ID PO5F1_MOUSE Reviewed; 352 AA. AC P20263; Q63843; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 24-JAN-2024, entry version 212. DE RecName: Full=POU domain, class 5, transcription factor 1; DE AltName: Full=NF-A3; 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=Oct-3, Oct-4, Otf-3, Otf3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RC TISSUE=Embryonic carcinoma; RX PubMed=1972777; DOI=10.1038/345686a0; RA Rosner M.H., Vigano M.A., Ozato K., Timmons P.M., Poirier F., Rigby P.W.J., RA Staudt L.; RT "A POU-domain transcription factor in early stem cells and germ cells of RT the mammalian embryo."; RL Nature 345:686-692(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION. RC TISSUE=Embryonic carcinoma; RX PubMed=1690859; DOI=10.1038/344435a0; RA Schoeler H.R., Ruppert S., Suzuki N., Chowdhury K., Gruss P.; RT "New type of POU domain in germ line-specific protein Oct-4."; RL Nature 344:435-439(1990). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION. RX PubMed=1967980; DOI=10.1016/0092-8674(90)90597-8; RA Okamoto K., Okazawa H., Okuda A., Sakai M., Muramatsu M., Hamada H.; RT "A novel octamer binding transcription factor is differentially expressed RT in mouse embryonic cells."; RL Cell 60:461-472(1990). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION, AND INDUCTION. RX PubMed=1915274; DOI=10.1002/j.1460-2075.1991.tb07850.x; RA Okazawa H., Okamoto K., Ishino F., Ishino-Kaneko T., Takeda S., Toyoda Y., RA Muramatsu M., Hamada H.; RT "The oct3 gene, a gene for an embryonic transcription factor, is controlled RT by a retinoic acid repressible enhancer."; RL EMBO J. 10:2997-3005(1991). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo; 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 [6] RP FUNCTION, AND INTERACTION WITH SOX2 AND SOX15. RX PubMed=15863505; DOI=10.1074/jbc.m501423200; RA Maruyama M., Ichisaka T., Nakagawa M., Yamanaka S.; RT "Differential roles for Sox15 and Sox2 in transcriptional control in mouse RT embryonic stem cells."; RL J. Biol. Chem. 280:24371-24379(2005). RN [7] RP FUNCTION, SUMOYLATION AT LYS-118, AND MUTAGENESIS OF LYS-118. RX PubMed=17097055; DOI=10.1016/j.bbrc.2006.10.130; RA Tsuruzoe S., Ishihara K., Uchimura Y., Watanabe S., Sekita Y., Aoto T., RA Saitoh H., Yuasa Y., Niwa H., Kawasuji M., Baba H., Nakao M.; RT "Inhibition of DNA binding of Sox2 by the SUMO conjugation."; RL Biochem. Biophys. Res. Commun. 351:920-926(2006). RN [8] RP BIOTECHNOLOGY. RX PubMed=16904174; DOI=10.1016/j.cell.2006.07.024; RA Takahashi K., Yamanaka S.; RT "Induction of pluripotent stem cells from mouse embryonic and adult RT fibroblast cultures by defined factors."; RL Cell 126:663-676(2006). RN [9] RP SUMOYLATION AT LYS-118, MUTAGENESIS OF LYS-118; GLU-120; LYS-215 AND RP LYS-244, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH UBE2I. RX PubMed=17496161; DOI=10.1096/fj.06-6914com; RA Zhang Z., Liao B., Xu M., Jin Y.; RT "Post-translational modification of POU domain transcription factor Oct-4 RT by SUMO-1."; RL FASEB J. 21:3042-3051(2007). RN [10] RP SUMOYLATION AT LYS-118, MUTAGENESIS OF LYS-118, FUNCTION, AND SUBCELLULAR RP LOCATION. RX PubMed=17525163; DOI=10.1074/jbc.m611041200; RA Wei F., Schoeler H.R., Atchison M.L.; RT "Sumoylation of Oct4 enhances its stability, DNA binding, and RT transactivation."; RL J. Biol. Chem. 282:21551-21560(2007). RN [11] RP FUNCTION, AND INTERACTION WITH ESRRB. RX PubMed=18662995; DOI=10.1128/mcb.00301-08; RA van den Berg D.L., Zhang W., Yates A., Engelen E., Takacs K., RA Bezstarosti K., Demmers J., Chambers I., Poot R.A.; RT "Estrogen-related receptor beta interacts with Oct4 to positively regulate RT Nanog gene expression."; RL Mol. Cell. Biol. 28:5986-5995(2008). RN [12] RP FUNCTION, AND INTERACTION WITH ZSCAN10. RX PubMed=19740739; DOI=10.1074/jbc.m109.016162; RA Yu H.B., Kunarso G., Hong F.H., Stanton L.W.; RT "Zfp206, Oct4, and Sox2 are integrated components of a transcriptional RT regulatory network in embryonic stem cells."; RL J. Biol. Chem. 284:31327-31335(2009). RN [13] RP UBIQUITINATION. RX PubMed=19997087; DOI=10.1038/cr.2009.136; RA Liao B., Jin Y.; RT "Wwp2 mediates Oct4 ubiquitination and its own auto-ubiquitination in a RT dosage-dependent manner."; RL Cell Res. 20:332-344(2010). RN [14] RP INTERACTION WITH ZNF322. RX PubMed=24550733; DOI=10.1371/journal.pgen.1004038; RA Ma H., Ng H.M., Teh X., Li H., Lee Y.H., Chong Y.M., Loh Y.H., RA Collins J.J., Feng B., Yang H., Wu Q.; RT "Zfp322a Regulates mouse ES cell pluripotency and enhances reprogramming RT efficiency."; RL PLoS Genet. 10:E1004038-E1004038(2014). RN [15] RP FUNCTION, INTERACTION WITH MAPK8; MAPK9; FBXW4 AND FBXW8, SUBCELLULAR RP LOCATION, PHOSPHORYLATION AT SER-347, AND MUTAGENESIS OF SER-347 AND RP 122-VAL--ASN-352. RX PubMed=29153991; DOI=10.1016/j.stemcr.2017.10.017; RA Bae K.B., Yu D.H., Lee K.Y., Yao K., Ryu J., Lim D.Y., Zykova T.A., RA Kim M.O., Bode A.M., Dong Z.; RT "Serine 347 Phosphorylation by JNKs Negatively Regulates OCT4 Protein RT Stability in Mouse Embryonic Stem Cells."; RL Stem Cell Reports 9:2050-2064(2017). RN [16] RP FUNCTION, AND INTERACTION WITH DDX56. RX PubMed=32703285; DOI=10.1186/s13287-020-01800-w; RA Wang J., Liu J., Ye M., Liu F., Wu S., Huang J., Shi G.; RT "Ddx56 maintains proliferation of mouse embryonic stem cells via ribosome RT assembly and interaction with the Oct4/Sox2 complex."; RL Stem Cell Res Ther 11:314-314(2020). RN [17] RP STRUCTURE BY NMR OF POU DOMAIN. RX PubMed=8097478; DOI=10.1016/0014-5793(93)80088-c; RA Morita E.H., Shirakawa M., Hayashi F., Imagawa M., Kyogoku Y.; RT "Secondary structure of the oct-3 POU homeodomain as determined by 1H-15N RT NMR spectroscopy."; RL FEBS Lett. 321:107-110(1993). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 131-282 IN COMPLEX WITH DNA, RP FUNCTION, UBIQUITINATION, AND MUTAGENESIS OF VAL-166; ASN-206; RP 206-ASN--LEU-210; 206-ASN--ALA-222; ASN-207; 207-ASN--ALA-222; GLU-208; RP ASN-209; LEU-210; GLN-211; GLU-212 AND 214-CYS--ALA-222. RX PubMed=23376973; DOI=10.1038/ncb2680; RA Esch D., Vahokoski J., Groves M.R., Pogenberg V., Cojocaru V., RA Vom Bruch H., Han D., Drexler H.C., Arauzo-Bravo M.J., Ng C.K., Jauch R., RA Wilmanns M., Scholer H.R.; RT "A unique Oct4 interface is crucial for reprogramming to pluripotency."; RL Nat. Cell Biol. 15:295-301(2013). CC -!