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Breakpoint cluster region protein (EC 2.7.11.1) (Renal carcinoma antigen NY-REN-26)

 BCR_HUMAN               Reviewed;        1271 AA.
P11274; P78501; Q12842; Q4LE80; Q6NZI3;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
03-APR-2007, sequence version 2.
13-FEB-2019, entry version 223.
RecName: Full=Breakpoint cluster region protein;
EC=2.7.11.1;
AltName: Full=Renal carcinoma antigen NY-REN-26;
Name=BCR; Synonyms=BCR1, D22S11;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT SER-796.
PubMed=3285291;
Lifshitz B., Fainstein E., Marcelle C., Shtivelman E., Amson R.,
Gale R.P., Canaani E.;
"bcr genes and transcripts.";
Oncogene 2:113-117(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHROMOSOMAL TRANSLOCATION.
PubMed=7665185; DOI=10.1006/geno.1995.1008;
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.;
"Sequence and analysis of the human ABL gene, the BCR gene, and
regions involved in the Philadelphia chromosomal translocation.";
Genomics 27:67-82(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
SER-796.
TISSUE=Brain;
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M.,
Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.;
"Preparation of a set of expression-ready clones of mammalian long
cDNAs encoding large proteins by the ORF trap cloning method.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-872, CHROMOSOMAL TRANSLOCATION,
INVOLVEMENT IN CML, AND VARIANT SER-796.
PubMed=3107980;
Hariharan I.K., Adams J.M.;
"cDNA sequence for human bcr, the gene that translocates to the abl
oncogene in chronic myeloid leukaemia.";
EMBO J. 6:115-119(1987).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-693, AND INVOLVEMENT IN CML.
PubMed=3540951; DOI=10.1073/pnas.83.24.9768;
Mes-Masson A.-M., McLaughlin J., Daley G.Q., Paskind M., Witte O.N.;
"Overlapping cDNA clones define the complete coding region for the
P210c-abl gene product associated with chronic myelogenous leukemia
cells containing the Philadelphia chromosome.";
Proc. Natl. Acad. Sci. U.S.A. 83:9768-9772(1986).
[6]
ERRATUM, AND SEQUENCE REVISION.
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 683-1271 (ISOFORM 1).
PubMed=2989703; DOI=10.1038/315758a0;
Heisterkamp N., Stam K., Groffen J., de Klein A., Grosveld G.;
"Structural organization of the bcr gene and its role in the Ph'
translocation.";
Nature 315:758-761(1985).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46 AND 275-426.
PubMed=2263470; DOI=10.1093/nar/18.23.7119;
Zhu Q.S., Heisterkamp N., Groffen J.;
"Unique organization of the human BCR gene promoter.";
Nucleic Acids Res. 18:7119-7125(1990).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 56-426.
PubMed=2825022; DOI=10.1038/330386a0;
Fainstein E., Marcelle C., Rosner A., Canaani E., Gale R.P.,
Dreazen O., Smith S.D., Croce C.M.;
"A new fused transcript in Philadelphia chromosome positive acute
lymphocytic leukaemia.";
Nature 330:386-388(1987).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 362-438, AND ALTERNATIVE SPLICING.
PubMed=2915904;
Romero P., Beran M., Shtalrid M., Andersson B., Talpaz M., Blick M.;
"Alternative 5' end of the bcr-abl transcript in chronic myelogenous
leukemia.";
Oncogene 4:93-98(1989).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 670-842, INVOLVEMENT IN CML, AND
VARIANT SER-796.
PubMed=2407300;
Selleri L., von Lindern M., Hermans A., Meijer D., Torelli G.,
Grosveld G.;
"Chronic myeloid leukemia may be associated with several bcr-abl
transcripts including the acute lymphoid leukemia-type 7 kb
transcript.";
Blood 75:1146-1153(1990).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-4.
PubMed=1900918; DOI=10.1128/MCB.11.4.1854;
Shah N.P., Witte O.N., Denny C.T.;
"Characterization of the BCR promoter in Philadelphia chromosome-
positive and -negative cell lines.";
Mol. Cell. Biol. 11:1854-1860(1991).
[13]
FUNCTION.
PubMed=1903516; DOI=10.1038/351400a0;
Diekmann D., Brill S., Garrett M.D., Totty N., Hsuan J., Monfries C.,
Hall C., Lim L., Hall A.;
"Bcr encodes a GTPase-activating protein for p21rac.";
Nature 351:400-402(1991).
[14]
INTERACTION WITH ABL1 SH2-DOMAIN.
PubMed=1712671; DOI=10.1016/0092-8674(91)90148-R;
Pendergast A.M., Muller A.J., Havlik M.H., Maru Y., Witte O.N.;
"BCR sequences essential for transformation by the BCR-ABL oncogene
bind to the ABL SH2 regulatory domain in a non-phosphotyrosine-
dependent manner.";
Cell 66:161-171(1991).
[15]
FUNCTION AS PROTEIN KINASE.
PubMed=1657398; DOI=10.1016/0092-8674(91)90521-Y;
Maru Y., Witte O.N.;
"The BCR gene encodes a novel serine/threonine kinase activity within
a single exon.";
Cell 67:459-468(1991).
[16]
PHOSPHORYLATION AT TYR-177 BY HCK, MUTAGENESIS OF TYR-177, AND
INTERACTION WITH HCK AND GRB2.
PubMed=9407116; DOI=10.1074/jbc.272.52.33260;
Warmuth M., Bergmann M., Priess A., Hauslmann K., Emmerich B.,
Hallek M.;
"The Src family kinase Hck interacts with Bcr-Abl by a kinase-
independent mechanism and phosphorylates the Grb2-binding site of
Bcr.";
J. Biol. Chem. 272:33260-33270(1997).
[17]
IDENTIFICATION AS A RENAL CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
PubMed=10508479;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
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.;
"Antigens recognized by autologous antibody in patients with renal-
cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1264, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[19]
INTERACTION WITH FES/FPS; ABL1; PIK3R1 AND GRB2, MUTAGENESIS OF
TYR-177, AND PHOSPHORYLATION AT TYR-246.
PubMed=15302586; DOI=10.1016/j.yexcr.2004.05.010;
Laurent C.E., Smithgall T.E.;
"The c-Fes tyrosine kinase cooperates with the breakpoint cluster
region protein (Bcr) to induce neurite extension in a Rac- and Cdc42-
dependent manner.";
Exp. Cell Res. 299:188-198(2004).
[20]
INTERACTION WITH PDZK1, AND MUTAGENESIS OF 1269-THR--GLU-1271 AND
VAL-1271.
PubMed=15494376; DOI=10.1242/jcs.01472;
Malmberg E.K., Andersson C.X., Gentzsch M., Chen J.H., Mengos A.,
Cui L., Hansson G.C., Riordan J.R.;
"Bcr (breakpoint cluster region) protein binds to PDZ-domains of
scaffold protein PDZK1 and vesicle coat protein Mint3.";
J. Cell Sci. 117:5535-5541(2004).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-459, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-177; SER-459 AND
SER-1264, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122; SER-215 AND
SER-459, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[27]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122; SER-139; SER-202;
SER-215; SER-222; SER-356; SER-377; SER-459; SER-463; SER-473;
SER-488; TYR-554; THR-641; TYR-644; THR-693 AND SER-894, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-459, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[30]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 3-72, AND
HOMOTETRAMERIZATION.
PubMed=11780146; DOI=10.1038/nsb747;
Zhao X., Ghaffari S., Lodish H., Malashkevich V.N., Kim P.S.;
"Structure of the Bcr-Abl oncoprotein oligomerization domain.";
Nat. Struct. Biol. 9:117-120(2002).
[31]
INTERACTION WITH SH2D5.
PubMed=25331951; DOI=10.1074/jbc.M114.615112;
Gray E.J., Petsalaki E., James D.A., Bagshaw R.D., Stacey M.M.,
Rocks O., Gingras A.C., Pawson T.;
"src homology 2 domain containing protein 5 (sh2d5) binds the
breakpoint cluster region protein, BCR, and regulates levels of Rac1-
GTP.";
J. Biol. Chem. 289:35397-35408(2014).
[32]
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.
PubMed=17344846; DOI=10.1038/nature05610;
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- 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.
{ECO:0000269|PubMed:1657398, ECO:0000269|PubMed:1903516}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
EC=2.7.11.1;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.1;
-!- SUBUNIT: Homotetramer. Interacts with PDZK1. May interact with
CCPG1 (By similarity). Interacts with FES/FPS, ABL1, PIK3R1 and
GRB2. Interacts with HCK. Interacts with SH2D5 (PubMed:25331951).
{ECO:0000250|UniProtKB:Q6PAJ1, ECO:0000269|PubMed:15302586,
ECO:0000269|PubMed:15494376, ECO:0000269|PubMed:1712671,
ECO:0000269|PubMed:25331951, ECO:0000269|PubMed:9407116}.
