CITE1_BOVIN
ID CITE1_BOVIN Reviewed; 195 AA.
AC Q9BDI3;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Cbp/p300-interacting transactivator 1;
DE AltName: Full=Melanocyte-specific protein 1;
GN Name=CITED1; Synonyms=MSG1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhuang D.Z., Chou Y.-T., Yang Y.-C.;
RT "Structural and functional conservation of MRG family in system
RT evolution.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via C-terminus) with CREBBP. Interacts with EGR2.
CC Homodimer. Binds to RBM14. Interacts (via N-terminus) with HSPA8; the
CC interaction suppresses the association of CITED1 with p300/CBP and
CC SMAD-mediated transcription transactivation. Interacts (via C-terminus)
CC with TOX3 (via HGM box); the interaction increases estrogen-response
CC element (ERE)-dependent transcription and protection against cell
CC death. Interacts with ESR1; the interaction occurs in a estrogen-
CC dependent manner (By similarity). Interacts (unphosphorylated form
CC preferentially and via C-terminus) with EP300 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Shuttles between the nucleus and the cytoplasm by a nuclear export
CC signal and (NES) in a CRM1-dependent manner. {ECO:0000250}.
CC -!- PTM: Phosphorylated. Phosphorylation changes in a cell cycle-dependent
CC manner and reduces its transcriptional cofactor activity (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CITED family. {ECO:0000305}.
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DR EMBL; AF362075; AAK27241.1; -; mRNA.
DR EMBL; BC102725; AAI02726.1; -; mRNA.
DR RefSeq; NP_776943.1; NM_174518.1.
DR RefSeq; XP_005228047.1; XM_005227990.2.
DR RefSeq; XP_005228048.1; XM_005227991.3.
DR RefSeq; XP_010820139.1; XM_010821837.2.
DR RefSeq; XP_010820140.1; XM_010821838.2.
DR RefSeq; XP_015317125.1; XM_015461639.1.
DR AlphaFoldDB; Q9BDI3; -.
DR STRING; 9913.ENSBTAP00000055749; -.
DR PaxDb; Q9BDI3; -.
DR Ensembl; ENSBTAT00000062996; ENSBTAP00000055749; ENSBTAG00000045925.
DR GeneID; 282182; -.
DR KEGG; bta:282182; -.
DR CTD; 4435; -.
DR VEuPathDB; HostDB:ENSBTAG00000045925; -.
DR VGNC; VGNC:27376; CITED1.
DR eggNOG; ENOG502RZBF; Eukaryota.
DR GeneTree; ENSGT00530000063624; -.
DR HOGENOM; CLU_100627_0_0_1; -.
DR InParanoid; Q9BDI3; -.
DR OrthoDB; 1378769at2759; -.
DR TreeFam; TF331915; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000045925; Expressed in granulosa cell and 99 other tissues.
DR ExpressionAtlas; Q9BDI3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
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:0001658; P:branching involved in ureteric bud morphogenesis; ISS:UniProtKB.
DR GO; GO:0030318; P:melanocyte differentiation; IBA:GO_Central.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS: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:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0071559; P:response to transforming growth factor beta; ISS:UniProtKB.
DR InterPro; IPR007576; CITED.
DR PANTHER; PTHR17045; PTHR17045; 1.
DR Pfam; PF04487; CITED; 1.
PE 2: Evidence at transcript level;
KW Activator; Apoptosis; Cytoplasm; Developmental protein; Differentiation;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..195
FT /note="Cbp/p300-interacting transactivator 1"
FT /id="PRO_0000285514"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 160..169
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 55..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..89
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 195 AA; 19998 MW; 3D1F312BD87535F1 CRC64;
MPTMSRPALD VKGGTSPVKE NANPEMNSLA YSNLGVKDRK AVAILHYPGV ASNGTKASGA
PTSSSGSPSP ISSSTATPPT KPPPFNLHPA PHLLASMQLQ KLNSQYHGMA AATPGQPGEA
EPLPNWGFGA QAGGAGSLSP SAGAQSPAII DSDPVDEEVL MSLVVELGLD RANELPELWL
GQNEFDFTAD FPSGS
