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P31748

- AKT_MLVAT

UniProt

P31748 - AKT_MLVAT

Protein

AKT kinase-transforming protein

Gene

V-AKT

Organism
AKT8 murine leukemia virus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei200 – 2001ATPPROSITE-ProRule annotation
    Active sitei295 – 2951Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi177 – 1859ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein serine/threonine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Host-virus interaction

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    AKT kinase-transforming protein (EC:2.7.11.1)
    Gene namesi
    Name:V-AKT
    OrganismiAKT8 murine leukemia virus
    Taxonomic identifieri11790 [NCBI]
    Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
    Virus hostiMus musculus (Mouse) [TaxID: 10090]

    Pathology & Biotechi

    Keywords - Diseasei

    Oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 501501AKT kinase-transforming proteinPRO_0000085614Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei347 – 3471PhosphotyrosineBy similarity

    Post-translational modificationi

    Autophosphorylated on threonine and serine residues.

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Subunit structurei

    Interacts with mouse THEM4.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliP31748.
    SMRiP31748. Positions 24-142, 165-498.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 129104PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini171 – 429259Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini430 – 50172AGC-kinase C-terminalAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 1 PH domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR017892. Pkinase_C.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00169. PH. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view]
    SMARTiSM00233. PH. 1 hit.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS51285. 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]

    Sequencei

    Sequence statusi: Complete.

    P31748-1 [UniParc]FASTAAdd to Basket

    « Hide

    AREETLIIIP GLPLSLGATD TMNDVAIVKE GWLHKRGEYI KTWRPRYFLL    50
    KNDGTFIGYK ERPQDVDQRE SPLNNFSVAQ CQLMKTERPR PNTFIIRCLQ 100
    WTTVIERTFH VETPEEREEW ATAIQTVADG LKRQEEETMD FRSGSPSDNS 150
    GAEEMEVSLA KPKHRVTMNE FEYLKLLGKG TFGKVILVKE KATGRYYAMK 200
    ILKKEVIVAK DEVAHTLTEN RVLQNSRHPF LTALKYSFQT HDRLCFVMEY 250
    ANGGELFFHL SRERVFSEDR ARFYGAEIVS ALDYLHSEKN VVYRDLKLEN 300
    LMLDKDGHIK ITDFGLCKEG IKDGATMKTF CGTPEYLAPE VLEDNDYGRA 350
    VDWWGLGVVM YEMMCGRLPF YNQDHEKLFE LILMEEIRFP RTLGPEAKSL 400
    LSGLLKKDPT QRLGGGSEDA KEIMQHRFFA NIVWQDVYEK KLSPPFKPQV 450
    TSETDTRYFD EEFTAQMITI TPPDQDDSME CVDSERRPHF PQFSYSASGT 500
    A 501
    Length:501
    Mass (Da):57,870
    Last modified:July 1, 1993 - v1
    Checksum:i5AEFDE58CD42F773
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M80675 Genomic DNA. Translation: AAA42545.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M80675 Genomic DNA. Translation: AAA42545.1 .

    3D structure databases

    ProteinModelPortali P31748.
    SMRi P31748. Positions 24-142, 165-498.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR017892. Pkinase_C.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00169. PH. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view ]
    SMARTi SM00233. PH. 1 hit.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS51285. 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 ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiAKT_MLVAT
    AccessioniPrimary (citable) accession number: P31748
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 86 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    This protein is synthesized as a Gag-Akt polyprotein.

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3