UTF1_MOUSE
ID UTF1_MOUSE Reviewed; 339 AA.
AC Q6J1H4; O70530;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Undifferentiated embryonic cell transcription factor 1;
GN Name=Utf1 {ECO:0000312|MGI:MGI:1276125};
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] {ECO:0000305, ECO:0000312|EMBL:BAA25403.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH ATF2 AND
RP TBP, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND PHOSPHORYLATION.
RC TISSUE=Teratocarcinoma {ECO:0000269|PubMed:9524124};
RX PubMed=9524124; DOI=10.1093/emboj/17.7.2019;
RA Okuda A., Fukushima A., Nishimoto M., Orimo A., Yamagishi T., Nabeshima Y.,
RA Kuro-o M., Nabeshima Y., Boon K., Keaveney M., Stunnenberg H.G.,
RA Muramatsu M.;
RT "UTF1, a novel transcriptional coactivator expressed in pluripotent
RT embryonic stem cells and extra-embryonic cells.";
RL EMBO J. 17:2019-2032(1998).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAA82667.1, ECO:0000312|PIR:JC7712}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RC STRAIN=BALB/cJ {ECO:0000269|PubMed:11467843};
RX PubMed=11467843; DOI=10.1006/bbrc.2001.5265;
RA Nishimoto M., Fukushima A., Miyagi S., Suzuki Y., Sugano S., Matsuda Y.,
RA Hori T., Muramatsu M., Okuda A.;
RT "Structural analyses of the UTF1 gene encoding a transcriptional
RT coactivator expressed in pluripotent embryonic stem cells.";
RL Biochem. Biophys. Res. Commun. 285:945-953(2001).
RN [3] {ECO:0000312|EMBL:AAT38948.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Xiang Y., Nie D.S., Lu G.X.;
RT "Mus musculus Melcg1 gene clone and function research.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP LEUCINE-ZIPPER DOMAIN.
RX PubMed=10329418; DOI=10.1006/bbrc.1999.0673;
RA Fukushima A., Nishimoto M., Okuda A., Muramatsu M.;
RT "Carboxy-terminally truncated form of a coactivator UTF1 stimulates
RT transcription from a variety of gene promoters through the TATA Box.";
RL Biochem. Biophys. Res. Commun. 258:519-523(1999).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-18; SER-48 AND
RP SER-54, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Acts as a transcriptional coactivator of ATF2.
CC {ECO:0000269|PubMed:9524124}.
CC -!- SUBUNIT: Binds to the N-terminal region of ATF2. Associates with the
CC TFIID complex through interaction with TBP.
CC {ECO:0000269|PubMed:9524124}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:11467843};
CC IsoId=Q6J1H4-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:11467843};
CC IsoId=Q6J1H4-2; Sequence=VSP_052292;
CC -!- TISSUE SPECIFICITY: Expressed mainly in pluripotent cells with
CC expression rapidly down-regulated upon cell differentiation.
CC {ECO:0000269|PubMed:9524124}.
CC -!- DEVELOPMENTAL STAGE: First detected in the embryo at the blastocyst
CC stage. Little or no expression detected in adult tissues.
CC {ECO:0000269|PubMed:9524124}.
CC -!- DOMAIN: The leucine-zipper domain is required for coactivation
CC activity. When this domain is deleted, the protein is able to stimulate
CC transcription from a number of gene promoters.
CC {ECO:0000269|PubMed:10329418}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:9524124}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAT38948.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D31647; BAA25403.1; -; mRNA.
DR EMBL; AB017360; BAA82667.1; -; Genomic_DNA.
DR EMBL; AY606111; AAT38948.1; ALT_INIT; mRNA.
DR CCDS; CCDS21958.1; -. [Q6J1H4-1]
DR PIR; JC7712; JC7712.
DR RefSeq; NP_033508.1; NM_009482.2. [Q6J1H4-1]
DR AlphaFoldDB; Q6J1H4; -.
DR BioGRID; 204468; 7.
DR STRING; 10090.ENSMUSP00000128848; -.
DR iPTMnet; Q6J1H4; -.
DR PhosphoSitePlus; Q6J1H4; -.
DR PaxDb; Q6J1H4; -.
DR PeptideAtlas; Q6J1H4; -.
DR PRIDE; Q6J1H4; -.
DR ProteomicsDB; 297950; -. [Q6J1H4-1]
DR DNASU; 22286; -.
DR Ensembl; ENSMUST00000168457; ENSMUSP00000128848; ENSMUSG00000047751. [Q6J1H4-1]
DR GeneID; 22286; -.
DR KEGG; mmu:22286; -.
DR UCSC; uc009kgf.1; mouse. [Q6J1H4-1]
DR CTD; 8433; -.
DR MGI; MGI:1276125; Utf1.
DR VEuPathDB; HostDB:ENSMUSG00000047751; -.
DR eggNOG; KOG4282; Eukaryota.
DR GeneTree; ENSGT00390000014419; -.
DR HOGENOM; CLU_074827_0_0_1; -.
DR InParanoid; Q6J1H4; -.
DR OMA; CRRRYKF; -.
DR PhylomeDB; Q6J1H4; -.
DR TreeFam; TF337319; -.
DR BioGRID-ORCS; 22286; 3 hits in 74 CRISPR screens.
DR PRO; PR:Q6J1H4; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q6J1H4; protein.
DR Bgee; ENSMUSG00000047751; Expressed in epiblast (generic) and 30 other tissues.
DR ExpressionAtlas; Q6J1H4; baseline and differential.
DR Genevisible; Q6J1H4; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0071837; F:HMG box domain binding; IPI:UniProtKB.
DR GO; GO:0017025; F:TBP-class protein binding; IPI:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR InterPro; IPR044822; Myb_DNA-bind_4.
DR Pfam; PF13837; Myb_DNA-bind_4; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative initiation; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..339
FT /note="Undifferentiated embryonic cell transcription factor
FT 1"
FT /id="PRO_0000274552"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..310
FT /note="Leucine-zipper"
FT COMPBIAS 201..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..42
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11467843"
FT /id="VSP_052292"
SQ SEQUENCE 339 AA; 36408 MW; 96AD8D6F8413F171 CRC64;
MLLRPRRLPA FSPPSPASPD AELRSAGDVP VTTSDAFATS GGMAEPGSPK APVSPDSAQR
TPWSARETEL LLGTLLQPAM WRSLLLDRRQ TLPTYRRVSA ALARQQVRRT PAQCRRRYKF
LKDKLRDSQG QPSGPFDNQI RQLMGLLGDD GPPRVRRRST GPGRPQRRGR SSLSALAPAP
APVEQEAELP LAAENDEPAP ALRFSSSTTK SAGAHRITSS PPLTSTDTLP PEPGHTFESS
PTPTPDHDVE TPNEPPGLSQ GRASSPQVAP QSLNTALLQT LTHLGDISTV LGPLRDQLST
LNQHVEHLRG SFDQTVSLAV GFILGSAASE RGILGDLRQ
