ID CRTC2_MOUSE Reviewed; 692 AA. AC Q3U182; Q3TA52; Q8BH09; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 2. DT 24-JAN-2024, entry version 134. DE RecName: Full=CREB-regulated transcription coactivator 2; DE AltName: Full=Transducer of regulated cAMP response element-binding protein 2; DE Short=TORC-2; DE Short=Transducer of CREB protein 2; GN Name=Crtc2; Synonyms=Torc2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=NOD; TISSUE=Spleen; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver, Mammary tumor, and Salivary gland; 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 [3] RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-171, AND TISSUE RP SPECIFICITY. RX PubMed=16148943; DOI=10.1038/nature03967; RA Koo S.-H., Flechner L., Qi L., Zhang X., Screaton R.A., Jeffries S., RA Hedrick S., Xu W., Boussouar F., Brindle P., Takemori H., Montminy M.; RT "The CREB coactivator TORC2 is a key regulator of fasting glucose RT metabolism."; RL Nature 437:1109-1111(2005). RN [4] RP FUNCTION, PHOSPHORYLATION AT SER-171, AND SUBCELLULAR LOCATION. RX PubMed=16308421; DOI=10.1126/science.1120781; RA Shaw R.J., Lamia K.A., Vasquez D., Koo S.-H., Bardeesy N., Depinho R.A., RA Montminy M., Cantley L.C.; RT "The kinase LKB1 mediates glucose homeostasis in liver and therapeutic RT effects of metformin."; RL Science 310:1642-1646(2005). RN [5] RP INTERACTION WITH COP1, PHOSPHORYLATION AT SER-171, SUBCELLULAR LOCATION, RP AND MUTAGENESIS OF SER-171; VAL-214; PRO-215 AND LYS-628. RX PubMed=17805301; DOI=10.1038/nature06128; RA Dentin R., Liu Y., Koo S.-H., Hedrick S., Vargas T., Heredia J., RA Yates J. III, Montminy M.; RT "Insulin modulates gluconeogenesis by inhibition of the coactivator RT TORC2."; RL Nature 449:366-369(2007). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-171; SER-434; RP SER-612; SER-622 AND SER-623, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [9] RP TISSUE SPECIFICITY. 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 [10] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-161, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryo; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [11] RP METHYLATION AT ARG-51; ARG-99; ARG-120; ARG-123; ARG-161 AND ARG-168. RX PubMed=24570487; DOI=10.1126/scisignal.2004479; RA Han H.S., Jung C.Y., Yoon Y.S., Choi S., Choi D., Kang G., Park K.G., RA Kim S.T., Koo S.H.; RT "Arginine methylation of CRTC2 is critical in the transcriptional control RT of hepatic glucose metabolism."; RL Sci. Signal. 7:RA19-RA19(2014). RN [12] RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-171. RX PubMed=29211348; DOI=10.1111/febs.14351; RA Sonntag T., Vaughan J.M., Montminy M.; RT "14-3-3 proteins mediate inhibitory effects of cAMP on salt-inducible RT kinases (SIKs)."; RL FEBS J. 285:467-480(2018). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-70; THR-169 AND RP SER-171, MUTAGENESIS OF SER-171 AND SER-275, AND INTERACTION WITH 14-3-3 RP PROTEINS. RX PubMed=28235073; DOI=10.1371/journal.pone.0173013; RA Sonntag T., Moresco J.J., Vaughan J.M., Matsumura S., Yates J.R. III, RA Montminy M.; RT "Analysis of a cAMP regulated coactivator family reveals an alternative RT phosphorylation motif for AMPK family members."; RL PLoS ONE 12:E0173013-E0173013(2017). RN [14] RP INTERACTION WITH YWHAE AND PPP3CA, AND PHOSPHORYLATION AT SER-171 AND RP SER-275. 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 (PubMed:29211348). Acts as a coactivator, in the SIK/TORC CC signaling pathway, being active when dephosphorylated CC (PubMed:29211348). Acts independently of CREB1 'Ser-133' CC phosphorylation. Enhances the interaction of CREB1 with TAF4. Regulates CC gluconeogenesis as a component of the LKB1/AMPK/TORC2 signaling CC pathway. Regulates the expression of specific genes such as the CC steroidogenic gene, StAR. Potent coactivator of PPARGC1A and inducer of CC mitochondrial biogenesis in muscle cells (By similarity). CC {ECO:0000250|UniProtKB:Q53ET0, ECO:0000269|PubMed:16148943, CC ECO:0000269|PubMed:16308421, ECO:0000269|PubMed:29211348}. CC -!- SUBUNIT: Binds, as a tetramer, through its N-terminal region, with the CC bZIP domain of CREB1. 'Arg-314' in the bZIP domain of CREB1 is CC essential for this interaction. Interaction, via its C-terminal, with CC TAF4, enhances recruitment of TAF4 to CREB1. Interacts with SIK2 (By CC similarity). Interacts with 14-3-3 proteins, YWHAB and YWHAG CC (PubMed:28235073). Interacts (probably when phosphorylated at Ser-171) CC with YWHAE (PubMed:30611118). Interacts with calmodulin-dependent CC catalytic subunit PPP3CA/calcineurin A (PubMed:30611118). Interaction CC with COP1 mediates nuclear export and degradation of CRTC2 CC (PubMed:17805301). {ECO:0000250|UniProtKB:Q53ET0, CC ECO:0000269|PubMed:17805301, ECO:0000269|PubMed:28235073, CC ECO:0000269|PubMed:30611118}. CC -!- INTERACTION: CC Q3U182; F6VAN0: Atf6; NbExp=2; IntAct=EBI-8018890, EBI-6171558; CC Q3U182; Q9R1A8: Cop1; NbExp=3; IntAct=EBI-8018890, EBI-15656898; CC Q3U182; P63328: Ppp3ca; NbExp=2; IntAct=EBI-8018890, EBI-397208; CC Q3U182; P18850: ATF6; Xeno; NbExp=2; IntAct=EBI-8018890, EBI-852157; CC Q3U182; P29994-1: Itpr1; Xeno; NbExp=2; IntAct=EBI-8018890, EBI-15683709; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16148943, CC ECO:0000269|PubMed:16308421, ECO:0000269|PubMed:17805301, CC ECO:0000269|PubMed:29211348}. Nucleus {ECO:0000269|PubMed:16148943, CC ECO:0000269|PubMed:16308421, ECO:0000269|PubMed:17805301, CC ECO:0000269|PubMed:29211348}. Note=Translocated from the nucleus to the CC cytoplasm on interaction of the phosphorylated form with 14-3-3 protein CC (By similarity). In response to cAMP levels and glucagon, relocated to CC the nucleus (PubMed:16148943). {ECO:0000250|UniProtKB:Q53ET0, CC ECO:0000269|PubMed:16148943}. CC -!- TISSUE SPECIFICITY: Expressed in the suprachiasmatic nucleus (SCN) of CC the brain. {ECO:0000269|PubMed:23699513}. CC -!- PTM: Phosphorylation/dephosphorylation states of Ser-171 are required CC for regulating transduction of CREB activity (PubMed:29211348). CC CRTCs/TORCs are inactive when phosphorylated, and active when CC dephosphorylated at this site (PubMed:29211348). This primary site of CC phosphorylation, is regulated by cAMP and calcium levels and is CC dependent on the phosphorylation of SIKs (SIK1 and SIK2) by LKB1 (By CC similarity). Following adenylyl cyclase activation, dephosphorylated at CC Ser-171 by PPP3CA/calcineurin A resulting in CRTC2 dissociation from CC 14-3-3 proteins and PPP3CA (PubMed:30611118). Phosphorylation at Ser- CC 275 by MARK2 is induced under low glucose conditions and CC dephosphorylated in response to glucose influx (By similarity). Both CC insulin and AMPK increase this phosphorylation of CRTC2 while glucagon CC suppresses it (By similarity). Phosphorylation at Ser-275 promotes CC interaction with 14-3-3 proteins and translocation to the cytoplasm (By CC similarity). {ECO:0000250|UniProtKB:Q53ET0, CC ECO:0000269|PubMed:29211348, ECO:0000269|PubMed:30611118}. CC -!- PTM: Asymmetric dimethylation of arginine resisues by PRMT6 enhances CC the association of CRTC2 with CREB on the promoters of gluconeogenic CC genes. {ECO:0000269|PubMed:24570487}. CC -!- SIMILARITY: Belongs to the TORC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK156192; BAE33618.1; -; mRNA. DR EMBL; AK172084; BAE42818.1; -; mRNA. DR EMBL; BC023831; AAH23831.1; -; mRNA. DR EMBL; BC032183; AAH32183.1; -; mRNA. DR EMBL; BC033300; AAH33300.1; -; mRNA. DR CCDS; CCDS38501.1; -. DR RefSeq; NP_083157.1; NM_028881.2. DR PDB; 5ZK1; X-ray; 3.05 A; C=17-58. DR PDB; 5ZKO; X-ray; 3.05 A; G/H=1-80. DR PDBsum; 5ZK1; -. DR PDBsum; 5ZKO; -. DR AlphaFoldDB; Q3U182; -. DR SMR; Q3U182; -. DR BioGRID; 216678; 9. DR DIP; DIP-46162N; -. DR ELM; Q3U182; -. DR IntAct; Q3U182; 11. DR STRING; 10090.ENSMUSP00000029545; -. DR GlyGen; Q3U182; 6 sites, 1 O-linked glycan (6 sites). DR iPTMnet; Q3U182; -. DR PhosphoSitePlus; Q3U182; -. DR EPD; Q3U182; -. DR jPOST; Q3U182; -. DR MaxQB; Q3U182; -. DR PaxDb; 10090-ENSMUSP00000029545; -. DR PeptideAtlas; Q3U182; -. DR ProteomicsDB; 285309; -. DR Pumba; Q3U182; -. DR Antibodypedia; 34141; 673 antibodies from 40 providers. DR DNASU; 74343; -. DR Ensembl; ENSMUST00000029545.15; ENSMUSP00000029545.9; ENSMUSG00000027936.19. DR GeneID; 74343; -. DR KEGG; mmu:74343; -. DR UCSC; uc008qbt.2; mouse. DR AGR; MGI:1921593; -. DR CTD; 200186; -. DR MGI; MGI:1921593; Crtc2. DR VEuPathDB; HostDB:ENSMUSG00000027936; -. DR eggNOG; ENOG502QVWA; Eukaryota. DR GeneTree; ENSGT00390000010652; -. DR InParanoid; Q3U182; -. DR OMA; YPRHIID; -. DR OrthoDB; 2906223at2759; -. DR PhylomeDB; Q3U182; -. DR TreeFam; TF321571; -. DR BioGRID-ORCS; 74343; 4 hits in 79 CRISPR screens. DR PRO; PR:Q3U182; -. DR Proteomes; UP000000589; Chromosome 3. DR RNAct; Q3U182; Protein. DR Bgee; ENSMUSG00000027936; Expressed in retinal neural layer and 211 other cell types or tissues. DR ExpressionAtlas; Q3U182; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0008140; F:cAMP response element binding protein binding; IBA:GO_Central. DR GO; GO:0003682; F:chromatin binding; ISO:MGI. DR GO; GO:0006094; P:gluconeogenesis; IDA:UniProtKB. DR GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB. DR GO; GO:0032793; P:positive regulation of CREB transcription factor activity; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI. 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; CREB-REGULATED TRANSCRIPTION COACTIVATOR; 1. DR PANTHER; PTHR13589:SF6; CREB-REGULATED TRANSCRIPTION COACTIVATOR 2; 1. DR Pfam; PF12886; TORC_C; 1. DR Pfam; PF12885; TORC_M; 1. DR Pfam; PF12884; TORC_N; 1. DR Genevisible; Q3U182; MM. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Cytoplasm; Isopeptide bond; KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Transcription; KW Transcription regulation; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:Q53ET0" FT CHAIN 2..692 FT /note="CREB-regulated transcription coactivator 2" FT /id="PRO_0000318529" FT REGION 1..30 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 209..215 FT /note="Required for interaction with COP1" FT /evidence="ECO:0000269|PubMed:17805301" FT REGION 283..307 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 336..484 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 272..288 FT /note="Nuclear export signal" FT /evidence="ECO:0000250" FT COMPBIAS 1..24 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 339..414 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 448..476 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 628 FT /note="Required for ubiquitination and degradation" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:Q53ET0" FT MOD_RES 51 FT /note="Asymmetric dimethylarginine; by PRMT6" FT /evidence="ECO:0000269|PubMed:24570487" FT MOD_RES 70 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:28235073, FT ECO:0007744|PubMed:21183079" FT MOD_RES 86 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q53ET0" FT MOD_RES 90 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q53ET0" FT MOD_RES 99 FT /note="Asymmetric dimethylarginine; by PRMT6" FT /evidence="ECO:0000269|PubMed:24570487" FT MOD_RES 120 FT /note="Asymmetric dimethylarginine; by PRMT6" FT /evidence="ECO:0000269|PubMed:24570487" FT MOD_RES 123 FT /note="Asymmetric dimethylarginine; by PRMT6" FT /evidence="ECO:0000269|PubMed:24570487" FT MOD_RES 136 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q53ET0" FT MOD_RES 161 FT /note="Asymmetric dimethylarginine; by PRMT6" FT /evidence="ECO:0000269|PubMed:24570487, FT ECO:0007744|PubMed:24129315" FT MOD_RES 168 FT /note="Asymmetric dimethylarginine; by PRMT6" FT /evidence="ECO:0000269|PubMed:24570487" FT MOD_RES 169 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:28235073" FT MOD_RES 171 FT /note="Phosphoserine; by AMPK, MARK2, SIK1 and SIK2" FT /evidence="ECO:0000269|PubMed:16148943, FT ECO:0000269|PubMed:16308421, ECO:0000269|PubMed:17805301, FT ECO:0000269|PubMed:28235073, ECO:0000269|PubMed:29211348, FT ECO:0000269|PubMed:30611118, ECO:0007744|PubMed:21183079" FT MOD_RES 192 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q53ET0" FT MOD_RES 275 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:30611118" FT MOD_RES 307 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q53ET0" FT MOD_RES 369 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q53ET0" FT MOD_RES 394 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q53ET0" FT MOD_RES 434 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 457 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q53ET0" FT MOD_RES 489 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q53ET0" FT MOD_RES 490 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q53ET0" FT MOD_RES 493 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q53ET0" FT MOD_RES 502 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q53ET0" FT MOD_RES 612 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 622 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 623 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT CROSSLNK 235 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q53ET0" FT MUTAGEN 171 FT /note="S->A: Up-regulates CREB transcription factor FT activity. Reduces interaction with 14-3-3 proteins." FT /evidence="ECO:0000269|PubMed:28235073" FT MUTAGEN 171 FT /note="S->A: Up-regulates CREB-mediated gluconeogenic gene FT expression. No degradation of CRTC2. Loss of SIK2-mediated FT phosphorylation." FT /evidence="ECO:0000269|PubMed:17805301" FT MUTAGEN 213 FT /note="K->R: No effect on COP1-mediated degradation of FT TORC1 under forksolin stimulation." FT MUTAGEN 214 FT /note="V->A: No interaction with COP1. Inhibition of FT degradation under exposure to FSK/INS." FT /evidence="ECO:0000269|PubMed:17805301" FT MUTAGEN 215 FT /note="P->A: No interaction with COP1. Inhibition of FT degradation under exposure to FSK/INS." FT /evidence="ECO:0000269|PubMed:17805301" FT MUTAGEN 275 FT /note="S->A: Does not affect interaction with 14-3-3 FT proteins." FT /evidence="ECO:0000269|PubMed:28235073" FT MUTAGEN 628 FT /note="K->R: Translocates to the nucleus and no FT COP1-mediated degradation." FT /evidence="ECO:0000269|PubMed:17805301" FT CONFLICT 195 FT /note="S -> G (in Ref. 1; BAE33618)" FT /evidence="ECO:0000305" FT CONFLICT 203 FT /note="G -> R (in Ref. 1; BAE42818)" FT /evidence="ECO:0000305" FT HELIX 22..44 FT /evidence="ECO:0007829|PDB:5ZK1" FT HELIX 48..55 FT /evidence="ECO:0007829|PDB:5ZK1" SQ SEQUENCE 692 AA; 73216 MW; 5BCBC416D45CFAD8 CRC64; MATSGANGPG SATASASNPR KFSEKIALQK QRQAEETAAF EEVMMDIGST RLQAQKLRLA YTRSSHYGGS LPNVNQIGCG LAEFQSPLHS PLDSSRSTRH HGLVERVQRD ARRMVSPLRR YPRHIDSSPY SPAYLSPPPE SGWRRMMPWG NLPAEKGQLF RLPSALNRTS SDSALHTSVM NPNPQDTYPG PTPPSVLPSR RGGGFLDGEM DAKVPAIEEN VVDDKHLLKP WDAKKLSSSS SRPRSCEVPG INIFPSPDQP ANVPVLPPAM NTGGSLPDLT NLHFPPPLPT PLDPEETVYP SLSGGNSTTN LTHTMTHLGI SGGLGLGPSY DVPGLHSPLS HPSLQSSLSN PNLQASLSSP QPQLQGSHSH PSLPASSLAH HALPTTSLGH PSLSAPALSS SSSSSSTSSP VLSAPPYPAS TPGASPRHRR VPLSPLSLPA GPADARRSQQ QLPKQFSPTM SPTLSSITQG VPLDTSKLPT DQRLPPYPYS PPSLVIPTHP PTPKSLQQLP SQACLVQPSG GQPPGRQPHY GALYPPGSSG HGQQPYHRPI NDFSLGNLEQ FNMESPSTSL VLDPPAFSEG PGFLGSEGSM SGPQDPHVLN HQNLTHCSRH GSGPNIILTG DSSPGFSKEI AAALAGVPGF EVSASGLELG LGLEDELRME PLGLEGLTML SDPCALLPDP AVEDSFRSDR LQ //