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P31748 (AKT_MLVAT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 84. 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:
AKT kinase-transforming protein

EC=2.7.11.1
Gene names
Name:V-AKT
OrganismAKT8 murine leukemia virus
Taxonomic identifier11790 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
Virus hostMus musculus (Mouse) [TaxID: 10090]

Protein attributes

Sequence length501 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Interacts with mouse THEM4. Ref.2

Domain

The AGC-kinase C-terminal mediates interaction with THEM4.

Post-translational modification

Autophosphorylated on threonine and serine residues.

Miscellaneous

This protein is synthesized as a Gag-Akt polyprotein.

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 PH domain.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processHost-virus interaction
   DiseaseOncogene
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological_processviral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 501501AKT kinase-transforming protein
PRO_0000085614

Regions

Domain26 – 129104PH
Domain171 – 429259Protein kinase
Domain430 – 50172AGC-kinase C-terminal
Nucleotide binding177 – 1859ATP By similarity

Sites

Active site2951Proton acceptor By similarity
Binding site2001ATP By similarity

Amino acid modifications

Modified residue3471Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
P31748 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 5AEFDE58CD42F773

FASTA50157,870
        10         20         30         40         50         60 
AREETLIIIP GLPLSLGATD TMNDVAIVKE GWLHKRGEYI KTWRPRYFLL KNDGTFIGYK 

        70         80         90        100        110        120 
ERPQDVDQRE SPLNNFSVAQ CQLMKTERPR PNTFIIRCLQ WTTVIERTFH VETPEEREEW 

       130        140        150        160        170        180 
ATAIQTVADG LKRQEEETMD FRSGSPSDNS GAEEMEVSLA KPKHRVTMNE FEYLKLLGKG 

       190        200        210        220        230        240 
TFGKVILVKE KATGRYYAMK ILKKEVIVAK DEVAHTLTEN RVLQNSRHPF LTALKYSFQT 

       250        260        270        280        290        300 
HDRLCFVMEY ANGGELFFHL SRERVFSEDR ARFYGAEIVS ALDYLHSEKN VVYRDLKLEN 

       310        320        330        340        350        360 
LMLDKDGHIK ITDFGLCKEG IKDGATMKTF CGTPEYLAPE VLEDNDYGRA VDWWGLGVVM 

       370        380        390        400        410        420 
YEMMCGRLPF YNQDHEKLFE LILMEEIRFP RTLGPEAKSL LSGLLKKDPT QRLGGGSEDA 

       430        440        450        460        470        480 
KEIMQHRFFA NIVWQDVYEK KLSPPFKPQV TSETDTRYFD EEFTAQMITI TPPDQDDSME 

       490        500 
CVDSERRPHF PQFSYSASGT A 

« Hide

References

[1]"A retroviral oncogene, akt, encoding a serine-threonine kinase containing an SH2-like region."
Bellacosa A., Testa J.R., Staal S.P., Tsichlis P.N.
Science 254:274-277(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Carboxyl-terminal modulator protein (CTMP), a negative regulator of PKB/Akt and v-Akt at the plasma membrane."
Maira S.-M., Galetic I., Brazil D.P., Kaech S., Ingley E., Thelen M., Hemmings B.A.
Science 294:374-380(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH THEM4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M80675 Genomic DNA. Translation: AAA42545.1.

3D structure databases

ProteinModelPortalP31748.
SMRP31748. Positions 24-142, 165-498.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR011993. PH_like_dom.
IPR017892. Pkinase_C.
IPR001849. Pleckstrin_homology.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
SMARTSM00233. PH. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAKT_MLVAT
AccessionPrimary (citable) accession number: P31748
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: February 19, 2014
This is version 84 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