Breakpoint cluster region protein - Mus musculus (Mouse)

Contribute

Send feedback

Read comments (?) or add your own

Q6PAJ1 (BCR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 81. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Breakpoint cluster region protein
EC=2.7.11.1

Gene names

Name:	Bcr
Synonyms:	Kiaa3017

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1270 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	GTPase-activating protein for RAC1 and CDC42. Promotes the exchange of RAC or CDC42-bound GDP by GTP, thereby activating them. Displays serine/threonine kinase activity By similarity.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Homotetramer. Interacts with PDZK1. Interacts with HCK, FES/FPS, ABL1, PIK3R1 and GRB2 By similarity. May interact with CCPG1. Ref.5
Domain	The region involved in binding to ABL1 SH2-domain is rich in serine residues and needs to be Ser/Thr phosphorylated prior to SH2 binding. This region is essential for the activation of the ABL1 tyrosine kinase By similarity. The DH domain is involved in interaction with CCPG1.
Post-translational modification	Autophosphorylated. Phosphorylated by FES/FPS on tyrosine residues, leading to down-regulation of the BCR kinase activity. Phosphorylation at Tyr-178 by HCK is important for interaction with GRB2 By similarity.
Sequence similarities	Contains 1 C2 domain. Contains 1 DH (DBL-homology) domain. Contains 1 PH domain. Contains 1 Rho-GAP domain.

Ontologies

Keywords
Disease	Proto-oncogene
Ligand	ATP-binding Nucleotide-binding
Molecular function	GTPase activation Guanine-nucleotide releasing factor Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin cytoskeleton organization Inferred from genetic interaction PubMed 17116687. Source: MGI brain development Inferred from genetic interaction PubMed 11684658. Source: MGI inner ear morphogenesis Inferred from genetic interaction PubMed 11921339. Source: MGI intracellular signal transduction Inferred from electronic annotation. Source: InterPro negative regulation of cell migration Inferred from genetic interaction PubMed 17116687. Source: MGI negative regulation of inflammatory response Inferred from mutant phenotype PubMed 19703997. Source: MGI negative regulation of neutrophil degranulation Inferred from genetic interaction PubMed 19703997. Source: MGI neuromuscular process controlling balance Inferred from genetic interaction PubMed 11921339. Source: MGI platelet-derived growth factor receptor signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of phagocytosis Inferred from genetic interaction PubMed 17116687. Source: MGI protein autophosphorylation Inferred from electronic annotation. Source: Compara regulation of cell cycle Inferred from direct assay PubMed 11809706. Source: MGI response to lipopolysaccharide Inferred from mutant phenotype PubMed 19703997. Source: MGI
Cellular_component	cytosol Inferred from direct assay PubMed 17116687. Source: MGI plasma membrane Inferred from direct assay PubMed 17116687. Source: MGI
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW Rac GTPase activator activity Inferred from genetic interaction PubMed 19703997. Source: MGI Rho guanyl-nucleotide exchange factor activity Inferred from electronic annotation. Source: InterPro phospholipid binding Inferred from electronic annotation. Source: InterPro protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1270

1270

Breakpoint cluster region protein

PRO_0000273731

Regions

Domain

497 – 690

194

Domain

707 – 865

159

Domain

869 – 1001

133

Domain

1053 – 1247

195

Rho-GAP

Region

198 – 387

190

Binding to ABL SH2-domain By similarity

Compositional bias

135 – 140

Poly-Ala

Compositional bias

317 – 384

Ser-rich

Amino acid modifications

Modified residue

122

Phosphoserine By similarity

Modified residue

178

Phosphotyrosine; by HCK By similarity

Modified residue

216

Phosphoserine By similarity

Modified residue

237

Phosphoserine Ref.6

Modified residue

247

Phosphotyrosine; by FES Ref.6

Modified residue

461

Phosphoserine Ref.7

Modified residue

1263

Phosphoserine By similarity

Experimental info

Sequence conflict

418

S → H in CAA37013. Ref.3

Sequence conflict

1213

P → S in AAH60270. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q6PAJ1 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 2F3E6D8485DE6717
Show »

FASTA

1,270

143,072

        10         20         30         40         50         60 
MVDSVGFAEA WRAQFPDSEP PRMELRSVGD IEQELERCKA SIRRLEQEVN QERFRMIYLQ 

        70         80         90        100        110        120 
TLLAKEKKSY DRQRWGFRRA AQPPDGAAEP RASAPRPPPA PADGADPAPV EESEARPDGE 

       130        140        150        160        170        180 
GSPSKGRSAS ARRPAAAASA DRDDRGPPTS VAALRSNFEK IRKGPAQPGS ADAEKPFYVN 

       190        200        210        220        230        240 
VEFHHERGLV KVNDKEVSDR ISSLGSQAMQ MERKKSQQSA GQGLGEAPRP HYRGRSSESS 

       250        260        270        280        290        300 
CGLDGDYEDA ELNPRFLKDN LINANGGNRP PWPPLEYQPY QSIYVGGMMV EGEGKSPLLR 

       310        320        330        340        350        360 
SQSTSEQEKR LTWPRRSYSP RSFEDSGGGY TPDCSSNENL TSSEEDFSSG QSSRVSPSPT 

       370        380        390        400        410        420 
TYRMFRDKSR SPSQNSQQSF DSSSPPTPQC QKRHRQCQVV VSEATIVGVR KTGQIWPSDG 

       430        440        450        460        470        480 
DSTFQGEADS SFGTPPGYGC AADQAEEQRR HQDGLPYIDD SPSSSPHLSS KGRGSLASGA 

       490        500        510        520        530        540 
LDPTKVSELD LEKGLEMRKW VLSGILASEE TYLSHLEALL LPMKPLKAAA TTSQPVLTSQ 

       550        560        570        580        590        600 
QIETIFFKVP ELYEIHKEFY DGLFPRVQQW SHQQRVGDLF QKLASQLGVY RAFVDNYGVA 

       610        620        630        640        650        660 
METAEKCCQA NAQFAEISEN LRARSNKDVK DSTTKNSLET LLYKPVDRVT RSTLVLHDLL 

       670        680        690        700        710        720 
KHTPSSHPDH SLLQDALRIS QNFLSSINEE ITPRRQSMTV KKGEHRQLLK DSFMVELVEG 

       730        740        750        760        770        780 
ARKLRHIFLF TDLLLCTKLK KQSGGKTQQY DCKWYIPLTD LSFQMVDELE ALPNIPLVPD 

       790        800        810        820        830        840 
EELDALKIKI SQIKSDIQRE KRANKGSKVM ERLRKKLSEQ ESLLLLMSPS MAFRVHSRNG 

       850        860        870        880        890        900 
KSYTFLISSD YERAEWRESI REQQKKCFKS FSLTSVELQM LTNSCVKLQT VHHIPLTINK 

       910        920        930        940        950        960 
EDDESPGLYG FLHVIVHSAT GFKQSSNLYC TLEVDSFGYF VNKAKTRVYR DTTEPNWNEE 

       970        980        990       1000       1010       1020 
FEIELEGSQT LRILCYEKCY NKMKMTKEDG ESADKLMGKG QVQLDPQTLQ DRDWQRTVID 

      1030       1040       1050       1060       1070       1080 
MNGIEVKLSV KFTSREFSLK RMPSRKQTGV FGVKIAVVTK RERSKVPYIV RQCVEEIERR 

      1090       1100       1110       1120       1130       1140 
GMEEVGIYRV SGVATDIQAL KAAFDVNNKD VSVMMSEMDV NAIAGTLKLY FRELPEPLFT 

      1150       1160       1170       1180       1190       1200 
DEFYPNFAEG IALSDPVAKE SCMLNLLLSL PEANLLTFLF LLDHLKRVAE KETVNKMSLH 

      1210       1220       1230       1240       1250       1260 
NLATVFGPTL LRPSEKESKL PANPSQPITM TDSWSLEVMS QVQVLLYFLQ LEAIPAPDSK 

