PO5F1_HUMAN
ID PO5F1_HUMAN Reviewed; 360 AA.
AC Q01860; A6NCS1; A6NLL8; D2IYK4; P31359; Q15167; Q15168; Q16422; Q5STF3;
AC Q5STF4;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=POU domain, class 5, transcription factor 1;
DE AltName: Full=Octamer-binding protein 3;
DE Short=Oct-3;
DE AltName: Full=Octamer-binding protein 4;
DE Short=Oct-4;
DE AltName: Full=Octamer-binding transcription factor 3;
DE Short=OTF-3;
GN Name=POU5F1; Synonyms=OCT3, OCT4, OTF3;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), VARIANTS ALA-322 AND
RP LEU-357, AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=1408763; DOI=10.1093/nar/20.17.4613;
RA Takeda J., Seino S., Bell G.I.;
RT "Human Oct3 gene family: cDNA sequences, alternative splicing, gene
RT organization, chromosomal location, and expression at low levels in adult
RT tissues.";
RL Nucleic Acids Res. 20:4613-4620(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RX PubMed=20604894; DOI=10.1111/j.1399-0039.2010.01526.x;
RA Stuart P.E., Nair R.P., Hiremagalore R., Kullavanijaya P.,
RA Kullavanijaya P., Tejasvi T., Lim H.W., Voorhees J.J., Elder J.T.;
RT "Comparison of MHC class I risk haplotypes in Thai and Caucasian psoriatics
RT shows locus heterogeneity at PSORS1.";
RL Tissue Antigens 76:387-397(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Peripheral blood leukocyte;
RX PubMed=16702430; DOI=10.1534/genetics.106.057034;
RA Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M.,
RA Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K.,
RA Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A.,
RA Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T.,
RA Inoko H., Bahram S.;
RT "Rapid evolution of major histocompatibility complex class I genes in
RT primates generates new disease alleles in humans via hitchhiking
RT diversity.";
RL Genetics 173:1555-1570(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shiina S., Tamiya G., Oka A., Inoko H.;
RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 188-274, AND TISSUE SPECIFICITY.
RC TISSUE=Heart, and Skeletal muscle;
RX PubMed=7908264; DOI=10.1111/j.1432-1033.1994.tb18676.x;
RA Wey E., Lyons G.E., Schaefer B.W.;
RT "A human POU domain gene, mPOU, is expressed in developing brain and
RT specific adult tissues.";
RL Eur. J. Biochem. 220:753-762(1994).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 212-283.
RX PubMed=8567814; DOI=10.1093/oxfordjournals.humrep.a135792;
RA Abdel-Rahman B., Fiddler M., Rappolee D., Pergament E.;
RT "Expression of transcription regulating genes in human preimplantation
RT embryos.";
RL Hum. Reprod. 10:2787-2792(1995).
RN [10]
RP IDENTIFICATION.
RX PubMed=16229821; DOI=10.1016/j.bbrc.2005.09.157;
RA Suo G., Han J., Wang X., Zhang J., Zhao Y., Zhao Y., Dai J.;
RT "Oct4 pseudogenes are transcribed in cancers.";
RL Biochem. Biophys. Res. Commun. 337:1047-1051(2005).
RN [11]
RP BIOTECHNOLOGY, AND FUNCTION.
RX PubMed=18035408; DOI=10.1016/j.cell.2007.11.019;
RA Takahashi K., Tanabe K., Ohnuki M., Narita M., Ichisaka T., Tomoda K.,
RA Yamanaka S.;
RT "Induction of pluripotent stem cells from adult human fibroblasts by
RT defined factors.";
RL Cell 131:861-872(2007).
RN [12]
RP INTERACTION WITH PKM, SUBCELLULAR LOCATION, DOMAIN, AND INDUCTION.
RX PubMed=18191611; DOI=10.1016/j.biocel.2007.11.009;
RA Lee J., Kim H.K., Han Y.-M., Kim J.;
RT "Pyruvate kinase isozyme type M2 (PKM2) interacts and cooperates with Oct-4
RT in regulating transcription.";
RL Int. J. Biochem. Cell Biol. 40:1043-1054(2008).
RN [13]
RP UBIQUITINATION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INTERACTION
RP WITH WWP2.
RX PubMed=19274063; DOI=10.1038/cr.2009.31;
RA Xu H., Wang W., Li C., Yu H., Yang A., Wang B., Jin Y.;
RT "WWP2 promotes degradation of transcription factor OCT4 in human embryonic
RT stem cells.";
RL Cell Res. 19:561-573(2009).
RN [14]
RP PHOSPHORYLATION AT SER-111, AND SUBCELLULAR LOCATION.
RX PubMed=23024368; DOI=10.1074/jbc.m112.386755;
RA Spelat R., Ferro F., Curcio F.;
RT "Serine 111 phosphorylation regulates OCT4A protein subcellular
RT distribution and degradation.";
RL J. Biol. Chem. 287:38279-38288(2012).
RN [15]
RP PHOSPHORYLATION AT SER-111; THR-235; SER-236; SER-289; SER-290 AND SER-355.
RX PubMed=22474382; DOI=10.1073/pnas.1203874109;
RA Brumbaugh J., Hou Z., Russell J.D., Howden S.E., Yu P., Ledvina A.R.,
RA Coon J.J., Thomson J.A.;
RT "Phosphorylation regulates human OCT4.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:7162-7168(2012).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH PCGF1.
RX PubMed=26687479; DOI=10.1038/srep18388;
RA Oliviero G., Munawar N., Watson A., Streubel G., Manning G., Bardwell V.,
RA Bracken A.P., Cagney G.;
RT "The variant Polycomb Repressor Complex 1 component PCGF1 interacts with a
RT pluripotency sub-network that includes DPPA4, a regulator of
RT embryogenesis.";
RL Sci. Rep. 5:18388-18388(2015).
RN [17]
RP 9AATAD MOTIF.
RX PubMed=34342803; DOI=10.1007/s12015-021-10225-8;
RA Piskacek M., Otasevic T., Repko M., Knight A.;
RT "The 9aaTAD Activation Domains in the Yamanaka Transcription Factors Oct4,
RT Sox2, Myc, and Klf4.";
RL Stem. Cell. Rev. Rep. 17:1934-1936(2021).
CC -!- FUNCTION: Transcription factor that binds to the octamer motif (5'-
CC ATTTGCAT-3'). Forms a trimeric complex with SOX2 or SOX15 on DNA and
CC controls the expression of a number of genes involved in embryonic
CC development such as YES1, FGF4, UTF1 and ZFP206. Critical for early
CC embryogenesis and for embryonic stem cell pluripotency.
CC {ECO:0000269|PubMed:18035408}.
CC -!- SUBUNIT: Interacts with PKM. Interacts with WWP2. Interacts with UBE2I
CC and ZSCAN10 (By similarity). Interacts with PCGF1 (PubMed:26687479).
CC Interacts with ESRRB; recruits ESRRB near the POU5F1-SOX2 element in
CC the NANOG proximal promoter; the interaction is DNA independent (By
CC similarity). Interacts with ZNF322 (By similarity). Interacts with
CC MAPK8 and MAPK9; the interaction allows MAPK8 and MAPK9 to
CC phosphorylate POU5F1 on Ser-355 (By similarity). Interacts (when
CC phosphorylated on Ser-355) with FBXW8 (By similarity). Interacts with
CC FBXW4 (By similarity). Interacts with SOX2 and SOX15; binds
CC synergistically with either SOX2 or SOX15 to DNA (By similarity).
CC {ECO:0000250|UniProtKB:P20263, ECO:0000269|PubMed:18191611,
CC ECO:0000269|PubMed:19274063, ECO:0000269|PubMed:26687479}.
CC -!- INTERACTION:
CC Q01860; P49711: CTCF; NbExp=2; IntAct=EBI-475687, EBI-932887;
CC Q01860; Q9UJU5: FOXD3; NbExp=2; IntAct=EBI-475687, EBI-475674;
CC Q01860; O95983: MBD3; NbExp=3; IntAct=EBI-475687, EBI-1783068;
CC Q01860; P48431: SOX2; NbExp=2; IntAct=EBI-475687, EBI-6124081;
CC Q01860; O00308: WWP2; NbExp=4; IntAct=EBI-475687, EBI-743923;
CC Q01860; Q8JSK4: E1A; Xeno; NbExp=2; IntAct=EBI-475687, EBI-7453955;
CC Q01860; P63158: Hmgb1; Xeno; NbExp=3; IntAct=EBI-475687, EBI-6665811;
CC Q01860; P03259; Xeno; NbExp=2; IntAct=EBI-475687, EBI-6947456;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Expressed in a diffuse
CC and slightly punctuate pattern. Colocalizes with MAPK8 and MAPK9 in the
CC nucleus. {ECO:0000250|UniProtKB:P20263, ECO:0000269|PubMed:18191611,
CC ECO:0000269|PubMed:19274063, ECO:0000269|PubMed:23024368}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A; Synonyms=Oct-3A, Oct3A;
CC IsoId=Q01860-1; Sequence=Displayed;
CC Name=B; Synonyms=Oct-3B, Oct3B;
CC IsoId=Q01860-2; Sequence=VSP_002333;
CC -!- TISSUE SPECIFICITY: Expressed in developing brain. Highest levels found
CC in specific cell layers of the cortex, the olfactory bulb, the
CC hippocampus and the cerebellum. Low levels of expression in adult
CC tissues. {ECO:0000269|PubMed:1408763, ECO:0000269|PubMed:7908264}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in undifferentiated embryonic
CC stem cells and expression decreases gradually after embryoid body (EB)
CC formation. {ECO:0000269|PubMed:19274063}.
CC -!- INDUCTION: Transcriptional activity is positively regulated by PKM.
CC {ECO:0000269|PubMed:18191611}.
CC -!- DOMAIN: The POU-specific domain mediates interaction with PKM.
CC {ECO:0000269|PubMed:18191611}.
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000269|PubMed:34342803}.
CC -!- PTM: Sumoylation enhances the protein stability, DNA binding and
CC transactivation activity. Sumoylation is required for enhanced YES1
CC expression. {ECO:0000250|UniProtKB:P20263}.
CC -!- PTM: Ubiquitinated; undergoes 'Lys-63'-linked polyubiquitination by
CC WWP2 leading to proteasomal degradation.
CC {ECO:0000250|UniProtKB:P20263}.
CC -!- PTM: ERK1/2-mediated phosphorylation at Ser-111 promotes nuclear
CC exclusion and proteasomal degradation. Phosphorylation at Thr-235 and
CC Ser-236 decrease DNA-binding and alters ability to activate
CC transcription. {ECO:0000269|PubMed:22474382,
CC ECO:0000269|PubMed:23024368}.
CC -!- BIOTECHNOLOGY: POU5F1/OCT4, SOX2, MYC/c-Myc and KLF4 are the four
CC Yamanaka factors. When combined, these factors are sufficient to
CC reprogram differentiated cells to an embryonic-like state designated
CC iPS (induced pluripotent stem) cells. iPS cells exhibit the morphology
CC and growth properties of ES cells and express ES cell marker genes.
CC {ECO:0000269|PubMed:18035408}.
CC -!- MISCELLANEOUS: Several pseudogenes of POU5F1 have been described on
CC chromosomes 1, 3, 8, 10 and 12. 2 of them, localized in chromosomes 8
CC and 10, are transcribed in cancer tissues but not in normal ones and
CC may be involved in the regulation of POU5F1 gene activity in
CC carcinogenesis.
CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-5
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Oct-4 entry;
CC URL="https://en.wikipedia.org/wiki/Oct-4";
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DR EMBL; Z11898; CAA77951.1; -; mRNA.
DR EMBL; Z11899; CAA77952.1; -; mRNA.
DR EMBL; GQ472773; ACZ95700.1; -; Genomic_DNA.
DR EMBL; AB088113; BAC54946.1; -; Genomic_DNA.
DR EMBL; AB202105; BAE78630.1; -; Genomic_DNA.
DR EMBL; AB103619; BAF31281.1; -; Genomic_DNA.
DR EMBL; BA000025; BAB63311.1; -; Genomic_DNA.
DR EMBL; AL662833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL773544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX088580; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR388229; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR847794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03367.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03368.1; -; Genomic_DNA.
DR EMBL; BC117435; AAI17436.1; -; mRNA.
DR EMBL; BC117437; AAI17438.1; -; mRNA.
DR EMBL; Z21963; CAA79974.1; -; mRNA.
DR EMBL; Z21964; CAA79975.1; -; mRNA.
DR EMBL; S81255; AAB35990.1; -; mRNA.
DR CCDS; CCDS34391.1; -. [Q01860-1]
DR PIR; S25561; S25561.
DR PIR; S32652; S32652.
DR RefSeq; NP_001272916.1; NM_001285987.1. [Q01860-2]
DR RefSeq; NP_002692.2; NM_002701.5. [Q01860-1]
DR PDB; 6T90; EM; 3.05 A; K=1-360.
DR PDB; 6YOV; EM; 3.42 A; K=1-360.
DR PDBsum; 6T90; -.
DR PDBsum; 6YOV; -.
DR AlphaFoldDB; Q01860; -.
DR SMR; Q01860; -.
DR BioGRID; 111456; 328.
DR CORUM; Q01860; -.
DR DIP; DIP-33440N; -.
DR ELM; Q01860; -.
DR IntAct; Q01860; 19.
DR MINT; Q01860; -.
DR STRING; 9606.ENSP00000259915; -.
DR BindingDB; Q01860; -.
DR ChEMBL; CHEMBL3580526; -.
DR DrugBank; DB00988; Dopamine.
DR DrugBank; DB00368; Norepinephrine.
DR iPTMnet; Q01860; -.
DR PhosphoSitePlus; Q01860; -.
DR SwissPalm; Q01860; -.
DR BioMuta; POU5F1; -.
DR DMDM; 400659; -.
DR EPD; Q01860; -.
DR jPOST; Q01860; -.
DR MassIVE; Q01860; -.
DR MaxQB; Q01860; -.
DR PaxDb; Q01860; -.
DR PeptideAtlas; Q01860; -.
DR PRIDE; Q01860; -.
DR ProteomicsDB; 58011; -. [Q01860-1]
DR ProteomicsDB; 58012; -. [Q01860-2]
DR Antibodypedia; 26854; 1500 antibodies from 51 providers.
DR DNASU; 5460; -.
DR Ensembl; ENST00000259915.13; ENSP00000259915.7; ENSG00000204531.21. [Q01860-1]
DR Ensembl; ENST00000376243.8; ENSP00000365419.4; ENSG00000206454.12. [Q01860-2]
DR Ensembl; ENST00000383524.4; ENSP00000373016.4; ENSG00000206454.12. [Q01860-1]
DR Ensembl; ENST00000412166.6; ENSP00000387646.2; ENSG00000229094.9. [Q01860-2]
DR Ensembl; ENST00000419095.2; ENSP00000413622.2; ENSG00000235068.9. [Q01860-2]
DR Ensembl; ENST00000429314.2; ENSP00000387619.2; ENSG00000237582.10. [Q01860-2]
DR Ensembl; ENST00000429603.2; ENSP00000392877.2; ENSG00000233911.9. [Q01860-1]
DR Ensembl; ENST00000433063.6; ENSP00000405041.2; ENSG00000235068.9. [Q01860-1]
DR Ensembl; ENST00000433348.2; ENSP00000412665.2; ENSG00000230336.9. [Q01860-2]
DR Ensembl; ENST00000434616.2; ENSP00000388842.2; ENSG00000229094.9. [Q01860-1]
DR Ensembl; ENST00000437747.6; ENSP00000391681.2; ENSG00000237582.10. [Q01860-1]
DR Ensembl; ENST00000451077.6; ENSP00000391507.2; ENSG00000233911.9. [Q01860-2]
DR Ensembl; ENST00000454714.6; ENSP00000400047.2; ENSG00000230336.9. [Q01860-1]
DR GeneID; 5460; -.
DR KEGG; hsa:5460; -.
DR MANE-Select; ENST00000259915.13; ENSP00000259915.7; NM_002701.6; NP_002692.2.
DR UCSC; uc003nsv.4; human. [Q01860-1]
DR CTD; 5460; -.
DR DisGeNET; 5460; -.
DR GeneCards; POU5F1; -.
DR HGNC; HGNC:9221; POU5F1.
DR HPA; ENSG00000204531; Tissue enhanced (kidney).
DR MIM; 164177; gene.
DR neXtProt; NX_Q01860; -.
DR OpenTargets; ENSG00000204531; -.
DR PharmGKB; PA33545; -.
DR VEuPathDB; HostDB:ENSG00000204531; -.
DR eggNOG; KOG3802; Eukaryota.
DR GeneTree; ENSGT00940000155046; -.
DR HOGENOM; CLU_066243_0_0_1; -.
DR InParanoid; Q01860; -.
DR OMA; CPQPYEF; -.
DR PhylomeDB; Q01860; -.
DR TreeFam; TF316413; -.
DR PathwayCommons; Q01860; -.
DR Reactome; R-HSA-2892245; POU5F1 (OCT4), SOX2, NANOG repress genes related to differentiation.
DR Reactome; R-HSA-2892247; POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.
DR Reactome; R-HSA-452723; Transcriptional regulation of pluripotent stem cells.
DR SignaLink; Q01860; -.
DR SIGNOR; Q01860; -.
DR BioGRID-ORCS; 5460; 111 hits in 1029 CRISPR screens.
DR GenomeRNAi; 5460; -.
DR Pharos; Q01860; Tbio.
DR PRO; PR:Q01860; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q01860; protein.
DR Bgee; ENSG00000204531; Expressed in right uterine tube and 100 other tissues.
DR ExpressionAtlas; Q01860; baseline and differential.
DR Genevisible; Q01860; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IDA:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; IDA:HGNC-UCL.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:HGNC-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:BHF-UCL.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:BHF-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL.
DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR GO; GO:0001824; P:blastocyst development; ISS:BHF-UCL.
DR GO; GO:0003130; P:BMP signaling pathway involved in heart induction; IMP:BHF-UCL.
DR GO; GO:0060913; P:cardiac cell fate determination; IDA:BHF-UCL.
DR GO; GO:0060795; P:cell fate commitment involved in formation of primary germ layer; IMP:BHF-UCL.
DR GO; GO:0001714; P:endodermal cell fate specification; IDA:MGI.
DR GO; GO:1902894; P:negative regulation of miRNA transcription; IDA:ARUK-UCL.
DR GO; GO:0060965; P:negative regulation of miRNA-mediated gene silencing; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IDA:BHF-UCL.
DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0009786; P:regulation of asymmetric cell division; ISS:BHF-UCL.
DR GO; GO:0090308; P:regulation of DNA methylation-dependent heterochromatin assembly; IDA:BHF-UCL.
DR GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0090081; P:regulation of heart induction by regulation of canonical Wnt signaling pathway; IMP:BHF-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:HGNC-UCL.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IDA:UniProtKB.
DR CDD; cd00086; homeodomain; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR013847; POU.
DR InterPro; IPR000327; POU_dom.
DR InterPro; IPR015585; POU_dom_5.
DR PANTHER; PTHR11636:SF86; PTHR11636:SF86; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF00157; Pou; 1.
DR PRINTS; PR00028; POUDOMAIN.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00352; POU; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS00035; POU_1; 1.
DR PROSITE; PS00465; POU_2; 1.
DR PROSITE; PS51179; POU_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Developmental protein;
KW DNA-binding; Homeobox; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..360
FT /note="POU domain, class 5, transcription factor 1"
FT /id="PRO_0000100747"
FT DOMAIN 138..212
FT /note="POU-specific"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00530"
FT DNA_BIND 230..289
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..186
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P20263"
FT REGION 193..196
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P20263"
FT MOTIF 4..12
FT /note="9aaTAD"
FT /evidence="ECO:0000269|PubMed:34342803"
FT BINDING 157
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250|UniProtKB:P20263"
FT BINDING 164
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250|UniProtKB:P20263"
FT MOD_RES 111
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000269|PubMed:22474382,
FT ECO:0000269|PubMed:23024368"
FT MOD_RES 235
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22474382"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22474382"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22474382"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22474382"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22474382"
FT CROSSLNK 123
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:P20263"
FT VAR_SEQ 1..135
FT /note="MAGHLASDFAFSPPPGGGGDGPGGPEPGWVDPRTWLSFQGPPGGPGIGPGVG
FT PGSEVWGIPPCPPPYEFCGGMAYCGPQVGVGLVPQGGLETSQPEGEAGVGVESNSDGAS
FT PEPCTVTPGAVKLEKEKLEQNPEE -> MHFYRLFLGATRRFLNPEWKGEIDNWCVYVL
FT TSLLPFKIQ (in isoform B)"
FT /evidence="ECO:0000303|PubMed:1408763"
FT /id="VSP_002333"
FT VARIANT 226
FT /note="L -> F (in dbSNP:rs1150767)"
FT /id="VAR_046203"
FT VARIANT 322
FT /note="T -> A"
FT /evidence="ECO:0000269|PubMed:1408763"
FT /id="VAR_003774"
FT VARIANT 351
FT /note="T -> I (in dbSNP:rs1061120)"
FT /id="VAR_046204"
FT VARIANT 357
FT /note="M -> L"
FT /evidence="ECO:0000269|PubMed:1408763"
FT /id="VAR_003775"
FT CONFLICT 189
FT /note="A -> G (in Ref. 8; CAA79974)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="I -> T (in Ref. 8; CAA79974)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="V -> L (in Ref. 8; CAA79974)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="R -> G (in Ref. 8; CAA79975)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="R -> Q (in Ref. 8; CAA79975)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="Q -> R (in Ref. 8; CAA79975)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="D -> DVVR (in Ref. 9; AAB35990)"
FT /evidence="ECO:0000305"
FT HELIX 139..159
FT /evidence="ECO:0007829|PDB:6T90"
FT HELIX 164..175
FT /evidence="ECO:0007829|PDB:6T90"
FT HELIX 181..188
FT /evidence="ECO:0007829|PDB:6T90"
FT HELIX 194..209
FT /evidence="ECO:0007829|PDB:6T90"
SQ SEQUENCE 360 AA; 38571 MW; 934C58DAEA0C535B CRC64;
MAGHLASDFA FSPPPGGGGD GPGGPEPGWV DPRTWLSFQG PPGGPGIGPG VGPGSEVWGI
PPCPPPYEFC GGMAYCGPQV GVGLVPQGGL ETSQPEGEAG VGVESNSDGA SPEPCTVTPG
AVKLEKEKLE QNPEESQDIK ALQKELEQFA KLLKQKRITL GYTQADVGLT LGVLFGKVFS
QTTICRFEAL QLSFKNMCKL RPLLQKWVEE ADNNENLQEI CKAETLVQAR KRKRTSIENR
VRGNLENLFL QCPKPTLQQI SHIAQQLGLE KDVVRVWFCN RRQKGKRSSS DYAQREDFEA
AGSPFSGGPV SFPLAPGPHF GTPGYGSPHF TALYSSVPFP EGEAFPPVSV TTLGSPMHSN
