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P40259

- CD79B_HUMAN

UniProt

P40259 - CD79B_HUMAN

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Protein
B-cell antigen receptor complex-associated protein beta chain
Gene
CD79B, B29, IGB
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

GO - Biological processi

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

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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini29 – 159131Extracellular Reviewed prediction
Add
BLAST
Transmembranei160 – 18021Helical; Reviewed prediction
Add
BLAST
Topological domaini181 – 22949Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. B cell receptor complex Source: Ensembl
  2. Golgi apparatus Source: HPA
  3. cytoplasm Source: HPA
  4. external side of plasma membrane Source: Ensembl
  5. extracellular vesicular exosome Source: UniProt
  6. integral component of plasma membrane Source: ProtInc
  7. nucleus Source: HPA
  8. plasma membrane Source: HPA
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 Publication
Add
BLAST
Chaini29 – 229201B-cell antigen receptor complex-associated protein beta chain
PRO_0000014560Add
BLAST

Amino acid modifications

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

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.1 Publication

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 138101Ig-like V-type
Add
BLAST
Domaini185 – 21329ITAM
Add
BLAST

Sequence similaritiesi

Contains 1 ITAM domain.

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

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.
VSP_047222
Alternative sequencei41 – 144104Missing in isoform Short.
VSP_002477Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti58 – 581G → A in AAB24822. 1 Publication
Sequence conflicti58 – 581G → R in AAA58387. 1 Publication
Sequence conflicti84 – 841E → A in AAB24822. 1 Publication

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 143 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

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