Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P40259 (CD79B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:CD79B
Synonyms:B29, IGB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length229 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10 Ref.11 Ref.12

Subunit structure

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. Ref.14

Subcellular location

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.

Tissue specificity

B-cells.

Post-translational modification

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

Involvement in disease

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. Ref.15

Sequence similarities

Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Contains 1 ITAM domain.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: P40259-1)

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.
Isoform Short (identifier: P40259-2)

The sequence of this isoform differs from the canonical sequence as follows:
     41-144: Missing.
Isoform 3 (identifier: P40259-3)

The sequence of this isoform differs from the canonical sequence as follows:
     23-23: A → AA
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Ref.9
Chain29 – 229201B-cell antigen receptor complex-associated protein beta chain
PRO_0000014560

Regions

Topological domain29 – 159131Extracellular Potential
Transmembrane160 – 18021Helical; Potential
Topological domain181 – 22949Cytoplasmic Potential
Domain38 – 138101Ig-like V-type
Domain185 – 21329ITAM

Amino acid modifications

Modified residue1961Phosphotyrosine; by SRC-type Tyr-kinases By similarity
Modified residue2071Phosphotyrosine; by SRC-type Tyr-kinases By similarity
Glycosylation731N-linked (GlcNAc...) Potential
Glycosylation1011N-linked (GlcNAc...) Potential
Glycosylation1271N-linked (GlcNAc...) Potential
Glycosylation1281N-linked (GlcNAc...) Potential
Disulfide bond43 ↔ 126 Ref.14
Disulfide bond65 ↔ 122 Ref.14
Disulfide bond136Interchain (with C-119 in alpha chain) Ref.14

Natural variations

Alternative sequence231A → AA in isoform 3.
VSP_047222
Alternative sequence41 – 144104Missing in isoform Short.
VSP_002477
Natural variant1371G → S in AGM6. Ref.15
VAR_057833

Experimental info

Sequence conflict581G → A in AAB24822. Ref.3
Sequence conflict581G → R in AAA58387. Ref.1
Sequence conflict841E → A in AAB24822. Ref.3

Secondary structure

........................ 229
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: C467175567D10883

FASTA22926,048
        10         20         30         40         50         60 
MARLALSPVP SHWMVALLLL LSAEPVPAAR SEDRYRNPKG SACSRIWQSP RFIARKRGFT 

        70         80         90        100        110        120 
VKMHCYMNSA SGNVSWLWKQ EMDENPQQLK LEKGRMEESQ NESLATLTIQ GIRFEDNGIY 

       130        140        150        160        170        180 
FCQQKCNNTS EVYQGCGTEL RVMGFSTLAQ LKQRNTLKDG IIMIQTLLII LFIIVPIFLL 

       190        200        210        220 
LDKDDSKAGM EEDHTYEGLD IDQTATYEDI VTLRTGEVKW SVGEHPGQE 

« Hide

Isoform Short [UniParc].

Checksum: 6CEE8C7A4F0AB1C0
Show »

FASTA12514,030
Isoform 3 [UniParc].

Checksum: FE9E79CA0CE5BBC9
Show »

FASTA23026,119

References

« Hide 'large scale' references
[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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

CD79Bbase

CD79B mutation db

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA46527. I54534.
RefSeqNP_000617.1. NM_000626.2.
NP_001035022.1. NM_001039933.1.
NP_067613.1. NM_021602.2.
UniGeneHs.89575.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3KG5X-ray3.20A/B26-159[»]
DisProtDP00503.
ProteinModelPortalP40259.
SMRP40259. Positions 43-188.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107412. 8 interactions.
DIPDIP-59497N.
IntActP40259. 1 interaction.
STRING9606.ENSP00000376544.

PTM databases

PhosphoSiteP40259.

Polymorphism databases

DMDM728994.

Proteomic databases

PaxDbP40259.
PRIDEP40259.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000006750; ENSP00000006750; ENSG00000007312. [P40259-1]
ENST00000349817; ENSP00000245862; ENSG00000007312. [P40259-2]
ENST00000392795; ENSP00000376544; ENSG00000007312. [P40259-3]
GeneID974.
KEGGhsa:974.
UCSCuc002jdp.1. human. [P40259-1]
uc002jdr.1. human. [P40259-2]

Organism-specific databases

CTD974.
GeneCardsGC17M062006.
HGNCHGNC:1699. CD79B.
HPACAB009751.
HPA009178.
MIM147245. gene.
612692. phenotype.
neXtProtNX_P40259.
Orphanet33110. Autosomal agammaglobulinemia.
PharmGKBPA26238.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG46934.
HOGENOMHOG000049137.
HOVERGENHBG050855.
KOK06507.
OMADQTATYE.
OrthoDBEOG7HTHJ8.
PhylomeDBP40259.
TreeFamTF336032.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkP40259.

Gene expression databases

BgeeP40259.
CleanExHS_CD79B.
GenevestigatorP40259.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
IPR003110. Phos_immunorcpt_sig_ITAM.
[Graphical view]
PfamPF02189. ITAM. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTSM00409. IG. 1 hit.
SM00077. ITAM. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 1 hit.
PS51055. ITAM_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCD79B.
GenomeRNAi974.
NextBio4082.
PROP40259.
SOURCESearch...

Entry information

Entry nameCD79B_HUMAN
AccessionPrimary (citable) accession number: P40259
Secondary accession number(s): Q53FS2, Q9BU06
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries