Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P20263

- PO5F1_MOUSE

UniProt

P20263 - PO5F1_MOUSE

Protein

POU domain, class 5, transcription factor 1

Gene

Pou5f1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi223 – 28260HomeoboxPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: MGI
    2. DNA binding Source: MGI
    3. protein binding Source: UniProtKB
    4. protein heterodimerization activity Source: MGI
    5. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
    6. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
    7. RNA polymerase II transcription coactivator activity Source: Ensembl
    8. sequence-specific DNA binding Source: MGI
    9. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: BHF-UCL
    10. sequence-specific DNA binding transcription factor activity Source: MGI
    11. transcription corepressor activity Source: MGI
    12. transcription factor binding Source: UniProtKB
    13. transcription regulatory region DNA binding Source: UniProtKB
    14. ubiquitin protein ligase binding Source: BHF-UCL

    GO - Biological processi

    1. blastocyst development Source: BHF-UCL
    2. cell fate commitment Source: MGI
    3. ectodermal cell fate commitment Source: MGI
    4. endodermal cell fate commitment Source: MGI
    5. endodermal cell fate specification Source: MGI
    6. germ-line stem cell maintenance Source: MGI
    7. mesodermal cell fate commitment Source: MGI
    8. mRNA transcription from RNA polymerase II promoter Source: BHF-UCL
    9. negative regulation of calcium ion-dependent exocytosis Source: MGI
    10. negative regulation of cell differentiation Source: MGI
    11. negative regulation of transcription, DNA-templated Source: MGI
    12. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    13. positive regulation of transcription, DNA-templated Source: MGI
    14. positive regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
    15. regulation of asymmetric cell division Source: BHF-UCL
    16. regulation of transcription, DNA-templated Source: MGI
    17. response to cytokine Source: Ensembl
    18. response to organic substance Source: MGI
    19. response to retinoic acid Source: MGI
    20. stem cell differentiation Source: MGI
    21. stem cell maintenance Source: MGI
    22. transcription from RNA polymerase II promoter Source: BHF-UCL
    23. trophectodermal cell differentiation Source: MGI

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_216222. Transcriptional regulation of pluripotent stem cells.
    REACT_220962. POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.

    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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:101893. Pou5f1.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus 2 PublicationsPROSITE-ProRule annotation
    Note: Expressed in a diffuse and slightly punctuate pattern.

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. nuclear transcription factor complex Source: MGI
    3. nucleolus Source: MGI
    4. nucleoplasm Source: BHF-UCL
    5. nucleus Source: BHF-UCL
    6. transcriptional repressor complex Source: MGI
    7. transcription factor complex Source: MGI

    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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi118 – 1181K → 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 Publications
    Mutagenesisi120 – 1201E → A: Absence of sumoylation. Enhanced protein degradation. Reduced self-renewal ability in ES cells. 55% lower expression of YES1. 1 Publication
    Mutagenesisi215 – 2151K → 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 Publication
    Mutagenesisi244 – 2441K → 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 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 352352POU domain, class 5, transcription factor 1PRO_0000100749Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei106 – 1061Phosphoserine; by MAPKBy similarity
    Cross-linki118 – 118Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei228 – 2281PhosphothreonineBy similarity
    Modified residuei229 – 2291PhosphoserineBy similarity
    Modified residuei282 – 2821PhosphoserineBy similarity
    Modified residuei347 – 3471PhosphoserineBy similarity

    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

    PRIDEiP20263.

    PTM databases

    PhosphoSiteiP20263.

    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

    BgeeiP20263.
    CleanExiMM_POU5F1.
    GenevestigatoriP20263.

    Interactioni

    Subunit structurei

    Interacts with PKM. Interacts with WWP2 By similarity. Interacts with UBE2I and ZSCAN10.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Cdk1P114404EBI-1606219,EBI-846949
    Ewsr1Q6154513EBI-1606219,EBI-1606991
    Mta2Q9R1906EBI-1606219,EBI-904134
    NanogQ80Z644EBI-1606219,EBI-2312517
    Nr0b1Q610665EBI-1606219,EBI-2312665
    Parp1P111032EBI-1606219,EBI-642213
    PkmP524806EBI-1606219,EBI-647785
    Smad3Q8BUN513EBI-1606219,EBI-2337983
    Sox2P484324EBI-1606219,EBI-2313612
    Wdr5P619657EBI-1606219,EBI-1247084

    Protein-protein interaction databases

    BioGridi202313. 298 interactions.
    DIPiDIP-29931N.
    IntActiP20263. 137 interactions.
    STRINGi10090.ENSMUSP00000025271.

    Structurei

    Secondary structure

    1
    352
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi132 – 15221
    Helixi157 – 16812
    Helixi174 – 1818
    Helixi187 – 20418
    Helixi208 – 2125
    Beta strandi223 – 2253
    Helixi232 – 2398
    Turni240 – 2445
    Helixi250 – 25910
    Helixi264 – 27916

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OCPNMR-A217-282[»]
    3L1PX-ray2.80A/B131-282[»]
    ProteinModelPortaliP20263.
    SMRiP20263. Positions 131-282.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20263.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini131 – 20575POU-specificPROSITE-ProRule annotationAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Contains 1 homeobox DNA-binding domain.PROSITE-ProRule annotation
    Contains 1 POU-specific domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Homeobox

    Phylogenomic databases

    eggNOGiNOG329627.
    GeneTreeiENSGT00750000117482.
    HOGENOMiHOG000089941.
    HOVERGENiHBG057998.
    InParanoidiP20263.
    KOiK09367.
    OMAiLENMFLQ.
    OrthoDBiEOG7DJSMG.
    PhylomeDBiP20263.
    TreeFamiTF316413.

