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P20263 (PO5F1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Pou5f1
Synonyms:Oct-3, Oct-4, Otf-3, Otf3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length352 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.9

Subunit structure

Interacts with PKM. Interacts with WWP2 By similarity. Interacts with UBE2I and ZSCAN10. Ref.8 Ref.10

Subcellular location

Cytoplasm By similarity. Nucleus. Note: Expressed in a diffuse and slightly punctuate pattern. Ref.8 Ref.9

Tissue specificity

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. Ref.1 Ref.2

Developmental stage

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

Induction

Repressed by retinoic acid (RA). Ref.2 Ref.4

Domain

The POU-specific domain mediates interaction with PKM By similarity. Ref.12

Post-translational modification

Sumoylation enhances the protein stability, DNA binding and transactivation activity. Sumoylation is required for enhanced YES1 expression. Ref.6 Ref.8 Ref.9

Ubiquitinated; undergoes 'Lys-63'-linked polyubiquitination by WWP2 leading to proteasomal degradation. Ref.11

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.

Biotechnological use

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. Ref.7

Sequence similarities

Belongs to the POU transcription factor family. Class-5 subfamily.

Contains 1 homeobox DNA-binding domain.

Contains 1 POU-specific domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   DomainHomeobox
   LigandDNA-binding
   Molecular functionDevelopmental protein
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processblastocyst development

Inferred from expression pattern PubMed 21258368. Source: BHF-UCL

cell fate commitment

Inferred from mutant phenotype PubMed 9814708. Source: MGI

ectodermal cell fate commitment

Inferred from direct assay PubMed 10742100. Source: MGI

endodermal cell fate commitment

Inferred from direct assay PubMed 10742100. Source: MGI

endodermal cell fate specification

Inferred from sequence orthology PubMed 21245162. Source: MGI

germ-line stem cell maintenance

Inferred from mutant phenotype PubMed 15486564. Source: MGI

mRNA transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 15047715. Source: BHF-UCL

mesodermal cell fate commitment

Inferred from direct assay PubMed 10742100. Source: MGI

negative regulation of calcium ion-dependent exocytosis

Inferred from direct assay PubMed 2357966. Source: MGI

negative regulation of cell differentiation

Inferred from genetic interaction PubMed 16325584. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from genetic interaction PubMed 16325584. Source: MGI

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.3. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.1PubMed 9649510. Source: MGI

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.3. Source: MGI

regulation of asymmetric cell division

Inferred from expression pattern PubMed 21258368. Source: BHF-UCL

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12665572. Source: MGI

response to cytokine

Inferred from electronic annotation. Source: Ensembl

response to organic substance

Inferred from direct assay PubMed 18400104. Source: MGI

response to retinoic acid

Inferred from direct assay PubMed 18400104. Source: MGI

stem cell differentiation

Inferred from direct assay PubMed 20123909. Source: MGI

stem cell maintenance

Inferred from mutant phenotype PubMed 14502573PubMed 16767105PubMed 20720539PubMed 9814708. Source: MGI

transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 15047715. Source: BHF-UCL

trophectodermal cell differentiation

Inferred from genetic interaction PubMed 16325584. Source: MGI

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 19480014PubMed 7958450. Source: MGI

nuclear transcription factor complex

Inferred from direct assay PubMed 22344693. Source: MGI

nucleolus

Inferred from direct assay PubMed 19480014. Source: MGI

nucleoplasm

Inferred from direct assay PubMed 21076177. Source: BHF-UCL

nucleus

Inferred from direct assay PubMed 18662995PubMed 21258368. Source: BHF-UCL

transcription factor complex

Inferred from direct assay PubMed 17507372PubMed 7969117. Source: MGI

transcriptional repressor complex

Inferred from direct assay PubMed 16325584. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay PubMed 12665572Ref.3. Source: MGI

RNA polymerase II transcription coactivator activity

Inferred from electronic annotation. Source: Ensembl

chromatin binding

Inferred from direct assay PubMed 15988017PubMed 18467660PubMed 21295276. Source: MGI

protein heterodimerization activity

Inferred from direct assay PubMed 22344693. Source: MGI

sequence-specific DNA binding

Inferred from direct assay PubMed 16518401Ref.2PubMed 18400104PubMed 19796622PubMed 7945330PubMed 7969117PubMed 8960364PubMed 9649510. Source: MGI

sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from direct assay PubMed 15047715. Source: BHF-UCL