-!- INTERACTION:
P62993:GRB2; NbExp=8; IntAct=EBI-712838, EBI-401755;
P18031:PTPN1; NbExp=3; IntAct=EBI-8658094, EBI-968788;
Q6ZV89-1:SH2D5; NbExp=2; IntAct=EBI-712838, EBI-15101685;
A2AM67:Sh2d5 (xeno); NbExp=7; IntAct=EBI-712838, EBI-15101945;
Q8JZW5:Sh2d5 (xeno); NbExp=2; IntAct=EBI-712838, EBI-15101675;
Q9H2K2:TNKS2; NbExp=3; IntAct=EBI-712838, EBI-4398527;
P04637:TP53; NbExp=2; IntAct=EBI-712838, EBI-366083;
-!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
membrane, postsynaptic density {ECO:0000250|UniProtKB:Q6PAJ1}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P11274-1; Sequence=Displayed;
Name=2;
IsoId=P11274-2; Sequence=VSP_024352;
Note=No experimental confirmation available.;
-!- 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.
-!- DOMAIN: The DH domain is involved in interaction with CCPG1.
{ECO:0000250}.
-!- PTM: 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. {ECO:0000269|PubMed:15302586,
ECO:0000269|PubMed:9407116}.
-!- 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.
{ECO:0000269|PubMed:2407300, ECO:0000269|PubMed:3107980,
ECO:0000269|PubMed:3540951}. Note=The gene represented in this
entry is involved in disease pathogenesis.
-!- DISEASE: Note=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). {ECO:0000269|PubMed:3107980,
ECO:0000269|PubMed:7665185}.
-!- SEQUENCE CAUTION:
Sequence=BAE06073.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BCRID55.html";
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EMBL; Y00661; CAA68676.1; -; mRNA.
EMBL; U07000; AAB60388.1; -; Genomic_DNA.
EMBL; AB209991; BAE06073.1; ALT_INIT; mRNA.
EMBL; X02596; CAA26441.1; -; mRNA.
EMBL; M15025; AAA35594.1; -; Genomic_DNA.
EMBL; X52828; CAA37010.1; -; Genomic_DNA.
EMBL; X52829; CAA37011.1; -; Genomic_DNA.
EMBL; X14676; CAA32806.1; -; mRNA.
EMBL; M64437; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS13806.1; -. [P11274-1]
CCDS; CCDS13807.1; -. [P11274-2]
PIR; A26664; TVHUA2.
PIR; A91064; TVHUBR.
RefSeq; NP_004318.3; NM_004327.3. [P11274-1]
RefSeq; NP_067585.2; NM_021574.2. [P11274-2]
UniGene; Hs.517461; -.
UniGene; Hs.684909; -.
UniGene; Hs.715409; -.
PDB; 1K1F; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-72.
PDB; 2AIN; NMR; -; B=1266-1271.
PDB; 5N6R; NMR; -; A=487-702.
PDB; 5N7E; X-ray; 1.65 A; B=487-702.
PDB; 5OC7; X-ray; 1.65 A; A/D=704-893.
PDBsum; 1K1F; -.
PDBsum; 2AIN; -.
PDBsum; 5N6R; -.
PDBsum; 5N7E; -.
PDBsum; 5OC7; -.
ProteinModelPortal; P11274; -.
SMR; P11274; -.
BioGrid; 107083; 81.
ELM; P11274; -.
IntAct; P11274; 35.
MINT; P11274; -.
STRING; 9606.ENSP00000303507; -.
BindingDB; P11274; -.
ChEMBL; CHEMBL5146; -.
DrugBank; DB06616; Bosutinib.
DrugBank; DB08901; Ponatinib.
iPTMnet; P11274; -.
PhosphoSitePlus; P11274; -.
BioMuta; BCR; -.
DMDM; 143811366; -.
EPD; P11274; -.
jPOST; P11274; -.
MaxQB; P11274; -.
PaxDb; P11274; -.
PeptideAtlas; P11274; -.
PRIDE; P11274; -.
ProteomicsDB; 52729; -.
ProteomicsDB; 52730; -. [P11274-2]
Ensembl; ENST00000305877; ENSP00000303507; ENSG00000186716. [P11274-1]
Ensembl; ENST00000359540; ENSP00000352535; ENSG00000186716. [P11274-2]
GeneID; 613; -.
KEGG; hsa:613; -.
UCSC; uc002zww.4; human. [P11274-1]
CTD; 613; -.
DisGeNET; 613; -.
EuPathDB; HostDB:ENSG00000186716.19; -.
GeneCards; BCR; -.
H-InvDB; HIX0016226; -.
H-InvDB; HIX0016271; -.
H-InvDB; HIX0027936; -.
H-InvDB; HIX0041406; -.
HGNC; HGNC:1014; BCR.
HPA; CAB010421; -.
HPA; CAB018545; -.
HPA; HPA038337; -.
MalaCards; BCR; -.
MIM; 151410; gene.
MIM; 608232; phenotype.
neXtProt; NX_P11274; -.
OpenTargets; ENSG00000186716; -.
Orphanet; 521; Chronic myeloid leukemia.
Orphanet; 261330; Distal 22q11.2 microdeletion syndrome.
Orphanet; 99860; Precursor B-cell acute lymphoblastic leukemia.
Orphanet; 99861; Precursor T-cell acute lymphoblastic leukemia.
PharmGKB; PA25321; -.
eggNOG; KOG4269; Eukaryota.
eggNOG; ENOG410XPGZ; LUCA.
GeneTree; ENSGT00940000153491; -.
HOGENOM; HOG000006779; -.
HOVERGEN; HBG004165; -.
InParanoid; P11274; -.
KO; K08878; -.
OMA; DRIMGKG; -.
OrthoDB; 762492at2759; -.
PhylomeDB; P11274; -.
TreeFam; TF105082; -.
Reactome; R-HSA-1839117; Signaling by cytosolic FGFR1 fusion mutants.
Reactome; R-HSA-194840; Rho GTPase cycle.
Reactome; R-HSA-5655302; Signaling by FGFR1 in disease.
SignaLink; P11274; -.
SIGNOR; P11274; -.
ChiTaRS; BCR; human.
EvolutionaryTrace; P11274; -.
GeneWiki; BCR_(gene); -.
GenomeRNAi; 613; -.
PRO; PR:P11274; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000186716; Expressed in 215 organ(s), highest expression level in adenohypophysis.
ExpressionAtlas; P11274; baseline and differential.
Genevisible; P11274; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
GO; GO:0099092; C:postsynaptic density, intracellular component; IEA:Ensembl.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0032991; C:protein-containing complex; IDA:MGI.
GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005096; F:GTPase activator activity; TAS:Reactome.
GO; GO:0016301; F:kinase activity; TAS:Reactome.
GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:ProtInc.
GO; GO:0004713; F:protein tyrosine kinase activity; TAS:Reactome.
GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
GO; GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0060216; P:definitive hemopoiesis; IEA:Ensembl.
GO; GO:0048872; P:homeostasis of number of cells; IEA:Ensembl.
GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl.
GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
GO; GO:0060313; P:negative regulation of blood vessel remodeling; IEA:Ensembl.
GO; GO:0002692; P:negative regulation of cellular extravasation; IEA:Ensembl.
GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
GO; GO:0043314; P:negative regulation of neutrophil degranulation; IEA:Ensembl.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IEA:Ensembl.
GO; GO:0060268; P:negative regulation of respiratory burst; IEA:Ensembl.
GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0050766; P:positive regulation of phagocytosis; IEA:Ensembl.
GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:Ensembl.
GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
GO; GO:0043114; P:regulation of vascular permeability; IEA:Ensembl.
GO; GO:0003014; P:renal system process; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd00160; RhoGEF; 1.
Gene3D; 1.10.555.10; -; 1.
Gene3D; 1.20.900.10; -; 1.
Gene3D; 2.60.40.150; -; 1.
Gene3D; 4.10.280.30; -; 1.
InterPro; IPR037769; Abr/Bcr.
InterPro; IPR015123; Bcr-Abl_oncoprot_oligo.
InterPro; IPR036481; Bcr-Abl_oncoprot_oligo_sf.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR035899; DBL_dom_sf.
InterPro; IPR000219; DH-domain.
InterPro; IPR001331; GDS_CDC24_CS.
InterPro; IPR001849; PH_domain.
InterPro; IPR008936; Rho_GTPase_activation_prot.
InterPro; IPR000198; RhoGAP_dom.
PANTHER; PTHR23182; PTHR23182; 1.
Pfam; PF09036; Bcr-Abl_Oligo; 1.
Pfam; PF00168; C2; 1.
Pfam; PF00620; RhoGAP; 1.
Pfam; PF00621; RhoGEF; 1.
SMART; SM00239; C2; 1.
SMART; SM00233; PH; 1.
SMART; SM00324; RhoGAP; 1.
SMART; SM00325; RhoGEF; 1.
SUPFAM; SSF48065; SSF48065; 1.
SUPFAM; SSF48350; SSF48350; 1.
SUPFAM; SSF69036; SSF69036; 1.
PROSITE; PS50004; C2; 1.
PROSITE; PS00741; DH_1; 1.
PROSITE; PS50010; DH_2; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS50238; RHOGAP; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Cell junction; Cell membrane; Chromosomal rearrangement;
Complete proteome; GTPase activation;
Guanine-nucleotide releasing factor; Kinase; Membrane; Methylation;
Nucleotide-binding; Phosphoprotein; Polymorphism;
Postsynaptic cell membrane; Proto-oncogene; Reference proteome;
Serine/threonine-protein kinase; Synapse; Transferase.
