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UniProtKB/Swiss-Prot entry P00520


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

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Entry information
Entry name ABL1_MOUSE
Primary accession number P00520
Secondary accession numbers P97896 Q61252 Q61253 Q61254 Q61255 Q61256 Q61257 Q61258 Q61259 Q61260 Q61261 Q6PCM5 Q8C1X4
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on February 15, 2005 (Sequence version 3)
Annotations were last modified on    September 2, 2008 (Entry version 123)
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
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM I).
TISSUE=Testis;
PubMed=3317402 [NCBI, ExPASy, EBI, Israel, Japan]
Oppi C., Shore S.K., Reddy E.P.;
"Nucleotide sequence of testis-derived c-abl cDNAs: implications for testis-specific transcription and abl oncogene activation.";
Proc. Natl. Acad. Sci. U.S.A. 84:8200-8204(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I).
STRAIN=ICR;
TISSUE=Embryo;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IV).
STRAIN=C57BL/6;
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-187 (ISOFORMS I; II; III AND IV).
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).
[5]
NUCLEOTIDE SEQUENCE OF 85-182.
DOI=10.1016/0092-8674(84)90228-9; PubMed=6319018 [NCBI, ExPASy, EBI, Israel, Japan]
Wang J.Y.J., Ledley F., Goff S., Lee R., Groner Y., Baltimore D.;
"The mouse c-abl locus: molecular cloning and characterization.";
Cell 36:349-356(1984).
[6]
ALTERNATIVE SPLICING.
PubMed=3283651 [NCBI, ExPASy, EBI, Israel, Japan]
Bernards A., Paskind M., Baltimore D.;
"Four murine c-abl mRNAs arise by usage of two transcriptional promoters and alternative splicing.";
Oncogene 2:297-304(1988).
[7]
FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCALIZATION, PHOSPHORYLATION AT SER-446, AND MUTAGENESIS OF SER-446.
DOI=10.1038/386732a0; PubMed=9109492 [NCBI, ExPASy, EBI, Israel, Japan]
Kharbanda S., Pandey P., Jin S., Inoue S., Bharti A., Yuan Z.-M., Weichselbaum R., Weaver D., Kufe D.;
"Functional interaction between DNA-PK and c-Abl in response to DNA damage.";
Nature 386:732-735(1997).
[8]
SUBCELLULAR LOCALIZATION.
DOI=10.1073/pnas.95.13.7457; PubMed=9636171 [NCBI, ExPASy, EBI, Israel, Japan]
Taagepera S., McDonald D., Loeb J.E., Whitaker L.L., McElroy A.K., Wang J.Y., Hope T.J.;
"Nuclear-cytoplasmic shuttling of C-ABL tyrosine kinase.";
Proc. Natl. Acad. Sci. U.S.A. 95:7457-7462(1998).
[9]
IDENTIFICATION IN A TRIMOLECULAR COMPLEX WITH CDK5 AND CABLES1, AND INTERACTION WITH CABLES1.
TISSUE=Brain;
DOI=10.1016/S0896-6273(00)81200-3; PubMed=10896159 [NCBI, ExPASy, EBI, Israel, Japan]
Zukerberg L.R., Patrick G.N., Nikolic M., Humbert S., Wu C.-L., Lanier L.M., Gertler F.B., Vidal M., Van Etten R.A., Tsai L.-H.;
"Cables links Cdk5 and c-Abl and facilitates Cdk5 tyrosine phosphorylation, kinase upregulation, and neurite outgrowth.";
Neuron 26:633-646(2000).
[10]
INTERACTION WITH PSTPIP1.
DOI=10.1016/S1097-2765(00)00138-6; PubMed=11163214 [NCBI, ExPASy, EBI, Israel, Japan]
Cong F., Spencer S., Cote J.F., Wu Y., Tremblay M.L., Lasky L.A., Goff S.P.;
"Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine phosphatase to the c-Abl kinase to mediate Abl dephosphorylation.";
Mol. Cell 6:1413-1423(2000).
[11]
INTERACTION WITH CRK, AND FUNCTION.
DOI=10.1074/jbc.M100095200; PubMed=11279004 [NCBI, ExPASy, EBI, Israel, Japan]
Kain K.H., Klemke R.L.;
"Inhibition of cell migration by Abl family tyrosine kinases through uncoupling of Crk-CAS complexes.";
J. Biol. Chem. 276:16185-16192(2001).
[12]
INTERACTION WITH ZDHHC16.
DOI=10.1074/jbc.M202388200; PubMed=12021275 [NCBI, ExPASy, EBI, Israel, Japan]
Li B., Cong F., Tan C.P., Wang S.X., Goff S.P.;
"Aph2, a protein with a zf-DHHC motif, interacts with c-Abl and has pro-apoptotic activity.";
J. Biol. Chem. 277:28870-28876(2002).
[13]
FUNCTION, ENZYME REGULATION, INTERACTION WITH CRK, AUTOPHOSPHORYLATION AT TYR-226 AND TYR-393, AND MUTAGENESIS OF TYR-226; LYS-271 AND TYR-393.
DOI=10.1128/MCB.23.11.3884-3896.2003; PubMed=12748290 [NCBI, ExPASy, EBI, Israel, Japan]
Tanis K.Q., Veach D., Duewel H.S., Bornmann W.G., Koleske A.J.;
"Two distinct phosphorylation pathways have additive effects on Abl family kinase activation.";
Mol. Cell. Biol. 23:3884-3896(2003).
[14]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 61-121.
DOI=10.1038/nsb0894-546; PubMed=7664083 [NCBI, ExPASy, EBI, Israel, Japan]
Musacchio A., Saraste M., Wilmanns M.;
"High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides.";
Nat. Struct. Biol. 1:546-551(1994).
[15]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 229-515.
DOI=10.1126/science.289.5486.1938; PubMed=10988075 [NCBI, ExPASy, EBI, Israel, Japan]
Schindler T., Bornmann W., Pellicena P., Miller W.T., Clarkson B., Kuriyan J.;
"Structural mechanism for STI-571 inhibition of abelson tyrosine kinase.";
Science 289:1938-1942(2000).
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
J02995; AAA88241.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK090095; BAC41088.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC059260; AAH59260.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U14721; AAB60451.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U14720; AAB60451.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U14721; AAB60450.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U14720; AAB60450.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U14721; AAB60448.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13835; AAB60448.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U14721; AAB60449.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13835; AAB60449.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X07539; CAA30411.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X07539; CAA30412.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X07540; CAA30413.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X07541; CAA30414.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M12263; AAA37136.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M12264; AAA37137.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M12265; AAA37138.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M12266; AAA37134.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K03228; AAA37135.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A39962; A39962.
S00774; S00774.
RefSeq NP_033724.2; -.
UniGene Mm.1318
3D structure databases
PDB
1ABO; X-ray; 2.00 A; A/B=61-121.[ExPASy / RCSB / EBI]
1ABQ; X-ray; 2.80 A; A=61-121.[ExPASy / RCSB / EBI]
1FPU; X-ray; 2.40 A; A/B=229-515.[ExPASy / RCSB / EBI]
1IEP; X-ray; 2.10 A; A/B=229-515.[ExPASy / RCSB / EBI]
1M52; X-ray; 2.60 A; A/B=229-515.[ExPASy / RCSB / EBI]
1OPJ; X-ray; 1.75 A; A/B=229-515.[ExPASy / RCSB / EBI]
1OPK; X-ray; 1.80 A; A=27-515.[ExPASy / RCSB / EBI]
2HZN; X-ray; 2.70 A; A=229-515.[ExPASy / RCSB / EBI]
2QOH; X-ray; 1.95 A; A/B=229-515.[ExPASy / RCSB / EBI]
2Z60; X-ray; 1.95 A; A=229-515.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1ABO; -.
1ABQ; -.
1FPU; -.
1IEP; -.
1M52; -.
1OPJ; -.
1OPK; -.
2HZN; -.
2QOH; -.
2Z60; -.
SMR P00520; 1017-1123.
ModBase P00520.
Protein-protein interaction databases
IntAct P00520; -.
PTM databases
PhosphoSite P00520; -.
Organism-specific databases
MGI MGI:87859; Abl1.
Gene expression databases
ArrayExpress P00520; -.
CleanEx MM_ABL1; -.
GermOnline ENSMUSG00000026842; Mus musculus.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from UniProtKB).
GO:0005634; Cellular component: nucleus (inferred from direct assay from UniProtKB).
GO:0005524; Molecular function: ATP binding (inferred from direct assay 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:0019904; Molecular function: protein domain specific binding (inferred from physical interaction from MGI).
GO:0004713; Molecular function: protein tyrosine kinase activity (inferred from direct assay from UniProtKB).
GO:0030036; Biological process: actin cytoskeleton organization (inferred from direct assay from UniProtKB).
GO:0018108; Biological process: peptidyl-tyrosine phosphorylation (inferred from direct assay from UniProtKB).
GO:0051726; Biological process: regulation of cell cycle (inferred from direct assay from MGI).
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 P00520.
Genome annotation databases
Ensembl ENSMUSG00000026842; Mus musculus. [Contig view]
GeneID 11350; -.
Phylogenomic databases
HOVERGEN P00520; -.
Other
LinkHub P00520; -.
SOURCE Abl1; Mus musculus.
ProtoNet P00520.
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; Proto-oncogene; SH2 domain; SH3 domain; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1123  1123     Proto-oncogene tyrosine-protein kinase ABL1. PRO_0000088051
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   804   1012  209     Pro-rich. 
COMPBIAS   891    897  7     Poly-Pro. 
ACT_SITE   363    363        Proton acceptor (By similarity). 
BINDING   271    271        ATP. 
MOD_RES   185    185        Phosphotyrosine (By similarity). 
MOD_RES   226    226        Phosphotyrosine (By similarity). 
MOD_RES   253    253        Phosphotyrosine (By similarity). 
MOD_RES   257    257        Phosphotyrosine (By similarity). 
MOD_RES   264    264        Phosphotyrosine (By similarity). 
MOD_RES   393    393        Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases. 
MOD_RES   394    394        Phosphothreonine (By similarity). 
MOD_RES   446    446        Phosphoserine. 
MOD_RES   469    469        Phosphotyrosine (By similarity). 
MOD_RES   569    569        Phosphoserine (By similarity). 
MOD_RES   682    682        Phosphoserine (By similarity). 
MOD_RES   803    803        Phosphoserine (By similarity). 
MOD_RES   807    807        Phosphoserine (By similarity). 
VAR_SEQ   1     26        MLEICLKLVGCKSKKGLSSSSSCYLE -> MISFDLLSDELHLKLLVLDV (in isoform II). VSP_004959
VAR_SEQ   1     26        MLEICLKLVGCKSKKGLSSSSSCYLE -> MSQRWTYTKCRVQRDPALPFM (in isoform III). VSP_004958
VAR_SEQ   1     26        MLEICLKLVGCKSKKGLSSSSSCYLE -> MGQQPGKVLGDQRRPSLPALHFIKGAGKRDSSRHGGPHCN VFVEH (in isoform IV). VSP_004960
MUTAGEN   226    226        Y->F: Minimal reduction in ability to autophosphorylate. 
MUTAGEN   271    271        K->M: Loss of kinase activity. 
MUTAGEN   393    393        Y->F: Minimal reduction in ability to autophosphorylate. 
MUTAGEN   446    446        S->A: No effect on basal activity, but abolishes ionizing radiation-induced activation. 
MUTAGEN   1083   1083        L->A: Loss of nuclear export. 
CONFLICT   184    187        LYVS -> VGDW (in Ref. 4; AAB60451/AAB60450). 
CONFLICT   782    786        PPRLV -> LPGWL (in Ref. 1; AAA88241). 
CONFLICT   987    987        D -> G (in Ref. 2; BAC41088). 
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      
HELIX   141    143  3      
STRAND   148    153  6      
STRAND   155    157  3      
STRAND   161    167  7      
STRAND   170    175  6      
STRAND   184    187  4      
STRAN