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 12665572Ref.3Ref.1PubMed 2357966. Source: MGI

transcription corepressor activity

Inferred from direct assay PubMed 16325584. Source: MGI

transcription factor binding

Inferred from physical interaction PubMed 17541407PubMed 19816951. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from direct assay PubMed 17541407. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction PubMed 15047715. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 352352POU domain, class 5, transcription factor 1
PRO_0000100749

Regions

Domain131 – 20575POU-specific
DNA binding223 – 28260Homeobox

Amino acid modifications

Modified residue1061Phosphoserine; by MAPK By similarity
Modified residue2281Phosphothreonine By similarity
Modified residue2291Phosphoserine By similarity
Modified residue2821Phosphoserine By similarity
Modified residue3471Phosphoserine By similarity
Cross-link118Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.6 Ref.8 Ref.9

Experimental info

Mutagenesis1181K → 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. Ref.6 Ref.8 Ref.9
Mutagenesis1201E → A: Absence of sumoylation. Enhanced protein degradation. Reduced self-renewal ability in ES cells. 55% lower expression of YES1. Ref.8
Mutagenesis2151K → 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. Ref.8
Mutagenesis2441K → 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. Ref.8
Sequence conflict1 – 2828Missing in CAA36682. Ref.2
Sequence conflict291V → M in CAA36682. Ref.2
Sequence conflict311P → S in AAA39844. Ref.4
Sequence conflict311P → S in AAB19896. Ref.4

Secondary structure

.................... 352
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20263 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 757E41DF52286714

FASTA35238,216
        10         20         30         40         50         60 
MAGHLASDFA FSPPPGGGDG SAGLEPGWVD PRTWLSFQGP PGGPGIGPGS EVLGISPCPP 

        70         80         90        100        110        120 
AYEFCGGMAY CGPQVGLGLV PQVGVETLQP EGQAGARVES NSEGTSSEPC ADRPNAVKLE 

       130        140        150        160        170        180 
KVEPTPEESQ DMKALQKELE QFAKLLKQKR ITLGYTQADV GLTLGVLFGK VFSQTTICRF 

       190        200        210        220        230        240 
EALQLSLKNM CKLRPLLEKW VEEADNNENL QEICKSETLV QARKRKRTSI ENRVRWSLET 

       250        260        270        280        290        300 
MFLKCPKPSL QQITHIANQL GLEKDVVRVW FCNRRQKGKR SSIEYSQREE YEATGTPFPG 

       310        320        330        340        350 
GAVSFPLPPG PHFGTPGYGS PHFTTLYSVP FPEGEAFPSV PVTALGSPMH SN 

« Hide

References

« Hide 'large scale' references
[1]"A POU-domain transcription factor in early stem cells and germ cells of the mammalian embryo."
Rosner M.H., Vigano M.A., Ozato K., Timmons P.M., Poirier F., Rigby P.W.J., Staudt L.
Nature 345:686-692(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Embryonic carcinoma.
[2]"New type of POU domain in germ line-specific protein Oct-4."
Schoeler H.R., Ruppert S., Suzuki N., Chowdhury K., Gruss P.
Nature 344:435-439(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
Tissue: Embryonic carcinoma.
[3]"A novel octamer binding transcription factor is differentially expressed in mouse embryonic cells."
Okamoto K., Okazawa H., Okuda A., Sakai M., Muramatsu M., Hamada H.
Cell 60:461-472(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"The oct3 gene, a gene for an embryonic transcription factor, is controlled by a retinoic acid repressible enhancer."
Okazawa H., Okamoto K., Ishino F., Ishino-Kaneko T., Takeda S., Toyoda Y., Muramatsu M., Hamada H.
EMBO J. 10:2997-3005(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION, INDUCTION.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo.
[6]"Inhibition of DNA binding of Sox2 by the SUMO conjugation."
Tsuruzoe S., Ishihara K., Uchimura Y., Watanabe S., Sekita Y., Aoto T., Saitoh H., Yuasa Y., Niwa H., Kawasuji M., Baba H., Nakao M.
Biochem. Biophys. Res. Commun. 351:920-926(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-118, MUTAGENESIS OF LYS-118.
[7]"Induction of pluripotent stem cells from mouse embryonic and adult fibroblast cultures by defined factors."
Takahashi K., Yamanaka S.
Cell 126:663-676(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOTECHNOLOGY.
[8]"Post-translational modification of POU domain transcription factor Oct-4 by SUMO-1."
Zhang Z., Liao B., Xu M., Jin Y.
FASEB J. 21:3042-3051(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-118, MUTAGENESIS OF LYS-118; GLU-120; LYS-215 AND LYS-244, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH UBE2I.
[9]"Sumoylation of Oct4 enhances its stability, DNA binding, and transactivation."
Wei F., Schoeler H.R., Atchison M.L.
J. Biol. Chem. 282:21551-21560(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-118, MUTAGENESIS OF LYS-118, FUNCTION, SUBCELLULAR LOCATION.
[10]"Zfp206, Oct4, and Sox2 are integrated components of a transcriptional regulatory network in embryonic stem cells."
Yu H.B., Kunarso G., Hong F.H., Stanton L.W.
J. Biol. Chem. 284:31327-31335(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZSCAN10.
[11]"Wwp2 mediates Oct4 ubiquitination and its own auto-ubiquitination in a dosage-dependent manner."
Liao B., Jin Y.
Cell Res. 20:332-344(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[12]"Secondary structure of the oct-3 POU homeodomain as determined by 1H-15N NMR spectroscopy."
Morita E.H., Shirakawa M., Hayashi F., Imagawa M., Kyogoku Y.
FEBS Lett. 321:107-110(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF POU DOMAIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M34381 mRNA. Translation: AAA39844.1. Sequence problems.
X52437 mRNA. Translation: CAA36682.1.
S58426 expand/collapse EMBL AC list , S58422, S58423, S58424, S58425 Genomic DNA. Translation: AAB19896.1.
BC068268 mRNA. Translation: AAH68268.1.
PIRA34672.
S17313.
RefSeqNP_038661.2. NM_013633.3.
UniGeneMm.17031.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OCPNMR-A217-282[»]
3L1PX-ray2.80A/B131-282[»]
ProteinModelPortalP20263.
SMRP20263. Positions 131-282.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202313. 298 interactions.
DIPDIP-29931N.
IntActP20263. 137 interactions.
STRING10090.ENSMUSP00000025271.

PTM databases

PhosphoSiteP20263.

Proteomic databases

PRIDEP20263.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025271; ENSMUSP00000025271; ENSMUSG00000024406.
GeneID18999.
KEGGmmu:18999.
UCSCuc008chu.2. mouse.

Organism-specific databases

CTD5460.
MGIMGI:101893. Pou5f1.

Phylogenomic databases

eggNOGNOG329627.
GeneTreeENSGT00750000117482.
HOGENOMHOG000089941.
HOVERGENHBG057998.
InParanoidP20263.
KOK09367.
OMALENMFLQ.
OrthoDBEOG7DJSMG.
PhylomeDBP20263.
TreeFamTF316413.

Gene expression databases

BgeeP20263.
CleanExMM_POU5F1.
GenevestigatorP20263.

Family and domain databases

Gene3D1.10.10.60. 1 hit.
1.10.260.40. 1 hit.
InterProIPR017970. Homeobox_CS.
IPR001356. Homeobox_dom.
IPR009057. Homeodomain-like.
IPR010982. Lambda_DNA-bd_dom.
IPR013847. POU.
IPR015585. POU_dom_5/6.
IPR000327. POU_specific.
[Graphical view]
PANTHERPTHR11636:SF15. PTHR11636:SF15. 1 hit.
PfamPF00046. Homeobox. 1 hit.
PF00157. Pou. 1 hit.
[Graphical view]
PRINTSPR00028. POUDOMAIN.
SMARTSM00389. HOX. 1 hit.
SM00352. POU. 1 hit.
[Graphical view]
SUPFAMSSF46689. SSF46689. 1 hit.
SSF47413. SSF47413. 1 hit.
PROSITEPS00027. HOMEOBOX_1. 1 hit.
PS50071. HOMEOBOX_2. 1 hit.
PS00035. POU_1. 1 hit.
PS00465. POU_2. 1 hit.
PS51179. POU_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP20263.
NextBio295410.
PROP20263.
SOURCESearch...

Entry information

Entry namePO5F1_MOUSE
AccessionPrimary (citable) accession number: P20263
Secondary accession number(s): Q63843
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: April 16, 2014
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot