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P40259

- CD79B_HUMAN

UniProt

P40259 - CD79B_HUMAN

Protein

B-cell antigen receptor complex-associated protein beta chain

Gene

CD79B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Required in cooperation with CD79A for initiation of the signal transduction cascade activated by the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Enhances phosphorylation of CD79A, possibly by recruiting kinases which phosphorylate CD79A or by recruiting proteins which bind to CD79A and protect it from dephosphorylation.3 Publications

    GO - Molecular functioni

    1. transmembrane signaling receptor activity Source: InterPro

    GO - Biological processi

    1. B cell receptor signaling pathway Source: Ensembl
    2. immune response Source: ProtInc
    3. signal transduction Source: ProtInc

    Keywords - Biological processi

    Adaptive immunity, Immunity

    Enzyme and pathway databases

    ReactomeiREACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    SignaLinkiP40259.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    B-cell antigen receptor complex-associated protein beta chain
    Alternative name(s):
    B-cell-specific glycoprotein B29
    Ig-beta
    Immunoglobulin-associated B29 protein
    CD_antigen: CD79b
    Gene namesi
    Name:CD79B
    Synonyms:B29, IGB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:1699. CD79B.

    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: Ensembl
    2. cytoplasm Source: HPA
    3. external side of plasma membrane Source: Ensembl
    4. extracellular vesicular exosome Source: UniProt
    5. Golgi apparatus Source: HPA
    6. integral component of plasma membrane Source: ProtInc
    7. nucleus Source: HPA
    8. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Agammaglobulinemia 6, autosomal recessive (AGM6) [MIM:612692]: 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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti137 – 1371G → S in AGM6. 1 Publication
    VAR_057833

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi612692. phenotype.
    Orphaneti33110. Autosomal agammaglobulinemia.
    PharmGKBiPA26238.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 28281 PublicationAdd
    BLAST
    Chaini29 – 229201B-cell antigen receptor complex-associated protein beta chainPRO_0000014560Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi43 ↔ 1261 PublicationPROSITE-ProRule annotation
    Disulfide bondi65 ↔ 1221 PublicationPROSITE-ProRule annotation
    Glycosylationi73 – 731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi101 – 1011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi127 – 1271N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi128 – 1281N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi136 – 136Interchain (with C-119 in alpha chain)1 PublicationPROSITE-ProRule annotation
    Modified residuei196 – 1961Phosphotyrosine; by SRC-type Tyr-kinasesPROSITE-ProRule annotation
    Modified residuei207 – 2071Phosphotyrosine; by SRC-type Tyr-kinasesPROSITE-ProRule annotation

    Post-translational modificationi

    Phosphorylated on tyrosine upon B-cell activation by SRC-type Tyr-kinases such as BLK, LYN and SYK.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP40259.
    PaxDbiP40259.
    PRIDEiP40259.

    PTM databases

    PhosphoSiteiP40259.

    Expressioni

    Tissue specificityi

    B-cells.

    Gene expression databases

    BgeeiP40259.
    CleanExiHS_CD79B.
    GenevestigatoriP40259.

    Organism-specific databases

    HPAiCAB009751.
    HPA009178.

    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 with LYN By similarity.By similarity

    Protein-protein interaction databases

    BioGridi107412. 8 interactions.
    DIPiDIP-59497N.
    IntActiP40259. 1 interaction.
    STRINGi9606.ENSP00000376544.

    Structurei

    Secondary structure

    1
    229
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi47 – 493
    Beta strandi51 – 566
    Beta strandi61 – 666
    Beta strandi75 – 8410
    Turni93 – 953
    Beta strandi96 – 1005
    Beta strandi102 – 1098
    Turni114 – 1163
    Beta strandi118 – 1258
    Turni127 – 1293
    Beta strandi132 – 1343
    Beta strandi138 – 1436

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3KG5X-ray3.20A/B26-159[»]
    DisProtiDP00503.
    ProteinModelPortaliP40259.
    SMRiP40259. Positions 43-145.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini29 – 159131ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini181 – 22949CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei160 – 18021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini38 – 138101Ig-like V-typeAdd
    BLAST
    Domaini185 – 21329ITAMPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 ITAM domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG46934.
    HOGENOMiHOG000049137.
    HOVERGENiHBG050855.
    KOiK06507.
    OMAiDQTATYE.
    OrthoDBiEOG7HTHJ8.
    PhylomeDBiP40259.
    TreeFamiTF336032.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR013106. Ig_V-set.
    IPR003110. Phos_immunorcpt_sig_ITAM.
    [Graphical view]
    PfamiPF02189. ITAM. 1 hit.
    PF07686. V-set. 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]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: P40259-1) [UniParc]FASTAAdd to Basket

