Search Results
Overview
| Uniprot ID | A0A286XBE6 |
|---|---|
| Protein Name | E3 ubiquitin-protein ligase PPP1R11 |
| Gene Name | PPP1R11 |
| Organism | Cavia porcellus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 31 | ENRSLTIKLRKRKPE |
| 40 | RKRKPEKKVEWTSDT |
| 59 | HMGRRSSKCCCIYEK |
Function
Atypical E3 ubiquitin-protein ligase which ubiquitinates TLR2 at 'Lys-754' leading to its degradation by the proteasome. Plays a role in regulating inflammatory cytokine release and gram-positive bacterial clearance by functioning, in part, through the ubiquitination and degradation of TLR2. Inhibitor of protein phosphatase 1
Protein Sequence
10
MAEAGAGLSE
20
TVTETTVTVT
30
TEPENRSLTI
40
KLRKRKPEKK
50
VEWTSDTVDN
60
EHMGRRSSKC
70
CCIYEKPRAF
80
GESSTESEEE
90
EEEGCGHTHC
100
VRGHRKGRRQ
110
ATPGPTPTTP
120
PQPPDPTQPP
PGPMQH
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0008157 | protein phosphatase 1 binding |
| Molecular Function | GO:0004865 | protein serine/threonine phosphatase inhibitor activity |
| Molecular Function | GO:0061630 | ubiquitin protein ligase activity |
| Biological Process | GO:0006511 | ubiquitin-dependent protein catabolic process |
Reference
[1] Feng J, Chen X, Li R, Xie Y, Zhang X et al.. Lactylome analysis reveals potential target modified proteins in the retina of form-deprivation myopia.. iScience 27(9):110606. 2024 Sep 20. PMID: 39246443.