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P15530

- CD79B_MOUSE

UniProt

P15530 - CD79B_MOUSE

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Protein

B-cell antigen receptor complex-associated protein beta chain

Gene

Cd79b

Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

GO - Cellular componenti

  1. B cell receptor complex Source: MGI
  2. external side of plasma membrane Source: MGI
  3. integral component of membrane Source: UniProtKB-KW
  4. plasma membrane Source: Reactome
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 ↔ 1241 PublicationPROSITE-ProRule annotation
Disulfide bondi65 ↔ 1201 PublicationPROSITE-ProRule annotation
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)1 PublicationPROSITE-ProRule annotation
Modified residuei195 – 1951Phosphotyrosine; by SRC-type Tyr-kinases1 PublicationPROSITE-ProRule annotation
Modified residuei206 – 2061Phosphotyrosine; by SRC-type Tyr-kinases1 PublicationPROSITE-ProRule annotation

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 – 495
Beta strandi51 – 566
Beta strandi61 – 7111
Beta strandi73 – 786
Beta strandi84 – 863
Turni90 – 934
Beta strandi94 – 996
Beta strandi102 – 1076
Helixi112 – 1143
Beta strandi116 – 1249
Beta strandi131 – 1344
Beta strandi137 – 1426

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP15530.

Topological domain

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

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei159 – 18022HelicalSequence AnalysisAdd
BLAST

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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS48960.1.
PIRi B60228.
RefSeqi NP_032365.1. NM_008339.2.
UniGenei Mm.2987.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3KHO X-ray 3.11 A/B 27-159 [» ]
3KHQ X-ray 1.70 A 27-159 [» ]
ProteinModelPortali P15530.
SMRi P15530. Positions 43-142.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200546. 1 interaction.
DIPi DIP-59498N.
STRINGi 10090.ENSMUSP00000048239.

PTM databases

PhosphoSitei P15530.

Proteomic databases

PaxDbi P15530.
PRIDEi P15530.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000167143 ; ENSMUSP00000129029 ; ENSMUSG00000040592 .
GeneIDi 15985.
KEGGi mmu:15985.
UCSCi uc007lyt.2. mouse.

Organism-specific databases

CTDi 974.
MGIi MGI:96431. Cd79b.

Phylogenomic databases

eggNOGi NOG46934.
GeneTreei ENSGT00510000048811.
HOVERGENi HBG050855.
InParanoidi P15530.
KOi K06507.

Enzyme and pathway databases

Reactomei REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Miscellaneous databases

EvolutionaryTracei P15530.
NextBioi 288780.
PROi P15530.
SOURCEi Search...

Gene expression databases

Bgeei P15530.
CleanExi MM_CD79B.
ExpressionAtlasi P15530. baseline and differential.
Genevestigatori P15530.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
InterProi IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
IPR003110. Phos_immunorcpt_sig_ITAM.
[Graphical view ]
Pfami PF02189. ITAM. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view ]
SMARTi SM00409. IG. 1 hit.
SM00077. ITAM. 1 hit.
[Graphical view ]
PROSITEi PS50835. IG_LIKE. 1 hit.
PS51055. ITAM_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 139 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