CHAIN 1 1271 Breakpoint cluster region protein.
/FTId=PRO_0000080933.
DOMAIN 498 691 DH. {ECO:0000255|PROSITE-
ProRule:PRU00062}.
DOMAIN 708 866 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 870 1002 C2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
DOMAIN 1054 1248 Rho-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00172}.
REGION 1 426 Kinase.
REGION 197 385 Binding to ABL SH2-domain.
COMPBIAS 824 827 Poly-Leu.
SITE 426 427 Breakpoint for translocation to form BCR-
ABL oncogene.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 122 122 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 139 139 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 177 177 Phosphotyrosine; by HCK.
{ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:9407116}.
MOD_RES 202 202 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 215 215 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 222 222 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 236 236 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PAJ1}.
MOD_RES 246 246 Phosphotyrosine; by FES.
{ECO:0000269|PubMed:15302586}.
MOD_RES 356 356 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 377 377 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 382 382 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PAJ1}.
MOD_RES 385 385 Phosphothreonine.
{ECO:0000250|UniProtKB:Q6PAJ1}.
MOD_RES 459 459 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 463 463 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 471 471 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q6PAJ1}.
MOD_RES 473 473 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 488 488 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 554 554 Phosphotyrosine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 641 641 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 644 644 Phosphotyrosine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 693 693 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 894 894 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1264 1264 Phosphoserine.
{ECO:0000244|PubMed:15144186,
ECO:0000244|PubMed:19690332}.
VAR_SEQ 961 1004 Missing (in isoform 2).
{ECO:0000303|PubMed:3285291}.
/FTId=VSP_024352.
VARIANT 400 400 S -> P (in a bladder transitional cell
carcinoma sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041883.
VARIANT 413 413 I -> M (in dbSNP:rs56321828).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041884.
VARIANT 558 558 K -> T (in dbSNP:rs4437065).
/FTId=VAR_051983.
VARIANT 752 752 D -> E (in dbSNP:rs12484731).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041885.
VARIANT 796 796 N -> S (in dbSNP:rs140504).
{ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:2407300,
ECO:0000269|PubMed:3107980,
ECO:0000269|PubMed:3285291,
ECO:0000269|Ref.3}.
/FTId=VAR_031552.
VARIANT 910 910 Y -> C (in dbSNP:rs35537221).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041886.
VARIANT 949 949 V -> I (in dbSNP:rs2229038).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041887.
VARIANT 1037 1037 E -> K (in dbSNP:rs776552570).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_031553.
VARIANT 1091 1091 V -> M (in dbSNP:rs778229520).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041888.
VARIANT 1096 1096 T -> A (in dbSNP:rs745459086).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041889.
VARIANT 1104 1104 A -> G (in dbSNP:rs11558696).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041890.
VARIANT 1106 1106 D -> N (in dbSNP:rs879255379).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041891.
VARIANT 1127 1127 T -> M (in dbSNP:rs35812689).
/FTId=VAR_031554.
VARIANT 1149 1149 A -> T (in dbSNP:rs200099830).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041892.
VARIANT 1161 1161 E -> K. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_041893.
VARIANT 1187 1187 K -> E (in dbSNP:rs1195127922).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041894.
VARIANT 1189 1189 V -> M (in dbSNP:rs55816482).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041895.
VARIANT 1204 1204 A -> G (in dbSNP:rs56265970).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041896.
VARIANT 1235 1235 W -> R (in dbSNP:rs55719322).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041897.
MUTAGEN 177 177 Y->F: Abolishes interaction with FES and
GRB2. {ECO:0000269|PubMed:15302586,
ECO:0000269|PubMed:9407116}.
MUTAGEN 1269 1271 Missing: Abolishes interaction with
PDZK1. {ECO:0000269|PubMed:15494376}.
MUTAGEN 1271 1271 V->A: Reduces interaction with PDZK1.
{ECO:0000269|PubMed:15494376}.
CONFLICT 287 287 M -> I (in Ref. 1; CAA68676).
{ECO:0000305}.
CONFLICT 418 418 G -> D (in Ref. 1; CAA68676).
{ECO:0000305}.
CONFLICT 483 483 E -> K (in Ref. 1; CAA68676).
{ECO:0000305}.
CONFLICT 560 560 F -> S (in Ref. 1; CAA68676).
{ECO:0000305}.
CONFLICT 690 690 E -> D (in Ref. 11). {ECO:0000305}.
CONFLICT 733 733 D -> E (in Ref. 4; CAA26441).
{ECO:0000305}.
HELIX 4 14 {ECO:0000244|PDB:1K1F}.
HELIX 28 64 {ECO:0000244|PDB:1K1F}.
HELIX 492 521 {ECO:0000244|PDB:5N7E}.
HELIX 524 531 {ECO:0000244|PDB:5N7E}.
STRAND 533 535 {ECO:0000244|PDB:5N7E}.
HELIX 540 546 {ECO:0000244|PDB:5N7E}.
TURN 547 549 {ECO:0000244|PDB:5N7E}.
HELIX 550 569 {ECO:0000244|PDB:5N7E}.
HELIX 578 586 {ECO:0000244|PDB:5N7E}.
HELIX 588 611 {ECO:0000244|PDB:5N7E}.
HELIX 613 618 {ECO:0000244|PDB:5N7E}.
STRAND 630 634 {ECO:0000244|PDB:5N6R}.
HELIX 639 651 {ECO:0000244|PDB:5N7E}.
HELIX 653 661 {ECO:0000244|PDB:5N7E}.
HELIX 670 687 {ECO:0000244|PDB:5N7E}.
STRAND 694 697 {ECO:0000244|PDB:5N6R}.
STRAND 709 719 {ECO:0000244|PDB:5OC7}.
STRAND 722 740 {ECO:0000244|PDB:5OC7}.
STRAND 751 758 {ECO:0000244|PDB:5OC7}.
HELIX 759 761 {ECO:0000244|PDB:5OC7}.
STRAND 762 767 {ECO:0000244|PDB:5OC7}.
STRAND 830 838 {ECO:0000244|PDB:5OC7}.
STRAND 843 847 {ECO:0000244|PDB:5OC7}.
HELIX 851 865 {ECO:0000244|PDB:5OC7}.
HELIX 876 885 {ECO:0000244|PDB:5OC7}.
STRAND 1268 1271 {ECO:0000244|PDB:2AIN}.
SEQUENCE 1271 AA; 142819 MW; 4BF66FA1E9D205FE CRC64;
MVDPVGFAEA WKAQFPDSEP PRMELRSVGD IEQELERCKA SIRRLEQEVN QERFRMIYLQ
TLLAKEKKSY DRQRWGFRRA AQAPDGASEP RASASRPQPA PADGADPPPA EEPEARPDGE
GSPGKARPGT ARRPGAAASG ERDDRGPPAS VAALRSNFER IRKGHGQPGA DAEKPFYVNV
EFHHERGLVK VNDKEVSDRI SSLGSQAMQM ERKKSQHGAG SSVGDASRPP YRGRSSESSC
GVDGDYEDAE LNPRFLKDNL IDANGGSRPP WPPLEYQPYQ SIYVGGMMEG EGKGPLLRSQ
STSEQEKRLT WPRRSYSPRS FEDCGGGYTP DCSSNENLTS SEEDFSSGQS SRVSPSPTTY
RMFRDKSRSP SQNSQQSFDS SSPPTPQCHK RHRHCPVVVS EATIVGVRKT GQIWPNDGEG
AFHGDADGSF GTPPGYGCAA DRAEEQRRHQ DGLPYIDDSP SSSPHLSSKG RGSRDALVSG
ALESTKASEL DLEKGLEMRK WVLSGILASE ETYLSHLEAL LLPMKPLKAA ATTSQPVLTS
QQIETIFFKV PELYEIHKEF YDGLFPRVQQ WSHQQRVGDL FQKLASQLGV YRAFVDNYGV
AMEMAEKCCQ ANAQFAEISE NLRARSNKDA KDPTTKNSLE TLLYKPVDRV TRSTLVLHDL
LKHTPASHPD HPLLQDALRI SQNFLSSINE EITPRRQSMT VKKGEHRQLL KDSFMVELVE
GARKLRHVFL FTDLLLCTKL KKQSGGKTQQ YDCKWYIPLT DLSFQMVDEL EAVPNIPLVP
DEELDALKIK ISQIKNDIQR EKRANKGSKA TERLKKKLSE QESLLLLMSP SMAFRVHSRN
GKSYTFLISS DYERAEWREN IREQQKKCFR SFSLTSVELQ MLTNSCVKLQ TVHSIPLTIN
KEDDESPGLY GFLNVIVHSA TGFKQSSNLY CTLEVDSFGY FVNKAKTRVY RDTAEPNWNE
EFEIELEGSQ TLRILCYEKC YNKTKIPKED GESTDRLMGK GQVQLDPQAL QDRDWQRTVI
AMNGIEVKLS VKFNSREFSL KRMPSRKQTG VFGVKIAVVT KRERSKVPYI VRQCVEEIER
RGMEEVGIYR VSGVATDIQA LKAAFDVNNK DVSVMMSEMD VNAIAGTLKL YFRELPEPLF
TDEFYPNFAE GIALSDPVAK ESCMLNLLLS LPEANLLTFL FLLDHLKRVA EKEAVNKMSL
HNLATVFGPT LLRPSEKESK LPANPSQPIT MTDSWSLEVM SQVQVLLYFL QLEAIPAPDS
KRQSILFSTE V


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Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1424: Globo Sphingolipid Metabolism
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1545: miRNAs involved in DDR
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1675: Nitrogen metabolism

Related Genes :
[BCR BCR1 D22S11] Breakpoint cluster region protein (EC 2.7.11.1) (Renal carcinoma antigen NY-REN-26)
[STK11 LKB1 PJS] Serine/threonine-protein kinase STK11 (EC 2.7.11.1) (Liver kinase B1) (LKB1) (hLKB1) (Renal carcinoma antigen NY-REN-19)