    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

    MARLALSPVP SHWMVALLLL LSAEPVPAAR SEDRYRNPKG SACSRIWQSP    50
    RFIARKRGFT VKMHCYMNSA SGNVSWLWKQ EMDENPQQLK LEKGRMEESQ 100
    NESLATLTIQ GIRFEDNGIY FCQQKCNNTS EVYQGCGTEL RVMGFSTLAQ 150
    LKQRNTLKDG IIMIQTLLII LFIIVPIFLL LDKDDSKAGM EEDHTYEGLD 200
    IDQTATYEDI VTLRTGEVKW SVGEHPGQE 229
    Length:229
    Mass (Da):26,048
    Last modified:February 1, 1995 - v1
    Checksum:iC467175567D10883
    GO
    Isoform Short (identifier: P40259-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         41-144: Missing.

    Show »
    Length:125
    Mass (Da):14,030
    Checksum:i6CEE8C7A4F0AB1C0
    GO
    Isoform 3 (identifier: P40259-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         23-23: A → AA

    Note: No experimental confirmation available.

    Show »
    Length:230
    Mass (Da):26,119
    Checksum:iFE9E79CA0CE5BBC9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti58 – 581G → A in AAB24822. (PubMed:8419481)Curated
    Sequence conflicti58 – 581G → R in AAA58387. (PubMed:1534761)Curated
    Sequence conflicti84 – 841E → A in AAB24822. (PubMed:8419481)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti137 – 1371G → S in AGM6. 1 Publication
    VAR_057833

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei23 – 231A → AA in isoform 3. 1 PublicationVSP_047222
    Alternative sequencei41 – 144104Missing in isoform Short. 2 PublicationsVSP_002477Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M80461 mRNA. Translation: AAA58387.1.
    M89957 mRNA. Translation: AAA64459.1.
    S52229 mRNA. Translation: AAB24822.2.
    L27587 Genomic DNA. Translation: AAA72424.1.
    S79249 mRNA. Translation: AAC60654.1.
    X83539 mRNA. Translation: CAA58522.1.
    AK222954 mRNA. Translation: BAD96674.1.
    AK223210 mRNA. Translation: BAD96930.1.
    BC002975 mRNA. Translation: AAH02975.2.
    BC032651 mRNA. Translation: AAH32651.1.
    CCDSiCCDS11655.1. [P40259-1]
    CCDS11656.1. [P40259-2]
    CCDS42372.1. [P40259-3]
    PIRiI54534. A46527.
    RefSeqiNP_000617.1. NM_000626.2. [P40259-1]
    NP_001035022.1. NM_001039933.1. [P40259-3]
    NP_067613.1. NM_021602.2. [P40259-2]
    UniGeneiHs.89575.

    Genome annotation databases

    EnsembliENST00000006750; ENSP00000006750; ENSG00000007312. [P40259-1]
    ENST00000349817; ENSP00000245862; ENSG00000007312. [P40259-2]
    ENST00000392795; ENSP00000376544; ENSG00000007312. [P40259-3]
    GeneIDi974.
    KEGGihsa:974.
    UCSCiuc002jdp.1. human. [P40259-1]
    uc002jdr.1. human. [P40259-2]

    Polymorphism databases

    DMDMi728994.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    CD79Bbase

    CD79B mutation db

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M80461 mRNA. Translation: AAA58387.1 .
    M89957 mRNA. Translation: AAA64459.1 .
    S52229 mRNA. Translation: AAB24822.2 .
    L27587 Genomic DNA. Translation: AAA72424.1 .
    S79249 mRNA. Translation: AAC60654.1 .
    X83539 mRNA. Translation: CAA58522.1 .
    AK222954 mRNA. Translation: BAD96674.1 .
    AK223210 mRNA. Translation: BAD96930.1 .
    BC002975 mRNA. Translation: AAH02975.2 .
    BC032651 mRNA. Translation: AAH32651.1 .
    CCDSi CCDS11655.1. [P40259-1 ]
    CCDS11656.1. [P40259-2 ]
    CCDS42372.1. [P40259-3 ]
    PIRi I54534. A46527.
    RefSeqi NP_000617.1. NM_000626.2. [P40259-1 ]
    NP_001035022.1. NM_001039933.1. [P40259-3 ]
    NP_067613.1. NM_021602.2. [P40259-2 ]
    UniGenei Hs.89575.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3KG5 X-ray 3.20 A/B 26-159 [» ]
    DisProti DP00503.
    ProteinModelPortali P40259.
    SMRi P40259. Positions 43-145.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107412. 8 interactions.
    DIPi DIP-59497N.
    IntActi P40259. 1 interaction.
    STRINGi 9606.ENSP00000376544.

