Overview
| Uniprot ID | H0UYJ4 |
|---|
| Protein Name | 26S proteasome regulatory subunit 4 |
|---|
| Gene Name | PSMC1 |
|---|
| Organism | Cavia porcellus |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 21 |
DDKDKKKKYEPPVPT |
Function
Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC1 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides
Protein Sequence
10
IQSGGHGPGG
20
GKKDDKDKKK
30
KYEPPVPTRV
40
GKKKKKTKGP
50
DAASKLPLVT
60
PHTQCRLKLL
70
KLERIKDYLL
80
MEEEFIRNQE
90
QMKPLEEKQE
100
EERSKVDDLR
110
GTPMSVGTLE
120
EIIDDNHAIV
130
STSVGSEHYV
140
SILSFVDKDL
150
LEPGCSVLLN
160
HKVHAVIGVL
170
MDDTDPLVTV
180
MKVEKAPQET
190
YADIGGLDNQ
200
IQEIKESVEL
210
PLTHPEYYEE
220
MGIKPPKGVI
230
LYGPPGTGKT
240
LLAKAVANQT
250
SATFLRVVGS
260
ELIQKYLGDG
270
PKLVRELFRV
280
AEEHAPSIVF
290
IDEIDAIGTK
300
RYDSNSGGER
310
EIQRTMLELL
320
NQLDGFDSRG
330
DVKVIMATNR
340
IETLDPALIR
350
PGRIDRKIEF
360
PLPDEKTKKR
370
IFQIHTSRMT
380
LADDVTLDDL
390
IMAKDDLSGA
400
DIKAICTEAG
410
LMALRERRMK
420
VTNEDFKKSK
430
ENVLYKKQEG
TPEGLYL
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0000502 |
proteasome complex |
| Molecular Function |
GO:0005524 |
ATP binding |
| Molecular Function |
GO:0016887 |
ATP hydrolysis activity |
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.