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Protein

CREB-regulated transcription coactivator 2

Gene

CRTC2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

  1. gluconeogenesis Source: UniProtKB
  2. glucose homeostasis Source: UniProtKB
  3. histone H3-K9 acetylation Source: Ensembl
  4. positive regulation of CREB transcription factor activity Source: UniProtKB
  5. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  6. protein homotetramerization Source: InterPro
  7. transcription, DNA-templated Source: UniProtKB-KW
  8. viral process Source: UniProtKB-KW
Complete GO annotation...

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: UniProtKB
  3. nucleoplasm Source: HPA
Complete GO annotation...

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 – 701Phosphoserine3 Publications
Modified residuei86 – 861Phosphoserine2 Publications
Modified residuei90 – 901Phosphoserine3 Publications
Modified residuei99 – 991Asymmetric dimethylarginine; by PRMT6By similarity
Modified residuei120 – 1201Asymmetric dimethylarginine; by PRMT6By similarity
Modified residuei123 – 1231Asymmetric dimethylarginine; by PRMT6By similarity
Modified residuei136 – 1361Phosphoserine2 Publications
Modified residuei161 – 1611Asymmetric dimethylarginine; by PRMT6By similarity
Modified residuei168 – 1681Asymmetric dimethylarginine; by PRMT6By similarity
Modified residuei171 – 1711Phosphoserine; by AMPK, MARK2, SIK1 and SIK24 Publications
Modified residuei192 – 1921Phosphothreonine1 Publication
Modified residuei274 – 2741Phosphoserine; by MARK21 Publication
Modified residuei306 – 3061Phosphoserine1 Publication
Modified residuei368 – 3681Phosphoserine1 Publication
Modified residuei393 – 3931Phosphoserine1 Publication
Modified residuei433 – 4331Phosphoserine5 Publications
Modified residuei456 – 4561Phosphoserine1 Publication
Modified residuei488 – 4881Phosphotyrosine1 Publication
Modified residuei489 – 4891Phosphoserine1 Publication
Modified residuei490 – 4901Phosphoserine1 Publication
Modified residuei492 – 4921Phosphoserine1 Publication
Modified residuei501 – 5011Phosphothreonine2 Publications
Modified residuei613 – 6131Phosphoserine4 Publications
Modified residuei624 – 6241Phosphoserine3 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

BgeeiQ53ET0.
CleanExiHS_CRTC2.
ExpressionAtlasiQ53ET0. baseline and differential.
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. 15 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 – 4525Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000010652.
HOGENOMiHOG000111980.
HOVERGENiHBG058314.
InParanoidiQ53ET0.
KOiK16333.
OMAiHTLNHQN.
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

« Hide

        10         20         30         40         50
MATSGANGPG SATASASNPR KFSEKIALQK QRQAEETAAF EEVMMDIGST
60 70 80 90 100
RLQAQKLRLA YTRSSHYGGS LPNVNQIGSG LAEFQSPLHS PLDSSRSTRH
110 120 130 140 150
HGLVERVQRD PRRMVSPLRR YTRHIDSSPY SPAYLSPPPE SSWRRTMAWG
160 170 180 190 200
NFPAEKGQLF RLPSALNRTS SDSALHTSVM NPSPQDTYPG PTPPSILPSR
210 220 230 240 250
RGGILDGEMD PKVPAIEENL LDDKHLLKPW DAKKLSSSSS RPRSCEVPGI
260 270 280 290 300
NIFPSPDQPA NVPVLPPAMN TGGSLPDLTN LHFPPPLPTP LDPEETAYPS
310 320 330 340 350
LSGGNSTSNL THTMTHLGIS RGMGLGPGYD APGLHSPLSH PSLQSSLSNP
360 370 380 390 400
NLQASLSSPQ PQLQGSHSHP SLPASSLARH VLPTTSLGHP SLSAPALSSS
410 420 430 440 450
SSSSSTSSPV LGAPSYPAST PGASPHHRRV PLSPLSLLAG PADARRSQQQ
460 470 480 490 500
LPKQFSPTMS PTLSSITQGV PLDTSKLSTD QRLPPYPYSS PSLVLPTQPH
510 520 530 540 550
TPKSLQQPGL PSQSCSVQSS GGQPPGRQSH YGTPYPPGPS GHGQQSYHRP
560 570 580 590 600
MSDFNLGNLE QFSMESPSAS LVLDPPGFSE GPGFLGGEGP MGGPQDPHTF
610 620 630 640 650
NHQNLTHCSR HGSGPNIILT GDSSPGFSKE IAAALAGVPG FEVSAAGLEL
660 670 680 690
GLGLEDELRM EPLGLEGLNM LSDPCALLPD PAVEESFRSD RLQ
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi128308. 15 interactions.
DIPiDIP-29950N.
IntActiQ53ET0. 6 interactions.
MINTiMINT-1631979.
STRINGi9606.ENSP00000305873.

PTM databases

PhosphoSiteiQ53ET0.

Polymorphism databases

DMDMi167009135.

Proteomic databases

MaxQBiQ53ET0.
PaxDbiQ53ET0.
PRIDEiQ53ET0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi200186.
GeneCardsiGC01M153920.
HGNCiHGNC:27301. CRTC2.
HPAiHPA028454.
HPA028465.
MIMi608972. gene.
neXtProtiNX_Q53ET0.
PharmGKBiPA142672073.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG74259.
GeneTreeiENSGT00390000010652.
HOGENOMiHOG000111980.
HOVERGENiHBG058314.
InParanoidiQ53ET0.
KOiK16333.
OMAiHTLNHQN.
OrthoDBiEOG7MKW5P.
PhylomeDBiQ53ET0.
TreeFamiTF321571.

Miscellaneous databases

ChiTaRSiCRTC2. human.
GeneWikiiCRTC2.
GenomeRNAii200186.
NextBioi89862.
PROiQ53ET0.
SOURCEiSearch...

Gene expression databases

BgeeiQ53ET0.
CleanExiHS_CRTC2.
ExpressionAtlasiQ53ET0. baseline and differential.
GenevestigatoriQ53ET0.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: February 4, 2015
This is version 80 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.