Pou5f1
entrez
18999
canonical
uniprot
P20263
canonical
ensembl
ENSMUSG00000024406
resolver
ensp
ENSMUSP00000025271
resolver
enst
ENSMUST00000025271
resolver
genesymbol
Pou5f1
resolver
genesymbol_syn
Oct-3
resolver
genesymbol_syn
Oct-4
resolver
genesymbol_syn
Otf-3
resolver
genesymbol_syn
Otf3
resolver
uniprot
A0A2I6EDI9
resolver
uniprot
Q63843
resolver
uniprot_entry
A0A2I6EDI9_MOUSE
resolver
uniprot_entry
PO5F1_MOUSE
resolver
uniprot_sec
Q63843
resolver
amino_acid_sequence
MAGHLASDFAFSPPPGGGDGSAGLEPGWVDPRTWLSFQGPPGGPGIGPGSEVLGISPCPPAYEFCGGMAYCGPQVGLGLVPQVGVETLQPEGQAGARVESNSEGTSSEPCADRPNAVKLEKVEPTPEESQDMKALQKELEQFAKLLKQKRITLGYTQADVGLTLGVLFGKVFSQTTICRFEALQLSLKNMCKLRPLLEKWVEEADNNENLQEICKSETLVQARKRKRTSIENRVRWSLETMFLKCPKPSLQQITHIANQLGLEKDVVRVWFCNRRQKGKRSSIEYSQREEYEATGTPFPGGAVSFPLPPGPHFGTPGYGSPHFTTLYSVPFPEGEAFPSVPVTALGSPMHSN
uniprot
proteins
function
FUNCTION: Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3') (PubMed:1690859, PubMed:17525163, PubMed:1967980, PubMed:1972777, PubMed:23376973). Forms a trimeric complex with SOX2 or SOX15 on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206 (PubMed:15863505, PubMed:17097055, PubMed:17496161, PubMed:19740739). Critical for early embryogenesis and for embryonic stem cell pluripotency (PubMed:1690859, PubMed:17496161, PubMed:18662995, PubMed:18687992, PubMed:1972777, PubMed:19740739, PubMed:23376973, PubMed:29153991, PubMed:32703285). {ECO:0000269|PubMed:15863505, ECO:0000269|PubMed:1690859, ECO:0000269|PubMed:17097055, ECO:0000269|PubMed:17496161, ECO:0000269|PubMed:17525163, ECO:0000269|PubMed:18662995, ECO:0000269|PubMed:18687992, ECO:0000269|PubMed:1967980, ECO:0000269|PubMed:1972777, ECO:0000269|PubMed:19740739, ECO:0000269|PubMed:23376973, ECO:0000269|PubMed:29153991, ECO:0000269|PubMed:32703285}.
uniprot
proteins
mass_dalton
38216
uniprot
proteins
mutagenesis
MUTAGEN 118; /note="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."; /evidence="ECO:0000269|PubMed:17097055, ECO:0000269|PubMed:17496161, ECO:0000269|PubMed:17525163"; MUTAGEN 120; /note="E->A: Absence of sumoylation. Enhanced protein degradation. Reduced self-renewal ability in ES cells. 55% lower expression of YES1."; /evidence="ECO:0000269|PubMed:17496161"; MUTAGEN 122..352; /note="Missing: Loss of MAPK9 binding. Absence of Ser-347 phosphorylation."; /evidence="ECO:0000269|PubMed:29153991"; MUTAGEN 166; /note="V->K: No change in DNA binding. No loss of self-renewal ability in iPS cells. No change in nuclear location."; /evidence="ECO:0000269|PubMed:23376973"; MUTAGEN 206..222; /note="NNENLQEICKSETLVQA->SSSGSPTNLDKIAAQGR: Reduced DNA binding. Loss of self-renewal ability in iPS cells. No change in nuclear location."; /evidence="ECO:0000269|PubMed:23376973"; MUTAGEN 206..210; /note="NNENL->AAAAA: Loss of self-renewal ability in iPS cells."; /evidence="ECO:0000269|PubMed:23376973"; MUTAGEN 206; /note="N->A: No change in DNA binding. Reduced self-renewal ability in iPS cells. No change in nuclear location."; /evidence="ECO:0000269|PubMed:23376973"; MUTAGEN 207; /note="N->A: No change in DNA binding. No change in nuclear location."; /evidence="ECO:0000269|PubMed:23376973"; MUTAGEN 208; /note="E->A: No change in DNA binding. No loss of self-renewal ability in iPS cells. No change in nuclear location."; /evidence="ECO:0000269|PubMed:23376973"; MUTAGEN 209; /note="N->A: No change in DNA binding. Reduced self-renewal ability in iPS cells. No change in nuclear location."; /evidence="ECO:0000269|PubMed:23376973"; MUTAGEN 210; /note="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."; /evidence="ECO:0000269|PubMed:23376973"; MUTAGEN 211; /note="Q->A: No change in DNA binding. No loss of self-renewal ability in iPS cells. No change in nuclear location."; /evidence="ECO:0000269|PubMed:23376973"; MUTAGEN 211; /note="Q->R: No change in DNA binding. Loss of self-renewal ability in iPS cells. No change in nuclear location."; /evidence="ECO:0000269|PubMed:23376973"; MUTAGEN 212; /note="E->A: No change in DNA binding. No loss of self-renewal ability in iPS cells. No change in nuclear location."; /evidence="ECO:0000269|PubMed:23376973"; MUTAGEN 215; /note="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."; /evidence="ECO:0000269|PubMed:17496161"; MUTAGEN 244; /note="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."; /evidence="ECO:0000269|PubMed:17496161"; MUTAGEN 347; /note="S->A: Absence of phosphorylation. Reduced protein degradation. Reduced self-renewal ability in ES cells. No change in FBXW4 binding. Loss of FBXW8 binding."; /evidence="ECO:0000269|PubMed:29153991
uniprot
proteins
post_translational_modification
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}.
uniprot
proteins
protein_family
Class-5 subfamily
uniprot
proteins
protein_family
POU transcription factor family
uniprot
proteins
pubmed
11702949
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15831456
uniprot
proteins
pubmed
15863505
uniprot
proteins
pubmed
16904174
uniprot
proteins
pubmed
1690859
uniprot
proteins
pubmed
17097055
uniprot
proteins
pubmed
17496161
uniprot
proteins
pubmed
17525163
uniprot
proteins
pubmed
18662995
uniprot
proteins
pubmed
18687992
uniprot
proteins
pubmed
1915274
uniprot
proteins
pubmed
1967980
uniprot
proteins
pubmed
1972777
uniprot
proteins
pubmed
19740739
uniprot
proteins
pubmed
19997087
uniprot
proteins
pubmed
23376973
uniprot
proteins
pubmed
24550733
uniprot
proteins
pubmed
27984042
uniprot
proteins
pubmed
29153991
uniprot
proteins
pubmed
32703285
uniprot
proteins
pubmed
8097478
uniprot
proteins
sequence_length
352
uniprot
proteins
subcellular_location
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}.
uniprot
proteins