[1]	NUCLEOTIDE SEQUENCE. PubMed=6304726 [NCBI, ExPASy, EBI, Israel, Japan] Reddy E.P., Smith M.J., Srinivasan A.; "Nucleotide sequence of Abelson murine leukemia virus genome: structural similarity of its transforming gene product to other onc gene products with tyrosine-specific kinase activity."; Proc. Natl. Acad. Sci. U.S.A. 80:3623-3627(1983).
[2]	ERRATUM, AND SEQUENCE REVISION TO 588-746. Reddy E.P., Smith M.J., Srinivasan A.; Proc. Natl. Acad. Sci. U.S.A. 80:7372-7372(1983).
[3]	NUCLEOTIDE SEQUENCE OF 233-327. 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).

Comments

CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
INTERACTION:
O75896:TUSC2 (xeno); NbExp=1; IntAct=EBI-1550592, EBI-1052725;
MISCELLANEOUS: This protein is synthesized as a Gag-Abl polyprotein.
SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. ABL subfamily.
SIMILARITY: Contains 1 protein kinase domain.
SIMILARITY: Contains 1 SH2 domain.

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

V01541; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
K00010; AAA46470.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_955595.1; -.

3D structure databases

HSSP

Q61258; 1OPJ. [HSSP ENTRY / PDB]

SMR

P00521; 1-398, 640-746.

ModBase

P00521.

Protein-protein interaction databases

IntAct

P00521; -.

Ontologies

GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.

Family and domain databases

InterPro

IPR015015; F_actin_bd.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR000980; SH2.
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.
Pfam graphical view of domain structure.

PRINTS

PR00401; SH2DOMAIN.
PR00109; TYRKINASE.

ProDom

PD000001; Prot_kinase; 1.
PD000093; SH2; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00808; FABD; 1.
SM00252; SH2; 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.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

1491873; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Kinase; Nucleotide-binding; Oncogene; SH2 domain; Transferase; Tyrosine-protein kinase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 746`	`746`	`Tyrosine-protein kinase transforming protein Abl.`	`PRO_0000088057`
`DOMAIN`	`13 103`	`91`	`SH2.`
`DOMAIN`	`128 379`	`252`	`Protein kinase.`
`NP_BIND`	`134 142`	`9`	`ATP (By similarity).`
`ACT_SITE`	`249 249`		`Proton acceptor (By similarity).`
`BINDING`	`157 157`		`ATP (By similarity).`

Sequence information

Length: 746 AA [This is the length of the unprocessed precursor]

Molecular weight: 81872 Da [This is the MW of the unprocessed precursor]

CRC64: B9072FFF55FE9257 [This is a checksum on the sequence]

        10         20         30         40         50         60 
YITPVNSLEK HSWYHGPVSR NAAEYLLSSG INGSFLVRES ESSPGQRSIS LRYEGRVYHY 

        70         80         90        100        110        120 
RINTASDGKL YVSSESRFNT LAELVHHHST VADGLITTLH YPAPKRNKPT IYGVSPNYDK 

       130        140        150        160        170        180 
WEMERTDITM KHKLGGGQYG EVYEGVWKKY SLTVAVKTLK EDTMEVEEFL KEAAVMKEIK 

       190        200        210        220        230        240 
HPNLVQLLGV CTREPPFYII TEFMTYGNLL DYLRECNRQE VSAVVLLYMA TQISSAMEYL 

       250        260        270        280        290        300 
EKKNFIHRDL AARNCLVGEN HLVKVADFGL SRLMTGDTYT AHAGAKFPIK WTAPESLAYN 

       310        320        330        340        350        360 
KFSIKSDVWA FGVLLWEIAT YGMSPYPGID LSQVYELLEK DYRMERPEGC PEKVYELMRA 

       370        380        390        400        410        420 
CWQWNPSDRP SFAEIHQAFE TMFQESSISD EVEKELGKRG TRGGAGSMLQ APELPTKTRT 

       430        440        450        460        470        480 
CRRAAEQKAS PPSLTPKLLR RQVTASPSSG LSHKKEATKG SASGMGTPAT AEPAPPSNKV 

       490        500        510        520        530        540 
GLSKASSEEM RVRRHKHSSE SPGRDKGRLA KLKPAPPPPP ACTGKAGKPA QSPSQEAGEA 

       550        560        570        580        590        600 
GGPTKTKCTS LAMDAVNTDP TKAGPPGEGL RKPVPPSVPK PQSTAKPPGT PTSPVSTPST 

       610        620        630        640        650        660 
APAPSPLAGD QQPSSAAFIP LISTRVSLRK TRQPPERIAS GTITKGVVLD STEALCLAIS 

       670        680        690        700        710        720 
RNSEQMASHS AVLEAGKNLY TFCVSYVDSI QQMRNKFAFR EAINKLESNL RELQICPATA 

       730        740 
SSGPAATQDF SKLLSSVKEI SDIVRR

P00521 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools