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P11274 (BCR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 173. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Breakpoint cluster region protein

EC=2.7.11.1
Alternative name(s):
Renal carcinoma antigen NY-REN-26
Gene names
Name:BCR
Synonyms:BCR1, D22S11
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1271 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Ref.13 Ref.15

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Homotetramer. Interacts with PDZK1. May interact with CCPG1 By similarity. Interacts with FES/FPS, ABL1, PIK3R1 and GRB2. Interacts with HCK. Ref.14 Ref.16 Ref.19 Ref.20 Ref.28

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 and transforming potential of the chimeric BCR-ABL oncogene. Ref.14

The DH domain is involved in interaction with CCPG1 By similarity. Ref.14

Post-translational modification

Autophosphorylated. Phosphorylated by FES/FPS on tyrosine residues, leading to down-regulation of the BCR kinase activity. Phosphorylation at Tyr-177 by HCK is important for interaction with GRB2. Ref.16 Ref.19

Involvement in disease

Leukemia, chronic myeloid (CML) [MIM:608232]: A clonal myeloproliferative disorder of a pluripotent stem cell with a specific cytogenetic abnormality, the Philadelphia chromosome (Ph), involving myeloid, erythroid, megakaryocytic, B-lymphoid, and sometimes T-lymphoid cells, but not marrow fibroblasts.
Note: The gene represented in this entry is involved in disease pathogenesis.

A chromosomal aberration involving BCR has been found in patients with chronic myeloid leukemia. Translocation t(9;22)(q34;q11) with ABL1. The translocation produces a BCR-ABL found also in acute myeloid leukemia (AML) and acute lymphoblastic leukemia (ALL).

Sequence similarities

Contains 1 C2 domain.

Contains 1 DH (DBL-homology) domain.

Contains 1 PH domain.

Contains 1 Rho-GAP domain.

Sequence caution

The sequence BAE06073.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseProto-oncogene
   LigandATP-binding
Nucleotide-binding
   Molecular functionGTPase activation
Guanine-nucleotide releasing factor
Kinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

brain development

Inferred from electronic annotation. Source: Ensembl

inner ear morphogenesis

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

negative regulation of inflammatory response

Inferred from electronic annotation. Source: Ensembl

negative regulation of neutrophil degranulation

Inferred from electronic annotation. Source: Ensembl

neuromuscular process controlling balance

Inferred from electronic annotation. Source: Ensembl

peptidyl-tyrosine phosphorylation

Traceable author statement. Source: GOC

platelet-derived growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of phagocytosis

Inferred from electronic annotation. Source: Ensembl

protein autophosphorylation

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Traceable author statement Ref.15. Source: ProtInc

regulation of cell cycle

Inferred from electronic annotation. Source: Ensembl

regulation of small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement Ref.15. Source: ProtInc

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

plasma membrane

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from direct assay PubMed 23382219. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activator activity

Traceable author statement Ref.13. Source: ProtInc

Rac GTPase activator activity

Inferred from electronic annotation. Source: Ensembl

Rho guanyl-nucleotide exchange factor activity

Inferred from electronic annotation. Source: InterPro

kinase activity

Traceable author statement. Source: Reactome

protein binding

Inferred from physical interaction PubMed 10887132PubMed 21706016PubMed 22153077PubMed 8112292PubMed 8955135PubMed 8995379PubMed 9174058PubMed 9178913PubMed 9566916. Source: IntAct

protein serine/threonine kinase activity

Traceable author statement Ref.15. Source: ProtInc

protein tyrosine kinase activity

Traceable author statement. Source: Reactome

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P11274-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P11274-2)

The sequence of this isoform differs from the canonical sequence as follows:
     961-1004: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12711271Breakpoint cluster region protein
PRO_0000080933

Regions

Domain498 – 691194DH
Domain708 – 866159PH
Domain870 – 1002133C2
Domain1054 – 1248195Rho-GAP
Region1 – 426426Kinase
Region197 – 385189Binding to ABL SH2-domain
Compositional bias824 – 8274Poly-Leu

Sites

Site426 – 4272Breakpoint for translocation to form BCR-ABL oncogene

Amino acid modifications

Modified residue11N-acetylmethionine Ref.27
Modified residue1221Phosphoserine Ref.26
Modified residue1771Phosphotyrosine; by HCK Ref.16 Ref.24
Modified residue2151Phosphoserine Ref.26
Modified residue2361Phosphoserine By similarity
Modified residue2461Phosphotyrosine; by FES Ref.19
Modified residue4591Phosphoserine Ref.23 Ref.24 Ref.26
Modified residue12641Phosphoserine Ref.18 Ref.24

Natural variations

Alternative sequence961 – 100444Missing in isoform 2.
VSP_024352
Natural variant4001S → P in a bladder transitional cell carcinoma sample; somatic mutation. Ref.29
VAR_041883
Natural variant4131I → M. Ref.29
Corresponds to variant rs56321828 [ dbSNP | Ensembl ].
VAR_041884
Natural variant5581K → T.
Corresponds to variant rs4437065 [ dbSNP | Ensembl ].
VAR_051983
Natural variant7521D → E. Ref.29
Corresponds to variant rs12484731 [ dbSNP | Ensembl ].
VAR_041885
Natural variant7961N → S. Ref.1 Ref.3 Ref.4 Ref.11 Ref.29
Corresponds to variant rs140504 [ dbSNP | Ensembl ].
VAR_031552
Natural variant9101Y → C. Ref.29
Corresponds to variant rs35537221 [ dbSNP | Ensembl ].
VAR_041886
Natural variant9491V → I. Ref.29
Corresponds to variant rs2229038 [ dbSNP | Ensembl ].
VAR_041887
Natural variant10371E → K. Ref.29
Corresponds to variant rs16999516 [ dbSNP | Ensembl ].
VAR_031553
Natural variant10911V → M. Ref.29
VAR_041888
Natural variant10961T → A. Ref.29
VAR_041889
Natural variant11041A → G. Ref.29
VAR_041890
Natural variant11061D → N. Ref.29
VAR_041891
Natural variant11271T → M.
Corresponds to variant rs35812689 [ dbSNP | Ensembl ].
VAR_031554
Natural variant11491A → T. Ref.29
VAR_041892
Natural variant11611E → K. Ref.29
VAR_041893
Natural variant11871K → E. Ref.29
VAR_041894
Natural variant11891V → M. Ref.29
Corresponds to variant rs55816482 [ dbSNP | Ensembl ].
VAR_041895
Natural variant12041A → G. Ref.29
Corresponds to variant rs56265970 [ dbSNP | Ensembl ].
VAR_041896
Natural variant12351W → R. Ref.29
Corresponds to variant rs55719322 [ dbSNP | Ensembl ].
VAR_041897

Experimental info

Mutagenesis1771Y → F: Abolishes interaction with FES and GRB2. Ref.16 Ref.19
Mutagenesis1269 – 12713Missing: Abolishes interaction with PDZK1. Ref.20
Mutagenesis12711V → A: Reduces interaction with PDZK1. Ref.20
Sequence conflict2871M → I in CAA68676. Ref.1
Sequence conflict4181G → D in CAA68676. Ref.1
Sequence conflict4831E → K in CAA68676. Ref.1
Sequence conflict5601F → S in CAA68676. Ref.1
Sequence conflict6901E → D Ref.11
Sequence conflict7331D → E in CAA26441. Ref.4

Secondary structure

...... 1271
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 3, 2007. Version 2.
Checksum: 4BF66FA1E9D205FE

FASTA1,271142,819
        10         20         30         40         50         60 
MVDPVGFAEA WKAQFPDSEP PRMELRSVGD IEQELERCKA SIRRLEQEVN QERFRMIYLQ 

        70         80         90        100        110        120 
TLLAKEKKSY DRQRWGFRRA AQAPDGASEP RASASRPQPA PADGADPPPA EEPEARPDGE 

       130        140        150        160        170        180 
GSPGKARPGT ARRPGAAASG ERDDRGPPAS VAALRSNFER IRKGHGQPGA DAEKPFYVNV 

       190        200        210        220        230        240 
EFHHERGLVK VNDKEVSDRI SSLGSQAMQM ERKKSQHGAG SSVGDASRPP YRGRSSESSC 

       250        260        270        280        290        300 
GVDGDYEDAE LNPRFLKDNL IDANGGSRPP WPPLEYQPYQ SIYVGGMMEG EGKGPLLRSQ 

       310        320        330        340        350        360 
STSEQEKRLT WPRRSYSPRS FEDCGGGYTP DCSSNENLTS SEEDFSSGQS SRVSPSPTTY 

       370        380        390        400        410        420 
RMFRDKSRSP SQNSQQSFDS SSPPTPQCHK RHRHCPVVVS EATIVGVRKT GQIWPNDGEG 

       430        440        450        460        470        480 
AFHGDADGSF GTPPGYGCAA DRAEEQRRHQ DGLPYIDDSP SSSPHLSSKG RGSRDALVSG 

       490        500        510        520        530        540 
ALESTKASEL DLEKGLEMRK WVLSGILASE ETYLSHLEAL LLPMKPLKAA ATTSQPVLTS 

       550        560        570        580        590        600 
QQIETIFFKV PELYEIHKEF YDGLFPRVQQ WSHQQRVGDL FQKLASQLGV YRAFVDNYGV 

       610        620        630        640        650        660 
AMEMAEKCCQ ANAQFAEISE NLRARSNKDA KDPTTKNSLE TLLYKPVDRV TRSTLVLHDL 

       670        680        690        700        710        720 
LKHTPASHPD HPLLQDALRI SQNFLSSINE EITPRRQSMT VKKGEHRQLL KDSFMVELVE 

       730        740        750        760        770        780 
GARKLRHVFL FTDLLLCTKL KKQSGGKTQQ YDCKWYIPLT DLSFQMVDEL EAVPNIPLVP 

       790        800        810        820        830        840 
DEELDALKIK ISQIKNDIQR EKRANKGSKA TERLKKKLSE QESLLLLMSP SMAFRVHSRN 

       850        860        870        880        890        900 
GKSYTFLISS DYERAEWREN IREQQKKCFR SFSLTSVELQ MLTNSCVKLQ TVHSIPLTIN 

       910        920        930        940        950        960 
KEDDESPGLY GFLNVIVHSA TGFKQSSNLY CTLEVDSFGY FVNKAKTRVY RDTAEPNWNE 

       970        980        990       1000       1010       1020 
EFEIELEGSQ TLRILCYEKC YNKTKIPKED GESTDRLMGK GQVQLDPQAL QDRDWQRTVI 

      1030       1040       1050       1060       1070       1080 
AMNGIEVKLS VKFNSREFSL KRMPSRKQTG VFGVKIAVVT KRERSKVPYI VRQCVEEIER 

      1090       1100       1110       1120       1130       1140 
RGMEEVGIYR VSGVATDIQA LKAAFDVNNK DVSVMMSEMD VNAIAGTLKL YFRELPEPLF 

      1150       1160       1170       1180       1190       1200 
TDEFYPNFAE GIALSDPVAK ESCMLNLLLS LPEANLLTFL FLLDHLKRVA EKEAVNKMSL 

      1210       1220       1230       1240       1250       1260 
HNLATVFGPT LLRPSEKESK LPANPSQPIT MTDSWSLEVM SQVQVLLYFL QLEAIPAPDS 

      1270 
KRQSILFSTE V 

« Hide

Isoform 2 [UniParc].

Checksum: EFEE4915DE3FE893
Show »

