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B-cell antigen receptor complex-associated protein beta chain (B-cell-specific glycoprotein B29) (Ig-beta) (Immunoglobulin-associated B29 protein) (CD antigen CD79b)

 CD79B_HUMAN             Reviewed;         229 AA.
P40259; Q53FS2; Q9BU06;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
25-OCT-2017, entry version 170.
RecName: Full=B-cell antigen receptor complex-associated protein beta chain;
AltName: Full=B-cell-specific glycoprotein B29;
AltName: Full=Ig-beta;
AltName: Full=Immunoglobulin-associated B29 protein;
AltName: CD_antigen=CD79b;
Flags: Precursor;
Name=CD79B; Synonyms=B29, IGB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
PubMed=1534761; DOI=10.1002/eji.1830220641;
Mueller B.S., Cooper L., Terhorst C.;
"Cloning and sequencing of the cDNA encoding the human homologue of
the murine immunoglobulin-associated protein B29.";
Eur. J. Immunol. 22:1621-1625(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
PubMed=8486355; DOI=10.1006/geno.1993.1157;
Wood W.J. Jr., Thompson A.A., Korenberg J., Chen X.-N., May W.,
Wall R., Denny C.T.;
"Isolation and chromosomal mapping of the human immunoglobulin-
associated B29 gene (IGB).";
Genomics 16:187-192(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
PubMed=8419481;
Hashimoto S., Gregersen P.K., Chiorazzi N.;
"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.";
J. Immunol. 150:491-498(1993).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG).
PubMed=7913081; DOI=10.1007/BF00188178;
Hashimoto S., Chiorazzi N., Gregersen P.K.;
"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.";
Immunogenetics 40:145-149(1994).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
PubMed=7643857; DOI=10.1016/0161-5890(95)00023-8;
Hashimoto S., Chiorazzi N., Gregersen P.K.;
"Alternative splicing of CD79a (Ig-alpha/mb-1) and CD79b (Ig-beta/B29)
RNA transcripts in human B cells.";
Mol. Immunol. 32:651-659(1995).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
Koyama M., Nakamura T.;
Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Small intestine, and Spleen;
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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 29-45.
PubMed=7514267; DOI=10.1016/0161-5890(94)90061-2;
Vasile S., Coligan J.E., Yoshida M., Seon B.K.;
"Isolation and chemical characterization of the human B29 and mb-1
proteins of the B cell antigen receptor complex.";
Mol. Immunol. 31:419-427(1994).
[10]
FUNCTION.
PubMed=8617796; DOI=10.1074/jbc.271.9.5158;
Luisiri P., Lee Y.J., Eisfelder B.J., Clark M.R.;
"Cooperativity and segregation of function within the Ig-alpha/beta
heterodimer of the B cell antigen receptor complex.";
J. Biol. Chem. 271:5158-5163(1996).
[11]
FUNCTION.
PubMed=9057631;
Tseng J., Eisfelder B.J., Clark M.R.;
"B-cell antigen receptor-induced apoptosis requires both Ig alpha and
Ig beta.";
Blood 89:1513-1520(1997).
[12]
FUNCTION.
PubMed=12097390; DOI=10.4049/jimmunol.169.2.865;
Pelanda R., Braun U., Hobeika E., Nussenzweig M.C., Reth M.;
"B cell progenitors are arrested in maturation but have intact VDJ
recombination in the absence of Ig-alpha and Ig-beta.";
J. Immunol. 169:865-872(2002).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 26-159, SUBUNIT, AND
DISULFIDE BONDS.
PubMed=20696394; DOI=10.1016/j.str.2010.04.019;
Radaev S., Zou Z., Tolar P., Nguyen K., Nguyen A., Krueger P.D.,
Stutzman N., Pierce S., Sun P.D.;
"Structural and functional studies of Igalphabeta and its assembly
with the B cell antigen receptor.";
Structure 18:934-943(2010).
[15]
VARIANT AGM6 SER-137.
PubMed=17675462; DOI=10.4049/jimmunol.179.4.2055;
Dobbs A.K., Yang T., Farmer D., Kager L., Parolini O., Conley M.E.;
"A hypomorphic mutation in Igbeta (CD79b) in a patient with
immunodeficiency and a leaky defect in B cell development.";
J. Immunol. 179:2055-2059(2007).
-!- 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.
{ECO:0000269|PubMed:12097390, ECO:0000269|PubMed:8617796,
ECO:0000269|PubMed:9057631}.
-!- SUBUNIT: 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).
{ECO:0000250}.
-!- INTERACTION:
O43765:SGTA; NbExp=6; IntAct=EBI-2873732, EBI-347996;
Q96EQ0:SGTB; NbExp=4; IntAct=EBI-2873732, EBI-744081;
-!- 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. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=Long;
IsoId=P40259-1; Sequence=Displayed;
Name=Short;
IsoId=P40259-2; Sequence=VSP_002477;
Name=3;
IsoId=P40259-3; Sequence=VSP_047222;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: B-cells.
-!- PTM: Phosphorylated on tyrosine upon B-cell activation by SRC-type
Tyr-kinases such as BLK, LYN and SYK.
-!- 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. {ECO:0000269|PubMed:17675462}. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- WEB RESOURCE: Name=CD79Bbase; Note=CD79B mutation db;
URL="http://structure.bmc.lu.se/idbase/CD79Bbase/";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; M80461; AAA58387.1; -; mRNA.
EMBL; M89957; AAA64459.1; -; mRNA.
EMBL; S52229; AAB24822.2; -; mRNA.
EMBL; L27587; AAA72424.1; -; Genomic_DNA.
EMBL; S79249; AAC60654.1; -; mRNA.
EMBL; X83539; CAA58522.1; -; mRNA.
EMBL; AK222954; BAD96674.1; -; mRNA.
EMBL; AK223210; BAD96930.1; -; mRNA.
EMBL; BC002975; AAH02975.2; -; mRNA.
EMBL; BC032651; AAH32651.1; -; mRNA.
CCDS; CCDS11655.1; -. [P40259-1]
CCDS; CCDS11656.1; -. [P40259-2]
CCDS; CCDS42372.1; -. [P40259-3]
PIR; I54534; A46527.
RefSeq; NP_000617.1; NM_000626.3. [P40259-1]
RefSeq; NP_001035022.1; NM_001039933.2. [P40259-3]
RefSeq; NP_067613.1; NM_021602.3. [P40259-2]
UniGene; Hs.89575; -.
PDB; 3KG5; X-ray; 3.20 A; A/B=26-159.
PDBsum; 3KG5; -.
ProteinModelPortal; P40259; -.
SMR; P40259; -.
BioGrid; 107412; 110.
DIP; DIP-59497N; -.
ELM; P40259; -.
IntAct; P40259; 3.
STRING; 9606.ENSP00000376544; -.
iPTMnet; P40259; -.
PhosphoSitePlus; P40259; -.
BioMuta; CD79B; -.
DMDM; 728994; -.
EPD; P40259; -.
MaxQB; P40259; -.
PaxDb; P40259; -.
PeptideAtlas; P40259; -.
PRIDE; P40259; -.
TopDownProteomics; P40259-2; -. [P40259-2]
Ensembl; ENST00000006750; ENSP00000006750; ENSG00000007312. [P40259-1]
Ensembl; ENST00000349817; ENSP00000245862; ENSG00000007312. [P40259-2]
Ensembl; ENST00000392795; ENSP00000376544; ENSG00000007312. [P40259-3]
GeneID; 974; -.
KEGG; hsa:974; -.
UCSC; uc002jdp.2; human. [P40259-1]
CTD; 974; -.
DisGeNET; 974; -.
EuPathDB; HostDB:ENSG00000007312.12; -.
GeneCards; CD79B; -.
HGNC; HGNC:1699; CD79B.
HPA; CAB009751; -.
HPA; HPA009178; -.
MalaCards; CD79B; -.
MIM; 147245; gene.
MIM; 612692; phenotype.
neXtProt; NX_P40259; -.
OpenTargets; ENSG00000007312; -.
Orphanet; 33110; Autosomal agammaglobulinemia.
PharmGKB; PA26238; -.
eggNOG; ENOG410J02H; Eukaryota.
eggNOG; ENOG410Z4S5; LUCA.
GeneTree; ENSGT00510000048811; -.
HOGENOM; HOG000049137; -.
HOVERGEN; HBG050855; -.
InParanoid; P40259; -.
KO; K06507; -.
OMA; DQTATYE; -.
OrthoDB; EOG091G0O8L; -.
PhylomeDB; P40259; -.
TreeFam; TF336032; -.
Reactome; R-HSA-5690714; CD22 mediated BCR regulation.
Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SignaLink; P40259; -.
SIGNOR; P40259; -.
GeneWiki; CD79B; -.
GenomeRNAi; 974; -.
PRO; PR:P40259; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000007312; -.
CleanEx; HS_CD79B; -.
Genevisible; P40259; HS.
GO; GO:0019815; C:B cell receptor complex; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0042803; F:protein homodimerization activity; IMP:CAFA.
GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0030183; P:B cell differentiation; IBA:GO_Central.
GO; GO:0050853; P:B cell receptor signaling pathway; IBA:GO_Central.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0051260; P:protein homooligomerization; IMP:CAFA.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR013106; Ig_V-set.
InterPro; IPR003110; Phos_immunorcpt_sig_ITAM.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 1.
SMART; SM00077; ITAM; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS51055; ITAM_1; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Alternative splicing; Cell membrane;
Complete proteome; Direct protein sequencing; Disease mutation;
Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain;
Membrane; Phosphoprotein; Reference proteome; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 28 {ECO:0000269|PubMed:7514267}.
CHAIN 29 229 B-cell antigen receptor complex-
associated protein beta chain.
/FTId=PRO_0000014560.
TOPO_DOM 29 159 Extracellular. {ECO:0000255}.
TRANSMEM 160 180 Helical. {ECO:0000255}.
TOPO_DOM 181 229 Cytoplasmic. {ECO:0000255}.
DOMAIN 38 138 Ig-like V-type.
DOMAIN 185 213 ITAM. {ECO:0000255|PROSITE-
ProRule:PRU00379}.
MOD_RES 196 196 Phosphotyrosine; by SRC-type Tyr-kinases.
{ECO:0000250|UniProtKB:P15530,
ECO:0000255|PROSITE-ProRule:PRU00379}.
MOD_RES 207 207 Phosphotyrosine; by SRC-type Tyr-kinases.
{ECO:0000250|UniProtKB:P15530,
ECO:0000255|PROSITE-ProRule:PRU00379}.
CARBOHYD 73 73 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 101 101 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 127 127 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 128 128 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 43 126 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:20696394}.
DISULFID 65 122 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:20696394}.
DISULFID 136 136 Interchain (with C-119 in alpha chain).
{ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:20696394}.
VAR_SEQ 23 23 A -> AA (in isoform 3).
{ECO:0000303|Ref.7}.
/FTId=VSP_047222.
VAR_SEQ 41 144 Missing (in isoform Short).
{ECO:0000303|PubMed:7643857,
ECO:0000303|Ref.6}.
/FTId=VSP_002477.
VARIANT 137 137 G -> S (in AGM6; dbSNP:rs121912424).
{ECO:0000269|PubMed:17675462}.
/FTId=VAR_057833.
CONFLICT 58 58 G -> A (in Ref. 3; AAB24822).
{ECO:0000305}.
CONFLICT 58 58 G -> R (in Ref. 1; AAA58387).
{ECO:0000305}.
CONFLICT 84 84 E -> A (in Ref. 3; AAB24822).
{ECO:0000305}.
STRAND 47 49 {ECO:0000244|PDB:3KG5}.
STRAND 51 56 {ECO:0000244|PDB:3KG5}.
STRAND 61 66 {ECO:0000244|PDB:3KG5}.
STRAND 75 84 {ECO:0000244|PDB:3KG5}.
TURN 93 95 {ECO:0000244|PDB:3KG5}.
STRAND 96 100 {ECO:0000244|PDB:3KG5}.
STRAND 102 109 {ECO:0000244|PDB:3KG5}.
TURN 114 116 {ECO:0000244|PDB:3KG5}.
STRAND 118 125 {ECO:0000244|PDB:3KG5}.
TURN 127 129 {ECO:0000244|PDB:3KG5}.
STRAND 132 134 {ECO:0000244|PDB:3KG5}.
STRAND 138 143 {ECO:0000244|PDB:3KG5}.
SEQUENCE 229 AA; 26048 MW; C467175567D10883 CRC64;
MARLALSPVP SHWMVALLLL LSAEPVPAAR SEDRYRNPKG SACSRIWQSP RFIARKRGFT
VKMHCYMNSA SGNVSWLWKQ EMDENPQQLK LEKGRMEESQ NESLATLTIQ GIRFEDNGIY
FCQQKCNNTS EVYQGCGTEL RVMGFSTLAQ LKQRNTLKDG IIMIQTLLII LFIIVPIFLL
LDKDDSKAGM EEDHTYEGLD IDQTATYEDI VTLRTGEVKW SVGEHPGQE


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