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Q96B36

- AKTS1_HUMAN

UniProt

Q96B36 - AKTS1_HUMAN

Protein

Proline-rich AKT1 substrate 1

Gene

AKT1S1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    Subunit of mTORC1, which regulates cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino acids. Growth factor-stimulated mTORC1 activation involves a AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Within mTORC1, AKT1S1 negatively regulates mTOR activity in a manner that is dependent on its phosphorylation state and binding to 14-3-3 proteins. Inhibits RHEB-GTP-dependent mTORC1 activation. Substrate for AKT1 phosphorylation, but can also be activated by AKT1-independent mechanisms. May also play a role in nerve growth factor-mediated neuroprotection.3 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. epidermal growth factor receptor signaling pathway Source: Reactome
    2. Fc-epsilon receptor signaling pathway Source: Reactome
    3. fibroblast growth factor receptor signaling pathway Source: Reactome
    4. innate immune response Source: Reactome
    5. negative regulation of cell size Source: UniProtKB
    6. negative regulation of protein kinase activity Source: UniProtKB
    7. negative regulation of TOR signaling Source: UniProtKB
    8. neurotrophin TRK receptor signaling pathway Source: Reactome
    9. phosphatidylinositol-mediated signaling Source: Reactome
    10. regulation of neuron apoptotic process Source: UniProtKB

    Enzyme and pathway databases

    ReactomeiREACT_12564. AKT phosphorylates targets in the cytosol.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_200775. HSF1-dependent transactivation.
    SignaLinkiQ96B36.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proline-rich AKT1 substrate 1
    Alternative name(s):
    40 kDa proline-rich AKT substrate
    Gene namesi
    Name:AKT1S1Imported
    Synonyms:PRAS402 Publications
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:28426. AKT1S1.

    Subcellular locationi

    Cytoplasmcytosol By similarity
    Note: Found in the cytosolic fraction of the brain.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: UniProtKB
    3. nucleus Source: Ensembl
    4. protein complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi246 – 2461T → A: Suppresses S6K1 phosphorylation by mTORC1. 1 Publication

    Organism-specific databases

    PharmGKBiPA134943587.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 256256Proline-rich AKT1 substrate 1PRO_0000253446Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei88 – 881Phosphoserine3 Publications
    Modified residuei92 – 921Phosphoserine3 Publications
    Modified residuei183 – 1831Phosphoserine5 Publications
    Modified residuei202 – 2021Phosphoserine3 Publications
    Modified residuei203 – 2031Phosphoserine2 Publications
    Modified residuei211 – 2111Phosphoserine3 Publications
    Modified residuei212 – 2121Phosphoserine3 Publications
    Modified residuei246 – 2461Phosphothreonine; by PKB/AKT15 Publications

    Post-translational modificationi

    Phosphorylated by AKT1. Phosphorylation relieves inhibitory function on mTORC1.6 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ96B36.
    PaxDbiQ96B36.
    PRIDEiQ96B36.

    PTM databases

    PhosphoSiteiQ96B36.

    Expressioni

    Tissue specificityi

    Widely expressed with highest levels of expression in liver and heart. Expressed at higher levels in cancer cell lines (e.g. A-549 and HeLa) than in normal cell lines (e.g. HEK293).2 Publications

    Gene expression databases

    ArrayExpressiQ96B36.
    BgeeiQ96B36.
    CleanExiHS_AKT1S1.
    GenevestigatoriQ96B36.

    Organism-specific databases

    HPAiCAB021903.
    HPA043590.

    Interactioni

    Subunit structurei

    Part of the mammalian target of rapamycin complex 1 (mTORC1) which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR. mTORC1 binds to and is inhibited by FKBP12-rapamycin. Interacts directly with RPTOR. The phosphorylated form interacts with 14-3-3 proteins.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BMH1P293113EBI-720593,EBI-3661From a different organism.
    YWHAHQ049173EBI-720593,EBI-306940

    Protein-protein interaction databases

    BioGridi124059. 10 interactions.
    IntActiQ96B36. 11 interactions.
    MINTiMINT-3317903.
    STRINGi9606.ENSP00000341698.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96B36.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi35 – 439Poly-ProSequence Analysis
    Compositional biasi77 – 9620Pro-richSequence AnalysisAdd
    BLAST

    Phylogenomic databases

    eggNOGiNOG40718.
    HOVERGENiHBG059465.
    InParanoidiQ96B36.
    KOiK16184.
    OMAiCLHDIAQ.
    OrthoDBiEOG7X3QRW.
    PhylomeDBiQ96B36.

    Family and domain databases

    InterProiIPR026682. AKT1S1.
    [Graphical view]
    PANTHERiPTHR21844. PTHR21844. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 12 Publications (identifier: Q96B36-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MASGRPEELW EAVVGAAERF RARTGTELVL LTAAPPPPPR PGPCAYAAHG    50
    RGALAEAARR CLHDIALAHR AATAARPPAP PPAPQPPSPT PSPPRPTLAR 100
    EDNEEDEDEP TETETSGEQL GISDNGGLFV MDEDATLQDL PPFCESDPES 150
    TDDGSLSEET PAGPPTCSVP PASALPTQQY AKSLPVSVPV WGFKEKRTEA 200
    RSSDEENGPP SSPDLDRIAA SMRALVLREA EDTQVFGDLP RPRLNTSDFQ 250
    KLKRKY 256
    Length:256
    Mass (Da):27,383
    Last modified:December 1, 2001 - v1
    Checksum:iF6CB195CBB54326C
    GO
    Isoform 21 Publication (identifier: Q96B36-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-130: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:126
    Mass (Da):13,807
    Checksum:i2E34744BBEFEC1E9
    GO
    Isoform 3 (identifier: Q96B36-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MSFEGGDGAGPAMLATGTARM

    Note: No experimental confirmation available.

    Show »
    Length:276
    Mass (Da):29,262
    Checksum:i3866EE718A29CC48
    GO

    Sequence cautioni

    The sequence AAH00031.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti108 – 1081D → G in BAB70937. (PubMed:14702039)Curated
    Sequence conflicti196 – 1961K → M in BAB70937. (PubMed:14702039)Curated
    Sequence conflicti233 – 2331T → A in BAB70937. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti47 – 471A → P.1 Publication
    Corresponds to variant rs17850191 [ dbSNP | Ensembl ].
    VAR_028239

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 130130Missing in isoform 2. 1 PublicationVSP_052182Add
    BLAST
    Alternative sequencei1 – 11M → MSFEGGDGAGPAMLATGTAR M in isoform 3. 1 PublicationVSP_047536

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK055511 mRNA. Translation: BAB70937.1.
    AK092610 mRNA. Translation: BAG52583.1.
    AK316603 mRNA. Translation: BAG38190.1.
    AK226004 mRNA. No translation available.
    AC118341 Genomic DNA. No translation available.
    CH471177 Genomic DNA. Translation: EAW52570.1.
    CH471177 Genomic DNA. Translation: EAW52568.1.
    BC000031 mRNA. Translation: AAH00031.2. Different initiation.
    BC007416 mRNA. Translation: AAH07416.1.
    BC015562 mRNA. Translation: AAH15562.1.
    BC016043 mRNA. Translation: AAH16043.1.
    BC051844 mRNA. Translation: AAH51844.1.
    CCDSiCCDS12784.1. [Q96B36-1]
    CCDS59410.1. [Q96B36-3]
    RefSeqiNP_001092102.1. NM_001098632.2. [Q96B36-1]
    NP_001092103.1. NM_001098633.3. [Q96B36-1]
    NP_001265088.1. NM_001278159.1. [Q96B36-1]
    NP_001265089.1. NM_001278160.1. [Q96B36-1]
    NP_115751.3. NM_032375.5. [Q96B36-3]
    UniGeneiHs.515542.
    Hs.610819.

    Genome annotation databases

    EnsembliENST00000344175; ENSP00000341698; ENSG00000204673. [Q96B36-1]
    ENST00000391831; ENSP00000375707; ENSG00000204673. [Q96B36-1]
    ENST00000391832; ENSP00000375708; ENSG00000204673. [Q96B36-1]
    ENST00000391833; ENSP00000375709; ENSG00000204673. [Q96B36-1]
    ENST00000391834; ENSP00000375710; ENSG00000204673. [Q96B36-1]
    ENST00000391835; ENSP00000375711; ENSG00000204673. [Q96B36-3]
    GeneIDi84335.
    KEGGihsa:84335.
    UCSCiuc002pql.5. human.
    uc002pqm.5. human. [Q96B36-1]

    Polymorphism databases

    DMDMi74731194.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK055511 mRNA. Translation: BAB70937.1 .
    AK092610 mRNA. Translation: BAG52583.1 .
    AK316603 mRNA. Translation: BAG38190.1 .
    AK226004 mRNA. No translation available.
    AC118341 Genomic DNA. No translation available.
    CH471177 Genomic DNA. Translation: EAW52570.1 .
    CH471177 Genomic DNA. Translation: EAW52568.1 .
    BC000031 mRNA. Translation: AAH00031.2 . Different initiation.
    BC007416 mRNA. Translation: AAH07416.1 .
    BC015562 mRNA. Translation: AAH15562.1 .
    BC016043 mRNA. Translation: AAH16043.1 .
    BC051844 mRNA. Translation: AAH51844.1 .
    CCDSi CCDS12784.1. [Q96B36-1 ]
    CCDS59410.1. [Q96B36-3 ]
    RefSeqi NP_001092102.1. NM_001098632.2. [Q96B36-1 ]
    NP_001092103.1. NM_001098633.3. [Q96B36-1 ]
    NP_001265088.1. NM_001278159.1. [Q96B36-1 ]
    NP_001265089.1. NM_001278160.1. [Q96B36-1 ]
    NP_115751.3. NM_032375.5. [Q96B36-3 ]
    UniGenei Hs.515542.
    Hs.610819.

    3D structure databases

    ProteinModelPortali Q96B36.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124059. 10 interactions.
    IntActi Q96B36. 11 interactions.
    MINTi MINT-3317903.
    STRINGi 9606.ENSP00000341698.

    Chemistry

    BindingDBi Q96B36.
    ChEMBLi CHEMBL1255161.

    PTM databases

    PhosphoSitei Q96B36.

    Polymorphism databases

    DMDMi 74731194.

    Proteomic databases

    MaxQBi Q96B36.
    PaxDbi Q96B36.
    PRIDEi Q96B36.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000344175 ; ENSP00000341698 ; ENSG00000204673 . [Q96B36-1 ]
    ENST00000391831 ; ENSP00000375707 ; ENSG00000204673 . [Q96B36-1 ]
    ENST00000391832 ; ENSP00000375708 ; ENSG00000204673 . [Q96B36-1 ]
    ENST00000391833 ; ENSP00000375709 ; ENSG00000204673 . [Q96B36-1 ]
    ENST00000391834 ; ENSP00000375710 ; ENSG00000204673 . [Q96B36-1 ]
    ENST00000391835 ; ENSP00000375711 ; ENSG00000204673 . [Q96B36-3 ]
    GeneIDi 84335.
    KEGGi hsa:84335.
    UCSCi uc002pql.5. human.
    uc002pqm.5. human. [Q96B36-1 ]

    Organism-specific databases

    CTDi 84335.
    GeneCardsi GC19M050372.
    HGNCi HGNC:28426. AKT1S1.
    HPAi CAB021903.
    HPA043590.
    MIMi 610221. gene.
    neXtProti NX_Q96B36.
    PharmGKBi PA134943587.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG40718.
    HOVERGENi HBG059465.
    InParanoidi Q96B36.
    KOi K16184.
    OMAi CLHDIAQ.
    OrthoDBi EOG7X3QRW.
    PhylomeDBi Q96B36.

    Enzyme and pathway databases

    Reactomei REACT_12564. AKT phosphorylates targets in the cytosol.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_200775. HSF1-dependent transactivation.
    SignaLinki Q96B36.

    Miscellaneous databases

    ChiTaRSi AKT1S1. human.
    GeneWikii AKT1S1.
    GenomeRNAii 84335.
    NextBioi 35535165.
    PROi Q96B36.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96B36.
    Bgeei Q96B36.
    CleanExi HS_AKT1S1.
    Genevestigatori Q96B36.

    Family and domain databases

    InterProi IPR026682. AKT1S1.
    [Graphical view ]
    PANTHERi PTHR21844. PTHR21844. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Prostate and Synovium.
    2. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Coronary artery.
    3. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT PRO-47.
      Tissue: BrainImported, EyeImported and SkinImported.
    6. "Identification of a proline-rich Akt substrate as a 14-3-3 binding partner."
      Kovacina K.S., Park G.Y., Bae S.S., Guzzetta A.W., Schaefer E., Birnbaum M.J., Roth R.A.
      J. Biol. Chem. 278:10189-10194(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH 14-3-3, TISSUE SPECIFICITY, PHOSPHORYLATION AT THR-246.
    7. "Expression of proline-rich Akt-substrate PRAS40 in cell survival pathway and carcinogenesis."
      Huang B., Porter G.
      Acta Pharmacol. Sin. 26:1253-1258(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "PRAS40 is an insulin-regulated inhibitor of the mTORC1 protein kinase."
      Sancak Y., Thoreen C.C., Peterson T.R., Lindquist R.A., Kang S.A., Spooner E., Carr S.A., Sabatini D.M.
      Mol. Cell 25:903-915(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE TORC1 COMPLEX, INTERACTION WITH RPTOR.
    10. "Insulin signalling to mTOR mediated by the Akt/PKB substrate PRAS40."
      Vander Haar E., Lee S.-I., Bandhakavi S., Griffin T.J., Kim D.-H.
      Nat. Cell Biol. 9:316-323(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE TORC1 COMPLEX, MUTAGENESIS OF THR-246.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-92; SER-183; SER-202; SER-203; SER-211; SER-212 AND THR-246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-92; SER-183; SER-202; SER-211; SER-212 AND THR-246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-202; SER-203; SER-211; SER-212 AND THR-246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-92; SER-183 AND THR-246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiAKTS1_HUMAN
    AccessioniPrimary (citable) accession number: Q96B36
    Secondary accession number(s): A8MTQ1
    , B2RE93, J3KPM3, Q96BI4, Q96IK7, Q96NG2, Q9BWR5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 17, 2006
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 101 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

    External Data

    Dasty 3