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Protein

Undifferentiated embryonic cell transcription factor 1

Gene

UTF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a transcriptional coactivator of ATF2.1 Publication

GO - Molecular functioni

  • transcription coactivator activity Source: UniProtKB

GO - Biological processi

  • male gonad development Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • regulation of transcription from RNA polymerase II promoter Source: ProtInc
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Undifferentiated embryonic cell transcription factor 1
Gene namesi
Name:UTF1Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:12634. UTF1.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi296 – 2961L → P: Abolishes coactivation activity; when associated with P-303. 1 Publication
Mutagenesisi303 – 3031L → P: Abolishes coactivation activity; when associated with P-296. 1 Publication

Organism-specific databases

PharmGKBiPA37259.

Polymorphism and mutation databases

BioMutaiUTF1.
DMDMi74756257.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 341341Undifferentiated embryonic cell transcription factor 1PRO_0000274551Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei18 – 181PhosphoserineCombined sources
Modified residuei21 – 211PhosphoserineBy similarity
Modified residuei54 – 541PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ5T230.
PRIDEiQ5T230.

PTM databases

iPTMnetiQ5T230.
PhosphoSiteiQ5T230.

Expressioni

Gene expression databases

BgeeiQ5T230.
CleanExiHS_UTF1.
GenevisibleiQ5T230. HS.

Interactioni

Subunit structurei

Binds to the N-terminal region of ATF2. Associates with the TFIID complex through interaction with TBP.1 Publication

Protein-protein interaction databases

BioGridi114013. 2 interactions.
STRINGi9606.ENSP00000305906.

Structurei

3D structure databases

ProteinModelPortaliQ5T230.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni279 – 31032Leucine-zipperAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi5 – 273269Pro-richSequence analysisAdd
BLAST

Domaini

The leucine-zipper domain is required for coactivation activity. When this domain is deleted, the protein is able to stimulate transcription from a number of gene promoters (By similarity).By similarity

Phylogenomic databases

eggNOGiKOG4282. Eukaryota.
ENOG410YYXY. LUCA.
GeneTreeiENSGT00390000014419.
HOGENOMiHOG000060176.
HOVERGENiHBG094142.
InParanoidiQ5T230.
OMAiCRRRYKF.
OrthoDBiEOG7KWSJG.
PhylomeDBiQ5T230.
TreeFamiTF337319.

Sequencei

Sequence statusi: Complete.

Q5T230-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLRPRRPPP LAPPAPPSPA SPDPEPRTPG DAPGTPPRRP ASPSALGELG
60 70 80 90 100
LPVSPGSAQR TPWSARETEL LLGTLLQPAV WRALLLDRRQ ALPTYRRVSA
110 120 130 140 150
ALAQQQVRRT PAQCRRRYKF LKDKFREAHG QPPGPFDEQI RKLMGLLGDN
160 170 180 190 200
GRKRPRRRSP GSGRPQRARR PVPNAHAPAP SEPDATPLPT ARDRDADPTW
210 220 230 240 250
TLRFSPSPPK SADASPAPGS PPAPAPTALA TCIPEDRAPV RGPGSPPPPP
260 270 280 290 300
AREDPDSPPG RPEDCAPPPA APPSLNTALL QTLGHLGDIA NILGPLRDQL
310 320 330 340
LTLNQHVEQL RGAFDQTVSL AVGFILGSAA AERGVLRDPC Q
Length:341
Mass (Da):36,439
Last modified:December 21, 2004 - v1
Checksum:i65E58A4B4206FC05
GO

Sequence cautioni

The sequence AAT38949.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti73 – 731G → R.
Corresponds to variant rs11599284 [ dbSNP | Ensembl ].
VAR_051485

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011076 mRNA. Translation: BAA33463.2.
AY606112 mRNA. Translation: AAT38949.1. Different initiation.
AL445199 Genomic DNA. Translation: CAI17342.1.
CCDSiCCDS31318.1.
RefSeqiNP_003568.2. NM_003577.2.
UniGeneiHs.458406.

Genome annotation databases

EnsembliENST00000304477; ENSP00000305906; ENSG00000171794.
GeneIDi8433.
KEGGihsa:8433.
UCSCiuc001lmc.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011076 mRNA. Translation: BAA33463.2.
AY606112 mRNA. Translation: AAT38949.1. Different initiation.
AL445199 Genomic DNA. Translation: CAI17342.1.
CCDSiCCDS31318.1.
RefSeqiNP_003568.2. NM_003577.2.
UniGeneiHs.458406.

3D structure databases

ProteinModelPortaliQ5T230.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114013. 2 interactions.
STRINGi9606.ENSP00000305906.

PTM databases

iPTMnetiQ5T230.
PhosphoSiteiQ5T230.

Polymorphism and mutation databases

BioMutaiUTF1.
DMDMi74756257.

Proteomic databases

PaxDbiQ5T230.
PRIDEiQ5T230.

Protocols and materials databases

DNASUi8433.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000304477; ENSP00000305906; ENSG00000171794.
GeneIDi8433.
KEGGihsa:8433.
UCSCiuc001lmc.3. human.

Organism-specific databases

CTDi8433.
GeneCardsiUTF1.
HGNCiHGNC:12634. UTF1.
MIMi604130. gene.
neXtProtiNX_Q5T230.
PharmGKBiPA37259.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4282. Eukaryota.
ENOG410YYXY. LUCA.
GeneTreeiENSGT00390000014419.
HOGENOMiHOG000060176.
HOVERGENiHBG094142.
InParanoidiQ5T230.
OMAiCRRRYKF.
OrthoDBiEOG7KWSJG.
PhylomeDBiQ5T230.
TreeFamiTF337319.

Miscellaneous databases

GenomeRNAii8433.
NextBioi31550.
PROiQ5T230.
SOURCEiSearch...

Gene expression databases

BgeeiQ5T230.
CleanExiHS_UTF1.
GenevisibleiQ5T230. HS.

Family and domain databases

ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of functional domains of an embryonic stem cell coactivator UTF1 which are conserved and essential for potentiation of ATF-2 activity."
    Fukushima A., Okuda A., Nishimoto M., Seki N., Hori T.A., Muramatsu M.
    J. Biol. Chem. 273:25840-25849(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ATF2 AND TBP, PHOSPHORYLATION, MUTAGENESIS OF LEU-296 AND LEU-303.
    Tissue: Teratocarcinoma1 Publication.
  2. Fukushima A., Okuda A.
    Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Homo sapiens Helcg1 gene clone and function research."
    Xiang Y., Nie D.S., Lu G.X.
    Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-54, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiUTF1_HUMAN
AccessioniPrimary (citable) accession number: Q5T230
Secondary accession number(s): O75833, Q6J1H3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: December 21, 2004
Last modified: January 20, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.