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P15530 (CD79B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:Igb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length228 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.8 Ref.11 Ref.13 Ref.14

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. Ref.6 Ref.7 Ref.9 Ref.15

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. Ref.10 Ref.12 Ref.14

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. Ref.7 Ref.9

Sequence similarities

Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Contains 1 ITAM domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525
Chain26 – 228203B-cell antigen receptor complex-associated protein beta chain
PRO_0000014561

Regions

Topological domain26 – 158133Extracellular Potential
Transmembrane159 – 18022Helical; Potential
Topological domain181 – 22848Cytoplasmic Potential
Domain41 – 13292Ig-like V-type
Domain184 – 21229ITAM

Amino acid modifications

Modified residue1951Phosphotyrosine; by SRC-type Tyr-kinases Ref.9
Modified residue2061Phosphotyrosine; by SRC-type Tyr-kinases Ref.9
Glycosylation681N-linked (GlcNAc...) Potential
Glycosylation991N-linked (GlcNAc...) Potential
Glycosylation1301N-linked (GlcNAc...) Potential
Disulfide bond43 ↔ 135 Ref.15
Disulfide bond65 ↔ 120 Ref.15
Disulfide bond135Interchain (with C-113 in alpha chain) Ref.15

Secondary structure

........................ 228
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15530 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 9A3A2008648E8307

FASTA22825,726
        10         20         30         40         50         60 
MATLVLSSMP CHWLLFLLLL FSGEPVPAMT SSDLPLNFQG SPCSQIWQHP RFAAKKRSSM 

        70         80         90        100        110        120 
VKFHCYTNHS GALTWFRKRG SQQPQELVSE EGRIVQTQNG SVYTLTIQNI QYEDNGIYFC 

       130        140        150        160        170        180 
KQKCDSANHN VTDSCGTELL VLGFSTLDQL KRRNTLKDGI ILIQTLLIIL FIIVPIFLLL 

       190        200        210        220 
DKDDGKAGME EDHTYEGLNI DQTATYEDIV TLRTGEVKWS VGEHPGQE 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS48960.1.
PIRB60228.
RefSeqNP_032365.1. NM_008339.2.
UniGeneMm.2987.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3KHOX-ray3.11A/B27-159[»]
3KHQX-ray1.70A27-159[»]
ProteinModelPortalP15530.
SMRP15530. Positions 43-142.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-59498N.
STRING10090.ENSMUSP00000048239.

PTM databases

PhosphoSiteP15530.

Proteomic databases

PaxDbP15530.
PRIDEP15530.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000167143; ENSMUSP00000129029; ENSMUSG00000040592.
GeneID15985.
KEGGmmu:15985.
UCSCuc007lyt.2. mouse.

Organism-specific databases

CTD974.
MGIMGI:96431. Cd79b.

Phylogenomic databases

eggNOGNOG46934.
GeneTreeENSGT00510000048811.
HOVERGENHBG050855.
InParanoidP15530.
KOK06507.

Gene expression databases

ArrayExpressP15530.
BgeeP15530.
CleanExMM_CD79B.
GenevestigatorP15530.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
IPR003110. Phos_immunorcpt_sig_ITAM.
[Graphical view]
PfamPF02189. ITAM. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTSM00409. IG. 1 hit.
SM00077. ITAM. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 1 hit.
PS51055. ITAM_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP15530.
NextBio288780.
PROP15530.
SOURCESearch...

Entry information

Entry nameCD79B_MOUSE
AccessionPrimary (citable) accession number: P15530
Secondary accession number(s): Q4FJP4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 9, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot