ID CITE1_HUMAN Reviewed; 193 AA. AC Q99966; B5BU50; B5BUI2; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 2. DT 27-MAR-2024, entry version 178. DE RecName: Full=Cbp/p300-interacting transactivator 1; DE AltName: Full=Melanocyte-specific protein 1; GN Name=CITED1; Synonyms=MSG1; 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), AND VARIANT GLN-96. RX PubMed=8901575; DOI=10.1073/pnas.93.22.12298; RA Shioda T., Fenner M.H., Isselbacher K.J.; RT "msg1, a novel melanocyte-specific gene, encodes a nuclear protein and is RT associated with pigmentation."; RL Proc. Natl. Acad. Sci. U.S.A. 93:12298-12303(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLN-96. RX PubMed=19054851; DOI=10.1038/nmeth.1273; RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B., RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., RA Nomura N.; RT "Human protein factory for converting the transcriptome into an in vitro- RT expressed proteome."; RL Nat. Methods 5:1011-1017(2008). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLN-96. 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-96. 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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-86 (ISOFORM 2). RC TISSUE=Melanocyte; RA Hillier L., Allen M., Bowles L., Dubuque T., Geisel G., Jost S., RA Krizman D., Kucaba T., Lacy M., Le N., Lennon G., Marra M., Martin J., RA Moore B., Schellenberg K., Steptoe M., Tan F., Theising B., White Y., RA Wylie T., Waterston R., Wilson R.; RT "WashU-NCI human EST project."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. RN [7] RP INTERACTION WITH SMAD4. RX PubMed=9707553; DOI=10.1073/pnas.95.17.9785; RA Shioda T., Lechleider R.J., Dunwoodie S.L., Li H., Yahata T., RA de Caestecker M.P., Fenner M.H., Roberts A.B., Isselbacher K.J.; RT "Transcriptional activating activity of Smad4: roles of SMAD hetero- RT oligomerization and enhancement by an associating transactivator."; RL Proc. Natl. Acad. Sci. U.S.A. 95:9785-9790(1998). RN [8] RP FUNCTION, AND INTERACTION WITH CREBBP; EP300 AND HSPA8. RX PubMed=10722728; DOI=10.1074/jbc.275.12.8825; RA Yahata T., de Caestecker M.P., Lechleider R.J., Andriole S., Roberts A.B., RA Isselbacher K.J., Shioda T.; RT "The MSG1 non-DNA-binding transactivator binds to the p300/CBP RT coactivators, enhancing their functional link to the Smad transcription RT factors."; RL J. Biol. Chem. 275:8825-8834(2000). RN [9] RP FUNCTION, INTERACTION WITH ESR1, ASSOCIATION WITH CHROMATIN, AND RP MUTAGENESIS OF 155-GLU-GLU-156; 157-VAL-LEU-158; 159-MET-SER-160; RP 161-LEU-VAL-162; 163-VAL-GLU-164; LEU-165 AND 166-GLY-LEU-167. RX PubMed=11581164; DOI=10.1101/gad.906301; RA Yahata T., Shao W., Endoh H., Hur J., Coser K.R., Sun H., Ueda Y., Kato S., RA Isselbacher K.J., Brown M., Shioda T.; RT "Selective coactivation of estrogen-dependent transcription by CITED1 RT CBP/p300-binding protein."; RL Genes Dev. 15:2598-2612(2001). RN [10] RP INTERACTION WITH RBM14. RX PubMed=11443112; DOI=10.1074/jbc.m101517200; RA Iwasaki T., Chin W.W., Ko L.; RT "Identification and characterization of RRM-containing coactivator RT activator (CoAA) as TRBP-interacting protein, and its splice variant as a RT coactivator modulator (CoAM)."; RL J. Biol. Chem. 276:33375-33383(2001). RN [11] RP PHOSPHORYLATION, INTERACTION WITH EP300, SUBCELLULAR LOCATION, AND RP MUTAGENESIS OF SER-16; SER-63; SER-67; SER-71 AND SER-137. RX PubMed=16864582; DOI=10.1074/jbc.m602631200; RA Shi G., Boyle S.C., Sparrow D.B., Dunwoodie S.L., Shioda T., RA de Caestecker M.P.; RT "The transcriptional activity of CITED1 is regulated by phosphorylation in RT a cell cycle-dependent manner."; RL J. Biol. Chem. 281:27426-27435(2006). RN [12] 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 [13] RP FUNCTION, HOMODIMERIZATION, INDUCTION, AND INTERACTION WITH TOX3. RX PubMed=21172805; DOI=10.1242/jcs.068759; RA Dittmer S., Kovacs Z., Yuan S.H., Siszler G., Kogl M., Summer H., RA Geerts A., Golz S., Shioda T., Methner A.; RT "TOX3 is a neuronal survival factor that induces transcription depending on RT the presence of CITED1 or phosphorylated CREB in the transcriptionally RT active complex."; RL J. Cell Sci. 124:252-260(2011). RN [14] RP IDENTIFICATION BY 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). CC -!- FUNCTION: Transcriptional coactivator of the p300/CBP-mediated CC transcription complex. Enhances SMAD-mediated transcription by CC strengthening the functional link between the DNA-binding SMAD CC transcription factors and the p300/CBP transcription coactivator CC complex. Stimulates estrogen-dependent transactivation activity CC mediated by estrogen receptors signaling; stabilizes the interaction of CC estrogen receptor ESR1 and histone acetyltransferase EP300. Positively CC regulates TGF-beta signaling through its association with the CC SMAD/p300/CBP-mediated transcriptional coactivator complex. Induces CC transcription from estrogen-responsive promoters and protection against CC cell death. Potentiates EGR2-mediated transcriptional activation CC activity from the ERBB2 promoter. Acts as an inhibitor of osteoblastic CC mineralization through a cAMP-dependent parathyroid hormone receptor CC signaling. May play a role in pigmentation of melanocytes. Associates CC with chromatin to the estrogen-responsive TGF-alpha promoter region in CC a estrogen-dependent manner. {ECO:0000269|PubMed:10722728, CC ECO:0000269|PubMed:11581164, ECO:0000269|PubMed:21172805}. CC -!- SUBUNIT: Interacts (via C-terminus) with CREBBP. Interacts with EGR2 CC (By similarity). Homodimer. Binds to RBM14. Interacts (via N-terminus) CC with HSPA8; the interaction suppresses the association of CITED1 with CC p300/CBP and SMAD-mediated transcription transactivation. Interacts CC (via C-terminus) with TOX3 (via HGM box); the interaction increases CC estrogen-response element (ERE)-dependent transcription and protection CC against cell death. Interacts with ESR1; the interaction occurs in a CC estrogen-dependent manner (By similarity). Interacts (unphosphorylated CC form preferentially and via C-terminus) with EP300. {ECO:0000250, CC ECO:0000269|PubMed:10722728, ECO:0000269|PubMed:11443112, CC ECO:0000269|PubMed:11581164, ECO:0000269|PubMed:16864582, CC ECO:0000269|PubMed:21172805, ECO:0000269|PubMed:9707553}. CC -!- INTERACTION: CC Q99966; P15336: ATF2; NbExp=2; IntAct=EBI-2624951, EBI-1170906; CC Q99966; P55212: CASP6; NbExp=3; IntAct=EBI-2624951, EBI-718729; CC Q99966; P06307: CCK; NbExp=3; IntAct=EBI-2624951, EBI-6624398; CC Q99966; P03372: ESR1; NbExp=3; IntAct=EBI-2624951, EBI-78473; CC Q99966; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-2624951, EBI-10226858; CC Q99966; P05412: JUN; NbExp=2; IntAct=EBI-2624951, EBI-852823; CC Q99966; P13473-2: LAMP2; NbExp=3; IntAct=EBI-2624951, EBI-21591415; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16864582}. Cytoplasm CC {ECO:0000269|PubMed:16864582}. Note=Shuttles between the nucleus and CC the cytoplasm by a nuclear export signal and (NES) in a CRM1-dependent CC manner. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q99966-1; Sequence=Displayed; CC Name=2; CC IsoId=Q99966-2; Sequence=VSP_039897; CC -!- TISSUE SPECIFICITY: Expressed only in melanocytes and testis. CC -!- INDUCTION: Up-regulated by GPR39 in neuronal cells. CC {ECO:0000269|PubMed:21172805}. CC -!- PTM: Phosphorylated. Phosphorylation changes in a cell cycle-dependent CC manner and reduces its transcriptional coactivator activity. CC {ECO:0000269|PubMed:16864582}. CC -!- SIMILARITY: Belongs to the CITED family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=N30508; Type=Frameshift; Evidence={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; U65092; AAC51113.1; -; mRNA. DR EMBL; AB451286; BAG70100.1; -; mRNA. DR EMBL; AB451418; BAG70232.1; -; mRNA. DR EMBL; AL135749; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471213; EAW71819.1; -; Genomic_DNA. DR EMBL; BC004240; AAH04240.1; -; mRNA. DR EMBL; N30508; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS14419.1; -. [Q99966-1] DR CCDS; CCDS48136.1; -. [Q99966-2] DR PIR; JC6114; JC6114. DR RefSeq; NP_001138357.1; NM_001144885.1. [Q99966-2] DR RefSeq; NP_001138358.1; NM_001144886.1. [Q99966-1] DR RefSeq; NP_001138359.1; NM_001144887.1. [Q99966-1] DR RefSeq; NP_004134.2; NM_004143.3. [Q99966-1] DR RefSeq; XP_011529260.1; XM_011530958.1. DR AlphaFoldDB; Q99966; -. DR BioGRID; 110572; 37. DR CORUM; Q99966; -. DR IntAct; Q99966; 11. DR MINT; Q99966; -. DR STRING; 9606.ENSP00000401764; -. DR iPTMnet; Q99966; -. DR PhosphoSitePlus; Q99966; -. DR BioMuta; CITED1; -. DR DMDM; 296434447; -. DR MassIVE; Q99966; -. DR PaxDb; 9606-ENSP00000401764; -. DR PeptideAtlas; Q99966; -. DR ProteomicsDB; 78553; -. [Q99966-1] DR ProteomicsDB; 78554; -. [Q99966-2] DR Antibodypedia; 13694; 379 antibodies from 26 providers. DR DNASU; 4435; -. DR Ensembl; ENST00000246139.9; ENSP00000246139.5; ENSG00000125931.11. [Q99966-1] DR Ensembl; ENST00000373619.7; ENSP00000362721.3; ENSG00000125931.11. [Q99966-1] DR Ensembl; ENST00000431381.5; ENSP00000388548.1; ENSG00000125931.11. [Q99966-2] DR Ensembl; ENST00000445983.5; ENSP00000403274.1; ENSG00000125931.11. [Q99966-1] DR Ensembl; ENST00000453707.6; ENSP00000401764.2; ENSG00000125931.11. [Q99966-2] DR Ensembl; ENST00000651998.1; ENSP00000499148.1; ENSG00000125931.11. [Q99966-1] DR GeneID; 4435; -. DR KEGG; hsa:4435; -. DR MANE-Select; ENST00000651998.1; ENSP00000499148.1; NM_001144887.2; NP_001138359.1. DR UCSC; uc004eas.4; human. [Q99966-1] DR AGR; HGNC:1986; -. DR CTD; 4435; -. DR DisGeNET; 4435; -. DR GeneCards; CITED1; -. DR HGNC; HGNC:1986; CITED1. DR HPA; ENSG00000125931; Tissue enriched (epididymis). DR MIM; 300149; gene. DR neXtProt; NX_Q99966; -. DR OpenTargets; ENSG00000125931; -. DR PharmGKB; PA26523; -. DR VEuPathDB; HostDB:ENSG00000125931; -. DR eggNOG; ENOG502RZBF; Eukaryota. DR GeneTree; ENSGT00530000063624; -. DR HOGENOM; CLU_100627_0_0_1; -. DR InParanoid; Q99966; -. DR OrthoDB; 4213331at2759; -. DR PhylomeDB; Q99966; -. DR TreeFam; TF331915; -. DR PathwayCommons; Q99966; -. DR Reactome; R-HSA-8866907; Activation of the TFAP2 (AP-2) family of transcription factors. DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression. DR SignaLink; Q99966; -. DR SIGNOR; Q99966; -. DR BioGRID-ORCS; 4435; 16 hits in 779 CRISPR screens. DR ChiTaRS; CITED1; human. DR GeneWiki; CITED1; -. DR GenomeRNAi; 4435; -. DR Pharos; Q99966; Tbio. DR PRO; PR:Q99966; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q99966; Protein. DR Bgee; ENSG00000125931; Expressed in right testis and 96 other cell types or tissues. DR ExpressionAtlas; Q99966; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB. DR GO; GO:0070410; F:co-SMAD binding; IPI:BHF-UCL. DR GO; GO:0050693; F:LBD domain binding; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0007420; P:brain development; IEA:Ensembl. DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; ISS:UniProtKB. DR GO; GO:0060711; P:labyrinthine layer development; IEA:Ensembl. DR GO; GO:0042438; P:melanin biosynthetic process; ISS:UniProtKB. DR GO; GO:0030318; P:melanocyte differentiation; IEP:UniProtKB. DR GO; GO:0060231; P:mesenchymal to epithelial transition; TAS:BHF-UCL. DR GO; GO:0001656; P:metanephros development; TAS:BHF-UCL. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:UniProtKB. DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISS:UniProtKB. DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; TAS:BHF-UCL. DR GO; GO:0006913; P:nucleocytoplasmic transport; IDA:UniProtKB. DR GO; GO:0043473; P:pigmentation; IEP:UniProtKB. DR GO; GO:0001890; P:placenta development; ISS:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB. DR GO; GO:1902462; P:positive regulation of mesenchymal stem cell proliferation; TAS:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:GO_Central. DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; TAS:BHF-UCL. DR GO; GO:0042981; P:regulation of apoptotic process; IDA:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc. DR GO; GO:0051591; P:response to cAMP; ISS:UniProtKB. DR GO; GO:0034097; P:response to cytokine; ISS:UniProtKB. DR GO; GO:0043627; P:response to estrogen; IDA:UniProtKB. DR GO; GO:0032868; P:response to insulin; ISS:UniProtKB. DR GO; GO:0070555; P:response to interleukin-1; ISS:UniProtKB. DR GO; GO:0071105; P:response to interleukin-11; ISS:UniProtKB. DR GO; GO:0070669; P:response to interleukin-2; ISS:UniProtKB. DR GO; GO:0070670; P:response to interleukin-4; ISS:UniProtKB. DR GO; GO:0070741; P:response to interleukin-6; ISS:UniProtKB. DR GO; GO:0071104; P:response to interleukin-9; ISS:UniProtKB. DR GO; GO:0032496; P:response to lipopolysaccharide; ISS:UniProtKB. DR GO; GO:0071107; P:response to parathyroid hormone; ISS:UniProtKB. DR GO; GO:0071559; P:response to transforming growth factor beta; IDA:UniProtKB. DR GO; GO:0034341; P:response to type II interferon; ISS:UniProtKB. DR GO; GO:0060395; P:SMAD protein signal transduction; IDA:BHF-UCL. DR GO; GO:0060712; P:spongiotrophoblast layer development; IEA:Ensembl. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL. DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl. DR Gene3D; 6.10.140.2200; -; 1. DR InterPro; IPR007576; CITED. DR PANTHER; PTHR17045:SF6; CBP_P300-INTERACTING TRANSACTIVATOR 1; 1. DR PANTHER; PTHR17045; MELANOCYTE SPECIFIC GENE RELATED CITED; 1. DR Pfam; PF04487; CITED; 1. DR Genevisible; Q99966; HS. PE 1: Evidence at protein level; KW Activator; Alternative splicing; Apoptosis; Cytoplasm; KW Developmental protein; Differentiation; Nucleus; Phosphoprotein; KW Reference proteome; Transcription; Transcription regulation. FT CHAIN 1..193 FT /note="Cbp/p300-interacting transactivator 1" FT /id="PRO_0000144724" FT REGION 1..26 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 50..88 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 106..147 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 158..167 FT /note="Nuclear export signal" FT COMPBIAS 55..72 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 1 FT /note="M -> MEPSAQQLQLAASLPANLSNFCQGSEM (in isoform 2)" FT /evidence="ECO:0000303|Ref.6" FT /id="VSP_039897" FT VARIANT 96 FT /note="H -> Q (in dbSNP:rs3012627)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:19054851, ECO:0000269|PubMed:8901575, FT ECO:0000269|Ref.4" FT /id="VAR_053038" FT MUTAGEN 16 FT /note="S->A: Strongly reduces phosphorylation but does not FT interfere with its NES-dependent nuclear export; when FT associated with A-63; A-67; A-71 and A-137." FT /evidence="ECO:0000269|PubMed:16864582" FT MUTAGEN 63 FT /note="S->A: Strongly reduces phosphorylation but does not FT interfere with its NES-dependent nuclear export; when FT associated with A-16; A-67; A-71 and A-137." FT /evidence="ECO:0000269|PubMed:16864582" FT MUTAGEN 67 FT /note="S->A: Strongly reduces phosphorylation but does not FT interfere with its NES-dependent nuclear export; when FT associated with A-16; A-63; A-71 and A-137." FT /evidence="ECO:0000269|PubMed:16864582" FT MUTAGEN 71 FT /note="S->A: Strongly reduces phosphorylation but does not FT interfere with its NES-dependent nuclear export; when FT associated with A-16; A-63; A-67 and A-137." FT /evidence="ECO:0000269|PubMed:16864582" FT MUTAGEN 91 FT /note="L->A: Does not change subcellular localization; when FT associated with A-95." FT MUTAGEN 95 FT /note="M->A: Does not change subcellular localization; when FT associated with A-91." FT MUTAGEN 137 FT /note="S->A: Strongly reduces phosphorylation; when FT associated with A-16; A-63; A-67 and A-71." FT /evidence="ECO:0000269|PubMed:16864582" FT MUTAGEN 155..156 FT /note="EE->AA: Does not inhibit interaction with ESR1 and FT ER-coactivation activity." FT /evidence="ECO:0000269|PubMed:11581164" FT MUTAGEN 157..158 FT /note="VL->AA: Inhibits interaction with ESR1 and FT ER-coactivation activity." FT /evidence="ECO:0000269|PubMed:11581164" FT MUTAGEN 159..160 FT /note="MS->AA: Does not inhibit interaction with ESR1 and FT ER-coactivation activity." FT /evidence="ECO:0000269|PubMed:11581164" FT MUTAGEN 161..162 FT /note="LV->AA: Does not inhibit interaction with ESR1 and FT ER-coactivation activity." FT /evidence="ECO:0000269|PubMed:11581164" FT MUTAGEN 163..164 FT /note="VE->AA: Does not inhibit interaction with ESR1 and FT ER-coactivation activity." FT /evidence="ECO:0000269|PubMed:11581164" FT MUTAGEN 165 FT /note="L->A: Does not inhibit interaction with ESR1 and FT ER-coactivation activity. Localizes mainly in the nucleus; FT when associated with A-167." FT /evidence="ECO:0000269|PubMed:11581164" FT MUTAGEN 166..167 FT /note="GL->AA: Does not inhibit interaction with ESR1 and FT ER-coactivation activity. Localizes mainly in the nucleus; FT when associated with A-165." FT /evidence="ECO:0000269|PubMed:11581164" FT MUTAGEN 176 FT /note="L->A: Does not change subcellular localization; when FT associated with A-178." FT MUTAGEN 178 FT /note="L->A: Does not change subcellular localization; when FT associated with A-176." SQ SEQUENCE 193 AA; 19896 MW; 9B0CF50CA639ECCB CRC64; MPTTSRPALD VKGGTSPAKE DANQEMSSVA YSNLAVKDRK AVAILHYPGV ASNGTKASGA PTSSSGSPIG SPTTTPPTKP PSFNLHPAPH LLASMHLQKL NSQYQGMAAA TPGQPGEAGP LQNWDFGAQA GGAESLSPSA GAQSPAIIDS DPVDEEVLMS LVVELGLDRA NELPELWLGQ NEFDFTADFP SSC //