- FUNCTION: Transcription factor that binds to the octamer motif (5'- CC ATTTGCAT-3') (PubMed:1972777, PubMed:1690859, PubMed:1967980, CC PubMed:17525163, PubMed:23376973). Forms a trimeric complex with SOX2 CC or SOX15 on DNA and controls the expression of a number of genes CC involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206 CC (PubMed:15863505, PubMed:17097055, PubMed:17496161, PubMed:19740739). CC Critical for early embryogenesis and for embryonic stem cell CC pluripotency (PubMed:1972777, PubMed:1690859, PubMed:17496161, CC PubMed:18662995, PubMed:19740739, PubMed:29153991, PubMed:23376973, CC PubMed:32703285). {ECO:0000269|PubMed:15863505, CC ECO:0000269|PubMed:1690859, ECO:0000269|PubMed:17097055, CC ECO:0000269|PubMed:17496161, ECO:0000269|PubMed:17525163, CC ECO:0000269|PubMed:18662995, ECO:0000269|PubMed:1967980, CC ECO:0000269|PubMed:1972777, ECO:0000269|PubMed:19740739, CC ECO:0000269|PubMed:23376973, ECO:0000269|PubMed:29153991, CC ECO:0000269|PubMed:32703285}. CC -!- SUBUNIT: Interacts with PKM. Interacts with WWP2 (By similarity). CC Interacts with UBE2I and ZSCAN10 (PubMed:17496161, PubMed:19740739). CC Interacts with PCGF1 (By similarity). Interacts with ESRRB; recruits CC ESRRB near the POU5F1-SOX2 element in the NANOG proximal promoter; the CC interaction is DNA independent (PubMed:18662995). Interacts with ZNF322 CC (PubMed:24550733). Interacts with MAPK8 and MAPK9; the interaction CC allows MAPK8 and MAPK9 to phosphorylate POU5F1 on Ser-347 CC (PubMed:29153991). Interacts (when phosphorylated on Ser-347) with CC FBXW8 (PubMed:29153991). Interacts with FBXW4 (PubMed:29153991). CC Interacts with SOX2 and SOX15; binds synergistically with either SOX2 CC or SOX15 to DNA (PubMed:15863505). Interacts with DDX56 CC (PubMed:32703285). {ECO:0000250|UniProtKB:Q01860, CC ECO:0000269|PubMed:15863505, ECO:0000269|PubMed:17496161, CC ECO:0000269|PubMed:18662995, ECO:0000269|PubMed:19740739, CC ECO:0000269|PubMed:24550733, ECO:0000269|PubMed:29153991, CC ECO:0000269|PubMed:32703285}. CC -!- INTERACTION: CC P20263; P11440: Cdk1; NbExp=4; IntAct=EBI-1606219, EBI-846949; CC P20263; Q61545: Ewsr1; NbExp=13; IntAct=EBI-1606219, EBI-1606991; CC P20263; Q9R190: Mta2; NbExp=6; IntAct=EBI-1606219, EBI-904134; CC P20263; Q80Z64: Nanog; NbExp=4; IntAct=EBI-1606219, EBI-2312517; CC P20263; Q61066: Nr0b1; NbExp=5; IntAct=EBI-1606219, EBI-2312665; CC P20263; P11103: Parp1; NbExp=2; IntAct=EBI-1606219, EBI-642213; CC P20263; P52480: Pkm; NbExp=6; IntAct=EBI-1606219, EBI-647785; CC P20263; Q8BUN5: Smad3; NbExp=13; IntAct=EBI-1606219, EBI-2337983; CC P20263; P48432: Sox2; NbExp=4; IntAct=EBI-1606219, EBI-2313612; CC P20263; Q62318-1: Trim28; NbExp=3; IntAct=EBI-1606219, EBI-6876996; CC P20263; P61965: Wdr5; NbExp=7; IntAct=EBI-1606219, EBI-1247084; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q01860}. Nucleus CC {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE- CC ProRule:PRU00530, ECO:0000269|PubMed:17496161, CC ECO:0000269|PubMed:17525163, ECO:0000269|PubMed:29153991}. CC Note=Expressed in a diffuse and slightly punctuate pattern (By CC similarity). Colocalizes with MAPK8 and MAPK9 in the nucleus CC (PubMed:29153991). {ECO:0000250|UniProtKB:Q01860, CC ECO:0000269|PubMed:29153991}. CC -!- TISSUE SPECIFICITY: Expressed the totipotent and pluripotent stem cells CC of the pregastrulation embryo. Also expressed in primordial germ cells CC and in the female germ line. Absent from adult tissues. CC {ECO:0000269|PubMed:1690859, ECO:0000269|PubMed:1972777}. CC -!- DEVELOPMENTAL STAGE: Down-regulated during differentiation to endoderm CC and mesoderm. {ECO:0000269|PubMed:1972777}. CC -!- INDUCTION: Repressed by retinoic acid (RA). CC {ECO:0000269|PubMed:1690859, ECO:0000269|PubMed:1915274, CC ECO:0000269|PubMed:1967980}. CC -!- DOMAIN: The POU-specific domain mediates interaction with PKM. CC {ECO:0000250|UniProtKB:Q01860}. CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large CC number of yeast and animal transcription factors. CC {ECO:0000250|UniProtKB:Q01860}. CC -!- PTM: Sumoylation enhances the protein stability, DNA binding and CC transactivation activity. Sumoylation is required for enhanced YES1 CC expression. {ECO:0000269|PubMed:17097055, ECO:0000269|PubMed:17496161, CC ECO:0000269|PubMed:17525163}. CC -!- PTM: Ubiquitinated; undergoes 'Lys-63'-linked polyubiquitination by CC WWP2 leading to proteasomal degradation. {ECO:0000269|PubMed:19997087, CC ECO:0000269|PubMed:23376973}. CC -!- PTM: ERK1/2-mediated phosphorylation at Ser-106 promotes nuclear CC exclusion and proteasomal degradation. Phosphorylation at Thr-228 and CC Ser-229 decrease DNA-binding and alters ability to activate CC transcription (By similarity). JNK1/2-mediated phosphorylation at Ser- CC 347 promotes proteasomal degradation (PubMed:29153991). CC {ECO:0000250|UniProtKB:Q01860, ECO:0000269|PubMed:29153991}. 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:16904174}. CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-5 CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M34381; AAA39844.1; ALT_SEQ; mRNA. DR EMBL; X52437; CAA36682.1; -; mRNA. DR EMBL; S58426; AAB19896.1; -; Genomic_DNA. DR EMBL; S58422; AAB19896.1; JOINED; Genomic_DNA. DR EMBL; S58423; AAB19896.1; JOINED; Genomic_DNA. DR EMBL; S58424; AAB19896.1; JOINED; Genomic_DNA. DR EMBL; S58425; AAB19896.1; JOINED; Genomic_DNA. DR EMBL; BC068268; AAH68268.1; -; mRNA. DR CCDS; CCDS37600.1; -. DR PIR; A34672; A34672. DR PIR; S17313; S17313. DR RefSeq; NP_038661.2; NM_013633.3. DR PDB; 1OCP; NMR; -; A=217-282. DR PDB; 3L1P; X-ray; 2.80 A; A/B=131-282. DR PDB; 6HT5; X-ray; 3.45 A; E=131-282. DR PDBsum; 1OCP; -. DR PDBsum; 3L1P; -. DR PDBsum; 6HT5; -. DR AlphaFoldDB; P20263; -. DR SMR; P20263; -. DR BioGRID; 202313; 306. DR DIP; DIP-29931N; -. DR IntAct; P20263; 141. DR MINT; P20263; -. DR STRING; 10090.ENSMUSP00000025271; -. DR GlyGen; P20263; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P20263; -. DR PhosphoSitePlus; P20263; -. DR PaxDb; 10090-ENSMUSP00000025271; -. DR PeptideAtlas; P20263; -. DR ProteomicsDB; 289861; -. DR DNASU; 18999; -. DR Ensembl; ENSMUST00000025271.17; ENSMUSP00000025271.10; ENSMUSG00000024406.17. DR GeneID; 18999; -. DR KEGG; mmu:18999; -. DR UCSC; uc008chu.2; mouse. DR AGR; MGI:101893; -. DR CTD; 5460; -. DR MGI; MGI:101893; Pou5f1. DR VEuPathDB; HostDB:ENSMUSG00000024406; -. DR eggNOG; KOG3802; Eukaryota. DR GeneTree; ENSGT00940000155046; -. DR HOGENOM; CLU_066243_0_0_1; -. DR InParanoid; P20263; -. DR OMA; CPQPYEF; -. DR OrthoDB; 4250502at2759; -. DR PhylomeDB; P20263; -. DR TreeFam; TF316413; -. DR BioGRID-ORCS; 18999; 9 hits in 79 CRISPR screens. DR ChiTaRS; Pou5f1; mouse. DR EvolutionaryTrace; P20263; -. DR PRO; PR:P20263; -. DR Proteomes; UP000000589; Chromosome 17. DR RNAct; P20263; Protein. DR Bgee; ENSMUSG00000024406; Expressed in epiblast (generic) and 64 other cell types or tissues. DR ExpressionAtlas; P20263; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:AgBase. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0001674; C:female germ cell nucleus; IDA:MGI. DR GO; GO:0043073; C:germ cell nucleus; IDA:MGI. DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI. DR GO; GO:0005739; C:mitochondrion; ISO:MGI. DR GO; GO:0005730; C:nucleolus; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; IDA:BHF-UCL. DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL. DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI. DR GO; GO:0017053; C:transcription repressor complex; IDA:MGI. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0031490; F:chromatin DNA binding; IDA:MGI. DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:AgBase. DR GO; GO:0019955; F:cytokine binding; IDA:AgBase. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:BHF-UCL. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI. DR GO; GO:0071837; F:HMG box domain binding; ISO:MGI. DR GO; GO:0070577; F:lysine-acetylated histone binding; IDA:MGI. DR GO; GO:0035198; F:miRNA binding; ISO:MGI. DR GO; GO:0070974; F:POU domain binding; ISO:MGI. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:0001162; F:RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding; IDA:MGI. 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:UniProtKB. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL. DR GO; GO:0001824; P:blastocyst development; IEP:BHF-UCL. DR GO; GO:0001832; P:blastocyst growth; IGI:MGI. DR GO; GO:0045165; P:cell fate commitment; IMP:MGI. DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI. DR GO; GO:0001712; P:ectodermal cell fate commitment; IDA:MGI. DR GO; GO:0001711; P:endodermal cell fate commitment; IDA:MGI. DR GO; GO:0001714; P:endodermal cell fate specification; ISO:MGI. DR GO; GO:0010467; P:gene expression; IMP:MGI. DR GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:MGI. DR GO; GO:0001710; P:mesodermal cell fate commitment; IDA:MGI. DR GO; GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; IDA:MGI. DR GO; GO:0045596; P:negative regulation of cell differentiation; IGI:MGI. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:0010629; P:negative regulation of gene expression; IDA:AgBase. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; IDA:CACAO. DR GO; GO:0009786; P:regulation of asymmetric cell division; IEP:BHF-UCL. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:BHF-UCL. DR GO; GO:0080021; P:response to benzoic acid; IEA:Ensembl. DR GO; GO:0010033; P:response to organic substance; IDA:MGI. DR GO; GO:0032526; P:response to retinoic acid; IDA:MGI. DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI. DR GO; GO:0048863; P:stem cell differentiation; IDA:MGI. DR GO; GO:0019827; P:stem cell population maintenance; IMP:UniProtKB. DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0001829; P:trophectodermal cell differentiation; IGI:MGI. DR GO; GO:0001830; P:trophectodermal cell fate commitment; IDA:MGI. DR CDD; cd00086; homeodomain; 1. DR Gene3D; 1.10.10.60; Homeodomain-like; 1. DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 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 PANTHER; PTHR11636; POU DOMAIN; 1. DR PANTHER; PTHR11636:SF86; POU DOMAIN, CLASS 5, TRANSCRIPTION FACTOR 1-RELATED; 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; Homeodomain-like; 1. DR SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 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. DR Genevisible; P20263; MM. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Developmental protein; DNA-binding; Homeobox; KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; KW Transcription; Transcription regulation; Ubl conjugation. FT CHAIN 1..352 FT /note="POU domain, class 5, transcription factor 1" FT /id="PRO_0000100749" FT DOMAIN 131..205 FT /note="POU-specific" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00530" FT DNA_BIND 223..282 FT /note="Homeobox" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108, FT ECO:0000269|PubMed:23376973" FT REGION 1..48 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 91..115 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 173..179 FT /note="DNA-binding" FT /evidence="ECO:0000269|PubMed:23376973, FT ECO:0007744|PDB:3L1P" FT REGION 186..189 FT /note="DNA-binding" FT /evidence="ECO:0000269|PubMed:23376973, FT ECO:0007744|PDB:3L1P" FT MOTIF 4..12 FT /note="9aaTAD" FT /evidence="ECO:0000250|UniProtKB:Q01860" FT COMPBIAS 94..109 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 150 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000269|PubMed:23376973, FT ECO:0007744|PDB:3L1P" FT BINDING 157 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000269|PubMed:23376973, FT ECO:0007744|PDB:3L1P" FT MOD_RES 106 FT /note="Phosphoserine; by MAPK" FT /evidence="ECO:0000250|UniProtKB:Q01860" FT MOD_RES 228 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q01860" FT MOD_RES 229 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q01860" FT MOD_RES 282 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q01860" FT MOD_RES 347 FT /note="Phosphoserine; by MAPK8 and MAPK9" FT /evidence="ECO:0000269|PubMed:29153991" FT CROSSLNK 118 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000269|PubMed:17097055, FT ECO:0000269|PubMed:17496161, ECO:0000269|PubMed:17525163" FT MUTAGEN 118 FT /note="K->R: Absence of sumoylation. Enhanced protein FT degradation. Reduced self-renewal ability in ES cells. 70% FT lower expression of YES1. Reduced DNA binding. No change in FT nuclear location. No change in nuclear localization. FT Absence of sumoylation; when associated with R-215 and FT R-244." FT /evidence="ECO:0000269|PubMed:17097055, FT ECO:0000269|PubMed:17496161, ECO:0000269|PubMed:17525163" FT MUTAGEN 120 FT /note="E->A: Absence of sumoylation. Enhanced protein FT degradation. Reduced self-renewal ability in ES cells. 55% FT lower expression of YES1." FT /evidence="ECO:0000269|PubMed:17496161" FT MUTAGEN 122..352 FT /note="Missing: Loss of MAPK9 binding. Absence of Ser-347 FT phosphorylation." FT /evidence="ECO:0000269|PubMed:29153991" FT MUTAGEN 166 FT /note="V->K: No change in DNA binding. No loss of FT self-renewal ability in iPS cells. No change in nuclear FT location." FT /evidence="ECO:0000269|PubMed:23376973" FT MUTAGEN 206..222 FT /note="NNENLQEICKSETLVQA->SSSGSPTNLDKIAAQGR: Reduced DNA FT binding. Loss of self-renewal ability in iPS cells. No FT change in nuclear location." FT /evidence="ECO:0000269|PubMed:23376973" FT MUTAGEN 206..210 FT /note="NNENL->AAAAA: Loss of self-renewal ability in iPS FT cells." FT /evidence="ECO:0000269|PubMed:23376973" FT MUTAGEN 206 FT /note="N->A: No change in DNA binding. Reduced self-renewal FT ability in iPS cells. No change in nuclear location." FT /evidence="ECO:0000269|PubMed:23376973" FT MUTAGEN 207 FT /note="N->A: No change in DNA binding. No change in nuclear FT location." FT /evidence="ECO:0000269|PubMed:23376973" FT MUTAGEN 208 FT /note="E->A: No change in DNA binding. No loss of FT self-renewal ability in iPS cells. No change in nuclear FT location." FT /evidence="ECO:0000269|PubMed:23376973" FT MUTAGEN 209 FT /note="N->A: No change in DNA binding. Reduced self-renewal FT ability in iPS cells. No change in nuclear location." FT /evidence="ECO:0000269|PubMed:23376973" FT MUTAGEN 210 FT /note="L->A: No change in DNA binding. Loss of self-renewal FT ability in iPS cells. No change in nuclear location. No FT loss of ability to bind SOX2. Reduced levels of CHD4 and FT SMARCA4 in a POU5F1 pulldown assay." FT /evidence="ECO:0000269|PubMed:23376973" FT MUTAGEN 211 FT /note="Q->A: No change in DNA binding. No loss of FT self-renewal ability in iPS cells. No change in nuclear FT location." FT /evidence="ECO:0000269|PubMed:23376973" FT MUTAGEN 211 FT /note="Q->R: No change in DNA binding. Loss of self-renewal FT ability in iPS cells. No change in nuclear location." FT /evidence="ECO:0000269|PubMed:23376973" FT MUTAGEN 212 FT /note="E->A: No change in DNA binding. No loss of FT self-renewal ability in iPS cells. No change in nuclear FT location." FT /evidence="ECO:0000269|PubMed:23376973" FT MUTAGEN 215 FT /note="K->R: No change in sumoylation; when associated with FT R-244. Loss of sumoylation. No change in nuclear FT localization; when associated with R-118 and R-244." FT /evidence="ECO:0000269|PubMed:17496161" FT MUTAGEN 244 FT /note="K->R: No change in sumoylation. No change in FT sumoylation; when associated with R-215. Loss of FT sumoylation; when associated with R-118 and R-215. No FT change in nuclear localization; when associated with R-118 FT and R-215." FT /evidence="ECO:0000269|PubMed:17496161" FT MUTAGEN 347 FT /note="S->A: Absence of phosphorylation. Reduced protein FT degradation. Reduced self-renewal ability in ES cells. No FT change in FBXW4 binding. Loss of FBXW8 binding." FT /evidence="ECO:0000269|PubMed:29153991" FT CONFLICT 1..28 FT /note="Missing (in Ref. 2; CAA36682)" FT /evidence="ECO:0000305" FT CONFLICT 29 FT /note="V -> M (in Ref. 2; CAA36682)" FT /evidence="ECO:0000305" FT CONFLICT 31 FT /note="P -> S (in Ref. 4; AAA39844/AAB19896)" FT /evidence="ECO:0000305" FT HELIX 132..152 FT /evidence="ECO:0007829|PDB:3L1P" FT HELIX 157..168 FT /evidence="ECO:0007829|PDB:3L1P" FT HELIX 174..181 FT /evidence="ECO:0007829|PDB:3L1P" FT HELIX 187..204 FT /evidence="ECO:0007829|PDB:3L1P" FT HELIX 208..212 FT /evidence="ECO:0007829|PDB:3L1P" FT STRAND 223..225 FT /evidence="ECO:0007829|PDB:1OCP" FT HELIX 232..239 FT /evidence="ECO:0007829|PDB:3L1P" FT TURN 240..244 FT /evidence="ECO:0007829|PDB:3L1P" FT HELIX 250..259 FT /evidence="ECO:0007829|PDB:3L1P" FT HELIX 264..279 FT /evidence="ECO:0007829|PDB:3L1P" SQ SEQUENCE 352 AA; 38216 MW; 757E41DF52286714 CRC64; MAGHLASDFA FSPPPGGGDG SAGLEPGWVD PRTWLSFQGP PGGPGIGPGS EVLGISPCPP AYEFCGGMAY CGPQVGLGLV PQVGVETLQP EGQAGARVES NSEGTSSEPC ADRPNAVKLE KVEPTPEESQ DMKALQKELE QFAKLLKQKR ITLGYTQADV GLTLGVLFGK VFSQTTICRF EALQLSLKNM CKLRPLLEKW VEEADNNENL QEICKSETLV QARKRKRTSI ENRVRWSLET MFLKCPKPSL QQITHIANQL GLEKDVVRVW FCNRRQKGKR SSIEYSQREE YEATGTPFPG GAVSFPLPPG PHFGTPGYGS PHFTTLYSVP FPEGEAFPSV PVTALGSPMH SN //