P00521 (ABL_MLVAB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine-protein kinase transforming protein Abl
EC=2.7.10.2

Alternative name(s):
V-abl

Gene names

Name:

ABL

Organism

Abelson murine leukemia virus

Taxonomic identifier

11788 [NCBI]

Taxonomic lineage

Viruses › Retro-transcribing viruses › Retroviridae › Orthoretrovirinae › Gammaretrovirus › unclassified Gammaretrovirus

Virus host

Mus musculus (Mouse) [TaxID: 10090]

Protein attributes

Sequence length	746 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Miscellaneous	This protein is synthesized as a Gag-Abl polyprotein.
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. ABL subfamily. Contains 1 protein kinase domain. Contains 1 SH2 domain.

Ontologies

Keywords
Disease	Oncogene
Domain	SH2 domain
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
Gene Ontology (GO)
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 746	746	Tyrosine-protein kinase transforming protein Abl		PRO_0000088057
Regions
	Domain	13 – 103	91	SH2
	Domain	128 – 379	252	Protein kinase
	Nucleotide binding	134 – 142	9	ATP By similarity
	Nucleotide binding	202 – 208	7	ATP By similarity
	Motif	267 – 291	25	Kinase activation loop By similarity
Sites
	Active site	249	1	Proton acceptor By similarity
	Binding site	157	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	P00521 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: B9072FFF55FE9257	FASTA	746	81,872
	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

References

[1]	"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." Reddy E.P., Smith M.J., Srinivasan A. Proc. Natl. Acad. Sci. U.S.A. 80:3623-3627(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	Erratum Reddy E.P., Smith M.J., Srinivasan A. Proc. Natl. Acad. Sci. U.S.A. 80:7372-7372(1983) Cited for: SEQUENCE REVISION TO 588-746.
[3]	"Homology between phosphotyrosine acceptor site of human c-abl and viral oncogene products." Groffen J., Heisterkamp N., Reynolds F.H. Jr., Stephenson J.R. Nature 304:167-169(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 233-327.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	V01541 Genomic DNA. No translation available. K00010 Genomic RNA. Translation: AAA46470.1.
RefSeq	NP_955595.1. NC_001499.1.
3D structure databases
ProteinModelPortal	P00521.
SMR	P00521. Positions 1-398, 640-746.
ModBase	Search...
Protein-protein interaction databases
IntAct	P00521. 1 interaction.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1491873.
Enzyme and pathway databases
BRENDA	2.7.10.2. 1.
SABIO-RK	P00521.
Family and domain databases
Gene3D	3.30.505.10. 1 hit.
InterPro	IPR015015. F-actin_binding. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR001245. Ser-Thr/Tyr_kinase_cat_dom. IPR000980. SH2. IPR008266. Tyr_kinase_AS. IPR020635. Tyr_kinase_cat_dom. [Graphical view]
Pfam	PF08919. F_actin_bind. 1 hit. PF07714. Pkinase_Tyr. 1 hit. PF00017. SH2. 1 hit. [Graphical view]
PRINTS	PR00401. SH2DOMAIN. PR00109. TYRKINASE.
SMART	SM00808. FABD. 1 hit. SM00252. SH2. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00109. PROTEIN_KINASE_TYR. 1 hit. PS50001. SH2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P00521.
ChEMBL	CHEMBL5166.

Entry information

Entry name

ABL_MLVAB

Accession

Primary (citable) accession number: P00521

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	April 3, 2013
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program