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POU domain, class 5, transcription factor 1 (NF-A3) (Octamer-binding protein 3) (Oct-3) (Octamer-binding protein 4) (Oct-4) (Octamer-binding transcription factor 3) (OTF-3)

 PO5F1_MOUSE             Reviewed;         352 AA.
P20263; Q63843;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 1.
12-SEP-2018, entry version 182.
RecName: Full=POU domain, class 5, transcription factor 1;
AltName: Full=NF-A3;
AltName: Full=Octamer-binding protein 3;
Short=Oct-3;
AltName: Full=Octamer-binding protein 4;
Short=Oct-4;
AltName: Full=Octamer-binding transcription factor 3;
Short=OTF-3;
Name=Pou5f1; Synonyms=Oct-3, Oct-4, Otf-3, Otf3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
TISSUE=Embryonic carcinoma;
PubMed=1972777; DOI=10.1038/345686a0;
Rosner M.H., Vigano M.A., Ozato K., Timmons P.M., Poirier F.,
Rigby P.W.J., Staudt L.;
"A POU-domain transcription factor in early stem cells and germ cells
of the mammalian embryo.";
Nature 345:686-692(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
INDUCTION.
TISSUE=Embryonic carcinoma;
PubMed=1690859; DOI=10.1038/344435a0;
Schoeler H.R., Ruppert S., Suzuki N., Chowdhury K., Gruss P.;
"New type of POU domain in germ line-specific protein Oct-4.";
Nature 344:435-439(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION.
PubMed=1967980; DOI=10.1016/0092-8674(90)90597-8;
Okamoto K., Okazawa H., Okuda A., Sakai M., Muramatsu M., Hamada H.;
"A novel octamer binding transcription factor is differentially
expressed in mouse embryonic cells.";
Cell 60:461-472(1990).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION, AND INDUCTION.
PubMed=1915274;
Okazawa H., Okamoto K., Ishino F., Ishino-Kaneko T., Takeda S.,
Toyoda Y., Muramatsu M., Hamada H.;
"The oct3 gene, a gene for an embryonic transcription factor, is
controlled by a retinoic acid repressible enhancer.";
EMBO J. 10:2997-3005(1991).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, SUMOYLATION AT LYS-118, AND MUTAGENESIS OF LYS-118.
PubMed=17097055; DOI=10.1016/j.bbrc.2006.10.130;
Tsuruzoe S., Ishihara K., Uchimura Y., Watanabe S., Sekita Y.,
Aoto T., Saitoh H., Yuasa Y., Niwa H., Kawasuji M., Baba H., Nakao M.;
"Inhibition of DNA binding of Sox2 by the SUMO conjugation.";
Biochem. Biophys. Res. Commun. 351:920-926(2006).
[7]
BIOTECHNOLOGY.
PubMed=16904174; DOI=10.1016/j.cell.2006.07.024;
Takahashi K., Yamanaka S.;
"Induction of pluripotent stem cells from mouse embryonic and adult
fibroblast cultures by defined factors.";
Cell 126:663-676(2006).
[8]
SUMOYLATION AT LYS-118, MUTAGENESIS OF LYS-118; GLU-120; LYS-215 AND
LYS-244, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH UBE2I.
PubMed=17496161; DOI=10.1096/fj.06-6914com;
Zhang Z., Liao B., Xu M., Jin Y.;
"Post-translational modification of POU domain transcription factor
Oct-4 by SUMO-1.";
FASEB J. 21:3042-3051(2007).
[9]
SUMOYLATION AT LYS-118, MUTAGENESIS OF LYS-118, FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=17525163; DOI=10.1074/jbc.M611041200;
Wei F., Schoeler H.R., Atchison M.L.;
"Sumoylation of Oct4 enhances its stability, DNA binding, and
transactivation.";
J. Biol. Chem. 282:21551-21560(2007).
[10]
FUNCTION, AND INTERACTION WITH ESRRB.
PubMed=18662995; DOI=10.1128/MCB.00301-08;
van den Berg D.L., Zhang W., Yates A., Engelen E., Takacs K.,
Bezstarosti K., Demmers J., Chambers I., Poot R.A.;
"Estrogen-related receptor beta interacts with Oct4 to positively
regulate Nanog gene expression.";
Mol. Cell. Biol. 28:5986-5995(2008).
[11]
FUNCTION, AND INTERACTION WITH ZSCAN10.
PubMed=19740739; DOI=10.1074/jbc.M109.016162;
Yu H.B., Kunarso G., Hong F.H., Stanton L.W.;
"Zfp206, Oct4, and Sox2 are integrated components of a transcriptional
regulatory network in embryonic stem cells.";
J. Biol. Chem. 284:31327-31335(2009).
[12]
UBIQUITINATION.
PubMed=19997087; DOI=10.1038/cr.2009.136;
Liao B., Jin Y.;
"Wwp2 mediates Oct4 ubiquitination and its own auto-ubiquitination in
a dosage-dependent manner.";
Cell Res. 20:332-344(2010).
[13]
INTERACTION WITH ZNF322.
PubMed=24550733; DOI=10.1371/journal.pgen.1004038;
Ma H., Ng H.M., Teh X., Li H., Lee Y.H., Chong Y.M., Loh Y.H.,
Collins J.J., Feng B., Yang H., Wu Q.;
"Zfp322a Regulates mouse ES cell pluripotency and enhances
reprogramming efficiency.";
PLoS Genet. 10:E1004038-E1004038(2014).
[14]
FUNCTION, INTERACTION WITH MAPK8; MAPK9; FBXW4 AND FBXW8, SUBCELLULAR
LOCATION, PHOSPHORYLATION AT SER-347, AND MUTAGENESIS OF SER-347 AND
122-VAL--ASN-352.
PubMed=29153991; DOI=10.1016/j.stemcr.2017.10.017;
Bae K.B., Yu D.H., Lee K.Y., Yao K., Ryu J., Lim D.Y., Zykova T.A.,
Kim M.O., Bode A.M., Dong Z.;
"Serine 347 Phosphorylation by JNKs Negatively Regulates OCT4 Protein
Stability in Mouse Embryonic Stem Cells.";
Stem Cell Reports 9:2050-2064(2017).
[15]
STRUCTURE BY NMR OF POU DOMAIN.
PubMed=8097478; DOI=10.1016/0014-5793(93)80088-C;
Morita E.H., Shirakawa M., Hayashi F., Imagawa M., Kyogoku Y.;
"Secondary structure of the oct-3 POU homeodomain as determined by 1H-
15N NMR spectroscopy.";
FEBS Lett. 321:107-110(1993).
[16]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 131-282 IN COMPLEX WITH DNA,
FUNCTION, UBIQUITINATION, AND MUTAGENESIS OF VAL-166; ASN-206;
206-ASN--LEU-210; 206-ASN--ALA-222; ASN-207; 207-ASN--ALA-222;
GLU-208; ASN-209; LEU-210; GLN-211; GLU-212 AND 214-CYS--ALA-222.
PubMed=23376973; DOI=10.1038/ncb2680;
Esch D., Vahokoski J., Groves M.R., Pogenberg V., Cojocaru V.,
Vom Bruch H., Han D., Drexler H.C., Arauzo-Bravo M.J., Ng C.K.,
Jauch R., Wilmanns M., Scholer H.R.;
"A unique Oct4 interface is crucial for reprogramming to
pluripotency.";
Nat. Cell Biol. 15:295-301(2013).
-!- FUNCTION: Transcription factor that binds to the octamer motif
(5'-ATTTGCAT-3') (PubMed:1972777, PubMed:1690859, PubMed:1967980,
PubMed:17525163, PubMed:23376973). 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 (PubMed:17097055, PubMed:17496161, PubMed:19740739).
Critical for early embryogenesis and for embryonic stem cell
pluripotency (PubMed:1972777, PubMed:1690859, PubMed:17496161,
PubMed:18662995, PubMed:19740739, PubMed:29153991,
PubMed:23376973). {ECO:0000269|PubMed:1690859,
ECO:0000269|PubMed:17097055, ECO:0000269|PubMed:17496161,
ECO:0000269|PubMed:17525163, ECO:0000269|PubMed:18662995,
ECO:0000269|PubMed:1967980, ECO:0000269|PubMed:1972777,
ECO:0000269|PubMed:19740739, ECO:0000269|PubMed:23376973,
ECO:0000269|PubMed:29153991}.
-!- SUBUNIT: Interacts with PKM. Interacts with WWP2 (By similarity).
Interacts with UBE2I and ZSCAN10 (PubMed:17496161,
PubMed:19740739). Interacts with PCGF1 (By similarity). Interacts
with ESRRB; recruits ESRRB near the POU5F1-SOX2 element in the
NANOG proximal promoter; the interaction is DNA independent
(PubMed:18662995). Interacts with ZNF322 (PubMed:24550733).
Interacts with MAPK8 and MAPK9; the interaction allows MAPK8 and
MAPK9 to phosphorylate POU5F1 on Ser-347 (PubMed:29153991).
Interacts (when phosphorylated on Ser-347) with FBXW8
(PubMed:29153991). Interacts with FBXW4 (PubMed:29153991).
{ECO:0000250|UniProtKB:Q01860, ECO:0000269|PubMed:17496161,
ECO:0000269|PubMed:18662995, ECO:0000269|PubMed:19740739,
ECO:0000269|PubMed:24550733, ECO:0000269|PubMed:29153991}.
-!- INTERACTION:
P11440:Cdk1; NbExp=4; IntAct=EBI-1606219, EBI-846949;
Q61545:Ewsr1; NbExp=13; IntAct=EBI-1606219, EBI-1606991;
Q9R190:Mta2; NbExp=6; IntAct=EBI-1606219, EBI-904134;
Q80Z64:Nanog; NbExp=4; IntAct=EBI-1606219, EBI-2312517;
Q61066:Nr0b1; NbExp=5; IntAct=EBI-1606219, EBI-2312665;
P11103:Parp1; NbExp=2; IntAct=EBI-1606219, EBI-642213;
P52480:Pkm; NbExp=6; IntAct=EBI-1606219, EBI-647785;
Q8BUN5:Smad3; NbExp=13; IntAct=EBI-1606219, EBI-2337983;
P48432:Sox2; NbExp=4; IntAct=EBI-1606219, EBI-2313612;
Q62318-1:Trim28; NbExp=3; IntAct=EBI-1606219, EBI-6876996;
P61965:Wdr5; NbExp=7; IntAct=EBI-1606219, EBI-1247084;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q01860}.
Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108,
ECO:0000255|PROSITE-ProRule:PRU00530, ECO:0000269|PubMed:17496161,
ECO:0000269|PubMed:17525163, ECO:0000269|PubMed:29153991}.
Note=Expressed in a diffuse and slightly punctuate pattern (By
similarity). Colocalizes with MAPK8 and MAPK9 in the nucleus
(PubMed:29153991). {ECO:0000250|UniProtKB:Q01860,
ECO:0000269|PubMed:29153991}.
-!- TISSUE SPECIFICITY: Expressed the totipotent and pluripotent stem
cells of the pregastrulation embryo. Also expressed in primordial
germ cells and in the female germ line. Absent from adult tissues.
{ECO:0000269|PubMed:1690859, ECO:0000269|PubMed:1972777}.
-!- DEVELOPMENTAL STAGE: Down-regulated during differentiation to
endoderm and mesoderm. {ECO:0000269|PubMed:1972777}.
-!- INDUCTION: Repressed by retinoic acid (RA).
{ECO:0000269|PubMed:1690859, ECO:0000269|PubMed:1915274,
ECO:0000269|PubMed:1967980}.
-!- DOMAIN: The POU-specific domain mediates interaction with PKM.
{ECO:0000250|UniProtKB:Q01860}.
-!- PTM: Sumoylation enhances the protein stability, DNA binding and
transactivation activity. Sumoylation is required for enhanced
YES1 expression. {ECO:0000269|PubMed:17097055,
ECO:0000269|PubMed:17496161, ECO:0000269|PubMed:17525163}.
-!- PTM: Ubiquitinated; undergoes 'Lys-63'-linked polyubiquitination
by WWP2 leading to proteasomal degradation.
{ECO:0000269|PubMed:19997087, ECO:0000269|PubMed:23376973}.
-!- PTM: 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). JNK1/2-mediated phosphorylation at
Ser-347 promotes proteasomal degradation (PubMed:29153991).
{ECO:0000250|UniProtKB:Q01860, ECO:0000269|PubMed:29153991}.
