P40259 (CD79B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	CD79B
Synonyms:	B29, IGB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	229 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 (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.

Ontologies

Keywords
Biological process	Adaptive immunity Immunity
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Disease	Disease mutation
Domain	Immunoglobulin domain Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	B cell receptor signaling pathway Inferred from electronic annotation. Source: Compara immune response Traceable author statement Ref.2. Source: ProtInc signal transduction Traceable author statement Ref.2. Source: ProtInc
Cellular_component	B cell receptor complex Inferred from electronic annotation. Source: Compara Golgi apparatus Inferred from direct assay. Source: HPA external side of plasma membrane Inferred from electronic annotation. Source: Compara integral to plasma membrane Traceable author statement Ref.2. Source: ProtInc nucleus Inferred from direct assay. Source: HPA
Molecular_function	transmembrane signaling receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 28

28

Ref.9

Chain

29 – 229

201

B-cell antigen receptor complex-associated protein beta chain

PRO_0000014560

Regions

Topological domain

29 – 159

131

Extracellular Potential

Transmembrane

160 – 180

21

Helical; Potential

Topological domain

181 – 229

49

Cytoplasmic Potential

Domain

38 – 138

101

Ig-like V-type

Domain

185 – 213

29

ITAM

Amino acid modifications

Modified residue

196

1

Phosphotyrosine; by SRC-type Tyr-kinases By similarity

Modified residue

207

1

Phosphotyrosine; by SRC-type Tyr-kinases By similarity

Glycosylation

73

1

N-linked (GlcNAc...) Potential

Glycosylation

101

1

N-linked (GlcNAc...) Potential

Glycosylation

127

1

N-linked (GlcNAc...) Potential

Glycosylation

128

1

N-linked (GlcNAc...) Potential

Disulfide bond

43 ↔ 126

Ref.14

Disulfide bond

65 ↔ 122

Ref.14

Disulfide bond

136

Interchain (with C-119 in alpha chain) Ref.14

Natural variations

Alternative sequence

41 – 144

104

Missing in isoform Short.

VSP_002477

Natural variant

137

1

G → S in AGM6. Ref.15

VAR_057833

Experimental info

Sequence conflict

23

1

A → AA in BAD96674. Ref.7

Sequence conflict

23

1

A → AA in BAD96930. Ref.7

Sequence conflict

58

1

G → A in AAB24822. Ref.3

Sequence conflict

58

1

G → R in AAA58387. Ref.1

Sequence conflict

84

1

E → A in AAB24822. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

229

Helix Strand Turn

Details...

Beta strand

47 – 49

3

Beta strand

51 – 56

6

Beta strand

61 – 66

6

Beta strand

75 – 84

10

Turn

93 – 95

3

Beta strand

96 – 100

5

Beta strand

102 – 109

8

Turn

114 – 116

3

Beta strand

118 – 125

8

Turn

127 – 129

3

Beta strand

132 – 134

3

Beta strand

138 – 143

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified February 1, 1995. Version 1. Checksum: C467175567D10883	FASTA	229	26,048
	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
	Isoform Short [UniParc]. Checksum: 6CEE8C7A4F0AB1C0	FASTA	125	14,030
	10 20 30 40 50 60 MARLALSPVP SHWMVALLLL LSAEPVPAAR SEDRYRNPKG FSTLAQLKQR NTLKDGIIMI 70 80 90 100 110 120 QTLLIILFII VPIFLLLDKD DSKAGMEEDH TYEGLDIDQT ATYEDIVTLR TGEVKWSVGE HPGQE

References

	« Hide 'large scale' referencesShow '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 LONG). 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.

IPI

IPI00027668.
IPI00218810.

PIR

A46527. I54534.

RefSeq

NP_000617.1. NM_000626.2.
NP_001035022.1. NM_001039933.1.
NP_067613.1. NM_021602.2.

UniGene

Hs.89575.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3KG5	X-ray	3.20	A/B	26-159	[»]

DisProt

DP00503.

ProteinModelPortal

P40259.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59497N.

IntAct

P40259. 1 interaction.

STRING

9606.ENSP00000376544.

PTM databases

PhosphoSite

P40259.

Polymorphism databases

DMDM

728994.

Proteomic databases

PaxDb

P40259.

PRIDE

P40259.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000006750; ENSP00000006750; ENSG00000007312.
ENST00000349817; ENSP00000245862; ENSG00000007312.
ENST00000392795; ENSP00000376544; ENSG00000007312.

GeneID

974.

KEGG

hsa:974.

UCSC

uc002jdp.1. human.
uc002jdr.1. human.

Organism-specific databases

CTD

974.

GeneCards

GC17M062006.

HGNC

HGNC:1699. CD79B.

HPA

CAB009751.
HPA009178.

MIM

147245. gene.
612692. phenotype.

neXtProt

NX_P40259.

Orphanet

33110. Autosomal agammaglobulinemia.

PharmGKB

PA26238.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG46934.

HOGENOM

HOG000049137.

HOVERGEN

HBG050855.

KO

K06507.

Enzyme and pathway databases

Pathway_Interaction_DB

bcr_5pathway. BCR signaling pathway.

Reactome

REACT_6900. Immune System.

Gene expression databases

Bgee

P40259.

CleanEx

HS_CD79B.

Genevestigator

P40259.

GermOnline

ENSG00000007312. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 1 hit.

InterPro

IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
IPR003110. Phos_immunorcpt_sig_ITAM.
[Graphical view]

Pfam

PF02189. ITAM. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]

SMART

SM00409. IG. 1 hit.
SM00077. ITAM. 1 hit.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 1 hit.
PS51055. ITAM_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

GenomeRNAi

974.

NextBio

4082.

SOURCE

Search...

Entry information

Entry name

CD79B_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.