FASTA1,227137,729

References

« Hide 'large scale' references
[1]"bcr genes and transcripts."
Lifshitz B., Fainstein E., Marcelle C., Shtivelman E., Amson R., Gale R.P., Canaani E.
Oncogene 2:113-117(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT SER-796.
[2]"Sequence and analysis of the human ABL gene, the BCR gene, and regions involved in the Philadelphia chromosomal translocation."
Chissoe S.L., Bodenteich A., Wang Y.-F., Wang Y.-P., Burian D., Clifton S.W., Crabtree J., Freeman A., Iyer K., Jian L., Ma Y., McLaury H.-J., Pan H.-Q., Sarhan O.H., Toth S., Wang Z., Zhang G., Heisterkamp N., Groffen J., Roe B.A.
Genomics 27:67-82(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method."
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT SER-796.
Tissue: Brain.
[4]"cDNA sequence for human bcr, the gene that translocates to the abl oncogene in chronic myeloid leukaemia."
Hariharan I.K., Adams J.M.
EMBO J. 6:115-119(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-872, VARIANT SER-796.
[5]"Overlapping cDNA clones define the complete coding region for the P210c-abl gene product associated with chronic myelogenous leukemia cells containing the Philadelphia chromosome."
Mes-Masson A.-M., McLaughlin J., Daley G.Q., Paskind M., Witte O.N.
Proc. Natl. Acad. Sci. U.S.A. 83:9768-9772(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-693.
[6]Erratum
Mes-Masson A.M., McLaughlin J., Daley G.Q., Paskind M., Witte O.N.
Proc. Natl. Acad. Sci. U.S.A. 84:2507-2507(1987)
Cited for: SEQUENCE REVISION.
[7]"Structural organization of the bcr gene and its role in the Ph' translocation."
Heisterkamp N., Stam K., Groffen J., de Klein A., Grosveld G.
Nature 315:758-761(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 683-1271 (ISOFORM 1).
[8]"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 1-46 AND 275-426.
[9]"A new fused transcript in Philadelphia chromosome positive acute lymphocytic leukaemia."
Fainstein E., Marcelle C., Rosner A., Canaani E., Gale R.P., Dreazen O., Smith S.D., Croce C.M.
Nature 330:386-388(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 56-426.
[10]"Alternative 5' end of the bcr-abl transcript in chronic myelogenous leukemia."
Romero P., Beran M., Shtalrid M., Andersson B., Talpaz M., Blick M.
Oncogene 4:93-98(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 362-438, ALTERNATIVE SPLICING.
[11]"Chronic myeloid leukemia may be associated with several bcr-abl transcripts including the acute lymphoid leukemia-type 7 kb transcript."
Selleri L., von Lindern M., Hermans A., Meijer D., Torelli G., Grosveld G.
Blood 75:1146-1153(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 670-842, VARIANT SER-796.
[12]"Characterization of the BCR promoter in Philadelphia chromosome-positive and -negative cell lines."
Shah N.P., Witte O.N., Denny C.T.
Mol. Cell. Biol. 11:1854-1860(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-4.
[13]"Bcr encodes a GTPase-activating protein for p21rac."
Diekmann D., Brill S., Garrett M.D., Totty N., Hsuan J., Monfries C., Hall C., Lim L., Hall A.
Nature 351:400-402(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"BCR sequences essential for transformation by the BCR-ABL oncogene bind to the ABL SH2 regulatory domain in a non-phosphotyrosine-dependent manner."
Pendergast A.M., Muller A.J., Havlik M.H., Maru Y., Witte O.N.
Cell 66:161-171(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ABL1 SH2-DOMAIN.
[15]"The BCR gene encodes a novel serine/threonine kinase activity within a single exon."
Maru Y., Witte O.N.
Cell 67:459-468(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS PROTEIN KINASE.
[16]"The Src family kinase Hck interacts with Bcr-Abl by a kinase-independent mechanism and phosphorylates the Grb2-binding site of Bcr."
Warmuth M., Bergmann M., Priess A., Hauslmann K., Emmerich B., Hallek M.
J. Biol. Chem. 272:33260-33270(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-177 BY HCK, MUTAGENESIS OF TYR-177, INTERACTION WITH HCK AND GRB2.
[17]"Antigens recognized by autologous antibody in patients with renal-cell carcinoma."
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J.
Int. J. Cancer 83:456-464(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
Tissue: Renal cell carcinoma.
[18]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1264, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"The c-Fes tyrosine kinase cooperates with the breakpoint cluster region protein (Bcr) to induce neurite extension in a Rac- and Cdc42-dependent manner."
Laurent C.E., Smithgall T.E.
Exp. Cell Res. 299:188-198(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FES/FPS; ABL1; PIK3R1 AND GRB2, MUTAGENESIS OF TYR-177, PHOSPHORYLATION AT TYR-246.
[20]"Bcr (breakpoint cluster region) protein binds to PDZ-domains of scaffold protein PDZK1 and vesicle coat protein Mint3."
Malmberg E.K., Andersson C.X., Gentzsch M., Chen J.H., Mengos A., Cui L., Hansson G.C., Riordan J.R.
J. Cell Sci. 117:5535-5541(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDZK1, MUTAGENESIS OF 1269-THR--GLU-1271 AND VAL-1271.
[21]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[23]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-459, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-177; SER-459 AND SER-1264, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[25]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122; SER-215 AND SER-459, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"Structure of the Bcr-Abl oncoprotein oligomerization domain."
Zhao X., Ghaffari S., Lodish H., Malashkevich V.N., Kim P.S.
Nat. Struct. Biol. 9:117-120(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 3-72, HOMOTETRAMERIZATION.
[29]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] PRO-400; MET-413; GLU-752; SER-796; CYS-910; ILE-949; LYS-1037; MET-1091; ALA-1096; GLY-1104; ASN-1106; THR-1149; LYS-1161; GLU-1187; MET-1189; GLY-1204 AND ARG-1235.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00661 mRNA. Translation: CAA68676.1.
U07000 Genomic DNA. Translation: AAB60388.1.
AB209991 mRNA. Translation: BAE06073.1. Different initiation.
X02596 mRNA. Translation: CAA26441.1.
M15025 Genomic DNA. Translation: AAA35594.1.
X52828 Genomic DNA. Translation: CAA37010.1.
X52829 Genomic DNA. Translation: CAA37011.1.
X14676 mRNA. Translation: CAA32806.1.
M64437 mRNA. No translation available.
CCDSCCDS13806.1. [P11274-1]
CCDS13807.1. [P11274-2]
PIRTVHUA2. A26664.
TVHUBR. A91064.
RefSeqNP_004318.3. NM_004327.3. [P11274-1]
NP_067585.2. NM_021574.2. [P11274-2]
UniGeneHs.517461.
Hs.715409.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K1FX-ray2.20A/B/C/D/E/F/G/H1-72[»]
2AINNMR-B1266-1271[»]
ProteinModelPortalP11274.
SMRP11274. Positions 1-67, 499-771, 1051-1257.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107083. 53 interactions.
IntActP11274. 21 interactions.
MINTMINT-1207264.
STRING9606.ENSP00000303507.