-!- BIOTECHNOLOGY: 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. {ECO:0000269|PubMed:16904174}.
-!- SIMILARITY: Belongs to the POU transcription factor family. Class-
5 subfamily. {ECO:0000305}.
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EMBL; M34381; AAA39844.1; ALT_SEQ; mRNA.
EMBL; X52437; CAA36682.1; -; mRNA.
EMBL; S58426; AAB19896.1; -; Genomic_DNA.
EMBL; S58422; AAB19896.1; JOINED; Genomic_DNA.
EMBL; S58423; AAB19896.1; JOINED; Genomic_DNA.
EMBL; S58424; AAB19896.1; JOINED; Genomic_DNA.
EMBL; S58425; AAB19896.1; JOINED; Genomic_DNA.
EMBL; BC068268; AAH68268.1; -; mRNA.
CCDS; CCDS37600.1; -.
PIR; A34672; A34672.
PIR; S17313; S17313.
RefSeq; NP_038661.2; NM_013633.3.
UniGene; Mm.17031; -.
PDB; 1OCP; NMR; -; A=217-282.
PDB; 3L1P; X-ray; 2.80 A; A/B=131-282.
PDBsum; 1OCP; -.
PDBsum; 3L1P; -.
ProteinModelPortal; P20263; -.
SMR; P20263; -.
BioGrid; 202313; 304.
DIP; DIP-29931N; -.
IntAct; P20263; 141.
MINT; P20263; -.
STRING; 10090.ENSMUSP00000025271; -.
iPTMnet; P20263; -.
PhosphoSitePlus; P20263; -.
PaxDb; P20263; -.
PeptideAtlas; P20263; -.
PRIDE; P20263; -.
Ensembl; ENSMUST00000025271; ENSMUSP00000025271; ENSMUSG00000024406.
GeneID; 18999; -.
KEGG; mmu:18999; -.
UCSC; uc008chu.2; mouse.
CTD; 5460; -.
MGI; MGI:101893; Pou5f1.
eggNOG; KOG3802; Eukaryota.
eggNOG; ENOG410XQ7X; LUCA.
GeneTree; ENSGT00760000118935; -.
HOGENOM; HOG000089941; -.
HOVERGEN; HBG057998; -.
InParanoid; P20263; -.
KO; K09367; -.
OMA; LENMFLQ; -.
OrthoDB; EOG091G0U0S; -.
PhylomeDB; P20263; -.
TreeFam; TF316413; -.
Reactome; R-MMU-452723; Transcriptional regulation of pluripotent stem cells.
EvolutionaryTrace; P20263; -.
PRO; PR:P20263; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000024406; Expressed in 75 organ(s), highest expression level in morula.
CleanEx; MM_POU5F1; -.
ExpressionAtlas; P20263; baseline and differential.
Genevisible; P20263; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0000790; C:nuclear chromatin; IDA:AgBase.
GO; GO:0044798; C:nuclear transcription factor complex; IDA:MGI.
GO; GO:0005730; C:nucleolus; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0005667; C:transcription factor complex; IDA:MGI.
GO; GO:0017053; C:transcriptional repressor complex; IDA:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
GO; GO:0019955; F:cytokine binding; IDA:AgBase.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
GO; GO:0001158; F:enhancer sequence-specific DNA binding; IDA:AgBase.
GO; GO:0071837; F:HMG box domain binding; ISO:MGI.
GO; GO:0035198; F:miRNA binding; ISO:MGI.
GO; GO:0070974; F:POU domain binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; IDA:MGI.
GO; GO:0001162; F:RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL.
GO; GO:0001824; P:blastocyst development; IEP:BHF-UCL.
GO; GO:0001832; P:blastocyst growth; IGI:MGI.
GO; GO:0003130; P:BMP signaling pathway involved in heart induction; ISO:MGI.
GO; GO:0060913; P:cardiac cell fate determination; ISO:MGI.
GO; GO:0045165; P:cell fate commitment; IMP:MGI.
GO; GO:0060795; P:cell fate commitment involved in formation of primary germ layer; ISO:MGI.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
GO; GO:0001712; P:ectodermal cell fate commitment; IDA:MGI.
