CRTC3_HUMAN
ID CRTC3_HUMAN Reviewed; 619 AA.
AC Q6UUV7; Q6DK61; Q6DK62; Q8NF38; Q9H6U2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=CREB-regulated transcription coactivator 3;
DE AltName: Full=Transducer of regulated cAMP response element-binding protein 3;
DE Short=TORC-3;
DE Short=Transducer of CREB protein 3;
GN Name=CRTC3; Synonyms=TORC3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP INTERACTION WITH CREB1, AND VARIANT ASN-72.
RX PubMed=14506290; DOI=10.1073/pnas.1932773100;
RA Iourgenko V., Zhang W., Mickanin C., Daly I., Jiang C., Hexham J.M.,
RA Orth A.P., Miraglia L., Meltzer J., Garza D., Chirn G.-W., McWhinnie E.,
RA Cohen D., Skelton J., Terry R., Yu Y., Bodian D., Buxton F.P., Zhu J.,
RA Song C., Labow M.A.;
RT "Identification of a family of cAMP response element-binding protein
RT coactivators by genome-scale functional analysis in mammalian cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12147-12152(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT ASN-72.
RC TISSUE=Spleen;
RX PubMed=12693554; DOI=10.1093/dnares/10.1.49;
RA Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N.,
RA Ohara O.;
RT "Characterization of long cDNA clones from human adult spleen. II. The
RT complete sequences of 81 cDNA clones.";
RL DNA Res. 10:49-57(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 217-619 (ISOFORM 1).
RC TISSUE=Hepatoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 292-619 (ISOFORM 1), AND VARIANT
RP SER-346.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=14536081; DOI=10.1016/j.molcel.2003.08.013;
RA Conkright M.D., Canettieri G., Screaton R., Guzman E., Miraglia L.,
RA Hogenesch J.B., Montminy M.;
RT "TORCs: transducers of regulated CREB activity.";
RL Mol. Cell 12:413-423(2003).
RN [7]
RP SUBCELLULAR LOCATION, FUNCTION, AND MUTAGENESIS OF TYR-282.
RX PubMed=15454081; DOI=10.1016/j.cell.2004.09.015;
RA Screaton R.A., Conkright M.D., Katoh Y., Best J.L., Canettieri G.,
RA Jeffries S., Guzman E., Niessen S., Yates J.R. III, Takemori H.,
RA Okamoto M., Montminy M.;
RT "The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive
RT coincidence detector.";
RL Cell 119:61-74(2004).
RN [8]
RP INTERACTION WITH HTLV-1 TAX (MICROBIAL INFECTION), AND FUNCTION.
RX PubMed=15466468; DOI=10.1074/jbc.m409021200;
RA Koga H., Ohshima T., Shimotohno K.;
RT "Enhanced activation of tax-dependent transcription of human T-cell
RT leukemia virus type I (HTLV-I) long terminal repeat by TORC3.";
RL J. Biol. Chem. 279:52978-52983(2004).
RN [9]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=15589160; DOI=10.1016/j.cub.2004.11.002;
RA Bittinger M.A., McWhinnie E., Meltzer J., Iourgenko V., Latario B., Liu X.,
RA Chen C.H., Song C., Garza D., Labow M.;
RT "Activation of cAMP response element-mediated gene expression by regulated
RT nuclear transport of TORC proteins.";
RL Curr. Biol. 14:2156-2161(2004).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=16817901; DOI=10.1111/j.1742-4658.2006.05291.x;
RA Katoh Y., Takemori H., Lin X.-Z., Tamura M., Muraoka M., Satoh T.,
RA Tsuchiya Y., Min L., Doi J., Miyauchi A., Witters L.A., Nakamura H.,
RA Okamoto M.;
RT "Silencing the constitutive active transcription factor CREB by the LKB1-
RT SIK signaling cascade.";
RL FEBS J. 273:2730-2748(2006).
RN [12]
RP INTERACTION WITH HTLV-1 TAX (MICROBIAL INFECTION).
RX PubMed=16809310; DOI=10.1128/jvi.00103-06;
RA Siu Y.-T., Chin K.-T., Siu K.-L., Yee Wai Choy E., Jeang K.-T., Jin D.-Y.;
RT "TORC1 and TORC2 coactivators are required for tax activation of the human
RT T-cell leukemia virus type 1 long terminal repeats.";
RL J. Virol. 80:7052-7059(2006).
RN [13]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16980408; DOI=10.1073/pnas.0606714103;
RA Wu Z., Huang X., Feng Y., Handschin C., Feng Y., Gullicksen P.S., Bare O.,
RA Labow M., Spiegelman B., Stevenson S.C.;
RT "Transducer of regulated CREB-binding proteins (TORCs) induce PGC-1alpha
RT transcription and mitochondrial biogenesis in muscle cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:14379-14384(2006).
RN [14]
RP INTERACTION WITH BCL3 IN BCL3/TORC3/CREB1 COMPLEX, AND FUNCTION.
RX PubMed=17644518; DOI=10.1074/jbc.m702656200;
RA Hishiki T., Ohshima T., Ego T., Shimotohno K.;
RT "BCL3 acts as a negative regulator of transcription from the human T-cell
RT leukemia virus type 1 long terminal repeat through interactions with
RT TORC3.";
RL J. Biol. Chem. 282:28335-28343(2007).
RN [15]
RP FUNCTION.
RX PubMed=17210223; DOI=10.1016/j.mce.2006.12.020;
RA Takemori H., Kanematsu M., Kajimura J., Hatano O., Katoh Y., Lin X.-Z.,
RA Min L., Yamazaki T., Doi J., Okamoto M.;
RT "Dephosphorylation of TORC initiates expression of the StAR gene.";
RL Mol. Cell. Endocrinol. 265:196-204(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391 AND SER-443, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329; SER-370 AND SER-443, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-62; SER-329; SER-332;
RP SER-370; SER-391; SER-396 AND SER-410, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-232, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [23]
RP INTERACTION WITH YWHAE; PPP2CA; PPP2R1A AND PPP2R2A, SUBCELLULAR LOCATION,
RP AND PHOSPHORYLATION AT SER-273 AND SER-391.
RX PubMed=30611118; DOI=10.1016/j.isci.2018.12.012;
RA Sonntag T., Ostojic J., Vaughan J.M., Moresco J.J., Yoon Y.S.,
RA Yates J.R. III, Montminy M.;
RT "Mitogenic Signals Stimulate the CREB Coactivator CRTC3 through PP2A
RT Recruitment.";
RL IScience 11:134-145(2018).
CC -!- FUNCTION: Transcriptional coactivator for CREB1 which activates
CC transcription through both consensus and variant cAMP response element
CC (CRE) sites. Acts as a coactivator, in the SIK/TORC signaling pathway,
CC being active when dephosphorylated and acts independently of CREB1
CC 'Ser-133' phosphorylation. Enhances the interaction of CREB1 with TAF4.
CC Regulates the expression of specific CREB-activated genes such as the
CC steroidogenic gene, StAR. Potent coactivator of PPARGC1A and inducer of
CC mitochondrial biogenesis in muscle cells. Also coactivator for TAX
CC activation of the human T-cell leukemia virus type 1 (HTLV-1) long
CC terminal repeats (LTR). {ECO:0000269|PubMed:14506290,
CC ECO:0000269|PubMed:15454081, ECO:0000269|PubMed:15466468,
CC ECO:0000269|PubMed:16817901, ECO:0000269|PubMed:16980408,
CC ECO:0000269|PubMed:17210223, ECO:0000269|PubMed:17644518}.
CC -!- SUBUNIT: Binding, as a tetramer, through its N-terminal region, with
CC the bZIP domain of CREB1 enhances recruitment of TAF4 to the promoter
CC (PubMed:14506290). 'Arg-314' in the bZIP domain of CREB1 is essential
CC for this interaction (PubMed:14506290). Interacts (when phosphorylated
CC at Ser-162 and Se-273) with 14-3-3 proteins (PubMed:30611118).
CC Interacts with YWHAE (PubMed:30611118). Interacts (when phosphorylated
CC at Ser-391) with phosphatase PP2A catalytic subunit PPP2CA and
CC regulatory subunits PPP2R1A and PPP2R2A (PubMed:30611118). Interacts,
CC via the N-terminal with the ankyrin repeats of BCL3, to form a complex
CC with CREB1 on CRE and TxRE responsive elements and represses HTLV-1
CC LTR-mediated transcription (PubMed:17644518).
CC {ECO:0000250|UniProtKB:Q91X84, ECO:0000269|PubMed:14506290,
CC ECO:0000269|PubMed:17644518, ECO:0000269|PubMed:30611118}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 protein Tax; this
CC interaction enhances tax transcriptional activity.
CC {ECO:0000269|PubMed:15466468, ECO:0000269|PubMed:16809310}.
CC -!- INTERACTION:
CC Q6UUV7; Q8N1Q1: CA13; NbExp=3; IntAct=EBI-3453588, EBI-11982647;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15454081,
CC ECO:0000269|PubMed:15589160, ECO:0000269|PubMed:16817901,
CC ECO:0000269|PubMed:30611118}. Cytoplasm {ECO:0000269|PubMed:15589160,
CC ECO:0000269|PubMed:16817901, ECO:0000269|PubMed:30611118}. Note=Appears
CC to be mainly nuclear (PubMed:15454081). Translocates to the nucleus
CC following adenylyl cyclase or MAP kinase activation (PubMed:30611118).
CC {ECO:0000269|PubMed:15454081, ECO:0000269|PubMed:30611118}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6UUV7-1; Sequence=Displayed;
CC Name=3;
CC IsoId=Q6UUV7-3; Sequence=VSP_031220;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in B and T lymphocytes.
CC Highest levels in lung. Also expressed in brain, colon, heart, kidney,
CC ovary, and prostate. Weak expression in liver, pancreas, muscle, small
CC intestine, spleen and stomach. {ECO:0000269|PubMed:14536081,
CC ECO:0000269|PubMed:16980408}.
CC -!- PTM: Phosphorylation/dephosphorylation states of Ser-273 are required
CC for regulating transduction of CREB activity (By similarity).
CC CRTCs/TORCs are inactive when phosphorylated, and active when
CC dephosphorylated at this site (By similarity). May be phosphorylated at
CC Ser-391 by MAPK3/ERK1 and/or MAPK1/ERK2 or by some cyclin-dependent
CC kinases such as CDK1,CDK2 or CDK5 (PubMed:30611118). Following adenylyl
CC cyclase activation, dephosphorylated at Ser-162 and Ser-273 resulting
CC in its dissociation from 14-3-3 proteins probably promoting CRTC3
CC translocation into the nucleus (PubMed:30611118).
CC {ECO:0000250|UniProtKB:Q91X84, ECO:0000269|PubMed:30611118}.
CC -!- SIMILARITY: Belongs to the TORC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC03424.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY360173; AAQ98858.1; -; mRNA.
DR EMBL; AK090443; BAC03424.1; ALT_FRAME; mRNA.
DR EMBL; AC021422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC103739; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK025521; BAB15160.1; -; mRNA.
DR EMBL; BC074730; AAH74730.2; -; mRNA.
DR EMBL; BC074731; AAH74731.3; -; mRNA.
DR CCDS; CCDS32331.1; -. [Q6UUV7-1]
DR CCDS; CCDS45348.1; -. [Q6UUV7-3]
DR RefSeq; NP_001036039.1; NM_001042574.2. [Q6UUV7-3]
DR RefSeq; NP_073606.3; NM_022769.4. [Q6UUV7-1]
DR AlphaFoldDB; Q6UUV7; -.
