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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    November 4, 2008 (Entry version 135)
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), AND ALTERNATIVE SPLICING.
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.
Livingston R.J., Rieder M.J., Shaffer T., Bertucci C., Baier C.N., Rajkumar N., Willa H.T., Daniels M., Downing T.K., Stanaway I.B., Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J., Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
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 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).
[13]
 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).
[14]
 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).
[15]
 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).
[16]
 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).
[17]
 STRUCTURE BY NMR OF SH2 DOMAIN.
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).
[18]
 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).
[19]
 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).
[20]
 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).
[21]
 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).
[22]
 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]
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=64-120.[ExPASy / RCSB / EBI]
1BBZ; X-ray; 1.65 A; A/C/G=64-121, E=65-121.[ExPASy / RCSB / EBI]
1JU5; NMR; -; C=62-121.[ExPASy / RCSB / EBI]
1OPL; X-ray; 3.42 A; A/B=4-512.[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=227-513.[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=228-512.[ExPASy / RCSB / EBI]
2G2F; X-ray; 2.70 A; A=229-512, B=228-512.[ExPASy / RCSB / EBI]
2G2H; X-ray; 2.00 A; A/B=229-512.[ExPASy / RCSB / EBI]
2G2I; X-ray; 3.12 A; A/B=228-512.[ExPASy / RCSB / EBI]
2GQG; X-ray; 2.40 A; A/B=229-500.[ExPASy / RCSB / EBI]
2HIW; X-ray; 2.20 A; A/B=228-512.[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=227-512.[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; -.
PTM databases
PhosphoSite P00519; -.
Polymorphism databases
NIEHS-SNPs ABL1.
Organism-specific databases
H-InvDB HIX0008474; -.
HGNC HGNC:76; ABL1.
GenAtlas ABL1.
HPA CAB002686; -.
MIM 189980; gene. [NCBI / EBI]
608232; phenotype. [NCBI / EBI]
Orphanet 521; Leukaemia, chronic myeloid.
PharmGKB PA24413; -.
GeneCards P00519.
Gene expression databases
ArrayExpress P00519; -.
CleanEx HS_ABL1; -.
GermOnline ENSG00000097007; Homo sapiens.
Ontologies
GO
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:0008022; Molecular function: protein C-terminus binding (inferred from physical interaction from UniProtKB).
GO:0004713; Molecular function: protein tyrosine kinase activity (inferred from direct assay from UniProtKB).
GO:0030036; Biological process: actin cytoskeleton organization (inferred from sequence or structural similarity from UniProtKB).
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_bd.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR000980; SH2.
IPR001452; SH3.
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.
PR00452; SH3DOMAIN.
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).
BLOCKS P00519.
ProtoNet P00519.
Genome annotation databases
Ensembl ENSG00000097007; Homo sapiens. [Contig view]
GeneID 25; -.
KEGG hsa:25; -.
Phylogenomic databases
HOVERGEN P00519; -.
Other
DrugBank DB00171; Adenosine triphosphate.
DB01254; Dasatinib.
DB00619; Imatinib.
LinkHub P00519; -.
NextBio 79; -.
SOURCE ABL1; Homo sapiens.
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