GO; GO:0001711; P:endodermal cell fate commitment; IDA:MGI.
GO; GO:0001714; P:endodermal cell fate specification; ISO:MGI.
GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:MGI.
GO; GO:0001710; P:mesodermal cell fate commitment; IDA:MGI.
GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; IDA:MGI.
GO; GO:0045596; P:negative regulation of cell differentiation; IGI:MGI.
GO; GO:0010629; P:negative regulation of gene expression; IDA:AgBase.
GO; GO:0060965; P:negative regulation of gene silencing by miRNA; ISO:MGI.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IMP:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:MGI.
GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0009786; P:regulation of asymmetric cell division; IEP:BHF-UCL.
GO; GO:0010468; P:regulation of gene expression; ISO:MGI.
GO; GO:0090081; P:regulation of heart induction by regulation of canonical Wnt signaling pathway; ISO:MGI.
GO; GO:0090308; P:regulation of methylation-dependent chromatin silencing; ISO:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0010033; P:response to organic substance; IDA:MGI.
GO; GO:0032526; P:response to retinoic acid; IDA:MGI.
GO; GO:0035019; P:somatic stem cell population maintenance; ISO:MGI.
GO; GO:0048863; P:stem cell differentiation; IDA:MGI.
GO; GO:0019827; P:stem cell population maintenance; IMP:UniProtKB.
GO; GO:0006366; P:transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0001829; P:trophectodermal cell differentiation; IGI:MGI.
CDD; cd00086; homeodomain; 1.
InterPro; IPR009057; Homeobox-like_sf.
InterPro; IPR017970; Homeobox_CS.
InterPro; IPR001356; Homeobox_dom.
InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
InterPro; IPR013847; POU.
InterPro; IPR000327; POU_dom.
InterPro; IPR015585; POU_dom_5.
PANTHER; PTHR11636:SF86; PTHR11636:SF86; 1.
Pfam; PF00046; Homeobox; 1.
Pfam; PF00157; Pou; 1.
PRINTS; PR00028; POUDOMAIN.
SMART; SM00389; HOX; 1.
SMART; SM00352; POU; 1.
SUPFAM; SSF46689; SSF46689; 1.
SUPFAM; SSF47413; SSF47413; 1.
PROSITE; PS00027; HOMEOBOX_1; 1.
PROSITE; PS50071; HOMEOBOX_2; 1.
PROSITE; PS00035; POU_1; 1.
PROSITE; PS00465; POU_2; 1.
PROSITE; PS51179; POU_3; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Developmental protein;
DNA-binding; Homeobox; Isopeptide bond; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 352 POU domain, class 5, transcription factor
1.
/FTId=PRO_0000100749.
DOMAIN 131 205 POU-specific. {ECO:0000255|PROSITE-
ProRule:PRU00530}.
DNA_BIND 223 282 Homeobox. {ECO:0000255|PROSITE-
ProRule:PRU00108,
ECO:0000269|PubMed:23376973}.
REGION 173 179 DNA binding. {ECO:0000244|PDB:3L1P,
ECO:0000269|PubMed:23376973}.
REGION 186 189 DNA binding. {ECO:0000244|PDB:3L1P,
ECO:0000269|PubMed:23376973}.
BINDING 150 150 DNA. {ECO:0000244|PDB:3L1P,
ECO:0000269|PubMed:23376973}.
BINDING 157 157 DNA. {ECO:0000244|PDB:3L1P,
ECO:0000269|PubMed:23376973}.
MOD_RES 106 106 Phosphoserine; by MAPK.
{ECO:0000250|UniProtKB:Q01860}.
MOD_RES 228 228 Phosphothreonine.
{ECO:0000250|UniProtKB:Q01860}.
MOD_RES 229 229 Phosphoserine.
{ECO:0000250|UniProtKB:Q01860}.
MOD_RES 282 282 Phosphoserine.
{ECO:0000250|UniProtKB:Q01860}.
MOD_RES 347 347 Phosphoserine; by MAPK8 and MAPK9.
{ECO:0000269|PubMed:29153991}.
CROSSLNK 118 118 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:17097055,
ECO:0000269|PubMed:17496161,
ECO:0000269|PubMed:17525163}.
MUTAGEN 118 118 K->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.
{ECO:0000269|PubMed:17097055,
ECO:0000269|PubMed:17496161,
ECO:0000269|PubMed:17525163}.
MUTAGEN 120 120 E->A: Absence of sumoylation. Enhanced
protein degradation. Reduced self-renewal
ability in ES cells. 55% lower expression
of YES1. {ECO:0000269|PubMed:17496161}.
MUTAGEN 122 352 Missing: Loss of MAPK9 binding. Absence
of Ser-347 phosphorylation.
{ECO:0000269|PubMed:29153991}.
MUTAGEN 166 166 V->K: No change in DNA binding. No loss
of self-renewal ability in iPS cells. No
change in nuclear location.
{ECO:0000269|PubMed:23376973}.
MUTAGEN 206 222 NNENLQEICKSETLVQA->SSSGSPTNLDKIAAQGR:
Reduced DNA binding. Loss of self-renewal
ability in iPS cells. No change in
nuclear location.
{ECO:0000269|PubMed:23376973}.
MUTAGEN 206 210 NNENL->AAAAA: Loss of self-renewal
ability in iPS cells.
{ECO:0000269|PubMed:23376973}.
MUTAGEN 206 206 N->A: No change in DNA binding. Reduced
self-renewal ability in iPS cells. No
change in nuclear location.
{ECO:0000269|PubMed:23376973}.
MUTAGEN 207 207 N->A: No change in DNA binding. No change
in nuclear location.
{ECO:0000269|PubMed:23376973}.
MUTAGEN 208 208 E->A: No change in DNA binding. No loss
of self-renewal ability in iPS cells. No
change in nuclear location.
{ECO:0000269|PubMed:23376973}.
MUTAGEN 209 209 N->A: No change in DNA binding. Reduced
self-renewal ability in iPS cells. No
change in nuclear location.
{ECO:0000269|PubMed:23376973}.
MUTAGEN 210 210 L->A: No change in DNA binding. Loss of
self-renewal ability in iPS cells. No
change in nuclear location. No loss of
ability to bind SOX2. Reduced levels of
CHD4 and SMARCA4 in a POU5F1 pulldown
assay. {ECO:0000269|PubMed:23376973}.
MUTAGEN 211 211 Q->A: No change in DNA binding. No loss
of self-renewal ability in iPS cells. No
change in nuclear location.
{ECO:0000269|PubMed:23376973}.
MUTAGEN 211 211 Q->R: No change in DNA binding. Loss of
self-renewal ability in iPS cells. No
change in nuclear location.
{ECO:0000269|PubMed:23376973}.
MUTAGEN 212 212 E->A: No change in DNA binding. No loss
of self-renewal ability in iPS cells. No
change in nuclear location.
{ECO:0000269|PubMed:23376973}.
MUTAGEN 215 215 K->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. {ECO:0000269|PubMed:17496161}.
MUTAGEN 244 244 K->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.
{ECO:0000269|PubMed:17496161}.
MUTAGEN 347 347 S->A: Absence of phosphorylation. Reduced
protein degradation. Reduced self-renewal
ability in ES cells. No change in FBXW4
binding. Loss of FBXW8 binding.
{ECO:0000269|PubMed:29153991}.
CONFLICT 1 28 Missing (in Ref. 2; CAA36682).
{ECO:0000305}.
CONFLICT 29 29 V -> M (in Ref. 2; CAA36682).
{ECO:0000305}.
CONFLICT 31 31 P -> S (in Ref. 4; AAA39844/AAB19896).
{ECO:0000305}.
HELIX 132 152 {ECO:0000244|PDB:3L1P}.
HELIX 157 168 {ECO:0000244|PDB:3L1P}.
HELIX 174 181 {ECO:0000244|PDB:3L1P}.
HELIX 187 204 {ECO:0000244|PDB:3L1P}.
HELIX 208 212 {ECO:0000244|PDB:3L1P}.
STRAND 223 225 {ECO:0000244|PDB:1OCP}.
HELIX 232 239 {ECO:0000244|PDB:3L1P}.
TURN 240 244 {ECO:0000244|PDB:3L1P}.
HELIX 250 259 {ECO:0000244|PDB:3L1P}.
HELIX 264 279 {ECO:0000244|PDB:3L1P}.
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


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