DR SMR; Q6UUV7; -.
DR BioGRID; 122294; 53.
DR DIP; DIP-59211N; -.
DR IntAct; Q6UUV7; 29.
DR STRING; 9606.ENSP00000268184; -.
DR GlyGen; Q6UUV7; 10 sites, 2 O-linked glycans (10 sites).
DR iPTMnet; Q6UUV7; -.
DR PhosphoSitePlus; Q6UUV7; -.
DR BioMuta; CRTC3; -.
DR DMDM; 167009130; -.
DR EPD; Q6UUV7; -.
DR jPOST; Q6UUV7; -.
DR MassIVE; Q6UUV7; -.
DR MaxQB; Q6UUV7; -.
DR PaxDb; Q6UUV7; -.
DR PeptideAtlas; Q6UUV7; -.
DR PRIDE; Q6UUV7; -.
DR ProteomicsDB; 67424; -. [Q6UUV7-1]
DR ProteomicsDB; 67425; -. [Q6UUV7-3]
DR Antibodypedia; 37539; 147 antibodies from 27 providers.
DR DNASU; 64784; -.
DR Ensembl; ENST00000268184.11; ENSP00000268184.6; ENSG00000140577.17. [Q6UUV7-1]
DR Ensembl; ENST00000420329.6; ENSP00000416573.2; ENSG00000140577.17. [Q6UUV7-3]
DR Ensembl; ENST00000691029.1; ENSP00000510507.1; ENSG00000140577.17. [Q6UUV7-1]
DR GeneID; 64784; -.
DR KEGG; hsa:64784; -.
DR MANE-Select; ENST00000268184.11; ENSP00000268184.6; NM_022769.5; NP_073606.3.
DR UCSC; uc002bpo.5; human. [Q6UUV7-1]
DR CTD; 64784; -.
DR DisGeNET; 64784; -.
DR GeneCards; CRTC3; -.
DR HGNC; HGNC:26148; CRTC3.
DR HPA; ENSG00000140577; Low tissue specificity.
DR MIM; 608986; gene.
DR neXtProt; NX_Q6UUV7; -.
DR OpenTargets; ENSG00000140577; -.
DR PharmGKB; PA142672074; -.
DR VEuPathDB; HostDB:ENSG00000140577; -.
DR eggNOG; ENOG502QV9G; Eukaryota.
DR GeneTree; ENSGT00390000010652; -.
DR HOGENOM; CLU_019357_3_0_1; -.
DR InParanoid; Q6UUV7; -.
DR OMA; EAQDSFH; -.
DR PhylomeDB; Q6UUV7; -.
DR TreeFam; TF321571; -.
DR PathwayCommons; Q6UUV7; -.
DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR Reactome; R-HSA-400253; Circadian Clock.
DR Reactome; R-HSA-9707616; Heme signaling.
DR SignaLink; Q6UUV7; -.
DR SIGNOR; Q6UUV7; -.
DR BioGRID-ORCS; 64784; 27 hits in 1089 CRISPR screens.
DR ChiTaRS; CRTC3; human.
DR GeneWiki; CRTC3; -.
DR GenomeRNAi; 64784; -.
DR Pharos; Q6UUV7; Tbio.
DR PRO; PR:Q6UUV7; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q6UUV7; protein.
DR Bgee; ENSG00000140577; Expressed in endothelial cell and 202 other tissues.
DR ExpressionAtlas; Q6UUV7; baseline and differential.
DR Genevisible; Q6UUV7; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008140; F:cAMP response element binding protein binding; IBA:GO_Central.
DR GO; GO:0097009; P:energy homeostasis; IEA:Ensembl.
DR GO; GO:0016042; P:lipid catabolic process; IEA:Ensembl.
DR GO; GO:0042116; P:macrophage activation; IMP:CACAO.
DR GO; GO:0071878; P:negative regulation of adenylate cyclase-activating adrenergic receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0050995; P:negative regulation of lipid catabolic process; IEA:Ensembl.
DR GO; GO:0032793; P:positive regulation of CREB transcription factor activity; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0051289; P:protein homotetramerization; IEA:InterPro.
DR InterPro; IPR024786; TORC.
DR InterPro; IPR024785; TORC_C.
DR InterPro; IPR024784; TORC_M.
DR InterPro; IPR024783; TORC_N.
DR PANTHER; PTHR13589; PTHR13589; 1.
DR Pfam; PF12886; TORC_C; 1.
DR Pfam; PF12885; TORC_M; 1.
DR Pfam; PF12884; TORC_N; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cytoplasm; Host-virus interaction;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..619
FT /note="CREB-regulated transcription coactivator 3"
FT /id="PRO_0000318531"
FT REGION 1..103
FT /note="Required for interaction with HTLV-1 TAX"
FT REGION 103..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..401
FT /note="Required for interaction with PPP2CA and PPP2R1A"
FT /evidence="ECO:0000250|UniProtKB:Q91X84"
FT COMPBIAS 122..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 160
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q91X84"
FT MOD_RES 162
FT /note="Phosphoserine; by SIK2"
FT /evidence="ECO:0000250|UniProtKB:Q91X84"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:30611118"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:30611118,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332"
FT CROSSLNK 232
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 551
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693554"
FT /id="VSP_031220"
FT VARIANT 72
FT /note="S -> N (in dbSNP:rs8033595)"
FT /evidence="ECO:0000269|PubMed:12693554,
FT ECO:0000269|PubMed:14506290"
FT /id="VAR_038758"
FT VARIANT 346
FT /note="L -> S"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038759"
FT MUTAGEN 282
FT /note="Y->F: Translocates to the cytoplasm. Represses basal
FT TORC3 activity towards CREB."
FT /evidence="ECO:0000269|PubMed:15454081"
FT CONFLICT 545
FT /note="P -> S (in Ref. 4; BAB15160)"
FT /evidence="ECO:0000305"
FT CONFLICT 616
FT /note="A -> T (in Ref. 2; BAC03424)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 619 AA; 66959 MW; A274B96DD1C2678E CRC64;
MAASPGSGSA NPRKFSEKIA LHTQRQAEET RAFEQLMTDL TLSRVQFQKL QQLRLTQYHG
GSLPNVSQLR SSASEFQPSF HQADNVRGTR HHGLVERPSR NRFHPLHRRS GDKPGRQFDG
SAFGANYSSQ PLDESWPRQQ PPWKDEKHPG FRLTSALNRT NSDSALHTSA LSTKPQDPYG
GGGQSAWPAP YMGFCDGENN GHGEVASFPG PLKEENLLNV PKPLPKQLWE TKEIQSLSGR
PRSCDVGGGN AFPHNGQNLG LSPFLGTLNT GGSLPDLTNL HYSTPLPASL DTTDHHFGSM
SVGNSVNNIP AAMTHLGIRS SSGLQSSRSN PSIQATLNKT VLSSSLNNHP QTSVPNASAL
HPSLRLFSLS NPSLSTTNLS GPSRRRQPPV SPLTLSPGPE AHQGFSRQLS STSPLAPYPT
SQMVSSDRSQ LSFLPTEAQA QVSPPPPYPA PQELTQPLLQ QPRAPEAPAQ QPQAASSLPQ
SDFQLLPAQG SSLTNFFPDV GFDQQSMRPG PAFPQQVPLV QQGSRELQDS FHLRPSPYSN
CGSLPNTILP EDSSTSLFKD LNSALAGLPE VSLNVDTPFP LEEELQIEPL SLDGLNMLSD
SSMGLLDPSV EETFRADRL
