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Protein

B-cell antigen receptor complex-associated protein beta chain

Gene

Cd79b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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.4 Publications

GO - Molecular functioni

  1. transmembrane signaling receptor activity Source: InterPro

GO - Biological processi

  1. B cell receptor signaling pathway Source: MGI
Complete GO annotation...

Keywords - Biological processi

Adaptive immunity, Immunity

Enzyme and pathway databases

ReactomeiREACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

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:Igb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:96431. Cd79b.

Subcellular locationi

Cell membrane 3 Publications; Single-pass type I membrane protein 3 Publications
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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 158133ExtracellularSequence AnalysisAdd
BLAST
Transmembranei159 – 18022HelicalSequence AnalysisAdd
BLAST
Topological domaini181 – 22848CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. B cell receptor complex Source: MGI
  2. cytoplasm Source: MGI
  3. external side of plasma membrane Source: MGI
  4. extracellular vesicular exosome Source: MGI
  5. Golgi apparatus Source: MGI
  6. integral component of membrane Source: UniProtKB-KW
  7. nucleoplasm Source: MGI
  8. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Add
BLAST
Chaini26 – 228203B-cell antigen receptor complex-associated protein beta chainPRO_0000014561Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi43 ↔ 124PROSITE-ProRule annotation1 Publication
Disulfide bondi65 ↔ 120PROSITE-ProRule annotation1 Publication
Glycosylationi68 – 681N-linked (GlcNAc...)Sequence Analysis
Glycosylationi99 – 991N-linked (GlcNAc...)Sequence Analysis
Glycosylationi130 – 1301N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi135 – 135Interchain (with C-113 in alpha chain)PROSITE-ProRule annotation1 Publication
Modified residuei195 – 1951Phosphotyrosine; by SRC-type Tyr-kinasesPROSITE-ProRule annotation1 Publication
Modified residuei206 – 2061Phosphotyrosine; by SRC-type Tyr-kinasesPROSITE-ProRule annotation1 Publication

Post-translational modificationi

Phosphorylated on tyrosine upon B-cell activation by SRC-type Tyr-kinases such as BLK, LYN and SYK.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP15530.
PRIDEiP15530.

PTM databases

PhosphoSiteiP15530.

Expressioni

Tissue specificityi

B-cells.

Gene expression databases

BgeeiP15530.
CleanExiMM_CD79B.
ExpressionAtlasiP15530. baseline and differential.
GenevestigatoriP15530.

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.4 Publications

Protein-protein interaction databases

BioGridi200546. 1 interaction.
DIPiDIP-59498N.
STRINGi10090.ENSMUSP00000048239.

Structurei

Secondary structure

1
228
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi45 – 495Combined sources
Beta strandi51 – 566Combined sources
Beta strandi61 – 7111Combined sources
Beta strandi73 – 786Combined sources
Beta strandi84 – 863Combined sources
Turni90 – 934Combined sources
Beta strandi94 – 996Combined sources
Beta strandi102 – 1076Combined sources
Helixi112 – 1143Combined sources
Beta strandi116 – 1249Combined sources
Beta strandi131 – 1344Combined sources
Beta strandi137 – 1426Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KHOX-ray3.11A/B27-159[»]
3KHQX-ray1.70A27-159[»]
ProteinModelPortaliP15530.
SMRiP15530. Positions 43-142.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15530.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 13292Ig-like V-typeAdd
BLAST
Domaini184 – 21229ITAMPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 ITAM domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG46934.
GeneTreeiENSGT00510000048811.
HOVERGENiHBG050855.
InParanoidiP15530.
KOiK06507.

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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15530-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATLVLSSMP CHWLLFLLLL FSGEPVPAMT SSDLPLNFQG SPCSQIWQHP
60 70 80 90 100
RFAAKKRSSM VKFHCYTNHS GALTWFRKRG SQQPQELVSE EGRIVQTQNG
110 120 130 140 150
SVYTLTIQNI QYEDNGIYFC KQKCDSANHN VTDSCGTELL VLGFSTLDQL
160 170 180 190 200
KRRNTLKDGI ILIQTLLIIL FIIVPIFLLL DKDDGKAGME EDHTYEGLNI
210 220
DQTATYEDIV TLRTGEVKWS VGEHPGQE
Length:228
Mass (Da):25,726
Last modified:April 1, 1990 - v1
Checksum:i9A3A2008648E8307
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03857 mRNA. Translation: AAA37274.1.
AK143573 mRNA. Translation: BAE25444.1.
CT010358 mRNA. Translation: CAJ18566.1.
BC012226 mRNA. Translation: AAH12226.1.
AF002279 Genomic DNA. Translation: AAB93965.1.
CCDSiCCDS48960.1.
PIRiB60228.
RefSeqiNP_032365.1. NM_008339.2.
UniGeneiMm.2987.

Genome annotation databases

EnsembliENSMUST00000167143; ENSMUSP00000129029; ENSMUSG00000040592.
GeneIDi15985.
KEGGimmu:15985.
UCSCiuc007lyt.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03857 mRNA. Translation: AAA37274.1.
AK143573 mRNA. Translation: BAE25444.1.
CT010358 mRNA. Translation: CAJ18566.1.
BC012226 mRNA. Translation: AAH12226.1.
AF002279 Genomic DNA. Translation: AAB93965.1.
CCDSiCCDS48960.1.
PIRiB60228.
RefSeqiNP_032365.1. NM_008339.2.
UniGeneiMm.2987.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KHOX-ray3.11A/B27-159[»]
3KHQX-ray1.70A27-159[»]
ProteinModelPortaliP15530.
SMRiP15530. Positions 43-142.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200546. 1 interaction.
DIPiDIP-59498N.
STRINGi10090.ENSMUSP00000048239.

PTM databases

PhosphoSiteiP15530.

Proteomic databases

PaxDbiP15530.
PRIDEiP15530.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000167143; ENSMUSP00000129029; ENSMUSG00000040592.
GeneIDi15985.
KEGGimmu:15985.
UCSCiuc007lyt.2. mouse.

Organism-specific databases

CTDi974.
MGIiMGI:96431. Cd79b.

Phylogenomic databases

eggNOGiNOG46934.
GeneTreeiENSGT00510000048811.
HOVERGENiHBG050855.
InParanoidiP15530.
KOiK06507.

Enzyme and pathway databases

ReactomeiREACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Miscellaneous databases

EvolutionaryTraceiP15530.
NextBioi288780.
PROiP15530.
SOURCEiSearch...

Gene expression databases

BgeeiP15530.
CleanExiMM_CD79B.
ExpressionAtlasiP15530. baseline and differential.
GenevestigatoriP15530.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "B29: a member of the immunoglobulin gene superfamily exclusively expressed on beta-lineage cells."
    Hermanson G.G., Eisenberg D., Kincade P.W., Wall R.
    Proc. Natl. Acad. Sci. U.S.A. 85:6890-6894(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: B-cell.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Spleen.
  3. "Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
    Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "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].
    Strain: FVB/N.
    Tissue: Salivary gland.
  5. "Immunoglobulin enhancer and promoter motifs 5' of the B29 B-cell-specific gene."
    Hermanson G.G., Briskin M., Sigman D., Wall R.
    Proc. Natl. Acad. Sci. U.S.A. 86:7341-7345(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
  6. "The MB-1/B29 heterodimer couples the B cell antigen receptor to multiple src family protein tyrosine kinases."
    Lin J., Justement L.B.
    J. Immunol. 149:1548-1555(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BLK.
  7. "B-cell antigen receptor motifs have redundant signalling capabilities and bind the tyrosine kinases PTK72, Lyn and Fyn."
    Law D.A., Chan V.W., Datta S.K., DeFranco A.L.
    Curr. Biol. 3:645-657(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LYN, PHOSPHORYLATION.
  8. "Activation of B- and T-cells by the cytoplasmic domains of the B-cell antigen receptor proteins Ig-alpha and Ig-beta."
    Taddie J.A., Hurley T.R., Hardwick B.S., Sefton B.M.
    J. Biol. Chem. 269:13529-13535(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Reconstitution of the B cell antigen receptor signaling components in COS cells."
    Saouaf S.J., Kut S.A., Fargnoli J., Rowley R.B., Bolen J.B., Mahajan S.
    J. Biol. Chem. 270:27072-27078(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BLK, PHOSPHORYLATION AT TYR-195 AND TYR-206.
  10. "A role for lipid rafts in B cell antigen receptor signaling and antigen targeting."
    Cheng P.C., Dykstra M.L., Mitchell R.N., Pierce S.K.
    J. Exp. Med. 190:1549-1560(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. "Ig alpha and Ig beta are required for efficient trafficking to late endosomes and to enhance antigen presentation."
    Siemasko K., Eisfelder B.J., Stebbins C., Kabak S., Sant A.J., Song W., Clark M.R.
    J. Immunol. 162:6518-6525(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Translocation of the B cell antigen receptor into lipid rafts reveals a novel step in signaling."
    Cheng P.C., Brown B.K., Song W., Pierce S.K.
    J. Immunol. 166:3693-3701(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  13. "Cooperative interaction of Ig(alpha) and Ig(beta) of the BCR regulates the kinetics and specificity of antigen targeting."
    Li C., Siemasko K., Clark M.R., Song W.
    Int. Immunol. 14:1179-1191(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Ig alpha/Ig beta complexes generate signals for B cell development independent of selective plasma membrane compartmentalization."
    Fuentes-Panana E.M., Bannish G., van der Voort D., King L.B., Monroe J.G.
    J. Immunol. 174:1245-1252(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  15. "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 (1.7 ANGSTROMS) OF 27-159, SUBUNIT, DISULFIDE BONDS.

Entry informationi

Entry nameiCD79B_MOUSE
AccessioniPrimary (citable) accession number: P15530
Secondary accession number(s): Q4FJP4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: March 4, 2015
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

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.