    PTM databases

    PhosphoSitei P40259.

    Polymorphism databases

    DMDMi 728994.

    Proteomic databases

    MaxQBi P40259.
    PaxDbi P40259.
    PRIDEi P40259.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000006750 ; ENSP00000006750 ; ENSG00000007312 . [P40259-1 ]
    ENST00000349817 ; ENSP00000245862 ; ENSG00000007312 . [P40259-2 ]
    ENST00000392795 ; ENSP00000376544 ; ENSG00000007312 . [P40259-3 ]
    GeneIDi 974.
    KEGGi hsa:974.
    UCSCi uc002jdp.1. human. [P40259-1 ]
    uc002jdr.1. human. [P40259-2 ]

    Organism-specific databases

    CTDi 974.
    GeneCardsi GC17M062006.
    HGNCi HGNC:1699. CD79B.
    HPAi CAB009751.
    HPA009178.
    MIMi 147245. gene.
    612692. phenotype.
    neXtProti NX_P40259.
    Orphaneti 33110. Autosomal agammaglobulinemia.
    PharmGKBi PA26238.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG46934.
    HOGENOMi HOG000049137.
    HOVERGENi HBG050855.
    KOi K06507.
    OMAi DQTATYE.
    OrthoDBi EOG7HTHJ8.
    PhylomeDBi P40259.
    TreeFami TF336032.

    Enzyme and pathway databases

    Reactomei REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    SignaLinki P40259.

    Miscellaneous databases

    GeneWikii CD79B.
    GenomeRNAii 974.
    NextBioi 4082.
    PROi P40259.
    SOURCEi Search...

    Gene expression databases

    Bgeei P40259.
    CleanExi HS_CD79B.
    Genevestigatori P40259.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR013106. Ig_V-set.
    IPR003110. Phos_immunorcpt_sig_ITAM.
    [Graphical view ]
    Pfami PF02189. ITAM. 1 hit.
    PF07686. V-set. 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. "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 LONG).
    2. "Isolation and chromosomal mapping of the human immunoglobulin-associated B29 gene (IGB)."
      Wood W.J. Jr., Thompson A.A., Korenberg J., Chen X.-N., May W., Wall R., Denny C.T.
      Genomics 16:187-192(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
    3. "The human Ig-beta cDNA sequence, a homologue of murine B29, is identical in B cell and plasma cell lines producing all the human Ig isotypes."
      Hashimoto S., Gregersen P.K., Chiorazzi N.
      J. Immunol. 150:491-498(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
    4. "The complete sequence of the human CD79b (Ig beta/B29) gene: identification of a conserved exon/intron organization, immunoglobulin-like regulatory regions, and allelic polymorphism."
      Hashimoto S., Chiorazzi N., Gregersen P.K.
      Immunogenetics 40:145-149(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG).
    5. "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 SHORT).
    6. Koyama M., Nakamura T.
      Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
    7. Suzuki Y., Sugano S., 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 3).
      Tissue: Small intestine and Spleen.
    8. "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] (ISOFORM LONG).
      Tissue: Lymph.
    9. "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 29-45.
    10. "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.
    11. "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.
    12. "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.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Structural and functional studies of Igalphabeta and its assembly with the B cell antigen receptor."
      Radaev S., Zou Z., Tolar P., Nguyen K., Nguyen A., Krueger P.D., Stutzman N., Pierce S., Sun P.D.
      Structure 18:934-943(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 26-159, SUBUNIT, DISULFIDE BONDS.
    15. "A hypomorphic mutation in Igbeta (CD79b) in a patient with immunodeficiency and a leaky defect in B cell development."
      Dobbs A.K., Yang T., Farmer D., Kager L., Parolini O., Conley M.E.
      J. Immunol. 179:2055-2059(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AGM6 SER-137.

    Entry informationi

    Entry nameiCD79B_HUMAN
    AccessioniPrimary (citable) accession number: P40259
    Secondary accession number(s): Q53FS2, Q9BU06
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 144 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 cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 17
      Human chromosome 17: 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