PO5F1_MOUSE
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 03-AUG-2022, entry version 204.
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 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 [17]
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 {ECO:0000269|PubMed:15863505, ECO:0000269|PubMed:1690859,
CC ECO:0000269|PubMed:17097055, ECO:0000269|PubMed:17496161,
CC ECO:0000269|PubMed:17525163, ECO:0000269|PubMed:18662995,
CC ECO:0000269|PubMed:1967980, ECO:0000269|PubMed:1972777,
CC ECO:0000269|PubMed:19740739, ECO:0000269|PubMed:23376973,
CC ECO:0000269|PubMed:29153991}.
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). {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 -!- 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}.
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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 iPTMnet; P20263; -.
DR PhosphoSitePlus; P20263; -.
DR PaxDb; P20263; -.
DR PeptideAtlas; P20263; -.
DR PRIDE; P20263; -.
DR ProteomicsDB; 289861; -.
DR DNASU; 18999; -.
DR Ensembl; ENSMUST00000025271; ENSMUSP00000025271; ENSMUSG00000024406.
DR GeneID; 18999; -.
DR KEGG; mmu:18999; -.
DR UCSC; uc008chu.2; mouse.
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; 841019at2759; -.
DR PhylomeDB; P20263; -.
DR TreeFam; TF316413; -.
DR BioGRID-ORCS; 18999; 9 hits in 74 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 61 other tissues.
DR ExpressionAtlas; P20263; baseline and differential.
DR Genevisible; P20263; MM.
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:0031491; F:nucleosome binding; IDA: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:0097043; P:histone H3-K56 acetylation; IDA: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: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:0045892; P:negative regulation of transcription, DNA-templated; 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 from RNA polymerase II promoter; IDA:CACAO.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0009786; P:regulation of asymmetric cell division; IEP:BHF-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
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; 1.10.260.40; -; 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; 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 R-
FT 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 self-
FT 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 self-
FT 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 self-
FT 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 self-
FT 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