[ROCK1] Rho-associated protein kinase 1 (EC 2.7.11.1) (Renal carcinoma antigen NY-REN-35) (Rho-associated, coiled-coil-containing protein kinase 1) (Rho-associated, coiled-coil-containing protein kinase I) (ROCK-I) (p160 ROCK-1) (p160ROCK)
[HSP90AA1 HSP90A HSPC1 HSPCA] Heat shock protein HSP 90-alpha (Heat shock 86 kDa) (HSP 86) (HSP86) (Lipopolysaccharide-associated protein 2) (LAP-2) (LPS-associated protein 2) (Renal carcinoma antigen NY-REN-38)
[GCC2 KIAA0336 RANBP2L4] GRIP and coiled-coil domain-containing protein 2 (185 kDa Golgi coiled-coil protein) (GCC185) (CLL-associated antigen KW-11) (CTCL tumor antigen se1-1) (Ran-binding protein 2-like 4) (RanBP2L4) (Renal carcinoma antigen NY-REN-53)
[IRAK4] Interleukin-1 receptor-associated kinase 4 (IRAK-4) (EC 2.7.11.1) (Renal carcinoma antigen NY-REN-64)
[USH1C AIE75] Harmonin (Antigen NY-CO-38/NY-CO-37) (Autoimmune enteropathy-related antigen AIE-75) (Protein PDZ-73) (Renal carcinoma antigen NY-REN-3) (Usher syndrome type-1C protein)
[EPHB2 DRT EPHT3 EPTH3 ERK HEK5 TYRO5] Ephrin type-B receptor 2 (EC 2.7.10.1) (Developmentally-regulated Eph-related tyrosine kinase) (ELK-related tyrosine kinase) (EPH tyrosine kinase 3) (EPH-like kinase 5) (EK5) (hEK5) (Renal carcinoma antigen NY-REN-47) (Tyrosine-protein kinase TYRO5) (Tyrosine-protein kinase receptor EPH-3) [Cleaved into: EphB2/CTF1; EphB2/CTF2]
[LMNA LMN1] Prelamin-A/C [Cleaved into: Lamin-A/C (70 kDa lamin) (Renal carcinoma antigen NY-REN-32)]
[ECI2 DRS1 HCA88 PECI] Enoyl-CoA delta isomerase 2, mitochondrial (EC 5.3.3.8) (DRS-1) (Delta(3),delta(2)-enoyl-CoA isomerase) (D3,D2-enoyl-CoA isomerase) (Diazepam-binding inhibitor-related protein 1) (DBI-related protein 1) (Dodecenoyl-CoA isomerase) (Hepatocellular carcinoma-associated antigen 88) (Peroxisomal 3,2-trans-enoyl-CoA isomerase) (pECI) (Renal carcinoma antigen NY-REN-1)
[NEK1 KIAA1901] Serine/threonine-protein kinase Nek1 (EC 2.7.11.1) (Never in mitosis A-related kinase 1) (NimA-related protein kinase 1) (Renal carcinoma antigen NY-REN-55)
[PLA2G16 HRASLS3 HREV107] HRAS-like suppressor 3 (HRSL3) (EC 3.1.1.32) (EC 3.1.1.4) (Adipose-specific phospholipase A2) (AdPLA) (Group XVI phospholipase A1/A2) (H-rev 107 protein homolog) (H-REV107) (HREV107-1) (HRAS-like suppressor 1) (HREV107-3) (Renal carcinoma antigen NY-REN-65)
[TRMT10C MRPP1 RG9MTD1] tRNA methyltransferase 10 homolog C (HBV pre-S2 trans-regulated protein 2) (Mitochondrial ribonuclease P protein 1) (Mitochondrial RNase P protein 1) (RNA (guanine-9-)-methyltransferase domain-containing protein 1) (Renal carcinoma antigen NY-REN-49) (mRNA methyladenosine-N(1)-methyltransferase) (EC 2.1.1.-) (tRNA (adenine(9)-N(1))-methyltransferase) (EC 2.1.1.218) (tRNA (guanine(9)-N(1))-methyltransferase) (EC 2.1.1.221)
[YTHDF2 HGRG8] YTH domain-containing family protein 2 (CLL-associated antigen KW-14) (High-glucose-regulated protein 8) (Renal carcinoma antigen NY-REN-2)
[CTNNA1] Catenin alpha-1 (Alpha E-catenin) (Cadherin-associated protein) (Renal carcinoma antigen NY-REN-13)
