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B1AKP8

- B1AKP8_HUMAN

UniProt

B1AKP8 - B1AKP8_HUMAN

Protein
Submitted name:

Serine/threonine-protein kinase mTOR

Gene

MTOR

Organism
Homo sapiens (Human)
Status
Unreviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 52 (01 Oct 2014)
      Sequence version 1 (08 Apr 2008)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. drug binding Source: InterPro
    3. protein serine/threonine kinase activity Source: Ensembl
    4. ribosome binding Source: Ensembl

    GO - Biological processi

    1. cellular response to hypoxia Source: Ensembl
    2. cellular response to nutrient levels Source: Ensembl
    3. germ cell development Source: Ensembl
    4. negative regulation of cell size Source: Ensembl
    5. negative regulation of macroautophagy Source: Ensembl
    6. negative regulation of NFAT protein import into nucleus Source: Ensembl
    7. peptidyl-serine phosphorylation Source: Ensembl
    8. peptidyl-threonine phosphorylation Source: Ensembl
    9. positive regulation of actin filament polymerization Source: Ensembl
    10. positive regulation of endothelial cell proliferation Source: Ensembl
    11. positive regulation of lamellipodium assembly Source: Ensembl
    12. positive regulation of myotube differentiation Source: Ensembl
    13. positive regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
    14. positive regulation of protein kinase B signaling Source: Ensembl
    15. positive regulation of stress fiber assembly Source: Ensembl
    16. positive regulation of translation Source: Ensembl
    17. protein autophosphorylation Source: Ensembl
    18. regulation of carbohydrate utilization Source: Ensembl
    19. regulation of fatty acid beta-oxidation Source: Ensembl
    20. regulation of glycogen biosynthetic process Source: Ensembl
    21. regulation of protein kinase activity Source: Ensembl
    22. regulation of Rac GTPase activity Source: Ensembl
    23. regulation of response to food Source: Ensembl
    24. response to amino acid Source: Ensembl
    25. response to insulin Source: Ensembl
    26. ruffle organization Source: Ensembl

    Keywords - Molecular functioni

    KinaseSAAS annotation, Transferase

    Keywords - Ligandi

    ATP-bindingSAAS annotation, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Submitted name:
    Serine/threonine-protein kinase mTORImported
    Gene namesi
    Name:MTORImported
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3942. MTOR.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. PML body Source: Ensembl
    3. TORC1 complex Source: Ensembl

    PTM / Processingi

    Proteomic databases

    PRIDEiB1AKP8.

    Expressioni

    Gene expression databases

    ArrayExpressiB1AKP8.

    Structurei

    3D structure databases

    ProteinModelPortaliB1AKP8.
    SMRiB1AKP8. Positions 230-319, 722-754.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Contains FAT domain.SAAS annotation
    Contains FATC domain.SAAS annotation
    Contains PI3K/PI4K domain.SAAS annotation

    Phylogenomic databases

    HOGENOMiHOG000049044.
    HOVERGENiHBG102007.
    OrthoDBiEOG7CCBQ4.

    Family and domain databases

    Gene3Di1.10.1070.11. 3 hits.
    1.20.120.150. 1 hit.
    InterProiIPR003152. FATC.
    IPR011009. Kinase-like_dom.
    IPR000403. PI3/4_kinase_cat_dom.
    IPR018936. PI3/4_kinase_CS.
    IPR003151. PIK-rel_kinase_FAT.
    IPR014009. PIK_FAT.
    IPR009076. Rapamycin-bd_dom.
    [Graphical view]
    PfamiPF02259. FAT. 1 hit.
    PF02260. FATC. 1 hit.
    PF00454. PI3_PI4_kinase. 1 hit.
    PF08771. Rapamycin_bind. 1 hit.
    [Graphical view]
    SMARTiSM00146. PI3Kc. 1 hit.
    [Graphical view]
    SUPFAMiSSF47212. SSF47212. 1 hit.
    SSF56112. SSF56112. 2 hits.
    PROSITEiPS51189. FAT. 1 hit.
    PS51190. FATC. 1 hit.
    PS00915. PI3_4_KINASE_1. 1 hit.
    PS00916. PI3_4_KINASE_2. 1 hit.
    PS50290. PI3_4_KINASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    B1AKP8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNFEAVLHYK HQNQARDEKK KLRHASGANI TNATTAATTA ATATTTASTE    50
    GSNSESEAES TENSPTPSPL QKKVTEDLSK TLLMYTVPAV QGFFRSISLS 100
    RGNNLQDTLR VLTLWFDYGH WPDVNEALVE GVKAIQIDTW LQVIPQLIAR 150
    IDTPRPLVGR LIHQLLTDIG RYHPQALIYP LTVASKSTTT ARHNAANKIL 200
    KNMCEHSNTL VQQAMMVSEE LIRVAILWHE MWHEGLEEAS RLYFGERNVK 250
    GMFEVLEPLH AMMERGPQTL KETSFNQAYG RDLMEAQEWC RKYMKSGNVK 300
    DLTQAWDLYY HVFRRISKQL PQLTSLELQY VSPKLLMCRD LELAVPGTYD 350
    PNQPIIRIQS IAPSLQVITS KQRPRKLTLM GSNGHEFVFL LKGHEDLRQD 400
    ERVMQLFGLV NTLLANDPTS LRKNLSIQRY AVIPLSTNSG LIGWVPHCDT 450
    LHALIRDYRE KKKILLNIEH RIMLRMAPDY DHLTLMQKVE VFEHAVNNTA 500
    GDDLAKLLWL KSPSSEVWFD RRTNYTRSLA VMSMVGYILG LGDRHPSNLM 550
    LDRLSGKILH IDFGDCFEVA MTREKFPEKI PFRLTRMLTN AMEVTGLDGN 600
    YRITCHTVME VLREHKDSVM AVLEAFVYDP LLNWRLMDTN TKGNKRSRTR 650
    TDSYSAGQSV EILDGVELGE PAHKKTGTTV PESIHSFIGD GLVKPEALNK 700
    KAIQIINRVR DKLTGRDFSH DDTLDVPTQV ELLIKQATSH ENLCQCYIGW 750
    CPFW 754
    Length:754
    Mass (Da):85,901
    Last modified:April 8, 2008 - v1
    Checksum:i0AC837B2544A1CEA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL049653 Genomic DNA. No translation available.
    AL109811 Genomic DNA. No translation available.
    AL391561 Genomic DNA. No translation available.
    KF495866 Genomic DNA. No translation available.

    Genome annotation databases

    EnsembliENST00000376838; ENSP00000366034; ENSG00000198793.
    UCSCiuc001asc.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL049653 Genomic DNA. No translation available.
    AL109811 Genomic DNA. No translation available.
    AL391561 Genomic DNA. No translation available.
    KF495866 Genomic DNA. No translation available.

    3D structure databases

    ProteinModelPortali B1AKP8.
    SMRi B1AKP8. Positions 230-319, 722-754.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi B1AKP8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000376838 ; ENSP00000366034 ; ENSG00000198793 .
    UCSCi uc001asc.3. human.

    Organism-specific databases

    HGNCi HGNC:3942. MTOR.
    GenAtlasi Search...

    Phylogenomic databases

    HOGENOMi HOG000049044.
    HOVERGENi HBG102007.
    OrthoDBi EOG7CCBQ4.

    Miscellaneous databases

    ChiTaRSi MTOR. human.
    NextBioi 35466581.

    Gene expression databases

    ArrayExpressi B1AKP8.

    Family and domain databases

    Gene3Di 1.10.1070.11. 3 hits.
    1.20.120.150. 1 hit.
    InterProi IPR003152. FATC.
    IPR011009. Kinase-like_dom.
    IPR000403. PI3/4_kinase_cat_dom.
    IPR018936. PI3/4_kinase_CS.
    IPR003151. PIK-rel_kinase_FAT.
    IPR014009. PIK_FAT.
    IPR009076. Rapamycin-bd_dom.
    [Graphical view ]
    Pfami PF02259. FAT. 1 hit.
    PF02260. FATC. 1 hit.
    PF00454. PI3_PI4_kinase. 1 hit.
    PF08771. Rapamycin_bind. 1 hit.
    [Graphical view ]
    SMARTi SM00146. PI3Kc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47212. SSF47212. 1 hit.
    SSF56112. SSF56112. 2 hits.
    PROSITEi PS51189. FAT. 1 hit.
    PS51190. FATC. 1 hit.
    PS00915. PI3_4_KINASE_1. 1 hit.
    PS00916. PI3_4_KINASE_2. 1 hit.
    PS50290. PI3_4_KINASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S., McLaren S., Milne S., Mistry S., Moore M.J., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R., Banerjee R., Bryant S.P., Burford D.C., Burrill W.D., Clegg S.M., Dhami P., Dovey O., Faulkner L.M., Gribble S.M., Langford C.F., Pandian R.D., Porter K.M., Prigmore E.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. Ensembl
      Submitted (FEB-2012) to UniProtKB
      Cited for: IDENTIFICATION.

    Entry informationi

    Entry nameiB1AKP8_HUMAN
    AccessioniPrimary (citable) accession number: B1AKP8
    Entry historyi
    Integrated into UniProtKB/TrEMBL: April 8, 2008
    Last sequence update: April 8, 2008
    Last modified: October 1, 2014
    This is version 52 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.

    Miscellaneousi

    Caution

    The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

    Keywords - Technical termi

    Complete proteome, Reference proteomeImported

    External Data

    Dasty 3