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UTF1_HUMAN
ID   UTF1_HUMAN              Reviewed;         341 AA.
AC   Q5T230; O75833; Q6J1H3;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Undifferentiated embryonic cell transcription factor 1;
GN   Name=UTF1 {ECO:0000312|HGNC:HGNC:12634};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ATF2 AND TBP,
RP   PHOSPHORYLATION, AND MUTAGENESIS OF LEU-296 AND LEU-303.
RC   TISSUE=Teratocarcinoma {ECO:0000269|PubMed:9748258};
RX   PubMed=9748258; DOI=10.1074/jbc.273.40.25840;
RA   Fukushima A., Okuda A., Nishimoto M., Seki N., Hori T.A., Muramatsu M.;
RT   "Characterization of functional domains of an embryonic stem cell
RT   coactivator UTF1 which are conserved and essential for potentiation of ATF-
RT   2 activity.";
RL   J. Biol. Chem. 273:25840-25849(1998).
RN   [2] {ECO:0000312|EMBL:AAT38949.1}
RP   SEQUENCE REVISION.
RA   Fukushima A., Okuda A.;
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000312|EMBL:AAT38949.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Xiang Y., Nie D.S., Lu G.X.;
RT   "Homo sapiens Helcg1 gene clone and function research.";
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000312|EMBL:AL445199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-54, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
CC   -!- FUNCTION: Acts as a transcriptional coactivator of ATF2.
CC       {ECO:0000269|PubMed:9748258}.
CC   -!- SUBUNIT: Binds to the N-terminal region of ATF2. Associates with the
CC       TFIID complex through interaction with TBP.
CC       {ECO:0000269|PubMed:9748258}.
CC   -!- INTERACTION:
CC       Q5T230; Q15642-2: TRIP10; NbExp=3; IntAct=EBI-12927594, EBI-6550597;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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 (By similarity).
CC       {ECO:0000250|UniProtKB:Q6J1H4}.
CC   -!- PTM: Phosphorylated. {ECO:0000269|PubMed:9748258}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAT38949.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB011076; BAA33463.2; -; mRNA.
DR   EMBL; AY606112; AAT38949.1; ALT_INIT; mRNA.
DR   EMBL; AL445199; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS31318.1; -.
DR   RefSeq; NP_003568.2; NM_003577.2.
DR   AlphaFoldDB; Q5T230; -.
DR   BioGRID; 114013; 4.
DR   IntAct; Q5T230; 3.
DR   STRING; 9606.ENSP00000305906; -.
DR   iPTMnet; Q5T230; -.
DR   PhosphoSitePlus; Q5T230; -.
DR   BioMuta; UTF1; -.
DR   DMDM; 74756257; -.
DR   EPD; Q5T230; -.
DR   jPOST; Q5T230; -.
DR   MassIVE; Q5T230; -.
DR   PaxDb; Q5T230; -.
DR   PeptideAtlas; Q5T230; -.
DR   PRIDE; Q5T230; -.
DR   ProteomicsDB; 64306; -.
DR   Antibodypedia; 32620; 258 antibodies from 34 providers.
DR   DNASU; 8433; -.
DR   Ensembl; ENST00000304477.3; ENSP00000305906.2; ENSG00000171794.4.
DR   GeneID; 8433; -.
DR   KEGG; hsa:8433; -.
DR   MANE-Select; ENST00000304477.3; ENSP00000305906.2; NM_003577.3; NP_003568.2.
DR   UCSC; uc001lmc.3; human.
DR   CTD; 8433; -.
DR   DisGeNET; 8433; -.
DR   GeneCards; UTF1; -.
DR   HGNC; HGNC:12634; UTF1.
DR   HPA; ENSG00000171794; Tissue enriched (testis).
DR   MIM; 604130; gene.
DR   neXtProt; NX_Q5T230; -.
DR   OpenTargets; ENSG00000171794; -.
DR   PharmGKB; PA37259; -.
DR   VEuPathDB; HostDB:ENSG00000171794; -.
DR   eggNOG; KOG4282; Eukaryota.
DR   GeneTree; ENSGT00940000163231; -.
DR   HOGENOM; CLU_074827_0_0_1; -.
DR   InParanoid; Q5T230; -.
DR   OMA; CRRRYKF; -.
DR   OrthoDB; 1201295at2759; -.
DR   PhylomeDB; Q5T230; -.
DR   TreeFam; TF337319; -.
DR   PathwayCommons; Q5T230; -.
DR   SignaLink; Q5T230; -.
DR   SIGNOR; Q5T230; -.
DR   BioGRID-ORCS; 8433; 14 hits in 1070 CRISPR screens.
DR   GenomeRNAi; 8433; -.
DR   Pharos; Q5T230; Tbio.
DR   PRO; PR:Q5T230; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q5T230; protein.
DR   Bgee; ENSG00000171794; Expressed in right testis and 11 other tissues.
DR   Genevisible; Q5T230; HS.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR   GO; GO:0008584; P:male gonad development; IEP:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR   InterPro; IPR044822; Myb_DNA-bind_4.
DR   Pfam; PF13837; Myb_DNA-bind_4; 1.
PE   1: Evidence at protein level;
KW   Activator; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..341
FT                   /note="Undifferentiated embryonic cell transcription factor
FT                   1"
FT                   /id="PRO_0000274551"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          146..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          279..310
FT                   /note="Leucine-zipper"
FT   COMPBIAS        1..40
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..228
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..273
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         18
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         21
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6J1H4"
FT   MOD_RES         54
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   VARIANT         73
FT                   /note="G -> R (in dbSNP:rs11599284)"
FT                   /id="VAR_051485"
FT   MUTAGEN         296
FT                   /note="L->P: Abolishes coactivation activity; when
FT                   associated with P-303."
FT                   /evidence="ECO:0000269|PubMed:9748258"
FT   MUTAGEN         303
FT                   /note="L->P: Abolishes coactivation activity; when
FT                   associated with P-296."
FT                   /evidence="ECO:0000269|PubMed:9748258"
SQ   SEQUENCE   341 AA;  36439 MW;  65E58A4B4206FC05 CRC64;
     MLLRPRRPPP LAPPAPPSPA SPDPEPRTPG DAPGTPPRRP ASPSALGELG LPVSPGSAQR
     TPWSARETEL LLGTLLQPAV WRALLLDRRQ ALPTYRRVSA ALAQQQVRRT PAQCRRRYKF
     LKDKFREAHG QPPGPFDEQI RKLMGLLGDN GRKRPRRRSP GSGRPQRARR PVPNAHAPAP
     SEPDATPLPT ARDRDADPTW TLRFSPSPPK SADASPAPGS PPAPAPTALA TCIPEDRAPV
     RGPGSPPPPP AREDPDSPPG RPEDCAPPPA APPSLNTALL QTLGHLGDIA NILGPLRDQL
     LTLNQHVEQL RGAFDQTVSL AVGFILGSAA AERGVLRDPC Q
 
 
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