CD79B_HUMAN
ID CD79B_HUMAN Reviewed; 229 AA.
AC P40259; Q53FS2; Q9BU06;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=B-cell antigen receptor complex-associated protein beta chain;
DE AltName: Full=B-cell-specific glycoprotein B29;
DE AltName: Full=Ig-beta;
DE AltName: Full=Immunoglobulin-associated B29 protein;
DE AltName: CD_antigen=CD79b;
DE Flags: Precursor;
GN Name=CD79B; Synonyms=B29, IGB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RX PubMed=1534761; DOI=10.1002/eji.1830220641;
RA Mueller B.S., Cooper L., Terhorst C.;
RT "Cloning and sequencing of the cDNA encoding the human homologue of the
RT murine immunoglobulin-associated protein B29.";
RL Eur. J. Immunol. 22:1621-1625(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RX PubMed=8486355; DOI=10.1006/geno.1993.1157;
RA Wood W.J. Jr., Thompson A.A., Korenberg J., Chen X.-N., May W., Wall R.,
RA Denny C.T.;
RT "Isolation and chromosomal mapping of the human immunoglobulin-associated
RT B29 gene (IGB).";
RL Genomics 16:187-192(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RX PubMed=8419481;
RA Hashimoto S., Gregersen P.K., Chiorazzi N.;
RT "The human Ig-beta cDNA sequence, a homologue of murine B29, is identical
RT in B cell and plasma cell lines producing all the human Ig isotypes.";
RL J. Immunol. 150:491-498(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG).
RX PubMed=7913081; DOI=10.1007/bf00188178;
RA Hashimoto S., Chiorazzi N., Gregersen P.K.;
RT "The complete sequence of the human CD79b (Ig beta/B29) gene:
RT identification of a conserved exon/intron organization, immunoglobulin-like
RT regulatory regions, and allelic polymorphism.";
RL Immunogenetics 40:145-149(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RX PubMed=7643857; DOI=10.1016/0161-5890(95)00023-8;
RA Hashimoto S., Chiorazzi N., Gregersen P.K.;
RT "Alternative splicing of CD79a (Ig-alpha/mb-1) and CD79b (Ig-beta/B29) RNA
RT transcripts in human B cells.";
RL Mol. Immunol. 32:651-659(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RA Koyama M., Nakamura T.;
RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Small intestine, and Spleen;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC TISSUE=Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 29-45.
RX PubMed=7514267; DOI=10.1016/0161-5890(94)90061-2;
RA Vasile S., Coligan J.E., Yoshida M., Seon B.K.;
RT "Isolation and chemical characterization of the human B29 and mb-1 proteins
RT of the B cell antigen receptor complex.";
RL Mol. Immunol. 31:419-427(1994).
RN [10]
RP FUNCTION.
RX PubMed=8617796; DOI=10.1074/jbc.271.9.5158;
RA Luisiri P., Lee Y.J., Eisfelder B.J., Clark M.R.;
RT "Cooperativity and segregation of function within the Ig-alpha/beta
RT heterodimer of the B cell antigen receptor complex.";
RL J. Biol. Chem. 271:5158-5163(1996).
RN [11]
RP FUNCTION.
RX PubMed=9057631;
RA Tseng J., Eisfelder B.J., Clark M.R.;
RT "B-cell antigen receptor-induced apoptosis requires both Ig alpha and Ig
RT beta.";
RL Blood 89:1513-1520(1997).
RN [12]
RP FUNCTION.
RX PubMed=12097390; DOI=10.4049/jimmunol.169.2.865;
RA Pelanda R., Braun U., Hobeika E., Nussenzweig M.C., Reth M.;
RT "B cell progenitors are arrested in maturation but have intact VDJ
RT recombination in the absence of Ig-alpha and Ig-beta.";
RL J. Immunol. 169:865-872(2002).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 26-159, SUBUNIT, AND DISULFIDE
RP BONDS.
RX PubMed=20696394; DOI=10.1016/j.str.2010.04.019;
RA Radaev S., Zou Z., Tolar P., Nguyen K., Nguyen A., Krueger P.D.,
RA Stutzman N., Pierce S., Sun P.D.;
RT "Structural and functional studies of Igalphabeta and its assembly with the
RT B cell antigen receptor.";
RL Structure 18:934-943(2010).
RN [15]
RP VARIANT AGM6 SER-137.
RX PubMed=17675462; DOI=10.4049/jimmunol.179.4.2055;
RA Dobbs A.K., Yang T., Farmer D., Kager L., Parolini O., Conley M.E.;
RT "A hypomorphic mutation in Igbeta (CD79b) in a patient with
RT immunodeficiency and a leaky defect in B cell development.";
RL J. Immunol. 179:2055-2059(2007).
CC -!- FUNCTION: Required in cooperation with CD79A for initiation of the
CC signal transduction cascade activated by the B-cell antigen receptor
CC complex (BCR) which leads to internalization of the complex,
CC trafficking to late endosomes and antigen presentation. Enhances
CC phosphorylation of CD79A, possibly by recruiting kinases which
CC phosphorylate CD79A or by recruiting proteins which bind to CD79A and
CC protect it from dephosphorylation. {ECO:0000269|PubMed:12097390,
CC ECO:0000269|PubMed:8617796, ECO:0000269|PubMed:9057631}.
CC -!- SUBUNIT: Heterodimer of alpha and beta chains; disulfide-linked. Part
CC of the B-cell antigen receptor complex where the alpha/beta chain
CC heterodimer is non-covalently associated with an antigen-specific
CC membrane-bound surface immunoglobulin of two heavy chains and two light
CC chains. Interacts with LYN (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P40259; O43765: SGTA; NbExp=6; IntAct=EBI-2873732, EBI-347996;
CC P40259; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-2873732, EBI-744081;
CC P40259-1; P40259-1: CD79B; NbExp=3; IntAct=EBI-15869023, EBI-15869023;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Note=Following antigen binding, the BCR has been shown to
CC translocate from detergent-soluble regions of the cell membrane to
CC lipid rafts although signal transduction through the complex can also
CC occur outside lipid rafts. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Long;
CC IsoId=P40259-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P40259-2; Sequence=VSP_002477;
CC Name=3;
CC IsoId=P40259-3; Sequence=VSP_047222;
CC -!- TISSUE SPECIFICITY: B-cells.
CC -!- PTM: Phosphorylated on tyrosine upon B-cell activation by SRC-type Tyr-
CC kinases such as BLK, LYN and SYK.
CC -!- DISEASE: Agammaglobulinemia 6, autosomal recessive (AGM6) [MIM:612692]:
CC A primary immunodeficiency characterized by profoundly low or absent
CC serum antibodies and low or absent circulating B-cells due to an early
CC block of B-cell development. Affected individuals develop severe
CC infections in the first years of life. {ECO:0000269|PubMed:17675462}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- WEB RESOURCE: Name=CD79Bbase; Note=CD79B mutation db;
CC URL="http://structure.bmc.lu.se/idbase/CD79Bbase/";
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DR EMBL; M80461; AAA58387.1; -; mRNA.
DR EMBL; M89957; AAA64459.1; -; mRNA.
DR EMBL; S52229; AAB24822.2; -; mRNA.
DR EMBL; L27587; AAA72424.1; -; Genomic_DNA.
DR EMBL; S79249; AAC60654.1; -; mRNA.
DR EMBL; X83539; CAA58522.1; -; mRNA.
DR EMBL; AK222954; BAD96674.1; -; mRNA.
DR EMBL; AK223210; BAD96930.1; -; mRNA.
DR EMBL; BC002975; AAH02975.2; -; mRNA.
DR EMBL; BC032651; AAH32651.1; -; mRNA.
DR CCDS; CCDS11655.1; -. [P40259-1]
DR CCDS; CCDS11656.1; -. [P40259-2]
DR CCDS; CCDS42372.1; -. [P40259-3]
DR PIR; I54534; A46527.
DR RefSeq; NP_000617.1; NM_000626.3. [P40259-1]
DR RefSeq; NP_001035022.1; NM_001039933.2. [P40259-3]
DR RefSeq; NP_067613.1; NM_021602.3. [P40259-2]
DR PDB; 3KG5; X-ray; 3.20 A; A/B=26-159.
DR PDBsum; 3KG5; -.
DR AlphaFoldDB; P40259; -.
DR BMRB; P40259; -.
DR SMR; P40259; -.
DR BioGRID; 107412; 180.
DR DIP; DIP-59497N; -.
DR ELM; P40259; -.
DR IntAct; P40259; 95.
DR STRING; 9606.ENSP00000376544; -.
DR ChEMBL; CHEMBL3712852; -.
DR DrugBank; DB12240; Polatuzumab vedotin.
DR DrugCentral; P40259; -.
DR GlyGen; P40259; 5 sites.
DR iPTMnet; P40259; -.
DR PhosphoSitePlus; P40259; -.
DR BioMuta; CD79B; -.
DR DMDM; 728994; -.
DR EPD; P40259; -.
DR jPOST; P40259; -.
DR MassIVE; P40259; -.
DR MaxQB; P40259; -.
DR PaxDb; P40259; -.
DR PeptideAtlas; P40259; -.
DR PRIDE; P40259; -.
DR ProteomicsDB; 55356; -. [P40259-1]
DR ProteomicsDB; 55357; -. [P40259-2]
DR TopDownProteomics; P40259-2; -. [P40259-2]
DR ABCD; P40259; 22 sequenced antibodies.
