| UniProt ID | PO5F1_MOUSE | |
|---|---|---|
| UniProt AC | P20263 | |
| Protein Name | POU domain, class 5, transcription factor 1 | |
| Gene Name | Pou5f1 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 352 | |
| Subcellular Localization | Cytoplasm . Nucleus . Expressed in a diffuse and slightly punctuate pattern (By similarity). Colocalizes with MAPK8 and MAPK9 in the nucleus (PubMed:29153991). | |
| Protein Description | Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3'). [PubMed: 1972777] | |
| Protein Sequence | MAGHLASDFAFSPPPGGGDGSAGLEPGWVDPRTWLSFQGPPGGPGIGPGSEVLGISPCPPAYEFCGGMAYCGPQVGLGLVPQVGVETLQPEGQAGARVESNSEGTSSEPCADRPNAVKLEKVEPTPEESQDMKALQKELEQFAKLLKQKRITLGYTQADVGLTLGVLFGKVFSQTTICRFEALQLSLKNMCKLRPLLEKWVEEADNNENLQEICKSETLVQARKRKRTSIENRVRWSLETMFLKCPKPSLQQITHIANQLGLEKDVVRVWFCNRRQKGKRSSIEYSQREEYEATGTPFPGGAVSFPLPPGPHFGTPGYGSPHFTTLYSVPFPEGEAFPSVPVTALGSPMHSN | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 12 | Phosphorylation | LASDFAFSPPPGGGD CCCCCCCCCCCCCCC | 32.82 | 22006019 | |
| 106 | Phosphorylation | ESNSEGTSSEPCADR ECCCCCCCCCCCCCC | 43.49 | - | |
| 118 | Sumoylation | ADRPNAVKLEKVEPT CCCCCCEEEEECCCC | 48.82 | - | |
| 118 | Ubiquitination | ADRPNAVKLEKVEPT CCCCCCEEEEECCCC | 48.82 | - | |
| 118 | Sumoylation | ADRPNAVKLEKVEPT CCCCCCEEEEECCCC | 48.82 | 17525163 | |
| 137 | Ubiquitination | QDMKALQKELEQFAK HHHHHHHHHHHHHHH | 66.18 | - | |
| 144 | Ubiquitination | KELEQFAKLLKQKRI HHHHHHHHHHHHCCC | 56.49 | - | |
| 199 | Ubiquitination | KLRPLLEKWVEEADN HHHHHHHHHHHHHCC | 57.41 | - | |
| 215 | Ubiquitination | ENLQEICKSETLVQA CCHHHHHHHHHHHHH | 57.92 | - | |
| 228 | Phosphorylation | QARKRKRTSIENRVR HHHHHHCCCHHHHHH | 36.77 | - | |
| 228 | O-linked_Glycosylation | QARKRKRTSIENRVR HHHHHHCCCHHHHHH | 36.77 | 22608532 | |
| 229 | Phosphorylation | ARKRKRTSIENRVRW HHHHHCCCHHHHHHH | 31.75 | - | |
| 229 | O-linked_Glycosylation | ARKRKRTSIENRVRW HHHHHCCCHHHHHHH | 31.75 | 22608532 | |
| 282 | Phosphorylation | RQKGKRSSIEYSQRE CCCCCCCCCCHHHHH | 24.38 | - | |
| 343 | Phosphorylation | AFPSVPVTALGSPMH CCCCCCEEECCCCCC | 15.30 | - | |
| 347 | Phosphorylation | VPVTALGSPMHSN-- CCEEECCCCCCCC-- | 21.65 | 29153991 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 106 | S | Phosphorylation | Kinase | MAPK | - | Uniprot |
| 347 | S | Phosphorylation | Kinase | MAPK8 | P45983 | GPS |
| 347 | S | Phosphorylation | Kinase | MAPK8 | Q91Y86 | Uniprot |
| 347 | S | Phosphorylation | Kinase | MAPK9 | P45984 | GPS |
| 347 | S | Phosphorylation | Kinase | MAPK9 | Q9WTU6 | Uniprot |
| - | K | Ubiquitination | E3 ubiquitin ligase | Wwp2 | Q9DBH0 | PMID:22199232 |
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of PO5F1_MOUSE !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Sumoylation | |
| Reference | PubMed |
| "Sumoylation of Oct4 enhances its stability, DNA binding, andtransactivation."; Wei F., Schoeler H.R., Atchison M.L.; J. Biol. Chem. 282:21551-21560(2007). Cited for: SUMOYLATION AT LYS-118, MUTAGENESIS OF LYS-118, FUNCTION, ANDSUBCELLULAR LOCATION. | |
| "Post-translational modification of POU domain transcription factorOct-4 by SUMO-1."; Zhang Z., Liao B., Xu M., Jin Y.; FASEB J. 21:3042-3051(2007). Cited for: SUMOYLATION AT LYS-118, MUTAGENESIS OF LYS-118; GLU-120; LYS-215 ANDLYS-244, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH UBE2I. | |
| "Inhibition of DNA binding of Sox2 by the SUMO conjugation."; Tsuruzoe S., Ishihara K., Uchimura Y., Watanabe S., Sekita Y.,Aoto T., Saitoh H., Yuasa Y., Niwa H., Kawasuji M., Baba H., Nakao M.; Biochem. Biophys. Res. Commun. 351:920-926(2006). Cited for: SUMOYLATION AT LYS-118, AND MUTAGENESIS OF LYS-118. | |