Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

B0LPE5

- B0LPE5_HUMAN

UniProt

B0LPE5 - B0LPE5_HUMAN

Protein
Submitted name:

V-akt murine thymoma viral oncogene homolog 1

Gene

AKT1

Organism
Homo sapiens (Human)
Status
Unreviewed - Annotation score: 5 out of 5- Protein predictedi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 1 (18 Mar 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.SAAS annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. aging Source: Ensembl
    2. anagen Source: Ensembl
    3. apoptotic mitochondrial changes Source: Ensembl
    4. cell projection organization Source: Ensembl
    5. cellular response to epidermal growth factor stimulus Source: Ensembl
    6. cellular response to hypoxia Source: Ensembl
    7. cellular response to insulin stimulus Source: Ensembl
    8. cellular response to mechanical stimulus Source: Ensembl
    9. execution phase of apoptosis Source: Ensembl
    10. germ cell development Source: Ensembl
    11. glucose homeostasis Source: Ensembl
    12. glucose metabolic process Source: Ensembl
    13. glucose transport Source: Ensembl
    14. glycogen biosynthetic process Source: Ensembl
    15. glycogen cell differentiation involved in embryonic placenta development Source: Ensembl
    16. hyaluronan metabolic process Source: Ensembl
    17. inflammatory response Source: Ensembl
    18. labyrinthine layer blood vessel development Source: Ensembl
    19. maternal placenta development Source: Ensembl
    20. negative regulation of apoptotic process Source: Ensembl
    21. negative regulation of cell size Source: Ensembl
    22. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
    23. negative regulation of JNK cascade Source: Ensembl
    24. negative regulation of protein kinase activity Source: Ensembl
    25. negative regulation of release of cytochrome c from mitochondria Source: Ensembl
    26. osteoblast differentiation Source: Ensembl
    27. peptidyl-serine phosphorylation Source: Ensembl
    28. peripheral nervous system myelin maintenance Source: Ensembl
    29. positive regulation of apoptotic process Source: Ensembl
    30. positive regulation of cell growth Source: Ensembl
    31. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
    32. positive regulation of sodium ion transport Source: Ensembl
    33. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    34. positive regulation of vasoconstriction Source: Ensembl
    35. protein catabolic process Source: Ensembl
    36. protein kinase B signaling Source: Ensembl
    37. protein ubiquitination Source: Ensembl
    38. regulation of cell migration Source: Ensembl
    39. regulation of neuron projection development Source: Ensembl
    40. regulation of protein localization Source: Ensembl
    41. response to food Source: Ensembl
    42. striated muscle cell differentiation Source: Ensembl
    43. translation Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinaseSAAS annotation, Transferase

    Keywords - Ligandi

    ATP-bindingUniRule annotationSAAS annotation, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Submitted name:
    V-akt murine thymoma viral oncogene homolog 1Imported
    Submitted name:
    V-akt murine thymoma viral oncogene homolog 1, isoform CRA_aImported
    Gene namesi
    Name:AKT1Imported
    ORF Names:hCG_96740Imported
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. microtubule cytoskeleton Source: HPA
    3. nucleus Source: HPA
    4. spindle Source: Ensembl

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24684.

    Structurei

    3D structure databases

    SMRiB0LPE5. Positions 1-477.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Contains 1 PH domain.UniRule annotation
    Contains AGC-kinase C-terminal domain.SAAS annotation
    Contains PH domain.SAAS annotation

    Phylogenomic databases

    HOVERGENiHBG108317.
    KOiK04456.
    OMAiSRERVFP.
    PhylomeDBiB0LPE5.

    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.

    B0LPE5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDVAIVKEG WLHKRGEYIK TWRPRYFLLK NDGTFIGYKE RPQDVDQREA    50
    PLNNFSVAQC QLMKTERPRP NTFIIRCLQW TTVIERTFHV ETPEEREEWT 100
    TAIQTVADGL KKQEEEEMDF RSGSPSDNSG AEEMEVSLAK PKHRVTMNEF 150
    EYLKLLGKGT FGKVILVKEK ATGRYYAMKI LKKEVIVAKD EVAHTLTENR 200
    VLQNSRHPFL TALKYSFQTH DRLCFVMEYA NGGELFFHLS RERVFSEDRA 250
    RFYGAEIVSA LDYLHSEKNV VYRDLKLENL MLDKDGHIKI TDFGLCKEGI 300
    KDGATMKTFC GTPEYLAPEV LEDNDYGRAV DWWGLGVVMY EMMCGRLPFY 350
    NQDHEKLFEL ILMEEIRFPR TLGPEAKSLL SGLLKKDPKQ RLGGGSEDAK 400
    EIMQHRFFAG IVWQHVYEKK LSPPFKPQVT SETDTRYFDE EFTAQMITIT 450
    PPDQDDSMEC VDSERRPHFP QFSYSASGTA 480
    Length:480
    Mass (Da):55,686
    Last modified:March 18, 2008 - v1
    Checksum:i6EAFF4F8AD436714
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EU332835 Genomic DNA. Translation: ABY87524.1.
    JX512440 Genomic DNA. Translation: AGC09587.1.
    CH471061 Genomic DNA. Translation: EAW81881.1.
    CH471061 Genomic DNA. Translation: EAW81882.1.
    CH471061 Genomic DNA. Translation: EAW81883.1.
    RefSeqiNP_001014431.1. NM_001014431.1.
    NP_001014432.1. NM_001014432.1.
    NP_005154.2. NM_005163.2.
    XP_005267458.1. XM_005267401.1.
    UniGeneiHs.525622.

    Genome annotation databases

    GeneIDi207.
    KEGGihsa:207.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EU332835 Genomic DNA. Translation: ABY87524.1 .
    JX512440 Genomic DNA. Translation: AGC09587.1 .
    CH471061 Genomic DNA. Translation: EAW81881.1 .
    CH471061 Genomic DNA. Translation: EAW81882.1 .
    CH471061 Genomic DNA. Translation: EAW81883.1 .
    RefSeqi NP_001014431.1. NM_001014431.1.
    NP_001014432.1. NM_001014432.1.
    NP_005154.2. NM_005163.2.
    XP_005267458.1. XM_005267401.1.
    UniGenei Hs.525622.

    3D structure databases

    SMRi B0LPE5. Positions 1-477.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    DNASUi 207.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 207.
    KEGGi hsa:207.

    Organism-specific databases

    CTDi 207.
    PharmGKBi PA24684.

    Phylogenomic databases

    HOVERGENi HBG108317.
    KOi K04456.
    OMAi SRERVFP.
    PhylomeDBi B0LPE5.

    Miscellaneous databases

    ChiTaRSi AKT1. human.
    GenomeRNAii 207.
    NextBioi 828.

    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. "The sequence of the human genome."
      Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.
      , Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R., Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D., McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B., Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.
      Science 291:1304-1351(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
    2. Cited for: NUCLEOTIDE SEQUENCE.
    3. Rieder M.J., Johanson E.J., da Ponte S.H., Hastings N.C., Ahearn M.O., Bertucci C.B., Wong M.W., Yi Q., Nickerson D.A.
      Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
    4. Cited for: NUCLEOTIDE SEQUENCE.

    Entry informationi

    Entry nameiB0LPE5_HUMAN
    AccessioniPrimary (citable) accession number: B0LPE5
    Entry historyi
    Integrated into UniProtKB/TrEMBL: March 18, 2008
    Last sequence update: March 18, 2008
    Last modified: October 1, 2014
    This is version 65 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.