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Protein

POU domain, class 5, transcription factor 1

Gene

Pou5f1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3'). Forms a trimeric complex with SOX2 on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206. Critical for early embryogenesis and for embryonic stem cell pluripotency.2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi223 – 282HomeoboxPROSITE-ProRule annotationAdd BLAST60

GO - Molecular functioni

  • chromatin binding Source: MGI
  • chromatin DNA binding Source: MGI
  • cytokine binding Source: AgBase
  • DNA binding Source: MGI
  • enhancer sequence-specific DNA binding Source: AgBase
  • HMG box domain binding Source: Ensembl
  • miRNA binding Source: MGI
  • POU domain binding Source: Ensembl
  • protein heterodimerization activity Source: MGI
  • RNA binding Source: MGI
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  • RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding Source: MGI
  • RNA polymerase II transcription coactivator activity Source: Ensembl
  • RNA polymerase II transcription factor activity, sequence-specific DNA binding Source: BHF-UCL
  • sequence-specific DNA binding Source: UniProtKB
  • transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: NTNU_SB
  • transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding Source: MGI
  • transcription corepressor activity Source: MGI
  • transcription factor activity, sequence-specific DNA binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB
  • transcription regulatory region DNA binding Source: UniProtKB
  • transcription regulatory region sequence-specific DNA binding Source: MGI
  • ubiquitin protein ligase binding Source: BHF-UCL

GO - Biological processi

  • blastocyst development Source: BHF-UCL
  • blastocyst growth Source: MGI
  • BMP signaling pathway involved in heart induction Source: MGI
  • cardiac cell fate determination Source: MGI
  • cell fate commitment Source: MGI
  • cell fate commitment involved in formation of primary germ layer Source: MGI
  • cellular response to leukemia inhibitory factor Source: MGI
  • ectodermal cell fate commitment Source: MGI
  • endodermal cell fate commitment Source: MGI
  • endodermal cell fate specification Source: MGI
  • germ-line stem cell population maintenance Source: MGI
  • mesodermal cell fate commitment Source: MGI
  • mRNA transcription from RNA polymerase II promoter Source: BHF-UCL
  • negative regulation of calcium ion-dependent exocytosis Source: MGI
  • negative regulation of cell differentiation Source: MGI
  • negative regulation of gene expression Source: AgBase
  • negative regulation of gene silencing by miRNA Source: MGI
  • negative regulation of protein kinase B signaling Source: MGI
  • negative regulation of transcription, DNA-templated Source: MGI
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • positive regulation of catenin import into nucleus Source: MGI
  • positive regulation of gene expression Source: AgBase
  • positive regulation of protein kinase B signaling Source: MGI
  • positive regulation of SMAD protein import into nucleus Source: MGI
  • positive regulation of transcription, DNA-templated Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
  • regulation of asymmetric cell division Source: BHF-UCL
  • regulation of gene expression Source: MGI
  • regulation of heart induction by regulation of canonical Wnt signaling pathway Source: MGI
  • regulation of methylation-dependent chromatin silencing Source: MGI
  • regulation of transcription, DNA-templated Source: MGI
  • response to organic substance Source: MGI
  • response to retinoic acid Source: MGI
  • somatic stem cell population maintenance Source: MGI
  • stem cell differentiation Source: MGI
  • stem cell population maintenance Source: MGI
  • transcription from RNA polymerase II promoter Source: BHF-UCL
  • trophectodermal cell differentiation Source: MGI

Keywordsi

Molecular functionDevelopmental protein, DNA-binding
Biological processTranscription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-MMU-452723. Transcriptional regulation of pluripotent stem cells.

Names & Taxonomyi

Protein namesi
Recommended name:
POU domain, class 5, transcription factor 1
Alternative name(s):
NF-A3
Octamer-binding protein 3
Short name:
Oct-3
Octamer-binding protein 4
Short name:
Oct-4
Octamer-binding transcription factor 3
Short name:
OTF-3
Gene namesi
Name:Pou5f1
Synonyms:Oct-3, Oct-4, Otf-3, Otf3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:101893. Pou5f1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Biotechnological usei

POU5F1/OCT4, SOX2, MYC/c-Myc and KLF4 are the four Yamanaka factors. When combined, these factors are sufficient to reprogram differentiated cells to an embryonic-like state designated iPS (induced pluripotent stem) cells. iPS cells exhibit the morphology and growth properties of ES cells and express ES cell marker genes.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi118K → R: Absence of sumoylation. Enhanced protein degradation. Reduced self-renewal ability in ES cells. 70% lower expression of YES1. Reduced DNA binding. No change in nuclear location. No change in nuclear localization. Absence of sumoylation; when associated with R-215 and R-244. 3 Publications1
Mutagenesisi120E → A: Absence of sumoylation. Enhanced protein degradation. Reduced self-renewal ability in ES cells. 55% lower expression of YES1. 1 Publication1
Mutagenesisi215K → R: No change in sumoylation; when associated with R-244. Loss of sumoylation. No change in nuclear localization; when associated with R-118 and R-244. 1 Publication1
Mutagenesisi244K → R: No change in sumoylation. No change in sumoylation; when associated with R-215. Loss of sumoylation; when associated with R-118 and R-215. No change in nuclear localization; when associated with R-118 and R-215. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001007491 – 352POU domain, class 5, transcription factor 1Add BLAST352

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei106Phosphoserine; by MAPKBy similarity1
Cross-linki118Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei228PhosphothreonineBy similarity1
Modified residuei229PhosphoserineBy similarity1
Modified residuei282PhosphoserineBy similarity1
Modified residuei347PhosphoserineBy similarity1

Post-translational modificationi

Sumoylation enhances the protein stability, DNA binding and transactivation activity. Sumoylation is required for enhanced YES1 expression.3 Publications
Ubiquitinated; undergoes 'Lys-63'-linked polyubiquitination by WWP2 leading to proteasomal degradation.1 Publication
ERK1/2-mediated phosphorylation at Ser-106 promotes nuclear exclusion and proteasomal degradation. Phosphorylation at Thr-228 and Ser-229 decrease DNA-binding and alters ability to activate transcription (By similarity).By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP20263.
PeptideAtlasiP20263.
PRIDEiP20263.

PTM databases

iPTMnetiP20263.
PhosphoSitePlusiP20263.

Expressioni

Tissue specificityi

Expressed the totipotent and pluripotent stem cells of the pregastrulation embryo. Also expressed in primordial germ cells and in the female germ line. Absent from adult tissues.2 Publications

Developmental stagei

Down-regulated during differentiation to endoderm and mesoderm.1 Publication

Inductioni

Repressed by retinoic acid (RA).2 Publications

Gene expression databases

BgeeiENSMUSG00000024406.
CleanExiMM_POU5F1.
ExpressionAtlasiP20263. baseline and differential.
GenevisibleiP20263. MM.

Interactioni

Subunit structurei

Interacts with PKM. Interacts with WWP2 (By similarity). Interacts with UBE2I and ZSCAN10 (PubMed:17496161, PubMed:19740739). Interacts with PCGF1 (By similarity). Interacts with ESRRB; recruits ESRRB near the POU5F1-SOX2 element in the NANOG proximal promoter; the intercaction is DNA independent (PubMed:18662995).By similarity3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • cytokine binding Source: AgBase
  • HMG box domain binding Source: Ensembl
  • POU domain binding Source: Ensembl
  • protein heterodimerization activity Source: MGI
  • transcription factor binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi202313. 304 interactors.
DIPiDIP-29931N.
IntActiP20263. 142 interactors.
STRINGi10090.ENSMUSP00000025271.

Structurei

Secondary structure

1352
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi132 – 152Combined sources21
Helixi157 – 168Combined sources12
Helixi174 – 181Combined sources8
Helixi187 – 204Combined sources18
Helixi208 – 212Combined sources5
Beta strandi223 – 225Combined sources3
Helixi232 – 239Combined sources8
Turni240 – 244Combined sources5
Helixi250 – 259Combined sources10
Helixi264 – 279Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OCPNMR-A217-282[»]
3L1PX-ray2.80A/B131-282[»]
ProteinModelPortaliP20263.
SMRiP20263.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20263.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini131 – 205POU-specificPROSITE-ProRule annotationAdd BLAST75

Domaini

The POU-specific domain mediates interaction with PKM.By similarity

Sequence similaritiesi

Keywords - Domaini

Homeobox

Phylogenomic databases

eggNOGiKOG3802. Eukaryota.
ENOG410XQ7X. LUCA.
GeneTreeiENSGT00760000118935.
HOGENOMiHOG000089941.
HOVERGENiHBG057998.
InParanoidiP20263.
KOiK09367.
OMAiLENMFLQ.
OrthoDBiEOG091G0U0S.
PhylomeDBiP20263.
TreeFamiTF316413.

Family and domain databases

CDDicd00086. homeodomain. 1 hit.
InterProiView protein in InterPro
IPR009057. Homeobox-like_sf.
IPR017970. Homeobox_CS.
IPR001356. Homeobox_dom.
IPR010982. Lambda_DNA-bd_dom_sf.
IPR013847. POU.
IPR000327. POU_dom.
IPR015585. POU_dom_5.
PANTHERiPTHR11636:SF86. PTHR11636:SF86. 1 hit.
PfamiView protein in Pfam
PF00046. Homeobox. 1 hit.
PF00157. Pou. 1 hit.
PRINTSiPR00028. POUDOMAIN.
SMARTiView protein in SMART
SM00389. HOX. 1 hit.
SM00352. POU. 1 hit.
SUPFAMiSSF46689. SSF46689. 1 hit.
SSF47413. SSF47413. 1 hit.
PROSITEiView protein in PROSITE
PS00027. HOMEOBOX_1. 1 hit.
PS50071. HOMEOBOX_2. 1 hit.
PS00035. POU_1. 1 hit.
PS00465. POU_2. 1 hit.
PS51179. POU_3. 1 hit.

Sequencei

Sequence statusi: Complete.

P20263-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGHLASDFA FSPPPGGGDG SAGLEPGWVD PRTWLSFQGP PGGPGIGPGS
60 70 80 90 100
EVLGISPCPP AYEFCGGMAY CGPQVGLGLV PQVGVETLQP EGQAGARVES
110 120 130 140 150
NSEGTSSEPC ADRPNAVKLE KVEPTPEESQ DMKALQKELE QFAKLLKQKR
160 170 180 190 200
ITLGYTQADV GLTLGVLFGK VFSQTTICRF EALQLSLKNM CKLRPLLEKW
210 220 230 240 250
VEEADNNENL QEICKSETLV QARKRKRTSI ENRVRWSLET MFLKCPKPSL
260 270 280 290 300
QQITHIANQL GLEKDVVRVW FCNRRQKGKR SSIEYSQREE YEATGTPFPG
310 320 330 340 350
GAVSFPLPPG PHFGTPGYGS PHFTTLYSVP FPEGEAFPSV PVTALGSPMH

SN
Length:352
Mass (Da):38,216
Last modified:February 1, 1991 - v1
Checksum:i757E41DF52286714
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1 – 28Missing in CAA36682 (PubMed:1690859).CuratedAdd BLAST28
Sequence conflicti29V → M in CAA36682 (PubMed:1690859).Curated1
Sequence conflicti31P → S in AAA39844 (PubMed:1915274).Curated1
Sequence conflicti31P → S in AAB19896 (PubMed:1915274).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34381 mRNA. Translation: AAA39844.1. Sequence problems.
X52437 mRNA. Translation: CAA36682.1.
S58426
, S58422, S58423, S58424, S58425 Genomic DNA. Translation: AAB19896.1.
BC068268 mRNA. Translation: AAH68268.1.
CCDSiCCDS37600.1.
PIRiA34672.
S17313.
RefSeqiNP_038661.2. NM_013633.3.
UniGeneiMm.17031.

Genome annotation databases

EnsembliENSMUST00000025271; ENSMUSP00000025271; ENSMUSG00000024406.
GeneIDi18999.
KEGGimmu:18999.
UCSCiuc008chu.2. mouse.

Similar proteinsi

Entry informationi

Entry nameiPO5F1_MOUSE
AccessioniPrimary (citable) accession number: P20263
Secondary accession number(s): Q63843
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 22, 2017
This is version 175 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families