Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P11274

- BCR_HUMAN

UniProt

P11274 - BCR_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Breakpoint cluster region protein

Gene

BCR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei426 – 4272Breakpoint for translocation to form BCR-ABL oncogene

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. GTPase activator activity Source: ProtInc
  3. kinase activity Source: Reactome
  4. protein serine/threonine kinase activity Source: ProtInc
  5. protein tyrosine kinase activity Source: Reactome
  6. Rac GTPase activator activity Source: Ensembl
  7. Rho guanyl-nucleotide exchange factor activity Source: InterPro

GO - Biological processi

  1. actin cytoskeleton organization Source: Ensembl
  2. brain development Source: Ensembl
  3. inner ear morphogenesis Source: Ensembl
  4. negative regulation of cell migration Source: Ensembl
  5. negative regulation of inflammatory response Source: Ensembl
  6. negative regulation of neutrophil degranulation Source: Ensembl
  7. neuromuscular process controlling balance Source: Ensembl
  8. peptidyl-tyrosine phosphorylation Source: GOC
  9. platelet-derived growth factor receptor signaling pathway Source: Ensembl
  10. positive regulation of phagocytosis Source: Ensembl
  11. protein autophosphorylation Source: Ensembl
  12. protein phosphorylation Source: ProtInc
  13. regulation of cell cycle Source: Ensembl
  14. regulation of small GTPase mediated signal transduction Source: Reactome
  15. response to lipopolysaccharide Source: Ensembl
  16. signal transduction Source: ProtInc
  17. small GTPase mediated signal transduction Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation, Guanine-nucleotide releasing factor, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
REACT_121141. Signaling by FGFR1 fusion mutants.
SignaLinkiP11274.

Names & Taxonomyi

Protein namesi
Recommended name:
Breakpoint cluster region protein (EC:2.7.11.1)
Alternative name(s):
Renal carcinoma antigen NY-REN-26
Gene namesi
Name:BCR
Synonyms:BCR1, D22S11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:1014. BCR.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
  3. membrane Source: UniProtKB
  4. plasma membrane Source: Ensembl
  5. protein complex Source: MGI
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

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).

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi177 – 1771Y → F: Abolishes interaction with FES and GRB2. 2 Publications
Mutagenesisi1269 – 12713Missing: Abolishes interaction with PDZK1. 1 Publication
Mutagenesisi1271 – 12711V → A: Reduces interaction with PDZK1. 1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

MIMi608232. phenotype.
Orphaneti521. Chronic myeloid leukemia.
261330. Distal 22q11.2 microdeletion syndrome.
99860. Precursor B-cell acute lymphoblastic leukemia.
99861. Precursor T-cell acute lymphoblastic leukemia.
PharmGKBiPA25321.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12711271Breakpoint cluster region proteinPRO_0000080933Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei122 – 1221Phosphoserine1 Publication
Modified residuei177 – 1771Phosphotyrosine; by HCK2 Publications
Modified residuei215 – 2151Phosphoserine1 Publication
Modified residuei236 – 2361PhosphoserineBy similarity
Modified residuei246 – 2461Phosphotyrosine; by FES1 Publication
Modified residuei459 – 4591Phosphoserine3 Publications
Modified residuei1264 – 12641Phosphoserine2 Publications

Post-translational modificationi

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 GRB2.6 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP11274.
PaxDbiP11274.
PRIDEiP11274.

PTM databases

PhosphoSiteiP11274.

Expressioni

Gene expression databases

BgeeiP11274.
CleanExiHS_BCR.
ExpressionAtlasiP11274. baseline and differential.
GenevestigatoriP11274.

Organism-specific databases

HPAiHPA038337.

Interactioni

Subunit structurei

Homotetramer. Interacts with PDZK1. May interact with CCPG1 (By similarity). Interacts with FES/FPS, ABL1, PIK3R1 and GRB2. Interacts with HCK.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GRB2P629938EBI-712838,EBI-401755
PTPN1P180313EBI-8658094,EBI-968788
TNKS2Q9H2K23EBI-712838,EBI-4398527
TP53P046372EBI-712838,EBI-366083

Protein-protein interaction databases

BioGridi107083. 55 interactions.
IntActiP11274. 24 interactions.
MINTiMINT-1207264.
STRINGi9606.ENSP00000303507.

Structurei

Secondary structure

1
1271
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1411Combined sources
Helixi28 – 6437Combined sources
Beta strandi1268 – 12714Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K1FX-ray2.20A/B/C/D/E/F/G/H1-72[»]
2AINNMR-B1266-1271[»]
ProteinModelPortaliP11274.
SMRiP11274. Positions 1-67, 499-771, 1051-1257.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11274.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini498 – 691194DHPROSITE-ProRule annotationAdd
BLAST
Domaini708 – 866159PHPROSITE-ProRule annotationAdd
BLAST
Domaini870 – 1002133C2PROSITE-ProRule annotationAdd
BLAST
Domaini1054 – 1248195Rho-GAPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 426426KinaseAdd
BLAST
Regioni197 – 385189Binding to ABL SH2-domainAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi824 – 8274Poly-Leu

Domaini

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

Sequence similaritiesi

Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG267747.
GeneTreeiENSGT00760000119098.
HOGENOMiHOG000006779.
HOVERGENiHBG004165.
InParanoidiP11274.
KOiK08878.
OMAiKRANSHS.
OrthoDBiEOG7BP81P.
PhylomeDBiP11274.
TreeFamiTF105082.

Family and domain databases

Gene3Di1.10.555.10. 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.
InterProiIPR015123. Bcr-Abl_oncoprot_oligo.
IPR000008. C2_dom.
IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamiPF09036. Bcr-Abl_Oligo. 1 hit.
PF00168. C2. 1 hit.
PF00169. PH. 1 hit.
PF00620. RhoGAP. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 1 hit.
SM00233. PH. 1 hit.
SM00324. RhoGAP. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF48350. SSF48350. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF69036. SSF69036. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50238. RHOGAP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P11274-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MVDPVGFAEA WKAQFPDSEP PRMELRSVGD IEQELERCKA SIRRLEQEVN
60 70 80 90 100
QERFRMIYLQ TLLAKEKKSY DRQRWGFRRA AQAPDGASEP RASASRPQPA
110 120 130 140 150
PADGADPPPA EEPEARPDGE GSPGKARPGT ARRPGAAASG ERDDRGPPAS
160 170 180 190 200
VAALRSNFER IRKGHGQPGA DAEKPFYVNV EFHHERGLVK VNDKEVSDRI
210 220 230 240 250
SSLGSQAMQM ERKKSQHGAG SSVGDASRPP YRGRSSESSC GVDGDYEDAE
260 270 280 290 300
LNPRFLKDNL IDANGGSRPP WPPLEYQPYQ SIYVGGMMEG EGKGPLLRSQ
310 320 330 340 350
STSEQEKRLT WPRRSYSPRS FEDCGGGYTP DCSSNENLTS SEEDFSSGQS
360 370 380 390 400
SRVSPSPTTY RMFRDKSRSP SQNSQQSFDS SSPPTPQCHK RHRHCPVVVS
410 420 430 440 450
EATIVGVRKT GQIWPNDGEG AFHGDADGSF GTPPGYGCAA DRAEEQRRHQ
460 470 480 490 500
DGLPYIDDSP SSSPHLSSKG RGSRDALVSG ALESTKASEL DLEKGLEMRK
510 520 530 540 550
WVLSGILASE ETYLSHLEAL LLPMKPLKAA ATTSQPVLTS QQIETIFFKV
560 570 580 590 600
PELYEIHKEF YDGLFPRVQQ WSHQQRVGDL FQKLASQLGV YRAFVDNYGV
610 620 630 640 650
AMEMAEKCCQ ANAQFAEISE NLRARSNKDA KDPTTKNSLE TLLYKPVDRV
660 670 680 690 700
TRSTLVLHDL LKHTPASHPD HPLLQDALRI SQNFLSSINE EITPRRQSMT
710 720 730 740 750
VKKGEHRQLL KDSFMVELVE GARKLRHVFL FTDLLLCTKL KKQSGGKTQQ
760 770 780 790 800
YDCKWYIPLT DLSFQMVDEL EAVPNIPLVP DEELDALKIK ISQIKNDIQR
810 820 830 840 850
EKRANKGSKA TERLKKKLSE QESLLLLMSP SMAFRVHSRN GKSYTFLISS
860 870 880 890 900
DYERAEWREN IREQQKKCFR SFSLTSVELQ MLTNSCVKLQ TVHSIPLTIN
910 920 930 940 950
KEDDESPGLY GFLNVIVHSA TGFKQSSNLY CTLEVDSFGY FVNKAKTRVY
960 970 980 990 1000
RDTAEPNWNE EFEIELEGSQ TLRILCYEKC YNKTKIPKED GESTDRLMGK
1010 1020 1030 1040 1050
GQVQLDPQAL QDRDWQRTVI AMNGIEVKLS VKFNSREFSL KRMPSRKQTG
1060 1070 1080 1090 1100
VFGVKIAVVT KRERSKVPYI VRQCVEEIER RGMEEVGIYR VSGVATDIQA
1110 1120 1130 1140 1150
LKAAFDVNNK DVSVMMSEMD VNAIAGTLKL YFRELPEPLF TDEFYPNFAE
1160 1170 1180 1190 1200
GIALSDPVAK ESCMLNLLLS LPEANLLTFL FLLDHLKRVA EKEAVNKMSL
1210 1220 1230 1240 1250
HNLATVFGPT LLRPSEKESK LPANPSQPIT MTDSWSLEVM SQVQVLLYFL
1260 1270
QLEAIPAPDS KRQSILFSTE V
Length:1,271
Mass (Da):142,819
Last modified:April 3, 2007 - v2
Checksum:i4BF66FA1E9D205FE
GO
Isoform 2 (identifier: P11274-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     961-1004: Missing.

Note: No experimental confirmation available.

Show »
Length:1,227
Mass (Da):137,729
Checksum:iEFEE4915DE3FE893
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti287 – 2871M → I in CAA68676. (PubMed:3285291)Curated
Sequence conflicti418 – 4181G → D in CAA68676. (PubMed:3285291)Curated
Sequence conflicti483 – 4831E → K in CAA68676. (PubMed:3285291)Curated
Sequence conflicti560 – 5601F → S in CAA68676. (PubMed:3285291)Curated
Sequence conflicti690 – 6901E → D(PubMed:2407300)Curated
Sequence conflicti733 – 7331D → E in CAA26441. (PubMed:3107980)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti400 – 4001S → P in a bladder transitional cell carcinoma sample; somatic mutation. 1 Publication
VAR_041883
Natural varianti413 – 4131I → M.1 Publication
Corresponds to variant rs56321828 [ dbSNP | Ensembl ].
VAR_041884
Natural varianti558 – 5581K → T.
Corresponds to variant rs4437065 [ dbSNP | Ensembl ].
VAR_051983
Natural varianti752 – 7521D → E.1 Publication
Corresponds to variant rs12484731 [ dbSNP | Ensembl ].
VAR_041885
Natural varianti796 – 7961N → S.5 Publications
Corresponds to variant rs140504 [ dbSNP | Ensembl ].
VAR_031552
Natural varianti910 – 9101Y → C.1 Publication
Corresponds to variant rs35537221 [ dbSNP | Ensembl ].
VAR_041886
Natural varianti949 – 9491V → I.1 Publication
Corresponds to variant rs2229038 [ dbSNP | Ensembl ].
VAR_041887
Natural varianti1037 – 10371E → K.1 Publication
Corresponds to variant rs16999516 [ dbSNP | Ensembl ].
VAR_031553
Natural varianti1091 – 10911V → M.1 Publication
VAR_041888
Natural varianti1096 – 10961T → A.1 Publication
VAR_041889
Natural varianti1104 – 11041A → G.1 Publication
VAR_041890
Natural varianti1106 – 11061D → N.1 Publication
VAR_041891
Natural varianti1127 – 11271T → M.
Corresponds to variant rs35812689 [ dbSNP | Ensembl ].
VAR_031554
Natural varianti1149 – 11491A → T.1 Publication
VAR_041892
Natural varianti1161 – 11611E → K.1 Publication
VAR_041893
Natural varianti1187 – 11871K → E.1 Publication
VAR_041894
Natural varianti1189 – 11891V → M.1 Publication
Corresponds to variant rs55816482 [ dbSNP | Ensembl ].
VAR_041895
Natural varianti1204 – 12041A → G.1 Publication
Corresponds to variant rs56265970 [ dbSNP | Ensembl ].
VAR_041896
Natural varianti1235 – 12351W → R.1 Publication
Corresponds to variant rs55719322 [ dbSNP | Ensembl ].
VAR_041897

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei961 – 100444Missing in isoform 2. 1 PublicationVSP_024352Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13806.1. [P11274-1]
CCDS13807.1. [P11274-2]
PIRiA26664. TVHUA2.
A91064. TVHUBR.
RefSeqiNP_004318.3. NM_004327.3. [P11274-1]
NP_067585.2. NM_021574.2. [P11274-2]
UniGeneiHs.517461.
Hs.715409.

Genome annotation databases

EnsembliENST00000305877; ENSP00000303507; ENSG00000186716. [P11274-1]
ENST00000359540; ENSP00000352535; ENSG00000186716. [P11274-2]
GeneIDi613.
KEGGihsa:613.
UCSCiuc002zww.3. human. [P11274-1]
uc002zwx.3. human. [P11274-2]

Polymorphism databases

DMDMi143811366.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSi CCDS13806.1. [P11274-1 ]
CCDS13807.1. [P11274-2 ]
PIRi A26664. TVHUA2.
A91064. TVHUBR.
RefSeqi NP_004318.3. NM_004327.3. [P11274-1 ]
NP_067585.2. NM_021574.2. [P11274-2 ]
UniGenei Hs.517461.
Hs.715409.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1K1F X-ray 2.20 A/B/C/D/E/F/G/H 1-72 [» ]
2AIN NMR - B 1266-1271 [» ]
ProteinModelPortali P11274.
SMRi P11274. Positions 1-67, 499-771, 1051-1257.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107083. 55 interactions.
IntActi P11274. 24 interactions.
MINTi MINT-1207264.
STRINGi 9606.ENSP00000303507.

Chemistry

BindingDBi P11274.
ChEMBLi CHEMBL2096618.
DrugBanki DB06616. Bosutinib.
DB08901. Ponatinib.

PTM databases

PhosphoSitei P11274.

Polymorphism databases

DMDMi 143811366.

Proteomic databases

MaxQBi P11274.
PaxDbi P11274.
PRIDEi P11274.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000305877 ; ENSP00000303507 ; ENSG00000186716 . [P11274-1 ]
ENST00000359540 ; ENSP00000352535 ; ENSG00000186716 . [P11274-2 ]
GeneIDi 613.
KEGGi hsa:613.
UCSCi uc002zww.3. human. [P11274-1 ]
uc002zwx.3. human. [P11274-2 ]

Organism-specific databases

CTDi 613.
GeneCardsi GC22P023521.
H-InvDB HIX0016226.
HIX0016271.
HIX0027936.
HIX0041406.
HGNCi HGNC:1014. BCR.
HPAi HPA038337.
MIMi 151410. gene.
608232. phenotype.
neXtProti NX_P11274.
Orphaneti 521. Chronic myeloid leukemia.
261330. Distal 22q11.2 microdeletion syndrome.
99860. Precursor B-cell acute lymphoblastic leukemia.
99861. Precursor T-cell acute lymphoblastic leukemia.
PharmGKBi PA25321.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG267747.
GeneTreei ENSGT00760000119098.
HOGENOMi HOG000006779.
HOVERGENi HBG004165.
InParanoidi P11274.
KOi K08878.
OMAi KRANSHS.
OrthoDBi EOG7BP81P.
PhylomeDBi P11274.
TreeFami TF105082.

Enzyme and pathway databases

Reactomei REACT_11051. Rho GTPase cycle.
REACT_121141. Signaling by FGFR1 fusion mutants.
SignaLinki P11274.

Miscellaneous databases

ChiTaRSi BCR. human.
EvolutionaryTracei P11274.
GeneWikii BCR_(gene).
GenomeRNAii 613.
NextBioi 2485.
PROi P11274.
SOURCEi Search...

Gene expression databases

Bgeei P11274.
CleanExi HS_BCR.
ExpressionAtlasi P11274. baseline and differential.
Genevestigatori P11274.

Family and domain databases

Gene3Di 1.10.555.10. 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.
InterProi IPR015123. Bcr-Abl_oncoprot_oligo.
IPR000008. C2_dom.
IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view ]
Pfami PF09036. Bcr-Abl_Oligo. 1 hit.
PF00168. C2. 1 hit.
PF00169. PH. 1 hit.
PF00620. RhoGAP. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view ]
SMARTi SM00239. C2. 1 hit.
SM00233. PH. 1 hit.
SM00324. RhoGAP. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view ]
SUPFAMi SSF48065. SSF48065. 1 hit.
SSF48350. SSF48350. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF69036. SSF69036. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  23. 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. 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.
    , 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.

Entry informationi

Entry nameiBCR_HUMAN
AccessioniPrimary (citable) accession number: P11274
Secondary accession number(s): P78501
, Q12842, Q4LE80, Q6NZI3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: April 3, 2007
Last modified: November 26, 2014
This is version 177 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3