CITED1
entrez
4435
canonical
uniprot
Q99966
canonical
ensembl
ENSG00000125931
resolver
ensp
ENSP00000246139
resolver
ensp
ENSP00000362721
resolver
ensp
ENSP00000388548
resolver
ensp
ENSP00000499148
resolver
genesymbol
CITED1
resolver
genesymbol_syn
MSG1
resolver
hgnc
HGNC:1986
resolver
uniprot
B5BU50
resolver
uniprot
B5BUI2
resolver
uniprot_entry
CITE1_HUMAN
resolver
uniprot_sec
B5BU50
resolver
uniprot_sec
B5BUI2
resolver
amino_acid_sequence
MPTTSRPALDVKGGTSPAKEDANQEMSSVAYSNLAVKDRKAVAILHYPGVASNGTKASGAPTSSSGSPIGSPTTTPPTKPPSFNLHPAPHLLASMHLQKLNSQYQGMAAATPGQPGEAGPLQNWDFGAQAGGAESLSPSAGAQSPAIIDSDPVDEEVLMSLVVELGLDRANELPELWLGQNEFDFTADFPSSC
uniprot
proteins
function
FUNCTION: Transcriptional coactivator of the p300/CBP-mediated transcription complex. Enhances SMAD-mediated transcription by strengthening the functional link between the DNA-binding SMAD transcription factors and the p300/CBP transcription coactivator complex. Stimulates estrogen-dependent transactivation activity mediated by estrogen receptors signaling; stabilizes the interaction of estrogen receptor ESR1 and histone acetyltransferase EP300. Positively regulates TGF-beta signaling through its association with the SMAD/p300/CBP-mediated transcriptional coactivator complex. Induces transcription from estrogen-responsive promoters and protection against cell death. Potentiates EGR2-mediated transcriptional activation activity from the ERBB2 promoter. Acts as an inhibitor of osteoblastic mineralization through a cAMP-dependent parathyroid hormone receptor signaling. May play a role in pigmentation of melanocytes. Associates with chromatin to the estrogen-responsive TGF-alpha promoter region in a estrogen-dependent manner. {ECO:0000269|PubMed:10722728, ECO:0000269|PubMed:11581164, ECO:0000269|PubMed:21172805}.
uniprot
proteins
mass_dalton
19896
uniprot
proteins
mutagenesis
MUTAGEN 16; /note="S->A: Strongly reduces phosphorylation but does not interfere with its NES-dependent nuclear export; when associated with A-63; A-67; A-71 and A-137."; /evidence="ECO:0000269|PubMed:16864582"; MUTAGEN 63; /note="S->A: Strongly reduces phosphorylation but does not interfere with its NES-dependent nuclear export; when associated with A-16; A-67; A-71 and A-137."; /evidence="ECO:0000269|PubMed:16864582"; MUTAGEN 67; /note="S->A: Strongly reduces phosphorylation but does not interfere with its NES-dependent nuclear export; when associated with A-16; A-63; A-71 and A-137."; /evidence="ECO:0000269|PubMed:16864582"; MUTAGEN 71; /note="S->A: Strongly reduces phosphorylation but does not interfere with its NES-dependent nuclear export; when associated with A-16; A-63; A-67 and A-137."; /evidence="ECO:0000269|PubMed:16864582"; MUTAGEN 91; /note="L->A: Does not change subcellular localization; when associated with A-95."; MUTAGEN 95; /note="M->A: Does not change subcellular localization; when associated with A-91."; MUTAGEN 137; /note="S->A: Strongly reduces phosphorylation; when associated with A-16; A-63; A-67 and A-71."; /evidence="ECO:0000269|PubMed:16864582"; MUTAGEN 155..156; /note="EE->AA: Does not inhibit interaction with ESR1 and ER-coactivation activity."; /evidence="ECO:0000269|PubMed:11581164"; MUTAGEN 157..158; /note="VL->AA: Inhibits interaction with ESR1 and ER-coactivation activity."; /evidence="ECO:0000269|PubMed:11581164"; MUTAGEN 159..160; /note="MS->AA: Does not inhibit interaction with ESR1 and ER-coactivation activity."; /evidence="ECO:0000269|PubMed:11581164"; MUTAGEN 161..162; /note="LV->AA: Does not inhibit interaction with ESR1 and ER-coactivation activity."; /evidence="ECO:0000269|PubMed:11581164"; MUTAGEN 163..164; /note="VE->AA: Does not inhibit interaction with ESR1 and ER-coactivation activity."; /evidence="ECO:0000269|PubMed:11581164"; MUTAGEN 165; /note="L->A: Does not inhibit interaction with ESR1 and ER-coactivation activity. Localizes mainly in the nucleus; when associated with A-167."; /evidence="ECO:0000269|PubMed:11581164"; MUTAGEN 166..167; /note="GL->AA: Does not inhibit interaction with ESR1 and ER-coactivation activity. Localizes mainly in the nucleus; when associated with A-165."; /evidence="ECO:0000269|PubMed:11581164"; MUTAGEN 176; /note="L->A: Does not change subcellular localization; when associated with A-178."; MUTAGEN 178; /note="L->A: Does not change subcellular localization; when associated with A-176.
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. Phosphorylation changes in a cell cycle-dependent manner and reduces its transcriptional coactivator activity. {ECO:0000269|PubMed:16864582}.
uniprot
proteins
protein_family
CITED family
uniprot
proteins
pubmed
10722728
uniprot
proteins
pubmed
11443112
uniprot
proteins
pubmed
11581164
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
16864582
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19054851
uniprot
proteins
pubmed
21172805
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
8901575
uniprot
proteins
pubmed
9707553
uniprot
proteins
sequence_length
193
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16864582}. Cytoplasm {ECO:0000269|PubMed:16864582}. Note=Shuttles between the nucleus and the cytoplasm by a nuclear export signal and (NES) in a CRM1-dependent manner.
uniprot
proteins