      1270 
RQSILFSTEV

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[2]	"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] OF 212-1270. Strain: C57BL/6 and FVB/N. Tissue: Brain and Mammary gland.
[3]	"Unique organization of the human BCR gene promoter." Zhu Q.S., Heisterkamp N., Groffen J. Nucleic Acids Res. 18:7119-7125(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 276-428.
[4]	"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H. DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 561-1270. Tissue: Embryonic tail.
[5]	"Ccpg1, a novel scaffold protein that regulates the activity of the Rho guanine nucleotide exchange factor Dbs." Kostenko E.V., Olabisi O.O., Sahay S., Rodriguez P.L., Whitehead I.P. Mol. Cell. Biol. 26:8964-8975(2006) [PubMed] [Europe PMC] [Abstract] Cited for: POSSIBLE INTERACTION WITH CCPG1.
[6]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237 AND TYR-247, MASS SPECTROMETRY. Tissue: Mast cell.
[7]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC160402 Genomic DNA. No translation available. BC002193 mRNA. Translation: AAH02193.1. BC060270 mRNA. Translation: AAH60270.1. X52831 Genomic DNA. Translation: CAA37013.1. AK129482 mRNA. Translation: BAC98292.1.
IPI	IPI00380817.
PIR	S14193. S14194.
RefSeq	NP_001074881.1. NM_001081412.2.
UniGene	Mm.485801.
3D structure databases
ProteinModelPortal	Q6PAJ1.
SMR	Q6PAJ1. Positions 5-66, 498-770, 831-866, 1050-1256.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q6PAJ1. 1 interaction.
STRING	10090.ENSMUSP00000039247.
PTM databases
PhosphoSite	Q6PAJ1.
Proteomic databases
PaxDb	Q6PAJ1.
PRIDE	Q6PAJ1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000164107; ENSMUSP00000126377; ENSMUSG00000009681.
GeneID	110279.
KEGG	mmu:110279.
UCSC	uc007fqb.2. mouse.
Organism-specific databases
CTD	613.
MGI	MGI:88141. Bcr.
Rouge	Search...
Phylogenomic databases
eggNOG	NOG267747.
GeneTree	ENSGT00700000104029.
HOGENOM	HOG000006779.
HOVERGEN	HBG004165.
InParanoid	Q6PAJ1.
KO	K08878.
OMA	PPTPQCQ.
OrthoDB	EOG4FFD11.
Gene expression databases
ArrayExpress	Q6PAJ1.
Bgee	Q6PAJ1.
CleanEx	MM_BCR.
Genevestigator	Q6PAJ1.
Family and domain databases
Gene3D	1.10.555.10. 1 hit. 1.20.900.10. 1 hit. 2.30.29.30. 2 hits. 4.10.280.30. 1 hit.
InterPro	IPR015123. Bcr-Abl_oncoprot_oligo. IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR018029. C2_membr_targeting. IPR000219. DH-domain. IPR001331. GDS_CDC24_CS. IPR011993. PH_like_dom. IPR001849. Pleckstrin_homology. IPR008936. Rho_GTPase_activation_prot. IPR000198. RhoGAP_dom. [Graphical view]
Pfam	PF09036. Bcr-Abl_Oligo. 1 hit. PF00168. C2. 1 hit. PF00169. PH. 1 hit. PF00620. RhoGAP. 1 hit. PF00621. RhoGEF. 1 hit. [Graphical view]
SMART	SM00239. C2. 1 hit. SM00233. PH. 1 hit. SM00324. RhoGAP. 1 hit. SM00325. RhoGEF. 1 hit. [Graphical view]
SUPFAM	SSF69036. Bcr-Abl_oncoprot_oligo. 1 hit. SSF49562. C2_CaLB. 1 hit. SSF48065. DH-domain. 1 hit. SSF48350. Rho_GAP. 1 hit.
PROSITE	PS50004. C2. 1 hit. PS00741. DH_1. 1 hit. PS50010. DH_2. 1 hit. PS50003. PH_DOMAIN. 1 hit. PS50238. RHOGAP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	BCR. mouse.
NextBio	363683.
SOURCE	Search...

Entry information

Entry name

BCR_MOUSE

Accession

Primary (citable) accession number: Q6PAJ1
Secondary accession number(s): E9PZL3

Q99LW5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	July 27, 2011
Last modified:	May 29, 2013
This is version 81 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents