CITE1_HUMAN
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 03-AUG-2022, entry version 169.
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};
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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. [Q99966-2]
DR AlphaFoldDB; Q99966; -.
DR BioGRID; 110572; 36.
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; Q99966; -.
DR PeptideAtlas; Q99966; -.
DR PRIDE; Q99966; -.
DR ProteomicsDB; 78553; -. [Q99966-1]
DR ProteomicsDB; 78554; -. [Q99966-2]
DR Antibodypedia; 13694; 329 antibodies from 25 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 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; 1378769at2759; -.
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 705 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 94 other tissues.
DR ExpressionAtlas; Q99966; baseline and differential.
DR Genevisible; Q99966; HS.
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:0008022; F:protein C-terminus binding; IPI: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: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:0045892; P:negative regulation of transcription, DNA-templated; IDA: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: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:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
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:0034341; P:response to interferon-gamma; 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: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 InterPro; IPR007576; CITED.
DR PANTHER; PTHR17045; PTHR17045; 1.
DR Pfam; PF04487; CITED; 1.
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: Reduces strongly 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: Reduces strongly 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: Reduces strongly 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: Reduces strongly 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: Reduces strongly 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 ER-
FT 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 ER-
FT 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
