CRTC1_HUMAN
ID CRTC1_HUMAN Reviewed; 634 AA.
AC Q6UUV9; A6NMG5; O75114; Q6Y3A3; Q7LDZ2; Q8IUL3; Q8IZ34; Q8IZL1; Q8N6W3;
AC Q96AI8; Q9H801;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=CREB-regulated transcription coactivator 1;
DE AltName: Full=Mucoepidermoid carcinoma translocated protein 1;
DE AltName: Full=Transducer of regulated cAMP response element-binding protein 1;
DE Short=TORC-1;
DE Short=Transducer of CREB protein 1;
GN Name=CRTC1 {ECO:0000312|HGNC:HGNC:16062};
GN Synonyms=KIAA0616 {ECO:0000312|EMBL:BAA31591.1},
GN MECT1 {ECO:0000312|HGNC:HGNC:16062}, TORC1 {ECO:0000312|EMBL:AAQ98856.1},
GN WAMTP1 {ECO:0000303|PubMed:14720503};
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] {ECO:0000305, ECO:0000312|EMBL:AAQ98856.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, AND INTERACTION
RP WITH CREB1.
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] {ECO:0000305, ECO:0000312|EMBL:AAK93832.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND CHROMOSOMAL TRANSLOCATION WITH
RP MAML2.
RX PubMed=12539049; DOI=10.1038/ng1083;
RA Tonon G., Modi S., Wu L., Kubo A., Coxon A.B., Komiya T., O'Neil K.,
RA Stover K., El-Naggar A., Griffin J.D., Kirsch I.R., Kaye F.J.;
RT "t(11;19)(q21;p13) translocation in mucoepidermoid carcinoma creates a
RT novel fusion product that disrupts a Notch signaling pathway.";
RL Nat. Genet. 33:208-213(2003).
RN [3]
RP ERRATUM OF PUBMED:12539049.
RA Tonon G., Modi S., Wu L., Kubo A., Coxon A.B., Komiya T., O'Neil K.,
RA Stover K., El-Naggar A., Griffin J.D., Kirsch I.R., Kaye F.J.;
RL Nat. Genet. 33:408-408(2003).
RN [4] {ECO:0000305, ECO:0000312|EMBL:BAB14822.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Embryo {ECO:0000312|EMBL:BAB14822.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAC97072.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000305, ECO:0000312|EMBL:AAH28050.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ILE-311
RP AND ALA-328.
RC TISSUE=Brain {ECO:0000312|EMBL:AAH28050.1}, Colon, and
RC Eye {ECO:0000312|EMBL:AAH23614.2};
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 [8] {ECO:0000305, ECO:0000312|EMBL:AAP12463.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-104 (ISOFORMS 1/3), TISSUE SPECIFICITY, AND
RP CHROMOSOMAL TRANSLOCATION WITH MAML2.
RC TISSUE=Carcinoma {ECO:0000269|PubMed:14720503};
RX PubMed=14720503; DOI=10.1016/j.yexcr.2003.09.007;
RA Enlund F., Behboudi A., Andren Y., Oberg C., Lendahl U., Mark J.,
RA Stenman G.;
RT "Altered Notch signaling resulting from expression of a WAMTP1-MAML2 gene
RT fusion in mucoepidermoid carcinomas and benign Warthin's tumors.";
RL Exp. Cell Res. 292:21-28(2004).
RN [9] {ECO:0000305, ECO:0000312|EMBL:BAA31591.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-634 (ISOFORM 2).
RC TISSUE=Brain {ECO:0000312|EMBL:BAA31591.1};
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [10] {ECO:0000305}
RP FUNCTION, SUBUNIT, AND INTERACTION WITH CREB1 AND TAF4.
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 [11]
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 [12] {ECO:0000305}
RP CHROMOSOMAL TRANSLOCATION.
RX PubMed=15729701; DOI=10.1002/gcc.20168;
RA Behboudi A., Winnes M., Gorunova L., van den Oord J.J., Mertens F.,
RA Enlund F., Stenman G.;
RT "Clear cell hidradenoma of the skin-a third tumor type with a t(11;19)-
RT associated TORC1-MAML2 gene fusion.";
RL Genes Chromosomes Cancer 43:202-205(2005).
RN [13]
RP FUNCTION, PHOSPHORYLATION AT SER-151, AND SUBCELLULAR LOCATION.
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 [14]
RP INTERACTION WITH HTLV-1 TAX (MICROBIAL INFECTION), AND FUNCTION (MICROBIAL
RP 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 [15]
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 [16]
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 [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161, AND IDENTIFICATION BY
RP 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 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 FUNCTION.
RX PubMed=23699513; DOI=10.1523/jneurosci.4202-12.2013;
RA Sakamoto K., Norona F.E., Alzate-Correa D., Scarberry D., Hoyt K.R.,
RA Obrietan K.;
RT "Clock and light regulation of the CREB coactivator CRTC1 in the
RT suprachiasmatic circadian clock.";
RL J. Neurosci. 33:9021-9027(2013).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION BY
RP MASS 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [23]
RP INTERACTION WITH YWHAE AND PPP3CA, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 PGC1alpha and inducer
CC of mitochondrial biogenesis in muscle cells. In the hippocampus,
CC involved in late-phase long-term potentiation (L-LTP) maintenance at
CC the Schaffer collateral-CA1 synapses. May be required for dendritic
CC growth of developing cortical neurons (By similarity). In concert with
CC SIK1, regulates the light-induced entrainment of the circadian clock.
CC In response to light stimulus, coactivates the CREB-mediated
CC transcription of PER1 which plays an important role in the photic
CC entrainment of the circadian clock. {ECO:0000250|UniProtKB:Q157S1,
CC ECO:0000250|UniProtKB:Q68ED7, ECO:0000269|PubMed:23699513}.
CC -!- FUNCTION: (Microbial infection) Plays a role of coactivator for TAX
CC activation of the human T-cell leukemia virus type 1 (HTLV-1) long
CC terminal repeats (LTR). {ECO:0000269|PubMed:16809310}.
CC -!- SUBUNIT: Binds, as a tetramer, through its N-terminal region, with the
CC bZIP domain of CREB1 (PubMed:14536081). 'Arg-314' in the bZIP domain of
CC CREB1 is essential for this interaction (PubMed:14536081). Interaction,
CC via its C-terminal, with TAF4, enhances recruitment of TAF4 to CREB1
CC (PubMed:14536081). Interacts with 14-3-3 proteins, including YWHAE/14-
CC 3-3 epsilon (PubMed:30611118). Interacts with calmodulin-dependent
CC catalytic subunit PPP3CA/calcineurin A (PubMed:30611118).
CC {ECO:0000269|PubMed:14536081, ECO:0000269|PubMed:30611118}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HTLV1 Tax.
CC {ECO:0000269|PubMed:16809310}.
CC -!- INTERACTION:
CC Q6UUV9; P16220: CREB1; NbExp=6; IntAct=EBI-1644259, EBI-711855;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15589160}. Nucleus
CC {ECO:0000269|PubMed:15589160}. Note=Cytoplasmic when phosphorylated by
CC SIK or AMPK and when sequestered by 14-3-3 proteins (PubMed:16817901).
CC Translocated to the nucleus on Ser-151 dephosphorylation, instigated by
CC a number of factors including calcium ion and cAMP levels
CC (PubMed:15589160). Light stimulation triggers a nuclear accumulation in
CC the suprachiasmatic nucleus (SCN) of the brain (By similarity).
CC {ECO:0000250|UniProtKB:Q68ED7, ECO:0000269|PubMed:15589160,
CC ECO:0000269|PubMed:16817901}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:14506290};
CC IsoId=Q6UUV9-1; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=Q6UUV9-2; Sequence=VSP_051749;
CC Name=3 {ECO:0000269|PubMed:12539049};
CC IsoId=Q6UUV9-3; Sequence=VSP_051750, VSP_051751;
CC -!- TISSUE SPECIFICITY: Highly expressed in adult and fetal brain. Located
CC to specific regions such as the prefrontal cortex and cerebellum. Very
CC low expression in other tissues such as heart, spleen, lung, skeletal
CC muscle, salivary gland, ovary and kidney. {ECO:0000269|PubMed:14720503,
CC ECO:0000269|PubMed:16980408}.
CC -!- PTM: Phosphorylation/dephosphorylation states of Ser-151 are required
CC for regulating transduction of CREB activity. TORCs are inactive when
CC phosphorylated, and active when dephosphorylated at this site. This
CC primary site of phosphorylation is mediated by SIKs (SIK1 and SIK2), is
CC regulated by cAMP and calcium levels and is dependent on the
CC phosphorylation of SIKs by LKB1 (By similarity).
CC {ECO:0000250|UniProtKB:Q68ED7}.
CC -!- DISEASE: Note=A chromosomal aberration involving CRTC1 is found in
CC mucoepidermoid carcinomas, benign Warthin tumors and clear cell
CC hidradenomas. Translocation t(11;19)(q21;p13) with MAML2. The fusion
CC protein consists of the N-terminus of CRTC1 joined to the C-terminus of
CC MAML2. The reciprocal fusion protein consisting of the N-terminus of
CC MAML2 joined to the C-terminus of CRTC1 has been detected in a small
CC number of mucoepidermoid carcinomas.
CC -!- SIMILARITY: Belongs to the TORC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17075.3; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH23614.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAP12463.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CRTC1ID471ch19p13.html";
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DR EMBL; AY360171; AAQ98856.1; -; mRNA.
DR EMBL; AY040323; AAK93832.1; -; mRNA.
DR EMBL; AY040324; AAK93833.1; ALT_TERM; mRNA.
DR EMBL; AK024089; BAB14822.1; -; mRNA.
DR EMBL; AC003107; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC006123; AAC97072.1; -; Genomic_DNA.
DR EMBL; CH471106; EAW84730.1; -; Genomic_DNA.
DR EMBL; BC017075; AAH17075.3; ALT_INIT; mRNA.
DR EMBL; BC023614; AAH23614.2; ALT_INIT; mRNA.
DR EMBL; BC028050; AAH28050.1; -; mRNA.
DR EMBL; AB014516; BAA31591.1; -; mRNA.
DR EMBL; AY186997; AAP12462.1; ALT_TERM; mRNA.
DR EMBL; AY186998; AAP12463.1; ALT_INIT; mRNA.
DR CCDS; CCDS32963.1; -. [Q6UUV9-1]
DR CCDS; CCDS42525.1; -. [Q6UUV9-2]
DR PIR; T00388; T00388.
DR RefSeq; NP_001091952.1; NM_001098482.1. [Q6UUV9-2]
DR RefSeq; NP_056136.2; NM_015321.2. [Q6UUV9-1]
DR PDB; 7D8H; X-ray; 2.42 A; B=59-69.
DR PDB; 7D8P; X-ray; 2.00 A; C/D=146-156.
DR PDB; 7D9V; X-ray; 2.21 A; C/D=240-250.
DR PDBsum; 7D8H; -.
DR PDBsum; 7D8P; -.
DR PDBsum; 7D9V; -.
DR AlphaFoldDB; Q6UUV9; -.
DR SMR; Q6UUV9; -.
DR BioGRID; 116952; 23.
DR IntAct; Q6UUV9; 10.
DR STRING; 9606.ENSP00000345001; -.
DR GlyGen; Q6UUV9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6UUV9; -.
DR PhosphoSitePlus; Q6UUV9; -.
DR BioMuta; CRTC1; -.
DR DMDM; 68565585; -.
DR EPD; Q6UUV9; -.
DR jPOST; Q6UUV9; -.
DR MassIVE; Q6UUV9; -.
DR MaxQB; Q6UUV9; -.
DR PaxDb; Q6UUV9; -.
DR PeptideAtlas; Q6UUV9; -.
DR PRIDE; Q6UUV9; -.
DR ProteomicsDB; 67426; -. [Q6UUV9-1]
DR ProteomicsDB; 67427; -. [Q6UUV9-2]
DR ProteomicsDB; 67428; -. [Q6UUV9-3]
DR Antibodypedia; 15141; 380 antibodies from 41 providers.
DR DNASU; 23373; -.
DR Ensembl; ENST00000321949.13; ENSP00000323332.7; ENSG00000105662.16. [Q6UUV9-1]
DR Ensembl; ENST00000338797.10; ENSP00000345001.5; ENSG00000105662.16. [Q6UUV9-2]
DR GeneID; 23373; -.
DR KEGG; hsa:23373; -.
DR MANE-Select; ENST00000321949.13; ENSP00000323332.7; NM_015321.3; NP_056136.2.
DR UCSC; uc002nkb.5; human. [Q6UUV9-1]
DR CTD; 23373; -.
DR DisGeNET; 23373; -.
DR GeneCards; CRTC1; -.
DR HGNC; HGNC:16062; CRTC1.
DR HPA; ENSG00000105662; Low tissue specificity.
DR MIM; 607536; gene.
DR neXtProt; NX_Q6UUV9; -.
DR OpenTargets; ENSG00000105662; -.
DR PharmGKB; PA30730; -.
DR VEuPathDB; HostDB:ENSG00000105662; -.
DR eggNOG; ENOG502QU41; Eukaryota.
DR GeneTree; ENSGT00390000010652; -.
DR HOGENOM; CLU_019357_2_0_1; -.
DR InParanoid; Q6UUV9; -.
DR OMA; FNMVEGA; -.
DR OrthoDB; 1118500at2759; -.
DR PhylomeDB; Q6UUV9; -.
DR TreeFam; TF321571; -.
DR PathwayCommons; Q6UUV9; -.
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; Q6UUV9; -.
DR SIGNOR; Q6UUV9; -.
DR BioGRID-ORCS; 23373; 18 hits in 1079 CRISPR screens.
DR ChiTaRS; CRTC1; human.
DR GeneWiki; CRTC1; -.
DR GenomeRNAi; 23373; -.
DR Pharos; Q6UUV9; Tbio.
DR PRO; PR:Q6UUV9; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q6UUV9; protein.
DR Bgee; ENSG00000105662; Expressed in type B pancreatic cell and 152 other tissues.
DR ExpressionAtlas; Q6UUV9; baseline and differential.
DR Genevisible; Q6UUV9; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0008140; F:cAMP response element binding protein binding; IDA:UniProtKB.
DR GO; GO:0097009; P:energy homeostasis; IEA:Ensembl.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB.
DR GO; GO:0007613; P:memory; IEA:Ensembl.
DR GO; GO:1902631; P:negative regulation of membrane hyperpolarization; IEA:Ensembl.
DR GO; GO:0032793; P:positive regulation of CREB transcription factor activity; ISS:UniProtKB.
DR GO; GO:1900006; P:positive regulation of dendrite development; IEA:Ensembl.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0099527; P:postsynapse to nucleus signaling pathway; IEA:Ensembl.
DR GO; GO:0051289; P:protein homotetramerization; IEA:InterPro.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
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 3D-structure; Activator; Alternative splicing; Biological rhythms;
KW Chromosomal rearrangement; Cytoplasm; Host-virus interaction; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..634
FT /note="CREB-regulated transcription coactivator 1"
FT /id="PRO_0000096354"
FT REGION 110..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 242..258
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 110..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..396
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..429
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 42..43
FT /note="Breakpoint for translocation to form the MECT1-MAML2
FT and MAML2-MECT1 fusion proteins"
FT /evidence="ECO:0000269|PubMed:12539049,
FT ECO:0000269|PubMed:14720503"
FT SITE 575
FT /note="Required for ubiquitination and degradation"
FT /evidence="ECO:0000250"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68ED7"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 149
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q68ED7"
FT MOD_RES 151
FT /note="Phosphoserine; by SIK1 and SIK2"
FT /evidence="ECO:0000269|PubMed:16817901"
FT MOD_RES 161
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 81
FT /note="Q -> QPSGFLGEALAAAPVSL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14506290,
FT ECO:0000303|PubMed:9734811"
FT /id="VSP_051749"
FT VAR_SEQ 475..503
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12539049,
FT ECO:0000303|PubMed:14506290, ECO:0000303|PubMed:14702039"
FT /id="VSP_051750"
FT VAR_SEQ 580..634
FT /note="SLAGVGDVSFDSDSQFPLDELKIDPLTLDGLHMLNDPDMVLADPATEDTFRM
FT DRL -> HRGHLPDGPPVSGHAGTLPLSRPDGASPARGRPCSVPRQRPSL (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:12539049,
FT ECO:0000303|PubMed:14506290, ECO:0000303|PubMed:14702039"
FT /id="VSP_051751"
FT VARIANT 286
FT /note="T -> A (in dbSNP:rs3746266)"
FT /id="VAR_053934"
FT VARIANT 311
FT /note="V -> I (in dbSNP:rs36070283)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_053935"
FT VARIANT 328
FT /note="T -> A (in dbSNP:rs3746266)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_053936"
FT CONFLICT 84
FT /note="F -> S (in Ref. 4; BAB14822)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="P -> S (in Ref. 4; BAB14822)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="S -> G (in Ref. 4; BAB14822)"
FT /evidence="ECO:0000305"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:7D8P"
SQ SEQUENCE 634 AA; 67300 MW; ECDC427FF9D6920B CRC64;
MATSNNPRKF SEKIALHNQK QAEETAAFEE VMKDLSLTRA ARLQLQKSQY LQLGPSRGQY
YGGSLPNVNQ IGSGTMDLPF QTPFQSSGLD TSRTTRHHGL VDRVYRERGR LGSPHRRPLS
VDKHGRQADS CPYGTMYLSP PADTSWRRTN SDSALHQSTM TPTQPESFSS GSQDVHQKRV
LLLTVPGMEE TTSEADKNLS KQAWDTKKTG SRPKSCEVPG INIFPSADQE NTTALIPATH
NTGGSLPDLT NIHFPSPLPT PLDPEEPTFP ALSSSSSTGN LAANLTHLGI GGAGQGMSTP
GSSPQHRPAG VSPLSLSTEA RRQQASPTLS PLSPITQAVA MDALSLEQQL PYAFFTQAGS
QQPPPQPQPP PPPPPASQQP PPPPPPQAPV RLPPGGPLLP SASLTRGPQP PPLAVTVPSS
LPQSPPENPG QPSMGIDIAS APALQQYRTS AGSPANQSPT SPVSNQGFSP GSSPQHTSTL
GSVFGDAYYE QQMAARQANA LSHQLEQFNM MENAISSSSL YSPGSTLNYS QAAMMGLTGS
HGSLPDSQQL GYASHSGIPN IILTVTGESP PSLSKELTSS LAGVGDVSFD SDSQFPLDEL
KIDPLTLDGL HMLNDPDMVL ADPATEDTFR MDRL
