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Q53ET0

- CRTC2_HUMAN

UniProt

Q53ET0 - CRTC2_HUMAN

Protein

CREB-regulated transcription coactivator 2

Gene

CRTC2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 2 (05 Feb 2008)
      Previous versions | rss
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    Functioni

    Transcriptional coactivator for CREB1 which activates transcription through both consensus and variant cAMP response element (CRE) sites. Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated and acts independently of CREB1 'Ser-133' phosphorylation. Enhances the interaction of CREB1 with TAF4. Regulates gluconeogenesis as a component of the LKB1/AMPK/TORC2 signaling pathway. Regulates the expression of specific genes such as the steroidogenic gene, StAR. Potent coactivator of PPARGC1A and inducer of mitochondrial biogenesis in muscle cells. Also coactivator for TAX activation of the human T-cell leukemia virus type 1 (HTLV-1) long terminal repeats (LTR).7 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei629 – 6291Required for ubiquitination and degradationBy similarity

    GO - Molecular functioni

    1. cAMP response element binding protein binding Source: InterPro
    2. protein binding Source: IntAct

    GO - Biological processi

    1. gluconeogenesis Source: UniProtKB
    2. glucose homeostasis Source: UniProtKB
    3. positive regulation of CREB transcription factor activity Source: UniProtKB
    4. protein homotetramerization Source: InterPro
    5. transcription, DNA-templated Source: UniProtKB-KW
    6. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Host-virus interaction, Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CREB-regulated transcription coactivator 2
    Alternative name(s):
    Transducer of regulated cAMP response element-binding protein 2
    Short name:
    TORC-2
    Short name:
    Transducer of CREB protein 2
    Gene namesi
    Name:CRTC2
    Synonyms:TORC2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:27301. CRTC2.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Translocated from the nucleus to the cytoplasm on interaction of the phosphorylated form with 14-3-3 protein. In response to cAMP levels and glucagon, relocated to the nucleus.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi70 – 701S → A: No effect on cAMP- and calcium-regulated phosphorylation.
    Mutagenesisi171 – 1711S → A: Loss of cAMP- and calcium-regulated phosphorylation. Greatly reduced interaction with 14-3-3 proteins. Impaired phosphorylation under low glucose conditions and impaired interaction with 14-3-3 proteins; when associated with A-274. 3 Publications
    Mutagenesisi274 – 2741S → A: Impaired phosphorylation under low glucose conditions and impaired interaction with 14-3-3 proteins; when associated with A-171. 1 Publication
    Mutagenesisi368 – 3681S → A: Reduced cAMP- and calcium-regulated phosphorylation. 2 Publications
    Mutagenesisi393 – 3931S → A: No effect on cAMP- and calcium-regulated phosphorylation.

    Organism-specific databases

    PharmGKBiPA142672073.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 693692CREB-regulated transcription coactivator 2PRO_0000318528Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei51 – 511Asymmetric dimethylarginine; by PRMT6By similarity
    Modified residuei70 – 701Phosphoserine4 Publications
    Modified residuei86 – 861Phosphoserine3 Publications
    Modified residuei90 – 901Phosphoserine4 Publications
    Modified residuei99 – 991Asymmetric dimethylarginine; by PRMT6By similarity
    Modified residuei120 – 1201Asymmetric dimethylarginine; by PRMT6By similarity
    Modified residuei123 – 1231Asymmetric dimethylarginine; by PRMT6By similarity
    Modified residuei136 – 1361Phosphoserine3 Publications
    Modified residuei161 – 1611Asymmetric dimethylarginine; by PRMT6By similarity
    Modified residuei168 – 1681Asymmetric dimethylarginine; by PRMT6By similarity
    Modified residuei171 – 1711Phosphoserine; by AMPK, MARK2, SIK1 and SIK25 Publications
    Modified residuei192 – 1921Phosphothreonine2 Publications
    Modified residuei274 – 2741Phosphoserine; by MARK22 Publications
    Modified residuei306 – 3061Phosphoserine2 Publications
    Modified residuei368 – 3681Phosphoserine2 Publications
    Modified residuei393 – 3931Phosphoserine2 Publications
    Modified residuei433 – 4331Phosphoserine6 Publications
    Modified residuei456 – 4561Phosphoserine2 Publications
    Modified residuei488 – 4881Phosphotyrosine2 Publications
    Modified residuei489 – 4891Phosphoserine2 Publications
    Modified residuei490 – 4901Phosphoserine2 Publications
    Modified residuei492 – 4921Phosphoserine2 Publications
    Modified residuei501 – 5011Phosphothreonine3 Publications
    Modified residuei613 – 6131Phosphoserine5 Publications
    Modified residuei624 – 6241Phosphoserine4 Publications

    Post-translational modificationi

    Phosphorylation/dephosphorylation states of Ser-171 are required for regulating transduction of CREB activity. TORCs are inactive when phosphorylated, and active when dephosphorylated at this site. This primary site of phosphorylation, is regulated by cAMP and calcium levels and is dependent on the phosphorylation of SIKs (SIK1 and SIK2) by LKB1. Both insulin and AMPK increase this phosphorylation of CRTC2 while glucagon suppresses it. Phosphorylation at Ser-274 by MARK2 is induced under low glucose conditions and dephosphorylated in response to glucose influx. Phosphorylation at Ser-274 promotes interaction with 14-3-3 proteins and translocation to the cytoplasm.10 Publications
    Asymmetric dimethylation of arginine resisues by PRMT6 enhances the association of CRTC2 with CREB on the promoters of gluconeogenic genes.By similarity

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ53ET0.
    PaxDbiQ53ET0.
    PRIDEiQ53ET0.

    PTM databases

    PhosphoSiteiQ53ET0.

    Expressioni

    Tissue specificityi

    Most abundantly expressed in the thymus. Present in both B and T-lymphocytes. Highly expressed in HEK293T cells and in insulinomas. High levels also in spleen, ovary, muscle and lung, with highest levels in muscle. Lower levels found in brain, colon, heart, kidney, prostate, small intestine and stomach. Weak expression in liver and pancreas.3 Publications

    Gene expression databases

    ArrayExpressiQ53ET0.
    BgeeiQ53ET0.
    CleanExiHS_CRTC2.
    GenevestigatoriQ53ET0.

    Organism-specific databases

    HPAiHPA028454.
    HPA028465.

    Interactioni

    Subunit structurei

    Binds, as a tetramer, through its N-terminal region, with the bZIP domain of CREB1. 'Arg-314' in the bZIP domain of CREB1 is essential for this interaction. Interaction, via its C-terminal, with TAF4, enhances recruitment of TAF4 to CREB1 By similarity. Interacts with PPP3CA/calcineurin alpha, SIK2 and 14-3-3 proteins, YWHAB and YWHAG. Interaction with the human T-cell leukemia virus type 1 (HTLV-1) Tax protein is essential for optimal transcription activation by Tax. Interaction with RFWD2/COP1 mediates nuclear export and degradation of CRTC2 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BZLF1P032063EBI-1181987,EBI-2621186From a different organism.

    Protein-protein interaction databases

    BioGridi128308. 10 interactions.
    DIPiDIP-29950N.
    IntActiQ53ET0. 6 interactions.
    MINTiMINT-1631979.
    STRINGi9606.ENSP00000305873.

    Structurei

    Secondary structure

    1
    693
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi21 – 4525

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4HTMX-ray2.00A18-50[»]
    ProteinModelPortaliQ53ET0.
    SMRiQ53ET0. Positions 20-47.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi271 – 28717Nuclear export signalBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi236 – 2405Poly-Ser
    Compositional biasi336 – 40873Ser-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the TORC family.Curated

    Phylogenomic databases

    eggNOGiNOG74259.
    HOGENOMiHOG000111980.
    HOVERGENiHBG058314.
    InParanoidiQ53ET0.
    KOiK16333.
    OMAiTHCSRHG.
    OrthoDBiEOG7MKW5P.
    PhylomeDBiQ53ET0.
    TreeFamiTF321571.

    Family and domain databases

    InterProiIPR024786. TORC.
    IPR024785. TORC_C.
    IPR024784. TORC_M.
    IPR024783. TORC_N.
    [Graphical view]
    PANTHERiPTHR13589. PTHR13589. 1 hit.
    PfamiPF12886. TORC_C. 1 hit.
    PF12885. TORC_M. 1 hit.
    PF12884. TORC_N. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q53ET0-1 [UniParc]FASTAAdd to Basket

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    MATSGANGPG SATASASNPR KFSEKIALQK QRQAEETAAF EEVMMDIGST    50
    RLQAQKLRLA YTRSSHYGGS LPNVNQIGSG LAEFQSPLHS PLDSSRSTRH 100
    HGLVERVQRD PRRMVSPLRR YTRHIDSSPY SPAYLSPPPE SSWRRTMAWG 150
    NFPAEKGQLF RLPSALNRTS SDSALHTSVM NPSPQDTYPG PTPPSILPSR 200
    RGGILDGEMD PKVPAIEENL LDDKHLLKPW DAKKLSSSSS RPRSCEVPGI 250
    NIFPSPDQPA NVPVLPPAMN TGGSLPDLTN LHFPPPLPTP LDPEETAYPS 300
    LSGGNSTSNL THTMTHLGIS RGMGLGPGYD APGLHSPLSH PSLQSSLSNP 350
    NLQASLSSPQ PQLQGSHSHP SLPASSLARH VLPTTSLGHP SLSAPALSSS 400
    SSSSSTSSPV LGAPSYPAST PGASPHHRRV PLSPLSLLAG PADARRSQQQ 450
    LPKQFSPTMS PTLSSITQGV PLDTSKLSTD QRLPPYPYSS PSLVLPTQPH 500
    TPKSLQQPGL PSQSCSVQSS GGQPPGRQSH YGTPYPPGPS GHGQQSYHRP 550
    MSDFNLGNLE QFSMESPSAS LVLDPPGFSE GPGFLGGEGP MGGPQDPHTF 600
    NHQNLTHCSR HGSGPNIILT GDSSPGFSKE IAAALAGVPG FEVSAAGLEL 650
    GLGLEDELRM EPLGLEGLNM LSDPCALLPD PAVEESFRSD RLQ 693
    Length:693
    Mass (Da):73,302
    Last modified:February 5, 2008 - v2
    Checksum:iEE6C52E0ECDC1DF1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti323 – 3253MGL → HGP in AAQ98857. (PubMed:14506290)Curated
    Sequence conflicti499 – 4991P → S in BAD97279. 1 PublicationCurated

    Polymorphismi

    Variant Cys-379, under a dominant model, linked to a recessive mutation in LKB1, may be associated with susceptibility to type II or non-insulin-dependent diabetes mellitus (NIDDM).

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti147 – 1471M → V.
    Corresponds to variant rs11264680 [ dbSNP | Ensembl ].
    VAR_038756
    Natural varianti379 – 3791R → C.2 Publications
    Corresponds to variant rs150423770 [ dbSNP | Ensembl ].
    VAR_038757

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY360172 mRNA. Translation: AAQ98857.1.
    AK223559 mRNA. Translation: BAD97279.1.
    AL358472 Genomic DNA. Translation: CAI14017.1.
    BC028886 mRNA. Translation: AAH28886.1.
    BC053562 mRNA. Translation: AAH53562.1.
    CCDSiCCDS30875.1.
    RefSeqiNP_859066.1. NM_181715.2.
    UniGeneiHs.406392.

    Genome annotation databases

    EnsembliENST00000368633; ENSP00000357622; ENSG00000160741.
    GeneIDi200186.
    KEGGihsa:200186.
    UCSCiuc021pab.1. human.

    Polymorphism databases

    DMDMi167009135.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY360172 mRNA. Translation: AAQ98857.1 .
    AK223559 mRNA. Translation: BAD97279.1 .
    AL358472 Genomic DNA. Translation: CAI14017.1 .
    BC028886 mRNA. Translation: AAH28886.1 .
    BC053562 mRNA. Translation: AAH53562.1 .
    CCDSi CCDS30875.1.
    RefSeqi NP_859066.1. NM_181715.2.
    UniGenei Hs.406392.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4HTM X-ray 2.00 A 18-50 [» ]
    ProteinModelPortali Q53ET0.
    SMRi Q53ET0. Positions 20-47.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 128308. 10 interactions.
    DIPi DIP-29950N.
    IntActi Q53ET0. 6 interactions.
    MINTi MINT-1631979.
    STRINGi 9606.ENSP00000305873.

    PTM databases

    PhosphoSitei Q53ET0.

    Polymorphism databases

    DMDMi 167009135.

    Proteomic databases

    MaxQBi Q53ET0.
    PaxDbi Q53ET0.
    PRIDEi Q53ET0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368633 ; ENSP00000357622 ; ENSG00000160741 .
    GeneIDi 200186.
    KEGGi hsa:200186.
    UCSCi uc021pab.1. human.

    Organism-specific databases

    CTDi 200186.
    GeneCardsi GC01M153920.
    HGNCi HGNC:27301. CRTC2.
    HPAi HPA028454.
    HPA028465.
    MIMi 608972. gene.
    neXtProti NX_Q53ET0.
    PharmGKBi PA142672073.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG74259.
    HOGENOMi HOG000111980.
    HOVERGENi HBG058314.
    InParanoidi Q53ET0.
    KOi K16333.
    OMAi THCSRHG.
    OrthoDBi EOG7MKW5P.
    PhylomeDBi Q53ET0.
    TreeFami TF321571.

    Miscellaneous databases

    GeneWikii CRTC2.
    GenomeRNAii 200186.
    NextBioi 89862.
    PROi Q53ET0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q53ET0.
    Bgeei Q53ET0.
    CleanExi HS_CRTC2.
    Genevestigatori Q53ET0.

    Family and domain databases

    InterProi IPR024786. TORC.
    IPR024785. TORC_C.
    IPR024784. TORC_M.
    IPR024783. TORC_N.
    [Graphical view ]
    PANTHERi PTHR13589. PTHR13589. 1 hit.
    Pfami PF12886. TORC_C. 1 hit.
    PF12885. TORC_M. 1 hit.
    PF12884. TORC_N. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a family of cAMP response element-binding protein coactivators by genome-scale functional analysis in mammalian cells."
      Iourgenko V., Zhang W., Mickanin C., Daly I., Jiang C., Hexham J.M., Orth A.P., Miraglia L., Meltzer J., Garza D., Chirn G.-W., McWhinnie E., Cohen D., Skelton J., Terry R., Yu Y., Bodian D., Buxton F.P.
      , Zhu J., Song C., Labow M.A.
      Proc. Natl. Acad. Sci. U.S.A. 100:12147-12152(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT CYS-379, FUNCTION.
    2. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    3. "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.A., 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.S., 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.J., 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.I., 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.W., McLaren S., Milne S., Mistry S., Moore M.J.F., 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.M., 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.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Tissue: Brain.
    4. "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].
      Tissue: PNS and Urinary bladder.
    5. Cited for: FUNCTION, TISSUE SPECIFICITY.
    6. "The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive coincidence detector."
      Screaton R.A., Conkright M.D., Katoh Y., Best J.L., Canettieri G., Jeffries S., Guzman E., Niessen S., Yates J.R. III, Takemori H., Okamoto M., Montminy M.
      Cell 119:61-74(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CREB1; SIK2; PPP3CA; YWHAB AND YWHAG, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION, PHOSPHORYLATION AT SER-70; SER-90; SER-136; SER-171; SER-306; SER-368; SER-393; SER-433; SER-456; SER-489; SER-492 AND SER-613, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF SER-171 AND SER-368.
    7. "Activation of cAMP response element-mediated gene expression by regulated nuclear transport of TORC proteins."
      Bittinger M.A., McWhinnie E., Meltzer J., Iourgenko V., Latario B., Liu X., Chen C.H., Song C., Garza D., Labow M.
      Curr. Biol. 14:2156-2161(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
    8. "Silencing the constitutive active transcription factor CREB by the LKB1-SIK signaling cascade."
      Katoh Y., Takemori H., Lin X.-Z., Tamura M., Muraoka M., Satoh T., Tsuchiya Y., Min L., Doi J., Miyauchi A., Witters L.A., Nakamura H., Okamoto M.
      FEBS J. 273:2730-2748(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-171, MUTAGENESIS OF SER-171.
    9. "TORC1 and TORC2 coactivators are required for tax activation of the human T-cell leukemia virus type 1 long terminal repeats."
      Siu Y.-T., Chin K.-T., Siu K.-L., Yee Wai Choy E., Jeang K.-T., Jin D.-Y.
      J. Virol. 80:7052-7059(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HTLV-1 TAX, FUNCTION.
    10. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Transducer of regulated CREB-binding proteins (TORCs) induce PGC-1alpha transcription and mitochondrial biogenesis in muscle cells."
      Wu Z., Huang X., Feng Y., Handschin C., Feng Y., Gullicksen P.S., Bare O., Labow M., Spiegelman B., Stevenson S.C.
      Proc. Natl. Acad. Sci. U.S.A. 103:14379-14384(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    12. Cited for: FUNCTION, PHOSPHORYLATION AT SER-171.
    13. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Glucose controls CREB activity in islet cells via regulated phosphorylation of TORC2."
      Jansson D., Ng A.C., Fu A., Depatie C., Al Azzabi M., Screaton R.A.
      Proc. Natl. Acad. Sci. U.S.A. 105:10161-10166(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-171 AND SER-274, INTERACTION WITH 14-3-3, MUTAGENESIS OF SER-171; SER-274 AND SER-368.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-86; SER-90; SER-136; SER-433; THR-501; SER-613 AND SER-624, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    17. "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-70; SER-86; SER-90; THR-192; SER-433; TYR-488; SER-490; SER-613 AND SER-624, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "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 THR-501; SER-613 AND SER-624, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Single nucleotide polymorphisms in genes encoding LKB1 (STK11), TORC2 (CRTC2) and AMPK alpha2-subunit (PRKAA2) and risk of type 2 diabetes."
      Keshavarz P., Inoue H., Nakamura N., Yoshikawa T., Tanahashi T., Itakura M.
      Mol. Genet. Metab. 93:200-209(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CYS-379, INVOLVEMENT IN SUSCEPTIBILITY TO NIDDM.

    Entry informationi

    Entry nameiCRTC2_HUMAN
    AccessioniPrimary (citable) accession number: Q53ET0
    Secondary accession number(s): Q6UUV8, Q7Z3X7, Q8N332
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 76 of the entry and version 2 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3