Overview
| Uniprot ID | A0A286Y3W0 |
|---|
| Protein Name | Proteasome subunit alpha type |
|---|
| Gene Name | PSMA2 |
|---|
| Organism | Cavia porcellus |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 53 |
LATEKKQKSILYDER |
Function
Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex)
Protein Sequence
10
MAERGYSFSL
20
TTFSPSGKLV
30
QIEYALAAVA
40
GGAPSVGIKA
50
ANGVVLATEK
60
KQKSILYDER
70
SVHKVEPITK
80
HIGLVYSGMG
90
PDYRVLVHRA
100
RKLAQQYYLV
110
YQEPIPTAQL
120
VQRVASVMQE
130
YTQSGGVRPF
140
GVSLLICGWN
150
EGRPYLFQSD
160
PSGAYFAWKA
170
TAMGKNYVNG
180
KTFLEKRYNE
190
DLELEDAIHT
200
AILTLKESFE
210
GQMTEDNIEV
220
GICNEAGFRR
230
LTPTEVKDYL
AAIA
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0000932 |
P-body |
| Cellular Component |
GO:0019773 |
proteasome core complex, alpha-subunit complex |
| Biological Process |
GO:0043161 |
proteasome-mediated ubiquitin-dependent protein catabolic process |
| Biological Process |
GO:0061136 |
regulation of proteasomal protein catabolic process |
| Biological Process |
GO:0006979 |
response to oxidative stress |
| Biological Process |
GO:0009615 |
response to virus |
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.