Chemistry

BindingDBP11274.
ChEMBLCHEMBL2096618.

PTM databases

PhosphoSiteP11274.

Polymorphism databases

DMDM143811366.

Proteomic databases

MaxQBP11274.
PaxDbP11274.
PRIDEP11274.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000305877; ENSP00000303507; ENSG00000186716. [P11274-1]
ENST00000359540; ENSP00000352535; ENSG00000186716. [P11274-2]
GeneID613.
KEGGhsa:613.
UCSCuc002zww.3. human. [P11274-1]
uc002zwx.3. human. [P11274-2]

Organism-specific databases

CTD613.
GeneCardsGC22P023521.
H-InvDBHIX0016226.
HIX0016271.
HIX0027936.
HIX0041406.
HGNCHGNC:1014. BCR.
HPAHPA038337.
MIM151410. gene.
608232. phenotype.
neXtProtNX_P11274.
Orphanet521. Chronic myeloid leukemia.
261330. Distal 22q11.2 microdeletion syndrome.
99860. Precursor B-cell acute lymphoblastic leukemia.
99861. Precursor T-cell acute lymphoblastic leukemia.
PharmGKBPA25321.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG267747.
HOGENOMHOG000006779.
HOVERGENHBG004165.
InParanoidP11274.
KOK08878.
OMAKRANSHS.
OrthoDBEOG7BP81P.
PhylomeDBP11274.
TreeFamTF105082.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
SignaLinkP11274.

Gene expression databases

ArrayExpressP11274.
BgeeP11274.
CleanExHS_BCR.
GenevestigatorP11274.

Family and domain databases

Gene3D1.10.555.10. 1 hit.
1.20.900.10. 1 hit.
2.30.29.30. 2 hits.
2.60.40.150. 1 hit.
4.10.280.30. 1 hit.
InterProIPR015123. Bcr-Abl_oncoprot_oligo.
IPR000008. C2_dom.
IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamPF09036. Bcr-Abl_Oligo. 1 hit.
PF00168. C2. 1 hit.
PF00169. PH. 1 hit.
PF00620. RhoGAP. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTSM00239. C2. 1 hit.
SM00233. PH. 1 hit.
SM00324. RhoGAP. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMSSF48065. SSF48065. 1 hit.
SSF48350. SSF48350. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF69036. SSF69036. 1 hit.
PROSITEPS50004. C2. 1 hit.
PS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50238. RHOGAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBCR. human.
EvolutionaryTraceP11274.
GeneWikiBCR_(gene).
GenomeRNAi613.
NextBio2485.
PROP11274.
SOURCESearch...

Entry information

Entry nameBCR_HUMAN
AccessionPrimary (citable) accession number: P11274
Secondary accession number(s): P78501 expand/collapse secondary AC list , Q12842, Q4LE80, Q6NZI3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: April 3, 2007
Last modified: July 9, 2014
This is version 173 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM