Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

P11274

- BCR_HUMAN

UniProt

P11274 - BCR_HUMAN

Protein

Breakpoint cluster region protein

Gene

BCR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 175 (01 Oct 2014)
      Sequence version 2 (03 Apr 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 binding Source: IntAct
    5. protein serine/threonine kinase activity Source: ProtInc
    6. protein tyrosine kinase activity Source: Reactome
    7. Rac GTPase activator activity Source: Ensembl
    8. 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

    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

    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.
    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

    ArrayExpressiP11274.
    BgeeiP11274.
    CleanExiHS_BCR.
    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. 52 interactions.
    IntActiP11274. 23 interactions.
    MINTiMINT-1207264.
    STRINGi9606.ENSP00000303507.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MVDPVGFAEA WKAQFPDSEP PRMELRSVGD IEQELERCKA SIRRLEQEVN     50
    QERFRMIYLQ TLLAKEKKSY DRQRWGFRRA AQAPDGASEP RASASRPQPA 100
    PADGADPPPA EEPEARPDGE GSPGKARPGT ARRPGAAASG ERDDRGPPAS 150
    VAALRSNFER IRKGHGQPGA DAEKPFYVNV EFHHERGLVK VNDKEVSDRI 200
    SSLGSQAMQM ERKKSQHGAG SSVGDASRPP YRGRSSESSC GVDGDYEDAE 250
    LNPRFLKDNL IDANGGSRPP WPPLEYQPYQ SIYVGGMMEG EGKGPLLRSQ 300
    STSEQEKRLT WPRRSYSPRS FEDCGGGYTP DCSSNENLTS SEEDFSSGQS 350
    SRVSPSPTTY RMFRDKSRSP SQNSQQSFDS SSPPTPQCHK RHRHCPVVVS 400
    EATIVGVRKT GQIWPNDGEG AFHGDADGSF GTPPGYGCAA DRAEEQRRHQ 450
    DGLPYIDDSP SSSPHLSSKG RGSRDALVSG ALESTKASEL DLEKGLEMRK 500
    WVLSGILASE ETYLSHLEAL LLPMKPLKAA ATTSQPVLTS QQIETIFFKV 550
    PELYEIHKEF YDGLFPRVQQ WSHQQRVGDL FQKLASQLGV YRAFVDNYGV 600
    AMEMAEKCCQ ANAQFAEISE NLRARSNKDA KDPTTKNSLE TLLYKPVDRV 650
    TRSTLVLHDL LKHTPASHPD HPLLQDALRI SQNFLSSINE EITPRRQSMT 700
    VKKGEHRQLL KDSFMVELVE GARKLRHVFL FTDLLLCTKL KKQSGGKTQQ 750
    YDCKWYIPLT DLSFQMVDEL EAVPNIPLVP DEELDALKIK ISQIKNDIQR 800
    EKRANKGSKA TERLKKKLSE QESLLLLMSP SMAFRVHSRN GKSYTFLISS 850
    DYERAEWREN IREQQKKCFR SFSLTSVELQ MLTNSCVKLQ TVHSIPLTIN 900
    KEDDESPGLY GFLNVIVHSA TGFKQSSNLY CTLEVDSFGY FVNKAKTRVY 950
    RDTAEPNWNE EFEIELEGSQ TLRILCYEKC YNKTKIPKED GESTDRLMGK 1000
    GQVQLDPQAL QDRDWQRTVI AMNGIEVKLS VKFNSREFSL KRMPSRKQTG 1050
    VFGVKIAVVT KRERSKVPYI VRQCVEEIER RGMEEVGIYR VSGVATDIQA 1100
    LKAAFDVNNK DVSVMMSEMD VNAIAGTLKL YFRELPEPLF TDEFYPNFAE 1150
    GIALSDPVAK ESCMLNLLLS LPEANLLTFL FLLDHLKRVA EKEAVNKMSL 1200
    HNLATVFGPT LLRPSEKESK LPANPSQPIT MTDSWSLEVM SQVQVLLYFL 1250
    QLEAIPAPDS KRQSILFSTE V 1271
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 52 interactions.
    IntActi P11274. 23 interactions.
    MINTi MINT-1207264.
    STRINGi 9606.ENSP00000303507.

    Chemistry

    BindingDBi P11274.
    ChEMBLi CHEMBL2096618.

    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.
    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

    ArrayExpressi P11274.
    Bgeei P11274.
    CleanExi HS_BCR.
    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

    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: October 1, 2014
    This is version 175 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