.
    M31773 Genomic DNA. Translation: AAA39494.1.
    BC027633 mRNA. Translation: AAH27633.1.
    S59359 Genomic DNA. No translation available.
    CCDSiCCDS20967.1.
    PIRiA43540.
    RefSeqiNP_031681.2. NM_007655.3.
    UniGeneiMm.1355.

    Genome annotation databases

    EnsembliENSMUST00000003469; ENSMUSP00000003469; ENSMUSG00000003379.
    GeneIDi12518.
    KEGGimmu:12518.
    UCSCiuc009fqt.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13450 mRNA. Translation: CAA31801.1 .
    M31773 Genomic DNA. Translation: AAA39494.1 .
    BC027633 mRNA. Translation: AAH27633.1 .
    S59359 Genomic DNA. No translation available.
    CCDSi CCDS20967.1.
    PIRi A43540.
    RefSeqi NP_031681.2. NM_007655.3.
    UniGenei Mm.1355.

    3D structure databases

    ProteinModelPortali P11911.
    SMRi P11911. Positions 28-120.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198611. 3 interactions.
    STRINGi 10090.ENSMUSP00000003469.

    PTM databases

    PhosphoSitei P11911.

    Proteomic databases

    PaxDbi P11911.
    PRIDEi P11911.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000003469 ; ENSMUSP00000003469 ; ENSMUSG00000003379 .
    GeneIDi 12518.
    KEGGi mmu:12518.
    UCSCi uc009fqt.1. mouse.

    Organism-specific databases

    CTDi 973.
    MGIi MGI:101774. Cd79a.

    Phylogenomic databases

    eggNOGi NOG41728.
    GeneTreei ENSGT00510000049127.
    HOGENOMi HOG000074307.
    HOVERGENi HBG050854.
    InParanoidi P11911.
    KOi K06506.
    OMAi RKRWQNE.
    OrthoDBi EOG7J70GM.
    PhylomeDBi P11911.
    TreeFami TF336032.

    Enzyme and pathway databases

    Reactomei REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

    Miscellaneous databases

    NextBioi 281518.
    PROi P11911.
    SOURCEi Search...