DR Antibodypedia; 2218; 1044 antibodies from 42 providers.
DR DNASU; 974; -.
DR Ensembl; ENST00000006750.8; ENSP00000006750.4; ENSG00000007312.13. [P40259-1]
DR Ensembl; ENST00000349817.2; ENSP00000245862.2; ENSG00000007312.13. [P40259-2]
DR Ensembl; ENST00000392795.7; ENSP00000376544.3; ENSG00000007312.13. [P40259-3]
DR GeneID; 974; -.
DR KEGG; hsa:974; -.
DR MANE-Select; ENST00000006750.8; ENSP00000006750.4; NM_000626.4; NP_000617.1.
DR UCSC; uc002jdp.2; human. [P40259-1]
DR CTD; 974; -.
DR DisGeNET; 974; -.
DR GeneCards; CD79B; -.
DR HGNC; HGNC:1699; CD79B.
DR HPA; ENSG00000007312; Tissue enriched (lymphoid).
DR MalaCards; CD79B; -.
DR MIM; 147245; gene.
DR MIM; 612692; phenotype.
DR neXtProt; NX_P40259; -.
DR OpenTargets; ENSG00000007312; -.
DR Orphanet; 33110; Autosomal agammaglobulinemia.
DR PharmGKB; PA26238; -.
DR VEuPathDB; HostDB:ENSG00000007312; -.
DR eggNOG; ENOG502S7X8; Eukaryota.
DR GeneTree; ENSGT00940000154363; -.
DR HOGENOM; CLU_084230_0_0_1; -.
DR InParanoid; P40259; -.
DR OMA; YRGCGTE; -.
DR OrthoDB; 1234092at2759; -.
DR PhylomeDB; P40259; -.
DR TreeFam; TF336032; -.
DR PathwayCommons; P40259; -.
DR Reactome; R-HSA-5690714; CD22 mediated BCR regulation.
DR Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR SignaLink; P40259; -.
DR SIGNOR; P40259; -.
DR BioGRID-ORCS; 974; 17 hits in 1073 CRISPR screens.
DR ChiTaRS; CD79B; human.
DR GeneWiki; CD79B; -.
DR GenomeRNAi; 974; -.
DR Pharos; P40259; Tclin.
DR PRO; PR:P40259; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P40259; protein.
DR Bgee; ENSG00000007312; Expressed in granulocyte and 147 other tissues.
DR Genevisible; P40259; HS.
DR GO; GO:0019815; C:B cell receptor complex; IBA:GO_Central.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0042802; F:identical protein binding; IDA:CAFA.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0030183; P:B cell differentiation; IBA:GO_Central.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR DisProt; DP01487; -.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR039695; CD79a/CD79b.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR003110; Phos_immunorcpt_sig_ITAM.
DR PANTHER; PTHR14334; PTHR14334; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00077; ITAM; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51055; ITAM_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein;
KW Immunity; Immunoglobulin domain; Membrane; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:7514267"
FT CHAIN 29..229
FT /note="B-cell antigen receptor complex-associated protein
FT beta chain"
FT /id="PRO_0000014560"
FT TOPO_DOM 29..159
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 38..138
FT /note="Ig-like V-type"
FT DOMAIN 185..213
FT /note="ITAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 196
FT /note="Phosphotyrosine; by SRC-type Tyr-kinases"
FT /evidence="ECO:0000250|UniProtKB:P15530,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 207
FT /note="Phosphotyrosine; by SRC-type Tyr-kinases"
FT /evidence="ECO:0000250|UniProtKB:P15530,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:20696394"
FT DISULFID 65..122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:20696394"
FT DISULFID 136
FT /note="Interchain (with C-119 in alpha chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:20696394"
FT VAR_SEQ 23
FT /note="A -> AA (in isoform 3)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_047222"
FT VAR_SEQ 41..144
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:7643857, ECO:0000303|Ref.6"
FT /id="VSP_002477"
FT VARIANT 137
FT /note="G -> S (in AGM6; dbSNP:rs121912424)"
FT /evidence="ECO:0000269|PubMed:17675462"
FT /id="VAR_057833"
FT CONFLICT 58
FT /note="G -> A (in Ref. 3; AAB24822)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="G -> R (in Ref. 1; AAA58387)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="E -> A (in Ref. 3; AAB24822)"
FT /evidence="ECO:0000305"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:3KG5"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:3KG5"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:3KG5"
FT STRAND 75..84
FT /evidence="ECO:0007829|PDB:3KG5"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:3KG5"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:3KG5"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:3KG5"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:3KG5"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:3KG5"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:3KG5"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:3KG5"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:3KG5"
SQ 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
