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UniProtKB/Swiss-Prot entry P00519

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ABL1_HUMAN
Primary accession number P00519
Secondary accession numbers Q13869 Q13870 Q16133 Q45F09
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 24, 2006 (Sequence version 4)
Annotations were last modified on    June 16, 2009 (Entry version 145)
Name and origin of the protein
Protein name Proto-oncogene tyrosine-protein kinase ABL1
Synonyms EC 2.7.10.2
Abelson murine leukemia viral oncogene homolog 1
c-ABL
p150
Gene name
Name: ABL1
Synonyms: ABL, JTK7
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IA).
TISSUE=Fibroblast;
PubMed=2687768 [NCBI, ExPASy, EBI, Israel, Japan]
Fainstein E., Einat M., Gokkel E., Marcelle C., Croce C.M., Gale R.P., Canaani E.;
"Nucleotide sequence analysis of human abl and bcr-abl cDNAs.";
Oncogene 4:1477-1481(1989).
[2]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IA), ALTERNATIVE SPLICING, AND VARIANT PRO-140.
DOI=10.1016/0092-8674(86)90450-2; PubMed=3021337 [NCBI, ExPASy, EBI, Israel, Japan]
Shtivelman E., Lifshitz B., Gale R.P., Roe B.A., Canaani E.;
"Alternative splicing of RNAs transcribed from the human abl gene and from the bcr-abl fused gene.";
Cell 47:277-284(1986).
[3]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS IA AND IB).
TISSUE=Lung;
DOI=10.1006/geno.1995.1008; PubMed=7665185 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[4]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-706; PRO-852; SER-900 AND LEU-972.
NIEHS SNPs program;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
 NUCLEOTIDE SEQUENCE [MRNA] OF 27-40, AND SUBCELLULAR COMPONENT.
DOI=10.1038/330386a0; PubMed=2825022 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
 NUCLEOTIDE SEQUENCE OF 360-426.
DOI=10.1038/304167a0; PubMed=6191223 [NCBI, ExPASy, EBI, Israel, Japan]
Groffen J., Heisterkamp N., Reynolds F.H. Jr., Stephenson J.R.;
"Homology between phosphotyrosine acceptor site of human c-abl and viral oncogene products.";
Nature 304:167-169(1983).
[7]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 825-845.
PubMed=7545908 [NCBI, ExPASy, EBI, Israel, Japan]
Inokuchi K., Futaki M., Dan K., Nomura T.;
"Sequence analysis of the mutation at codon 834 and the sequence variation of codon 837 of c-abl gene.";
Leukemia 8:343-344(1994).
[8]
 MYRISTOYLATION OF ISOFORM IB.
PubMed=2542016 [NCBI, ExPASy, EBI, Israel, Japan]
Jackson P., Baltimore D.;
"N-terminal mutations activate the leukemogenic potential of the myristoylated form of c-abl.";
EMBO J. 8:449-456(1989).
[9]
 INTERACTION WITH INPPL1.
PubMed=10194451 [NCBI, ExPASy, EBI, Israel, Japan]
Wisniewski D., Strife A., Swendeman S., Erdjument-Bromage H., Geromanos S., Kavanaugh W.M., Tempst P., Clarkson B.;
"A novel SH2-containing phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase (SHIP2) is constitutively tyrosine phosphorylated and associated with src homologous and collagen gene (SHC) in chronic myelogenous leukemia progenitor cells.";
Blood 93:2707-2720(1999).
[10]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-185; TYR-226; TYR-253; TYR-257; TYR-264; TYR-393; THR-394 AND TYR-469, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.2436191100; PubMed=12522270 [NCBI, ExPASy, EBI, Israel, Japan]
Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T., Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.;
"Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003).
[11]
 INTERACTION WITH SORBS1.
DOI=10.1006/geno.2001.6541; PubMed=11374898 [NCBI, ExPASy, EBI, Israel, Japan]
Lin W.-H., Huang C.-J., Liu M.-W., Chang H.-M., Chen Y.-J., Tai T.-Y., Chuang L.-M.;
"Cloning, mapping, and characterization of the human sorbin and SH3 domain containing 1 (SORBS1) gene: a protein associated with c-Abl during insulin signaling in the hepatoma cell line Hep3B.";
Genomics 74:12-20(2001).
[12]
 INTERACTION WITH YWHAB; YWHAE; YWHAG; YWHAH; SFN AND YWHAZ, PHOSPHORYLATION AT THR-735, MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-735.
DOI=10.1038/ncb1228; PubMed=15696159 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshida K., Yamaguchi T., Natsume T., Kufe D., Miki Y.;
"JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of c-Abl in the apoptotic response to DNA damage.";
Nat. Cell Biol. 7:278-285(2005).
[13]
 INTERACTION WITH RIN1, AND FUNCTION.
DOI=10.1073/pnas.94.10.4954; PubMed=9144171 [NCBI, ExPASy, EBI, Israel, Japan]
Han L., Wong D., Dhaka A., Afar D.E.H., White M., Xie W., Herschman H., Witte O., Colicelli J.;
"Protein binding and signaling properties of RIN1 suggest a unique effector function.";
Proc. Natl. Acad. Sci. U.S.A. 94:4954-4959(1997).
[14]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569; SER-683; SER-805; SER-809 AND SER-949, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[15]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-185, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[16]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.T600062-MCP200; PubMed=17192257 [NCBI, ExPASy, EBI, Israel, Japan]
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.;
"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry.";
Mol. Cell. Proteomics 6:537-547(2007).
[17]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; TYR-185; TYR-393; SER-569; THR-613; SER-620; SER-659; SER-683; SER-718; THR-781; SER-805; SER-809; THR-814; THR-844; THR-852; SER-917; SER-919; SER-936 AND SER-977, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[18]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569; THR-844; THR-852 AND SER-917, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[19]
 STRUCTURE BY NMR OF SH2 DOMAIN.
DOI=10.1016/0092-8674(92)90437-H; PubMed=1505033 [NCBI, ExPASy, EBI, Israel, Japan]
Overduin M., Rios C.B., Mayer B.J., Baltimore D., Cowburn D.;
"Three-dimensional solution structure of the src homology 2 domain of c-abl.";
Cell 70:697-704(1992).
[20]
 STRUCTURE BY NMR OF SH2 DOMAIN.
DOI=10.1073/pnas.89.24.11673; PubMed=1281542 [NCBI, ExPASy, EBI, Israel, Japan]
Overduin M., Mayer B.J., Rios C.B., Baltimore D., Cowburn D.;
"Secondary structure of Src homology 2 domain of c-Abl by heteronuclear NMR spectroscopy in solution.";
Proc. Natl. Acad. Sci. U.S.A. 89:11673-11677(1992).
[21]
 3D-STRUCTURE MODELING OF SH3 DOMAIN.
DOI=10.1002/prot.340200302; PubMed=7892170 [NCBI, ExPASy, EBI, Israel, Japan]
Pisabarro M.T., Ortiz A.R., Serrano L., Wade R.C.;
"Homology modeling of the Abl-SH3 domain.";
Proteins 20:203-215(1994).
[22]
 STRUCTURE BY NMR OF SH3 DOMAIN.
DOI=10.1016/S0969-2126(01)00243-X; PubMed=8590002 [NCBI, ExPASy, EBI, Israel, Japan]
Gosser Y.Q., Zheng J., Overduin M., Mayer B.J., Cowburn D.;
"The solution structure of Abl SH3, and its relationship to SH2 in the SH(32) construct.";
Structure 3:1075-1086(1995).
[23]
 X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 64-121.
DOI=10.1006/jmbi.1998.1932; PubMed=9698566 [NCBI, ExPASy, EBI, Israel, Japan]
Pisabarro M.T., Serrano L., Wilmanns M.;
"Crystal structure of the abl-SH3 domain complexed with a designed high-affinity peptide ligand: implications for SH3-ligand interactions.";
J. Mol. Biol. 281:513-521(1998).
[24]
 STRUCTURE BY NMR OF 62-122 IN COMPLEX WITH CRK.
DOI=10.1073/pnas.212518799; PubMed=12384576 [NCBI, ExPASy, EBI, Israel, Japan]
Donaldson L.W., Gish G., Pawson T., Kay L.E., Forman-Kay J.D.;
"Structure of a regulatory complex involving the Abl SH3 domain, the Crk SH2 domain, and a Crk-derived phosphopeptide.";
Proc. Natl. Acad. Sci. U.S.A. 99:14053-14058(2002).
[25]
 VARIANTS GLY-47; LYS-166; VAL-706; LEU-810 AND LEU-972.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X16416; CAA34438.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M14752; AAA51561.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U07563; AAB60394.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U07563; AAB60393.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U07561; AAB60393.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ145721; AAZ38718.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S69223; AAD14034.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00216969; -.
IPI00221171; -.
PIR S08519; TVHUA.
RefSeq NP_005148.2; -.
UniGene Hs.431048
3D structure databases
PDB
1AB2; NMR; -; A=120-220.[ExPASy / RCSB / EBI]
1ABL; Model; -; A=65-121.[ExPASy / RCSB / EBI]
1AWO; NMR; -; A=65-119.[ExPASy / RCSB / EBI]
1BBZ; X-ray; 1.65 A; A/C/E/G=64-121.[ExPASy / RCSB / EBI]
1JU5; NMR; -; C=62-121.[ExPASy / RCSB / EBI]
1OPL; X-ray; 3.42 A; A/B=27-512.[ExPASy / RCSB / EBI]
1ZZP; NMR; -; A=1007-1130.[ExPASy / RCSB / EBI]
2ABL; X-ray; 2.50 A; A=57-218.[ExPASy / RCSB / EBI]
2E2B; X-ray; 2.20 A; A/B=229-515.[ExPASy / RCSB / EBI]
2F4J; X-ray; 1.91 A; A=229-513.[ExPASy / RCSB / EBI]
2FO0; X-ray; 2.27 A; A=38-512.[ExPASy / RCSB / EBI]
2G1T; X-ray; 1.80 A; A/B/C/D=229-512.[ExPASy / RCSB / EBI]
2G2F; X-ray; 2.70 A; A/B=229-512.[ExPASy / RCSB / EBI]
2G2H; X-ray; 2.00 A; A/B=229-512.[ExPASy / RCSB / EBI]
2G2I; X-ray; 3.12 A; A/B=229-512.[ExPASy / RCSB / EBI]
2GQG; X-ray; 2.40 A; A/B=229-500.[ExPASy / RCSB / EBI]
2HIW; X-ray; 2.20 A; A/B=230-512.[ExPASy / RCSB / EBI]
2HYY; X-ray; 2.40 A; A/B/C/D=228-500.[ExPASy / RCSB / EBI]
2HZ0; X-ray; 2.10 A; A/B=228-497.[ExPASy / RCSB / EBI]
2HZ4; X-ray; 2.80 A; A/B/C=228-500.[ExPASy / RCSB / EBI]
2HZI; X-ray; 1.70 A; A/B=229-500.[ExPASy / RCSB / EBI]
2O88; X-ray; 1.75 A; A/B=64-121.[ExPASy / RCSB / EBI]
2V7A; X-ray; 2.50 A; A/B=229-512.[ExPASy / RCSB / EBI]
3CS9; X-ray; 2.21 A; A/B/C/D=229-500.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AB2; -.
1ABL; -.
1AWO; -.
1BBZ; -.
1JU5; -.
1OPL; -.
1ZZP; -.
2ABL; -.
2E2B; -.
2F4J; -.
2FO0; -.
2G1T; -.
2G2F; -.
2G2H; -.
2G2I; -.
2GQG; -.
2HIW; -.
2HYY; -.
2HZ0; -.
2HZ4; -.
2HZI; -.
2O88; -.
2V7A; -.
3CS9; -.
ModBase P00519.
Protein-protein interaction databases
DIP DIP:1042N; -.
IntAct P00519; 158.
PTM databases
PhosphoSite P00519; -.
Enzyme and pathway databases
BRENDA 2.7.10.2; 247.
Pathway_Interaction_DB lis1pathway; Lissencephaly gene (LIS1) in neuronal migration and development.
trkrpathway; Neurotrophic factor-mediated Trk receptor signaling.
pdgfrbpathway; PDGFR-beta signaling pathway.
telomerasepathway; Regulation of Telomerase.
Organism-specific databases
GeneCards GC09P132579; -.
H-InvDB HIX0008474; -.
HGNC HGNC:76; ABL1.
GenAtlas ABL1.
HPA CAB002686; -.
MIM 189980; gene. [NCBI / EBI]
608232; phenotype. [NCBI / EBI]
Orphanet 521; Chronic myeloid leukemia.
PharmGKB PA24413; -.
Gene expression databases
ArrayExpress P00519; -.
Bgee P00519; -.
CleanEx HS_ABL1; -.
GermOnline ENSG00000097007; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005856; Cellular component: cytoskeleton (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005730; Cellular component: nucleolus (inferred from direct assay from MGI).
GO:0005524; Molecular function: ATP binding (inferred from direct assay from UniProtKB).
GO:0003677; Molecular function: DNA binding (non-traceable author statement from UniProtKB).
GO:0000287; Molecular function: magnesium ion binding (inferred from direct assay from UniProtKB).
GO:0030145; Molecular function: manganese ion binding (inferred from direct assay from UniProtKB).
GO:0004715; Molecular function: non-membrane spanning protein tyrosine kinase activity (inferred from electronic annotation from EC).
GO:0008022; Molecular function: protein C-terminus binding (inferred from physical interaction from UniProtKB).
GO:0030036; Biological process: actin cytoskeleton organization (inferred from sequence or structural similarity from UniProtKB).
GO:0007155; Biological process: cell adhesion (inferred from electronic annotation from UniProtKB-KW).
GO:0008630; Biological process: DNA damage response, signal transduction resulting in induction of apoptosis (traceable author statement from ProtInc).
GO:0006298; Biological process: mismatch repair (traceable author statement from ProtInc).
GO:0018108; Biological process: peptidyl-tyrosine phosphorylation (inferred from direct assay from UniProtKB).
GO:0051353; Biological process: positive regulation of oxidoreductase activity (inferred from direct assay from UniProtKB).
GO:0000115; Biological process: regulation of transcription during S-phase of mitotic cell cycle (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR015015; F-actin_binding.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_BS.
IPR000980; SH2.
IPR001452; SH3_domain.
IPR001245; Tyr_pkinase.
IPR008266; Tyr_pkinase_AS.
Graphical view of domain structure.
Gene3D G3DSA:3.30.505.10; SH2; 1.
Pfam PF08919; F_actin_bind; 1.
PF07714; Pkinase_Tyr; 1.
PF00017; SH2; 1.
PF00018; SH3_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00401; SH2DOMAIN.
PR00109; TYRKINASE.
ProDom PD000001; Prot_kinase; 1.
PD000093; SH2; 1.
PD000066; SH3; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00808; FABD; 1.
SM00252; SH2; 1.
SM00326; SH3; 1.
SM00219; TyrKc; 1.
SMART graphical view of domain structure.
PROSITE PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00109; PROTEIN_KINASE_TYR; 1.
PS50001; SH2; 1.
PS50002; SH3; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P00519; -.
Genome annotation databases
Ensembl ENSG00000097007; Homo sapiens. [Contig view]
GeneID 25; -.
KEGG hsa:25; -.
Phylogenomic databases
HOVERGEN P00519; -.
OMA P00519; GAFRESG.
Other
DrugBank DB00171; Adenosine triphosphate.
DB01254; Dasatinib.
DB00619; Imatinib.
NextBio 79; -.
PMAP-CutDB P00519; -.
SOURCE ABL1; Homo sapiens.
ProtoNet P00519.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; ATP-binding; Cell adhesion; Chromosomal rearrangement; Cytoplasm; Cytoskeleton; Kinase; Lipoprotein; Magnesium; Manganese; Metal-binding; Myristate; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene; SH2 domain; SH3 domain; Transferase; Tyrosine-protein kinase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1130  1130     Proto-oncogene tyrosine-protein kinase ABL1. PRO_0000088050
DOMAIN   61    121  61     SH3. 
DOMAIN   127    217  91     SH2. 
DOMAIN   242    493  252     Protein kinase. 
NP_BIND   248    256  9     ATP (By similarity). 
REGION   1     60  60     CAP. 
MOTIF   605    609  5     Nuclear localization signal (Potential). 
COMPBIAS   18     22  5     Poly-Ser. 
COMPBIAS   605    609  5     Poly-Lys. 
COMPBIAS   782   1019  238     Pro-rich. 
COMPBIAS   897    903  7     Poly-Pro. 
ACT_SITE   363    363        Proton acceptor (By similarity). 
BINDING   271    271        ATP (By similarity). 
SITE   26     27  2     Breakpoint for translocation to form BCR-ABL oncogene. 
MOD_RES   50     50        Phosphoserine. 
MOD_RES   185    185        Phosphotyrosine. 
MOD_RES   226    226        Phosphotyrosine; by autocatalysis. 
MOD_RES   253    253        Phosphotyrosine. 
MOD_RES   257    257        Phosphotyrosine. 
MOD_RES   264    264        Phosphotyrosine. 
MOD_RES   393    393        Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases. 
MOD_RES   394    394        Phosphothreonine. 
MOD_RES   446    446        Phosphoserine (By similarity). 
MOD_RES   469    469        Phosphotyrosine. 
MOD_RES   569    569        Phosphoserine. 
MOD_RES   613    613        Phosphothreonine. 
MOD_RES   620    620        Phosphoserine. 
MOD_RES   659    659        Phosphoserine. 
MOD_RES   683    683        Phosphoserine. 
MOD_RES   718    718        Phosphoserine. 
MOD_RES   735    735        Phosphothreonine. 
MOD_RES   781    781        Phosphothreonine. 
MOD_RES   805    805        Phosphoserine. 
MOD_RES   809    809        Phosphoserine. 
MOD_RES   814    814        Phosphothreonine. 
MOD_RES   844    844        Phosphothreonine. 
MOD_RES   852    852        Phosphothreonine. 
MOD_RES   917    917        Phosphoserine. 
MOD_RES   919    919        Phosphoserine. 
MOD_RES   936    936        Phosphoserine. 
MOD_RES   949    949        Phosphoserine. 
MOD_RES   977    977        Phosphoserine. 
VAR_SEQ   1     26        MLEICLKLVGCKSKKGLSSSSSCYLE -> MGQQPGKVLGDQRRPSLPALHFIKGAGKKESSRHGGPHCN VFVEH (in isoform IB). VSP_004957
VARIANT   47     47  1     R -> G (in a lung large cell carcinoma sample; somatic mutation). VAR_032676 
VARIANT   140    140  1     L -> P (in dbSNP:rs1064152 [NCBI]). VAR_051692 
VARIANT   166    166  1     R -> K (in a melanoma sample; somatic mutation). VAR_032677 
VARIANT   247    247  1     K -> R (in dbSNP:rs34549764 [NCBI]). VAR_051693 [3D]
VARIANT   706    706  1     G -> V. VAR_025043 
VARIANT   810    810  1     P -> L. VAR_032678 
VARIANT   852    852  1     T -> P. VAR_025044 
VARIANT   900    900  1     P -> S. VAR_025045 
VARIANT   968    968  1     S -> P (in dbSNP:rs1064165 [NCBI]). VAR_051694 
VARIANT   972    972  1     S -> L (in dbSNP:rs2229067 [NCBI]). VAR_025046 
MUTAGEN   735    735        T->A: Abolishes phosphorylation. Loss of binding YWHAS and YWHAZ. Localizes to the nucleus. No effect on kinase activity. 
CONFLICT   159    159        G -> S (in Ref. 2; AAA51561). 
CONFLICT   424    425        AF -> GK (in Ref. 6). 
CONFLICT   445    445        L -> R (in Ref. 2; AAA51561). 
CONFLICT   459    459        E -> K (in Ref. 2; AAA51561). 
CONFLICT   520    520        S -> T (in Ref. 2; AAA51561). 
CONFLICT   719    719        A -> V (in Ref. 2; AAA51561). 
CONFLICT   837    837        G -> E (in Ref. 1; CAA34438). 
CONFLICT   837    837        G -> W (in Ref. 2; AAA51561). 
CONFLICT   863    863        G -> R (in Ref. 2; AAA51561). 
CONFLICT   894    894        R -> K (in Ref. 2; AAA51561). 
CONFLICT   917    919        SPS -> RPG (in Ref. 2; AAA51561). 
CONFLICT   952    952        G -> A (in Ref. 2; AAA51561). 
CONFLICT   967    968        QS -> HP (in Ref. 2; AAA51561). 
CONFLICT   982    982        P -> PL (in Ref. 2; AAA51561). 
CONFLICT   1022   1022        Missing (in Ref. 2; AAA51561). 
CONFLICT   1045   1045        R -> G (in Ref. 2; AAA51561). 
CONFLICT   1103   1103        T -> S (in Ref. 2; AAA51561). 
HELIX   49     53  5      
HELIX   58     60  3      
STRAND   65     70  6      
STRAND   87     93  7      
STRAND   97    104  8      
STRAND   107    112  6      
HELIX   113    115  3      
STRAND   116    118  3      
HELIX   122    124  3      
STRAND   128    131  4      
HELIX   134    140  7      
STRAND   142    144  3      
STRAND   148    153  6      
STRAND   155    157  3      
STRAND   161    167  7      
STRAND   170    178  9      
STRAND   184    187  4      
STRAND   192    194  3      
HELIX   195    204  10      
STRAND   209    211  3      
HELIX   239    241  3      
STRAND   242    248  7      
HELIX   249    251  3      
STRAND   254    261  8      
HELIX   262    264  3      
STRAND   266    272  7      
HELIX   280    290  11      
STRAND   301    305  5      
STRAND   307    310  4      
STRAND   312    316  5      
HELIX   323    329  7      
TURN   332    334  3      
HELIX   337    357  21      
HELIX   366    368  3      
STRAND   369    371  3      
HELIX   373    375  3      
STRAND   377    379  3      
STRAND   389    391  3      
HELIX   403    405  3      
HELIX   408    413  6      
HELIX   418    433  16      
HELIX   445    447  3      
HELIX   448    453  6      
HELIX   466    475  10      
HELIX   480    482  3      
HELIX   486    509  24      
TURN   510    512  3      
HELIX   1029   1045  17      
TURN   1046   1048  3      
HELIX   1053   1070  18      
HELIX   1071   1073  3      
HELIX   1080   1097  18      
STRAND   1101   1104  4      
STRAND   1106   1108  3      
HELIX   1115   1128  14      
Sequence information
Length: 1130 AA [This is the length of the unprocessed precursor] Molecular weight: 122873 Da [This is the MW of the unprocessed precursor] CRC64: 85FE6C1C0E483EA2 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MLEICLKLVG CKSKKGLSSS SSCYLEEALQ RPVASDFEPQ GLSEAARWNS KENLLAGPSE 

        70         80         90        100        110        120 
NDPNLFVALY DFVASGDNTL SITKGEKLRV LGYNHNGEWC EAQTKNGQGW VPSNYITPVN 

       130        140        150        160        170        180 
SLEKHSWYHG PVSRNAAEYL LSSGINGSFL VRESESSPGQ RSISLRYEGR VYHYRINTAS 

       190        200        210        220        230        240 
DGKLYVSSES RFNTLAELVH HHSTVADGLI TTLHYPAPKR NKPTVYGVSP NYDKWEMERT 

       250        260        270        280        290        300 
DITMKHKLGG GQYGEVYEGV WKKYSLTVAV KTLKEDTMEV EEFLKEAAVM KEIKHPNLVQ 

       310        320        330        340        350        360 
LLGVCTREPP FYIITEFMTY GNLLDYLREC NRQEVNAVVL LYMATQISSA MEYLEKKNFI 

       370        380        390        400        410        420 
HRDLAARNCL VGENHLVKVA DFGLSRLMTG DTYTAHAGAK FPIKWTAPES LAYNKFSIKS 

       430        440        450        460        470        480 
DVWAFGVLLW EIATYGMSPY PGIDLSQVYE LLEKDYRMER PEGCPEKVYE LMRACWQWNP 

       490        500        510        520        530        540 
SDRPSFAEIH QAFETMFQES SISDEVEKEL GKQGVRGAVS TLLQAPELPT KTRTSRRAAE 

       550        560        570        580        590        600 
HRDTTDVPEM PHSKGQGESD PLDHEPAVSP LLPRKERGPP EGGLNEDERL LPKDKKTNLF 

       610        620        630        640        650        660 
SALIKKKKKT APTPPKRSSS FREMDGQPER RGAGEEEGRD ISNGALAFTP LDTADPAKSP 

       670        680        690        700        710        720 
KPSNGAGVPN GALRESGGSG FRSPHLWKKS STLTSSRLAT GEEEGGGSSS KRFLRSCSAS 

       730        740        750        760        770        780 
CVPHGAKDTE WRSVTLPRDL QSTGRQFDSS TFGGHKSEKP ALPRKRAGEN RSDQVTRGTV 

       790        800        810        820        830        840 
TPPPRLVKKN EEAADEVFKD IMESSPGSSP PNLTPKPLRR QVTVAPASGL PHKEEAGKGS 

       850        860        870        880        890        900 
ALGTPAAAEP VTPTSKAGSG APGGTSKGPA EESRVRRHKH SSESPGRDKG KLSRLKPAPP 

       910        920        930        940        950        960 
PPPAASAGKA GGKPSQSPSQ EAAGEAVLGA KTKATSLVDA VNSDAAKPSQ PGEGLKKPVL 

       970        980        990       1000       1010       1020 
PATPKPQSAK PSGTPISPAP VPSTLPSASS ALAGDQPSST AFIPLISTRV SLRKTRQPPE 

      1030       1040       1050       1060       1070       1080 
RIASGAITKG VVLDSTEALC LAISRNSEQM ASHSAVLEAG KNLYTFCVSY VDSIQQMRNK 

      1090       1100       1110       1120       1130 
FAFREAINKL ENNLRELQIC PATAGSGPAA TQDFSKLLSS VKEISDIVQR
P00519 in FASTA format

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