    Gene expression databases

    Bgeei P11911.
    CleanExi MM_CD79A.
    Genevestigatori P11911.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR013151. Immunoglobulin.
    IPR003110. Phos_immunorcpt_sig_ITAM.
    [Graphical view ]
    Pfami PF00047. ig. 1 hit.
    PF02189. ITAM. 1 hit.
    [Graphical view ]
    SMARTi SM00409. IG. 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. "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: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6 X DBA/2J.
    2. "Structure of the murine mb-1 gene encoding a putative sIgM-associated molecule."
      Kashiwamura S., Koyama T., Matsuo T., Steinmetz M., Kimoto M., Sakaguchi N.
      J. Immunol. 145:337-343(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: BALB/c.
      Tissue: Liver.
    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.
    4. "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].
      Strain: C57BL/6J.
      Tissue: Mammary gland.
    5. "Heterogeneously initiated transcription from the pre-B- and B-cell-specific mb-1 promoter: analysis of the requirement for upstream factor-binding sites and initiation site sequences."
      Travis A., Hagman J., Grosschedl R.
      Mol. Cell. Biol. 11:5756-5766(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
    6. "Identification of the genes encoding the IgM-alpha and Ig-beta components of the IgM antigen receptor complex by amino-terminal sequencing."
      Hombach J., Lottspeich F., Reth M.
      Eur. J. Immunol. 20:2795-2799(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-38.
    7. "IgM antigen receptor complex contains phosphoprotein products of B29 and mb-1 genes."
      Campbell K.S., Hager E.J., Friedrich R.J., Cambier J.C.
      Proc. Natl. Acad. Sci. U.S.A. 88:3982-3986(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-38.
    8. "The MB-1/B29 heterodimer couples the B cell antigen receptor to multiple src family protein tyrosine kinases."
      Lin J., Justement L.B.
      J. Immunol. 149:1548-1555(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BLK.
    9. "B-cell antigen receptor motifs have redundant signalling capabilities and bind the tyrosine kinases PTK72, Lyn and Fyn."
      Law D.A., Chan V.W., Datta S.K., DeFranco A.L.
      Curr. Biol. 3:645-657(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LYN, PHOSPHORYLATION.
    10. "Dual role of the tyrosine activation motif of the Ig-alpha protein during signal transduction via the B cell antigen receptor."
      Flaswinkel H., Reth M.
      EMBO J. 13:83-89(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-182, MUTAGENESIS OF TYR-176; TYR-182 AND TYR-193.
    11. "Analysis of Ig-alpha-tyrosine kinase interaction reveals two levels of binding specificity and tyrosine phosphorylated Ig-alpha stimulation of Fyn activity."
      Clark M.R., Johnson S.A., Cambier J.C.
      EMBO J. 13:1911-1919(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FYN AND LYN.
    12. "Activation of B- and T-cells by the cytoplasmic domains of the B-cell antigen receptor proteins Ig-alpha and Ig-beta."
      Taddie J.A., Hurley T.R., Hardwick B.S., Sefton B.M.
      J. Biol. Chem. 269:13529-13535(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Syk protein-tyrosine kinase is regulated by tyrosine-phosphorylated Ig alpha/Ig beta immunoreceptor tyrosine activation motif binding and autophosphorylation."
      Rowley R.B., Burkhardt A.L., Chao H.-G., Matsueda G.R., Bolen J.B.
      J. Biol. Chem. 270:11590-11594(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SYK.
    14. "Reconstitution of the B cell antigen receptor signaling components in COS cells."
      Saouaf S.J., Kut S.A., Fargnoli J., Rowley R.B., Bolen J.B., Mahajan S.
      J. Biol. Chem. 270:27072-27078(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BLK, PHOSPHORYLATION AT TYR-182 AND TYR-193.
    15. "A tyrosine-based signal present in Ig alpha mediates B cell receptor constitutive internalization."
      Cassard S., Salamero J., Hanau D., Spehner D., Davoust J., Fridman W.H., Bonnerot C.
      J. Immunol. 160:1767-1773(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF TYR-182 AND TYR-193.
    16. "A negative regulatory role for Ig-alpha during B cell development."
      Torres R.M., Hafen K.
      Immunity 11:527-536(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "A role for lipid rafts in B cell antigen receptor signaling and antigen targeting."
      Cheng P.C., Dykstra M.L., Mitchell R.N., Pierce S.K.
      J. Exp. Med. 190:1549-1560(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    18. "Ig alpha and Ig beta are required for efficient trafficking to late endosomes and to enhance antigen presentation."
      Siemasko K., Eisfelder B.J., Stebbins C., Kabak S., Sant A.J., Song W., Clark M.R.
      J. Immunol. 162:6518-6525(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "Association of SLP-65/BLNK with the B cell antigen receptor through a non-ITAM tyrosine of Ig-alpha."
      Engels N., Wollscheid B., Wienands J.
      Eur. J. Immunol. 31:2126-2134(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BLNK, PHOSPHORYLATION AT TYR-204, MUTAGENESIS OF TYR-204.
    20. "Interference with immunoglobulin (Ig)alpha immunoreceptor tyrosine-based activation motif (ITAM) phosphorylation modulates or blocks B cell development, depending on the availability of an Igbeta cytoplasmic tail."
      Kraus M., Pao L.I., Reichlin A., Hu Y., Canono B., Cambier J.C., Nussenzweig M.C., Rajewsky K.
      J. Exp. Med. 194:455-469(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF TYR-182 AND TYR-193.
    21. "Translocation of the B cell antigen receptor into lipid rafts reveals a novel step in signaling."
      Cheng P.C., Brown B.K., Song W., Pierce S.K.
      J. Immunol. 166:3693-3701(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    22. "Cooperative interaction of Ig(alpha) and Ig(beta) of the BCR regulates the kinetics and specificity of antigen targeting."
      Li C., Siemasko K., Clark M.R., Song W.
      Int. Immunol. 14:1179-1191(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    23. "Receptor-facilitated antigen presentation requires the recruitment of B cell linker protein to Igalpha."
      Siemasko K., Skaggs B.J., Kabak S., Williamson E., Brown B.K., Song W., Clark M.R.
      J. Immunol. 168:2127-2138(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BLNK, MUTAGENESIS OF TYR-176 AND TYR-204.
    24. "B cell progenitors are arrested in maturation but have intact VDJ recombination in the absence of Ig-alpha and Ig-beta."
      Pelanda R., Braun U., Hobeika E., Nussenzweig M.C., Reth M.
      J. Immunol. 169:865-872(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    25. "The direct recruitment of BLNK to immunoglobulin alpha couples the B-cell antigen receptor to distal signaling pathways."
      Kabak S., Skaggs B.J., Gold M.R., Affolter M., West K.L., Foster M.S., Siemasko K., Chan A.C., Aebersold R., Clark M.R.
      Mol. Cell. Biol. 22:2524-2535(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BLNK, MUTAGENESIS OF TYR-176 AND TYR-204.
    26. "Ig alpha/Ig beta complexes generate signals for B cell development independent of selective plasma membrane compartmentalization."
      Fuentes-Panana E.M., Bannish G., van der Voort D., King L.B., Monroe J.G.
      J. Immunol. 174:1245-1252(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    27. "The B cell receptor promotes B cell activation and proliferation through a non-ITAM tyrosine in the Igalpha cytoplasmic domain."
      Patterson H.C.K., Kraus M., Kim Y.-M., Ploegh H., Rajewsky K.
      Immunity 25:55-65(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF TYR-176 AND TYR-204.
    28. "The Ig-alpha ITAM is required for efficient differentiation but not proliferation of pre-B cells."
      Storch B., Meixlsperger S., Jumaa H.
      Eur. J. Immunol. 37:252-260(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF TYR-176; TYR-182; TYR-193 AND TYR-204.
    29. "Arginine methylation of the B cell antigen receptor promotes differentiation."
      Infantino S., Benz B., Waldmann T., Jung M., Schneider R., Reth M.
      J. Exp. Med. 207:711-719(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT ARG-198 BY PRMT1, MUTAGENESIS OF ARG-198.

    Entry informationi

    Entry nameiCD79A_MOUSE
    AccessioniPrimary (citable) accession number: P11911
    Secondary accession number(s): Q6GTY0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: July 24, 2007
    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

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3