    Family and domain databases

    Gene3Di1.10.10.60. 1 hit.
    1.10.260.40. 1 hit.
    InterProiIPR017970. Homeobox_CS.
    IPR001356. Homeobox_dom.
    IPR009057. Homeodomain-like.
    IPR010982. Lambda_DNA-bd_dom.
    IPR013847. POU.
    IPR015585. POU_dom_5.
    IPR000327. POU_specific.
    [Graphical view]
    PANTHERiPTHR11636:SF15. PTHR11636:SF15. 1 hit.
    PfamiPF00046. Homeobox. 1 hit.
    PF00157. Pou. 1 hit.
    [Graphical view]
    PRINTSiPR00028. POUDOMAIN.
    SMARTiSM00389. HOX. 1 hit.
    SM00352. POU. 1 hit.
    [Graphical view]
    SUPFAMiSSF46689. SSF46689. 1 hit.
    SSF47413. SSF47413. 1 hit.
    PROSITEiPS00027. 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]

    Sequencei

    Sequence statusi: Complete.

    P20263-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGHLASDFA FSPPPGGGDG SAGLEPGWVD PRTWLSFQGP PGGPGIGPGS    50
    EVLGISPCPP AYEFCGGMAY CGPQVGLGLV PQVGVETLQP EGQAGARVES 100
    NSEGTSSEPC ADRPNAVKLE KVEPTPEESQ DMKALQKELE QFAKLLKQKR 150
    ITLGYTQADV GLTLGVLFGK VFSQTTICRF EALQLSLKNM CKLRPLLEKW 200
    VEEADNNENL QEICKSETLV QARKRKRTSI ENRVRWSLET MFLKCPKPSL 250
    QQITHIANQL GLEKDVVRVW FCNRRQKGKR SSIEYSQREE YEATGTPFPG 300
    GAVSFPLPPG PHFGTPGYGS PHFTTLYSVP FPEGEAFPSV PVTALGSPMH 350
    SN 352
    Length:352
    Mass (Da):38,216
    Last modified:February 1, 1991 - v1
    Checksum:i757E41DF52286714
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 2828Missing in CAA36682. (PubMed:1690859)CuratedAdd
    BLAST
    Sequence conflicti29 – 291V → M in CAA36682. (PubMed:1690859)Curated
    Sequence conflicti31 – 311P → S in AAA39844. (PubMed:1915274)Curated
    Sequence conflicti31 – 311P → S in AAB19896. (PubMed:1915274)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS37600.1.
    PIRi A34672.
    S17313.
    RefSeqi NP_038661.2. NM_013633.3.
    UniGenei Mm.17031.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1OCP NMR - A 217-282 [» ]
    3L1P X-ray 2.80 A/B 131-282 [» ]
    ProteinModelPortali P20263.
    SMRi P20263. Positions 131-282.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202313. 298 interactions.
    DIPi DIP-29931N.
    IntActi P20263. 137 interactions.
    STRINGi 10090.ENSMUSP00000025271.

    PTM databases

    PhosphoSitei P20263.

    Proteomic databases

    PRIDEi P20263.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025271 ; ENSMUSP00000025271 ; ENSMUSG00000024406 .
    GeneIDi 18999.
    KEGGi mmu:18999.
    UCSCi uc008chu.2. mouse.

    Organism-specific databases

    CTDi 5460.
    MGIi MGI:101893. Pou5f1.

    Phylogenomic databases

    eggNOGi NOG329627.
    GeneTreei ENSGT00750000117482.
    HOGENOMi HOG000089941.
    HOVERGENi HBG057998.
    InParanoidi P20263.
    KOi K09367.
    OMAi LENMFLQ.
    OrthoDBi EOG7DJSMG.
    PhylomeDBi P20263.
    TreeFami TF316413.

    Enzyme and pathway databases

    Reactomei REACT_216222. Transcriptional regulation of pluripotent stem cells.
    REACT_220962. POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.

    Miscellaneous databases

    EvolutionaryTracei P20263.
    NextBioi 295410.
    PROi P20263.
    SOURCEi Search...

    Gene expression databases

    Bgeei P20263.
    CleanExi MM_POU5F1.
    Genevestigatori P20263.

    Family and domain databases

    Gene3Di 1.10.10.60. 1 hit.
    1.10.260.40. 1 hit.
    InterProi IPR017970. Homeobox_CS.
    IPR001356. Homeobox_dom.
    IPR009057. Homeodomain-like.
    IPR010982. Lambda_DNA-bd_dom.
    IPR013847. POU.
    IPR015585. POU_dom_5.
    IPR000327. POU_specific.
    [Graphical view ]
    PANTHERi PTHR11636:SF15. PTHR11636:SF15. 1 hit.
    Pfami PF00046. Homeobox. 1 hit.
    PF00157. Pou. 1 hit.
    [Graphical view ]
    PRINTSi PR00028. POUDOMAIN.
    SMARTi SM00389. HOX. 1 hit.
    SM00352. POU. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46689. SSF46689. 1 hit.
    SSF47413. SSF47413. 1 hit.
    PROSITEi 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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.

    Entry informationi

    Entry nameiPO5F1_MOUSE
    AccessioniPrimary (citable) accession number: P20263
    Secondary accession number(s): Q63843
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 147 of the entry and version 1 of the sequence. [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

    External Data

    Dasty 3