ID CITE1_MOUSE Reviewed; 203 AA. AC P97769; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 27-MAR-2024, entry version 161. DE RecName: Full=Cbp/p300-interacting transactivator 1; DE AltName: Full=Melanocyte-specific protein 1; GN Name=Cited1; Synonyms=Msg1; 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 [MRNA]. 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]. RC STRAIN=C57BL/6J; 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 [3] RP FUNCTION, AND INTERACTION WITH CREBBP AND EP300. 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 [4] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. 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 [5] RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND DEVELOPMENTAL RP STAGE. RX PubMed=14673158; DOI=10.1128/mcb.24.1.228-244.2004; RA Rodriguez T.A., Sparrow D.B., Scott A.N., Withington S.L., Preis J.I., RA Michalicek J., Clements M., Tsang T.E., Shioda T., Beddington R.S., RA Dunwoodie S.L.; RT "Cited1 is required in trophoblasts for placental development and for RT embryo growth and survival."; RL Mol. Cell. Biol. 24:228-244(2004). RN [6] RP INTERACTION WITH EGR2, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=17938205; DOI=10.1128/mcb.00866-07; RA Dillon R.L., Brown S.T., Ling C., Shioda T., Muller W.J.; RT "An EGR2/CITED1 transcription factor complex and the 14-3-3sigma tumor RT suppressor are involved in regulating ErbB2 expression in a transgenic- RT mouse model of human breast cancer."; RL Mol. Cell. Biol. 27:8648-8657(2007). RN [7] RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=18187554; DOI=10.1210/en.2007-0826; RA Yang D., Guo J., Divieti P., Shioda T., Bringhurst F.R.; RT "CBP/p300-interacting protein CITED1 modulates parathyroid hormone RT regulation of osteoblastic differentiation."; RL Endocrinology 149:1728-1735(2008). 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:14673158, ECO:0000269|PubMed:18187554}. CC -!- SUBUNIT: Homodimer. Binds to RBM14. Interacts (via N-terminus) with CC 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. Interacts (via C- CC terminus) with CREBBP. Interacts with EGR2. {ECO:0000250, CC ECO:0000269|PubMed:10722728, ECO:0000269|PubMed:17938205}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11581164, CC ECO:0000269|PubMed:14673158, ECO:0000269|PubMed:17938205}. Cytoplasm CC {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm by a CC nuclear export signal (NES) and in a CRM1-dependent manner. CC {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed in calvarial osteoblasts. Expressed in CC nulliparous mammary epithelial cells; absent in pregnant mice and in CC lacting mammary glands. Also expressed in mammary tumors (at protein CC level). Expressed only in melanocytes and testis. Expressed at high CC levels in the strongly pigmented melanoma cells but at low levels in CC the weakly pigmented cells. {ECO:0000269|PubMed:11581164, CC ECO:0000269|PubMed:17938205, ECO:0000269|PubMed:18187554}. CC -!- DEVELOPMENTAL STAGE: Expressed in trophectoderm-derived cells of the CC placenta. {ECO:0000269|PubMed:14673158}. CC -!- INDUCTION: Up-regulated by parathyroid hormone, forskolin and phorbol CC ester in osteoblasts. {ECO:0000269|PubMed:18187554}. CC -!- PTM: Phosphorylated. Phosphorylation changes in a cell cycle-dependent CC manner and reduces its transcriptional cofactor activity (By CC similarity). {ECO:0000250}. CC -!- DISRUPTION PHENOTYPE: Mice die shortly after birth. Mice show an CC abnormal placental development; the spongiotrophoblast layer is CC irregular in shape and enlarged while the labyrinthine layer is reduced CC in size, the blood spaces within the labyrinthine are disrupted. CC Produces more mineralized bone nodules and deposited twice as much CC calcium in the matrix. {ECO:0000269|PubMed:14673158, CC ECO:0000269|PubMed:18187554}. CC -!- SIMILARITY: Belongs to the CITED 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; U65091; AAC53048.1; -; mRNA. DR EMBL; BC052030; AAH52030.1; -; mRNA. DR CCDS; CCDS30322.1; -. DR PIR; JC6113; JC6113. DR RefSeq; NP_001263395.1; NM_001276466.1. DR RefSeq; NP_001263402.1; NM_001276473.1. DR RefSeq; NP_001263403.1; NM_001276474.1. DR RefSeq; NP_031735.1; NM_007709.4. DR AlphaFoldDB; P97769; -. DR BioGRID; 198721; 1. DR IntAct; P97769; 1. DR STRING; 10090.ENSMUSP00000098890; -. DR iPTMnet; P97769; -. DR PhosphoSitePlus; P97769; -. DR PaxDb; 10090-ENSMUSP00000098890; -. DR ProteomicsDB; 283923; -. DR Antibodypedia; 13694; 379 antibodies from 26 providers. DR DNASU; 12705; -. DR Ensembl; ENSMUST00000050551.10; ENSMUSP00000051789.4; ENSMUSG00000051159.17. DR Ensembl; ENSMUST00000101336.10; ENSMUSP00000098890.4; ENSMUSG00000051159.17. DR GeneID; 12705; -. DR KEGG; mmu:12705; -. DR UCSC; uc009tyn.3; mouse. DR AGR; MGI:108023; -. DR CTD; 4435; -. DR MGI; MGI:108023; Cited1. DR VEuPathDB; HostDB:ENSMUSG00000051159; -. DR eggNOG; ENOG502S282; Eukaryota. DR GeneTree; ENSGT00530000063624; -. DR HOGENOM; CLU_100627_0_0_1; -. DR InParanoid; P97769; -. DR OMA; NSQYHGV; -. DR OrthoDB; 4213331at2759; -. DR PhylomeDB; P97769; -. DR TreeFam; TF331915; -. DR Reactome; R-MMU-8866907; Activation of the TFAP2 (AP-2) family of transcription factors. DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression. DR BioGRID-ORCS; 12705; 1 hit in 79 CRISPR screens. DR ChiTaRS; Cited1; mouse. DR PRO; PR:P97769; -. DR Proteomes; UP000000589; Chromosome X. DR RNAct; P97769; Protein. DR Bgee; ENSMUSG00000051159; Expressed in placenta labyrinth and 175 other cell types or tissues. DR ExpressionAtlas; P97769; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB. DR GO; GO:0070410; F:co-SMAD binding; ISO:MGI. DR GO; GO:0050693; F:LBD domain binding; ISO:MGI. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0007420; P:brain development; IEP:UniProtKB. DR GO; GO:0000578; P:embryonic axis specification; ISO:MGI. DR GO; GO:0060711; P:labyrinthine layer development; IMP:MGI. DR GO; GO:0042438; P:melanin biosynthetic process; IDA:UniProtKB. DR GO; GO:0030318; P:melanocyte differentiation; IEP:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0003340; P:negative regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis; ISO:MGI. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB. DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:UniProtKB. DR GO; GO:0006913; P:nucleocytoplasmic transport; ISS:UniProtKB. DR GO; GO:0043473; P:pigmentation; IDA:UniProtKB. DR GO; GO:0001890; P:placenta development; IMP:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI. DR GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI. DR GO; GO:0051591; P:response to cAMP; IDA:UniProtKB. DR GO; GO:0034097; P:response to cytokine; IDA:UniProtKB. DR GO; GO:0043627; P:response to estrogen; ISO:MGI. DR GO; GO:0032868; P:response to insulin; IDA:UniProtKB. DR GO; GO:0070555; P:response to interleukin-1; IDA:UniProtKB. DR GO; GO:0071105; P:response to interleukin-11; IDA:UniProtKB. DR GO; GO:0070669; P:response to interleukin-2; IDA:UniProtKB. DR GO; GO:0070670; P:response to interleukin-4; IDA:UniProtKB. DR GO; GO:0070741; P:response to interleukin-6; IDA:UniProtKB. DR GO; GO:0071104; P:response to interleukin-9; IDA:UniProtKB. DR GO; GO:0032496; P:response to lipopolysaccharide; IDA:UniProtKB. DR GO; GO:0071107; P:response to parathyroid hormone; IDA:UniProtKB. DR GO; GO:0071559; P:response to transforming growth factor beta; ISS:UniProtKB. DR GO; GO:0034341; P:response to type II interferon; IDA:UniProtKB. DR GO; GO:0060395; P:SMAD protein signal transduction; ISO:MGI. DR GO; GO:0060712; P:spongiotrophoblast layer development; IMP:MGI. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:MGI. DR GO; GO:0001570; P:vasculogenesis; IMP:MGI. 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; P97769; MM. PE 1: Evidence at protein level; KW Activator; Apoptosis; Cytoplasm; Developmental protein; Differentiation; KW Nucleus; Phosphoprotein; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1..203 FT /note="Cbp/p300-interacting transactivator 1" FT /id="PRO_0000144725" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 51..86 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 168..177 FT /note="Nuclear export signal" FT /evidence="ECO:0000250" FT COMPBIAS 56..83 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 203 AA; 20800 MW; BE968A5182873003 CRC64; MPTMSRPALD VKGGTTSGKE DANQEMNSLA YSNLGVKDRK AVTVLHYPGV TANGAKANGV PTSSSGSTSP IGSPTATPSS KPPSFNLHPT PHLMASMQLQ KLNSQYQGAA ATAAAALTGA GLPGEEEPMQ NWVTAPLVVG GSPGSVSPPA GAQSPALIDS DPVDEEVLMS LVVELGLDRA NELPELWLGQ NEFDFTADFP SGC //