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P00521 (ABL_MLVAB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase transforming protein Abl

EC=2.7.10.2
Alternative name(s):
V-abl
Gene names
Name:ABL
OrganismAbelson murine leukemia virus
Taxonomic identifier11788 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusunclassified Gammaretrovirus
Virus hostMus musculus (Mouse) [TaxID: 10090]

Protein attributes

Sequence length746 AA.
Sequence statusComplete.
Protein existenceInferred 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 746746Tyrosine-protein kinase transforming protein Abl
PRO_0000088057

Regions

Domain13 – 10391SH2
Domain128 – 379252Protein kinase
Nucleotide binding134 – 1429ATP By similarity
Nucleotide binding202 – 2087ATP By similarity
Motif267 – 29125Kinase activation loop By similarity

Sites

Active site2491Proton acceptor By similarity
Binding site1571ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P00521 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: B9072FFF55FE9257

FASTA74681,872
        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 

« Hide

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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01541 Genomic DNA. No translation available.
K00010 Genomic RNA. Translation: AAA46470.1.

3D structure databases

ProteinModelPortalP00521.
SMRP00521. Positions 1-398, 640-746.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP00521. 1 interaction.

Chemistry

BindingDBP00521.
ChEMBLCHEMBL5166.

Proteomic databases

PRIDEP00521.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA2.7.10.2. 1.
SABIO-RKP00521.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR015015. F-actin_binding.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_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]
PfamPF08919. F_actin_bind. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTSM00808. FABD. 1 hit.
SM00252. SH2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameABL_MLVAB
AccessionPrimary (citable) accession number: P00521
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families