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 | ||
|
* 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. |
loading...
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. |