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CREB-regulated transcription coactivator 3 (Transducer of regulated cAMP response element-binding protein 3) (TORC-3) (Transducer of CREB protein 3)

 CRTC3_HUMAN             Reviewed;         619 AA.
Q6UUV7; Q6DK61; Q6DK62; Q8NF38; Q9H6U2;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
05-FEB-2008, sequence version 2.
12-SEP-2018, entry version 110.
RecName: Full=CREB-regulated transcription coactivator 3;
AltName: Full=Transducer of regulated cAMP response element-binding protein 3;
Short=TORC-3;
Short=Transducer of CREB protein 3;
Name=CRTC3; Synonyms=TORC3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, INTERACTION WITH CREB1, AND VARIANT ASN-72.
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] (ISOFORM 3), AND VARIANT
ASN-72.
TISSUE=Spleen;
PubMed=12693554; DOI=10.1093/dnares/10.1.49;
Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N.,
Ohara O.;
"Characterization of long cDNA clones from human adult spleen. II. The
complete sequences of 81 cDNA clones.";
DNA Res. 10:49-57(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 217-619 (ISOFORM 1).
TISSUE=Hepatoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 292-619 (ISOFORM 1), AND
VARIANT SER-346.
TISSUE=Brain;
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).
[6]
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).
[7]
SUBCELLULAR LOCATION, FUNCTION, AND MUTAGENESIS OF TYR-282.
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).
[8]
INTERACTION WITH HTLV-1 TAX (MICROBIAL INFECTION), AND FUNCTION.
PubMed=15466468; DOI=10.1074/jbc.M409021200;
Koga H., Ohshima T., Shimotohno K.;
"Enhanced activation of tax-dependent transcription of human T-cell
leukemia virus type I (HTLV-I) long terminal repeat by TORC3.";
J. Biol. Chem. 279:52978-52983(2004).
[9]
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).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
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).
[12]
INTERACTION WITH HTLV-1 TAX (MICROBIAL INFECTION).
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).
[13]
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).
[14]
INTERACTION WITH BCL3 IN BCL3/TORC3/CREB1 COMPLEX, AND FUNCTION.
PubMed=17644518; DOI=10.1074/jbc.M702656200;
Hishiki T., Ohshima T., Ego T., Shimotohno K.;
"BCL3 acts as a negative regulator of transcription from the human T-
cell leukemia virus type 1 long terminal repeat through interactions
with TORC3.";
J. Biol. Chem. 282:28335-28343(2007).
[15]
FUNCTION.
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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443, 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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391 AND SER-443, 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).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329; SER-370 AND
SER-443, 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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, 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).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-62; SER-329;
SER-332; SER-370; SER-391; SER-396 AND SER-410, 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).
[22]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-232, 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).
-!- 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 the expression of
specific CREB-activated 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:15454081, ECO:0000269|PubMed:15466468,
ECO:0000269|PubMed:16817901, ECO:0000269|PubMed:16980408,
ECO:0000269|PubMed:17210223, ECO:0000269|PubMed:17644518}.
-!- SUBUNIT: Binding, as a tetramer, through its N-terminal region,
with the bZIP domain of CREB1 enhances recruitment of TAF4 to the
promoter (PubMed:14506290). 'Arg-314' in the bZIP domain of CREB1
is essential for this interaction (By similarity). Interacts, via
the N-terminal with the ankyrin repeats of BCL3, to form a complex
with CREB1 on CRE and TxRE responsive elements and represses HTLV-
1 LTR-mediated transcription (PubMed:17644518).
{ECO:0000250|UniProtKB:Q91X84, ECO:0000269|PubMed:14506290,
ECO:0000269|PubMed:17644518}.
-!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 protein Tax;
this interaction enhances tax transcriptional activity.
{ECO:0000269|PubMed:15466468, ECO:0000269|PubMed:16809310}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15454081,
ECO:0000269|PubMed:15589160, ECO:0000269|PubMed:16817901}.
Cytoplasm {ECO:0000269|PubMed:15589160,
ECO:0000269|PubMed:16817901}. Note=Appears to be mainly nuclear.
{ECO:0000269|PubMed:15454081}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q6UUV7-1; Sequence=Displayed;
Name=3;
IsoId=Q6UUV7-3; Sequence=VSP_031220;
-!- TISSUE SPECIFICITY: Predominantly expressed in B and T
lymphocytes. Highest levels in lung. Also expressed in brain,
colon, heart, kidney, ovary, and prostate. Weak expression in
liver, pancreas, muscle, small intestine, spleen and stomach.
{ECO:0000269|PubMed:14536081, ECO:0000269|PubMed:16980408}.
-!- SIMILARITY: Belongs to the TORC family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC03424.1; Type=Frameshift; Positions=82; Evidence={ECO:0000305};
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EMBL; AY360173; AAQ98858.1; -; mRNA.
EMBL; AK090443; BAC03424.1; ALT_FRAME; mRNA.
EMBL; AC021422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC103739; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK025521; BAB15160.1; -; mRNA.
EMBL; BC074730; AAH74730.2; -; mRNA.
EMBL; BC074731; AAH74731.3; -; mRNA.
CCDS; CCDS32331.1; -. [Q6UUV7-1]
CCDS; CCDS45348.1; -. [Q6UUV7-3]
RefSeq; NP_001036039.1; NM_001042574.2. [Q6UUV7-3]
RefSeq; NP_073606.3; NM_022769.4. [Q6UUV7-1]
UniGene; Hs.567572; -.
ProteinModelPortal; Q6UUV7; -.
SMR; Q6UUV7; -.
BioGrid; 122294; 32.
DIP; DIP-59211N; -.
IntAct; Q6UUV7; 21.
STRING; 9606.ENSP00000268184; -.
iPTMnet; Q6UUV7; -.
PhosphoSitePlus; Q6UUV7; -.
BioMuta; CRTC3; -.
DMDM; 167009130; -.
EPD; Q6UUV7; -.
MaxQB; Q6UUV7; -.
PaxDb; Q6UUV7; -.
PeptideAtlas; Q6UUV7; -.
PRIDE; Q6UUV7; -.
ProteomicsDB; 67424; -.
ProteomicsDB; 67425; -. [Q6UUV7-3]
Ensembl; ENST00000268184; ENSP00000268184; ENSG00000140577. [Q6UUV7-1]
Ensembl; ENST00000420329; ENSP00000416573; ENSG00000140577. [Q6UUV7-3]
GeneID; 64784; -.
KEGG; hsa:64784; -.
UCSC; uc002bpo.5; human. [Q6UUV7-1]
CTD; 64784; -.
DisGeNET; 64784; -.
EuPathDB; HostDB:ENSG00000140577.15; -.
GeneCards; CRTC3; -.
HGNC; HGNC:26148; CRTC3.
HPA; HPA043735; -.
HPA; HPA063691; -.
MIM; 608986; gene.
neXtProt; NX_Q6UUV7; -.
OpenTargets; ENSG00000140577; -.
PharmGKB; PA142672074; -.
eggNOG; ENOG410IGNT; Eukaryota.
eggNOG; ENOG410XPDQ; LUCA.
GeneTree; ENSGT00390000010652; -.
HOGENOM; HOG000111980; -.
HOVERGEN; HBG058314; -.
InParanoid; Q6UUV7; -.
KO; K16334; -.
OMA; GFCDGEN; -.
OrthoDB; EOG091G03YN; -.
PhylomeDB; Q6UUV7; -.
TreeFam; TF321571; -.
Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
Reactome; R-HSA-400253; Circadian Clock.
SIGNOR; Q6UUV7; -.
ChiTaRS; CRTC3; human.
GeneWiki; CRTC3; -.
GenomeRNAi; 64784; -.
PRO; PR:Q6UUV7; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000140577; Expressed in 240 organ(s), highest expression level in female gonad.
CleanEx; HS_CRTC3; -.
ExpressionAtlas; Q6UUV7; baseline and differential.
Genevisible; Q6UUV7; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
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:0097009; P:energy homeostasis; IEA:Ensembl.
GO; GO:0042116; P:macrophage activation; IMP:CACAO.
GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; IEA:Ensembl.
GO; GO:0050995; P:negative regulation of lipid catabolic process; IEA:Ensembl.
GO; GO:0032793; P:positive regulation of CREB transcription factor activity; IBA:GO_Central.
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: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;
Activator; Alternative splicing; Complete proteome; Cytoplasm;
Host-virus interaction; Isopeptide bond; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 619 CREB-regulated transcription coactivator
3.
/FTId=PRO_0000318531.
REGION 1 103 Required for interaction with HTLV-1 TAX.
COMPBIAS 180 183 Poly-Gly.
COMPBIAS 444 451 Poly-Pro.
MOD_RES 4 4 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163}.
MOD_RES 62 62 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 160 160 Phosphothreonine.
{ECO:0000250|UniProtKB:Q91X84}.
MOD_RES 162 162 Phosphoserine; by SIK2.
{ECO:0000250|UniProtKB:Q91X84}.
MOD_RES 273 273 Phosphoserine.
{ECO:0000250|UniProtKB:Q91X84}.
MOD_RES 329 329 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 332 332 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 370 370 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 391 391 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 396 396 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 410 410 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 443 443 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
CROSSLNK 232 232 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 551 551 Missing (in isoform 3).
{ECO:0000303|PubMed:12693554}.
/FTId=VSP_031220.
VARIANT 72 72 S -> N (in dbSNP:rs8033595).
{ECO:0000269|PubMed:12693554,
ECO:0000269|PubMed:14506290}.
/FTId=VAR_038758.
VARIANT 346 346 L -> S. {ECO:0000269|PubMed:15489334}.
/FTId=VAR_038759.
MUTAGEN 282 282 Y->F: Translocates to the cytoplasm.
Represses basal TORC3 activity towards
CREB. {ECO:0000269|PubMed:15454081}.
CONFLICT 545 545 P -> S (in Ref. 4; BAB15160).
{ECO:0000305}.
CONFLICT 616 616 A -> T (in Ref. 2; BAC03424).
{ECO:0000305}.
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


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