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CREB-regulated transcription coactivator 2 (Transducer of regulated cAMP response element-binding protein 2) (TORC-2) (Transducer of CREB protein 2)

 CRTC2_HUMAN             Reviewed;         693 AA.
Q53ET0; Q6UUV8; Q7Z3X7; Q8N332;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
05-FEB-2008, sequence version 2.
23-MAY-2018, entry version 110.
RecName: Full=CREB-regulated transcription coactivator 2;
AltName: Full=Transducer of regulated cAMP response element-binding protein 2;
Short=TORC-2;
Short=Transducer of CREB protein 2;
Name=CRTC2; Synonyms=TORC2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], VARIANT CYS-379, AND FUNCTION.
PubMed=14506290; DOI=10.1073/pnas.1932773100;
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.;
"Identification of a family of cAMP response element-binding protein
coactivators by genome-scale functional analysis in mammalian cells.";
Proc. Natl. Acad. Sci. U.S.A. 100:12147-12152(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
TISSUE=Brain;
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=PNS, and Urinary bladder;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=14536081; DOI=10.1016/j.molcel.2003.08.013;
Conkright M.D., Canettieri G., Screaton R., Guzman E., Miraglia L.,
Hogenesch J.B., Montminy M.;
"TORCs: transducers of regulated CREB activity.";
Mol. Cell 12:413-423(2003).
[6]
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, AND MUTAGENESIS OF SER-171 AND SER-368.
PubMed=15454081; DOI=10.1016/j.cell.2004.09.015;
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.;
"The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive
coincidence detector.";
Cell 119:61-74(2004).
[7]
SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=15589160; DOI=10.1016/j.cub.2004.11.002;
Bittinger M.A., McWhinnie E., Meltzer J., Iourgenko V., Latario B.,
Liu X., Chen C.H., Song C., Garza D., Labow M.;
"Activation of cAMP response element-mediated gene expression by
regulated nuclear transport of TORC proteins.";
Curr. Biol. 14:2156-2161(2004).
[8]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-171, AND
MUTAGENESIS OF SER-171.
PubMed=16817901; DOI=10.1111/j.1742-4658.2006.05291.x;
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.;
"Silencing the constitutive active transcription factor CREB by the
LKB1-SIK signaling cascade.";
FEBS J. 273:2730-2748(2006).
[9]
INTERACTION WITH HTLV-1 TAX, AND FUNCTION.
PubMed=16809310; DOI=10.1128/JVI.00103-06;
Siu Y.-T., Chin K.-T., Siu K.-L., Yee Wai Choy E., Jeang K.-T.,
Jin D.-Y.;
"TORC1 and TORC2 coactivators are required for tax activation of the
human T-cell leukemia virus type 1 long terminal repeats.";
J. Virol. 80:7052-7059(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[11]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=16980408; DOI=10.1073/pnas.0606714103;
Wu Z., Huang X., Feng Y., Handschin C., Feng Y., Gullicksen P.S.,
Bare O., Labow M., Spiegelman B., Stevenson S.C.;
"Transducer of regulated CREB-binding proteins (TORCs) induce PGC-
1alpha transcription and mitochondrial biogenesis in muscle cells.";
Proc. Natl. Acad. Sci. U.S.A. 103:14379-14384(2006).
[12]
FUNCTION, AND PHOSPHORYLATION AT SER-171.
PubMed=17210223; DOI=10.1016/j.mce.2006.12.020;
Takemori H., Kanematsu M., Kajimura J., Hatano O., Katoh Y.,
Lin X.-Z., Min L., Yamazaki T., Doi J., Okamoto M.;
"Dephosphorylation of TORC initiates expression of the StAR gene.";
Mol. Cell. Endocrinol. 265:196-204(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[14]
PHOSPHORYLATION AT SER-171 AND SER-274, INTERACTION WITH 14-3-3, AND
MUTAGENESIS OF SER-171; SER-274 AND SER-368.
PubMed=18626018; DOI=10.1073/pnas.0800796105;
Jansson D., Ng A.C., Fu A., Depatie C., Al Azzabi M., Screaton R.A.;
"Glucose controls CREB activity in islet cells via regulated
phosphorylation of TORC2.";
Proc. Natl. Acad. Sci. U.S.A. 105:10161-10166(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-86; SER-90;
SER-136; SER-433; THR-501; SER-613 AND SER-624, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-86; SER-90;
THR-192; SER-433; TYR-488; SER-490; SER-613 AND SER-624, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-501; SER-613 AND
SER-624, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433; SER-613 AND
SER-624, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90 AND SER-613, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[24]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-234, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[25]
VARIANT CYS-379, AND INVOLVEMENT IN SUSCEPTIBILITY TO NIDDM.
PubMed=17950019; DOI=10.1016/j.ymgme.2007.08.125;
Keshavarz P., Inoue H., Nakamura N., Yoshikawa T., Tanahashi T.,
Itakura M.;
"Single nucleotide polymorphisms in genes encoding LKB1 (STK11), TORC2
(CRTC2) and AMPK alpha2-subunit (PRKAA2) and risk of type 2
diabetes.";
Mol. Genet. Metab. 93:200-209(2008).
-!- FUNCTION: 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). {ECO:0000269|PubMed:14506290,
ECO:0000269|PubMed:14536081, ECO:0000269|PubMed:15454081,
ECO:0000269|PubMed:16809310, ECO:0000269|PubMed:16817901,
ECO:0000269|PubMed:16980408, ECO:0000269|PubMed:17210223}.
-!- SUBUNIT: 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 and SIK2. Interacts with
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 COP1
mediates nuclear export and degradation of CRTC2 (By similarity).
{ECO:0000250|UniProtKB:Q3U182}.
-!- INTERACTION:
P18850:ATF6; NbExp=3; IntAct=EBI-1181987, EBI-852157;
P03206:BZLF1 (xeno); NbExp=3; IntAct=EBI-1181987, EBI-2621186;
Q15233:NONO; NbExp=2; IntAct=EBI-1181987, EBI-350527;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15589160}.
Nucleus {ECO:0000269|PubMed:15589160}. Note=Translocated from the
nucleus to the cytoplasm on interaction of the phosphorylated form
with 14-3-3 protein (PubMed:15454081). In response to cAMP levels
and glucagon, relocated to the nucleus (PubMed:15454081).
{ECO:0000269|PubMed:15454081}.
-!- TISSUE SPECIFICITY: 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.
{ECO:0000269|PubMed:14536081, ECO:0000269|PubMed:15454081,
ECO:0000269|PubMed:16980408}.
-!- PTM: 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.
{ECO:0000269|PubMed:15454081, ECO:0000269|PubMed:15589160,
ECO:0000269|PubMed:16817901, ECO:0000269|PubMed:17210223,
ECO:0000269|PubMed:18626018}.
-!- PTM: Asymmetric dimethylation of arginine resisues by PRMT6
enhances the association of CRTC2 with CREB on the promoters of
gluconeogenic genes. {ECO:0000250}.
-!- POLYMORPHISM: 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).
{ECO:0000269|PubMed:17950019}.
-!- SIMILARITY: Belongs to the TORC family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CRTC2ID50581ch1q21.html";
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EMBL; AY360172; AAQ98857.1; -; mRNA.
EMBL; AK223559; BAD97279.1; -; mRNA.
EMBL; AL358472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC028886; AAH28886.1; -; mRNA.
EMBL; BC053562; AAH53562.1; -; mRNA.
CCDS; CCDS30875.1; -.
RefSeq; NP_859066.1; NM_181715.2.
UniGene; Hs.406392; -.
PDB; 4HTM; X-ray; 2.00 A; A=18-50.
PDBsum; 4HTM; -.
ProteinModelPortal; Q53ET0; -.
SMR; Q53ET0; -.
BioGrid; 128308; 37.
DIP; DIP-29950N; -.
IntAct; Q53ET0; 18.
MINT; Q53ET0; -.
STRING; 9606.ENSP00000357622; -.
iPTMnet; Q53ET0; -.
PhosphoSitePlus; Q53ET0; -.
BioMuta; CRTC2; -.
DMDM; 167009135; -.
EPD; Q53ET0; -.
MaxQB; Q53ET0; -.
PaxDb; Q53ET0; -.
PeptideAtlas; Q53ET0; -.
PRIDE; Q53ET0; -.
Ensembl; ENST00000368633; ENSP00000357622; ENSG00000160741.
GeneID; 200186; -.
KEGG; hsa:200186; -.
UCSC; uc057leo.1; human.
CTD; 200186; -.
DisGeNET; 200186; -.
EuPathDB; HostDB:ENSG00000160741.16; -.
GeneCards; CRTC2; -.
HGNC; HGNC:27301; CRTC2.
HPA; HPA028454; -.
HPA; HPA028465; -.
MIM; 608972; gene.
neXtProt; NX_Q53ET0; -.
OpenTargets; ENSG00000160741; -.
PharmGKB; PA142672073; -.
eggNOG; ENOG410IGNT; Eukaryota.
eggNOG; ENOG410XPDQ; LUCA.
GeneTree; ENSGT00390000010652; -.
HOGENOM; HOG000111980; -.
HOVERGEN; HBG058314; -.
InParanoid; Q53ET0; -.
KO; K16333; -.
OMA; HTLNHQN; -.
OrthoDB; EOG091G03YN; -.
PhylomeDB; Q53ET0; -.
TreeFam; TF321571; -.
Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
Reactome; R-HSA-400253; Circadian Clock.
SIGNOR; Q53ET0; -.
ChiTaRS; CRTC2; human.
GeneWiki; CRTC2; -.
GenomeRNAi; 200186; -.
PRO; PR:Q53ET0; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000160741; -.
CleanEx; HS_CRTC2; -.
ExpressionAtlas; Q53ET0; baseline and differential.
Genevisible; Q53ET0; HS.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0008140; F:cAMP response element binding protein binding; IBA:GO_Central.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0006094; P:gluconeogenesis; ISS:UniProtKB.
GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
GO; GO:0043970; P:histone H3-K9 acetylation; IEA:Ensembl.
GO; GO:0032793; P:positive regulation of CREB transcription factor activity; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
GO; GO:0051289; P:protein homotetramerization; IEA:InterPro.
GO; GO:1901998; P:toxin transport; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR024786; TORC.
InterPro; IPR024785; TORC_C.
InterPro; IPR024784; TORC_M.
InterPro; IPR024783; TORC_N.
PANTHER; PTHR13589; PTHR13589; 1.
Pfam; PF12886; TORC_C; 1.
Pfam; PF12885; TORC_M; 1.
Pfam; PF12884; TORC_N; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Complete proteome; Cytoplasm;
Host-virus interaction; Isopeptide bond; Methylation; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
CHAIN 2 693 CREB-regulated transcription coactivator
2.
/FTId=PRO_0000318528.
MOTIF 271 287 Nuclear export signal. {ECO:0000250}.
COMPBIAS 236 240 Poly-Ser.
COMPBIAS 336 408 Ser-rich.
SITE 629 629 Required for ubiquitination and
degradation. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
MOD_RES 51 51 Asymmetric dimethylarginine; by PRMT6.
{ECO:0000250|UniProtKB:Q3U182}.
MOD_RES 70 70 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:15454081}.
MOD_RES 86 86 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 90 90 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:15454081}.
MOD_RES 99 99 Asymmetric dimethylarginine; by PRMT6.
{ECO:0000250|UniProtKB:Q3U182}.
MOD_RES 120 120 Asymmetric dimethylarginine; by PRMT6.
{ECO:0000250|UniProtKB:Q3U182}.
MOD_RES 123 123 Asymmetric dimethylarginine; by PRMT6.
{ECO:0000250|UniProtKB:Q3U182}.
MOD_RES 136 136 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:15454081}.
MOD_RES 161 161 Asymmetric dimethylarginine; by PRMT6.
{ECO:0000250|UniProtKB:Q3U182}.
MOD_RES 168 168 Asymmetric dimethylarginine; by PRMT6.
{ECO:0000250|UniProtKB:Q3U182}.
MOD_RES 169 169 Phosphothreonine.
{ECO:0000250|UniProtKB:Q3U182}.
MOD_RES 171 171 Phosphoserine; by AMPK, MARK2, SIK1 and
SIK2. {ECO:0000269|PubMed:15454081,
ECO:0000269|PubMed:16817901,
ECO:0000269|PubMed:17210223,
ECO:0000269|PubMed:18626018}.
MOD_RES 192 192 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 274 274 Phosphoserine; by MARK2.
{ECO:0000269|PubMed:18626018}.
MOD_RES 306 306 Phosphoserine.
{ECO:0000269|PubMed:15454081}.
MOD_RES 368 368 Phosphoserine.
{ECO:0000269|PubMed:15454081}.
MOD_RES 393 393 Phosphoserine.
{ECO:0000269|PubMed:15454081}.
MOD_RES 433 433 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15454081}.
MOD_RES 456 456 Phosphoserine.
{ECO:0000269|PubMed:15454081}.
MOD_RES 488 488 Phosphotyrosine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 489 489 Phosphoserine.
{ECO:0000269|PubMed:15454081}.
MOD_RES 490 490 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 492 492 Phosphoserine.
{ECO:0000269|PubMed:15454081}.
MOD_RES 501 501 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 613 613 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:15454081}.
MOD_RES 623 623 Phosphoserine.
{ECO:0000250|UniProtKB:Q3U182}.
MOD_RES 624 624 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
CROSSLNK 234 234 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 147 147 M -> V (in dbSNP:rs11264680).
/FTId=VAR_038756.
VARIANT 379 379 R -> C (in dbSNP:rs150423770).
{ECO:0000269|PubMed:14506290,
ECO:0000269|PubMed:17950019}.
/FTId=VAR_038757.
MUTAGEN 70 70 S->A: No effect on cAMP- and calcium-
regulated phosphorylation.
MUTAGEN 171 171 S->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.
{ECO:0000269|PubMed:15454081,
ECO:0000269|PubMed:16817901,
ECO:0000269|PubMed:18626018}.
MUTAGEN 274 274 S->A: Impaired phosphorylation under low
glucose conditions and impaired
interaction with 14-3-3 proteins; when
associated with A-171.
{ECO:0000269|PubMed:18626018}.
MUTAGEN 368 368 S->A: Reduced cAMP- and calcium-regulated
phosphorylation.
{ECO:0000269|PubMed:15454081,
ECO:0000269|PubMed:18626018}.
MUTAGEN 393 393 S->A: No effect on cAMP- and calcium-
regulated phosphorylation.
CONFLICT 323 325 MGL -> HGP (in Ref. 1; AAQ98857).
{ECO:0000305}.
CONFLICT 499 499 P -> S (in Ref. 2; BAD97279).
{ECO:0000305}.
HELIX 21 45 {ECO:0000244|PDB:4HTM}.
SEQUENCE 693 AA; 73302 MW; EE6C52E0ECDC1DF1 CRC64;
MATSGANGPG SATASASNPR KFSEKIALQK QRQAEETAAF EEVMMDIGST RLQAQKLRLA
YTRSSHYGGS LPNVNQIGSG LAEFQSPLHS PLDSSRSTRH HGLVERVQRD PRRMVSPLRR
YTRHIDSSPY SPAYLSPPPE SSWRRTMAWG NFPAEKGQLF RLPSALNRTS SDSALHTSVM
NPSPQDTYPG PTPPSILPSR RGGILDGEMD PKVPAIEENL LDDKHLLKPW DAKKLSSSSS
RPRSCEVPGI NIFPSPDQPA NVPVLPPAMN TGGSLPDLTN LHFPPPLPTP LDPEETAYPS
LSGGNSTSNL THTMTHLGIS RGMGLGPGYD APGLHSPLSH PSLQSSLSNP NLQASLSSPQ
PQLQGSHSHP SLPASSLARH VLPTTSLGHP SLSAPALSSS SSSSSTSSPV LGAPSYPAST
PGASPHHRRV PLSPLSLLAG PADARRSQQQ LPKQFSPTMS PTLSSITQGV PLDTSKLSTD
QRLPPYPYSS PSLVLPTQPH TPKSLQQPGL PSQSCSVQSS GGQPPGRQSH YGTPYPPGPS
GHGQQSYHRP MSDFNLGNLE QFSMESPSAS LVLDPPGFSE GPGFLGGEGP MGGPQDPHTF
NHQNLTHCSR HGSGPNIILT GDSSPGFSKE IAAALAGVPG FEVSAAGLEL GLGLEDELRM
EPLGLEGLNM LSDPCALLPD PAVEESFRSD RLQ


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