[NEDD9 CASL CASS2] Enhancer of filamentation 1 (hEF1) (CRK-associated substrate-related protein) (CAS-L) (CasL) (Cas scaffolding protein family member 2) (Neural precursor cell expressed developmentally down-regulated protein 9) (NEDD-9) (Renal carcinoma antigen NY-REN-12) (p105) [Cleaved into: Enhancer of filamentation 1 p55]
[AARS] Alanine--tRNA ligase, cytoplasmic (EC 6.1.1.7) (Alanyl-tRNA synthetase) (AlaRS) (Renal carcinoma antigen NY-REN-42)
[KIF21A KIAA1708 KIF2] Kinesin-like protein KIF21A (Kinesin-like protein KIF2) (Renal carcinoma antigen NY-REN-62)
[PPP2R5C KIAA0044] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform (PP2A B subunit isoform B'-gamma) (PP2A B subunit isoform B56-gamma) (PP2A B subunit isoform PR61-gamma) (PP2A B subunit isoform R5-gamma) (Renal carcinoma antigen NY-REN-29)
[LIMS1 PINCH PINCH1] LIM and senescent cell antigen-like-containing domain protein 1 (Particularly interesting new Cys-His protein 1) (PINCH-1) (Renal carcinoma antigen NY-REN-48)
[LDHA PIG19] L-lactate dehydrogenase A chain (LDH-A) (EC 1.1.1.27) (Cell proliferation-inducing gene 19 protein) (LDH muscle subunit) (LDH-M) (Renal carcinoma antigen NY-REN-59)
[RLIM RNF12] E3 ubiquitin-protein ligase RLIM (EC 2.3.2.27) (LIM domain-interacting RING finger protein) (RING finger LIM domain-binding protein) (R-LIM) (RING finger protein 12) (RING-type E3 ubiquitin transferase RLIM) (Renal carcinoma antigen NY-REN-43)
[RBPJ IGKJRB IGKJRB1 RBPJK RBPSUH] Recombining binding protein suppressor of hairless (CBF-1) (J kappa-recombination signal-binding protein) (RBP-J kappa) (RBP-J) (RBP-JK) (Renal carcinoma antigen NY-REN-30)
[LDHB] L-lactate dehydrogenase B chain (LDH-B) (EC 1.1.1.27) (LDH heart subunit) (LDH-H) (Renal carcinoma antigen NY-REN-46)
[CRYAB CRYA2 HSPB5] Alpha-crystallin B chain (Alpha(B)-crystallin) (Heat shock protein beta-5) (HspB5) (Renal carcinoma antigen NY-REN-27) (Rosenthal fiber component)
[MED6 ARC33] Mediator of RNA polymerase II transcription subunit 6 (Activator-recruited cofactor 33 kDa component) (ARC33) (Mediator complex subunit 6) (hMed6) (Renal carcinoma antigen NY-REN-28)
[CEP83 CCDC41] Centrosomal protein of 83 kDa (Cep83) (Coiled-coil domain-containing protein 41) (Renal carcinoma antigen NY-REN-58)
[MUC1 PUM] Mucin-1 (MUC-1) (Breast carcinoma-associated antigen DF3) (Cancer antigen 15-3) (CA 15-3) (Carcinoma-associated mucin) (Episialin) (H23AG) (Krebs von den Lungen-6) (KL-6) (PEMT) (Peanut-reactive urinary mucin) (PUM) (Polymorphic epithelial mucin) (PEM) (Tumor-associated epithelial membrane antigen) (EMA) (Tumor-associated mucin) (CD antigen CD227) [Cleaved into: Mucin-1 subunit alpha (MUC1-NT) (MUC1-alpha); Mucin-1 subunit beta (MUC1-beta) (MUC1-CT)]
[Bcr Kiaa3017] Breakpoint cluster region protein (EC 2.7.11.1)
[Pre C,C C core E PC pre-C pre-C/C PreC preC PreC/C preC/C precore-core HBVgp4] Capsid protein (Core antigen) (Core protein) (HBcAg) (p21.5)

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