CITE1_MOUSE
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 03-AUG-2022, entry version 152.
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}.
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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; P97769; -.
DR PRIDE; P97769; -.
DR ProteomicsDB; 283923; -.
DR Antibodypedia; 13694; 329 antibodies from 25 providers.
DR DNASU; 12705; -.
DR Ensembl; ENSMUST00000050551; ENSMUSP00000051789; ENSMUSG00000051159.
DR Ensembl; ENSMUST00000101336; ENSMUSP00000098890; ENSMUSG00000051159.
DR GeneID; 12705; -.
DR KEGG; mmu:12705; -.
DR UCSC; uc009tyn.3; mouse.
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; QSPTIID; -.
DR OrthoDB; 1378769at2759; -.
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 74 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 172 other tissues.
DR ExpressionAtlas; P97769; baseline and differential.
DR Genevisible; P97769; MM.
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:0008022; F:protein C-terminus 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: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:0045892; P:negative regulation of transcription, DNA-templated; ISS: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: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:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
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:0034341; P:response to interferon-gamma; 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: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 InterPro; IPR007576; CITED.
DR PANTHER; PTHR17045; PTHR17045; 1.
DR Pfam; PF04487; CITED; 1.
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
