Overview
| Uniprot ID | Q16186 |
| Protein Name | Proteasomal ubiquitin receptor ADRM1 |
| Gene Name | ADRM1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 42 |
GTTVTPDKRKGLVYI |
| 97 |
SGRVYVLKFKAGSKR |
Function
Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins (PubMed:16815440, PubMed:16906146, PubMed:16990800, PubMed:17139257, PubMed:18497817, PubMed:24752541, PubMed:25702870, PubMed:25702872). 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 (PubMed:16815440, PubMed:16906146, PubMed:16990800, PubMed:17139257, PubMed:18497817, PubMed:24752541, PubMed:25702870, PubMed:25702872). Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair (PubMed:16815440, PubMed:16906146, PubMed:16990800, PubMed:17139257, PubMed:18497817, PubMed:24752541, PubMed:25702870, PubMed:25702872). Within the complex, functions as a proteasomal ubiquitin receptor (PubMed:18497817). Engages and activates 19S-associated deubiquitinases UCHL5 and PSMD14 during protein degradation (PubMed:16906146, PubMed:16990800, PubMed:17139257, PubMed:24752541). UCHL5 reversibly associate with the 19S regulatory particle whereas PSMD14 is an intrinsic subunit of the proteasome lid subcomplex (PubMed:16906146, PubMed:16990800, PubMed:17139257, PubMed:24752541)
Protein Sequence
10
MTTSGALFPS
20
LVPGSRGASN
30
KYLVEFRAGK
40
MSLKGTTVTP
50
DKRKGLVYIQ
60
QTDDSLIHFC
70
WKDRTSGNVE
80
DDLIIFPDDC
90
EFKRVPQCPS
100
GRVYVLKFKA
110
GSKRLFFWMQ
120
EPKTDQDEEH
130
CRKVNEYLNN
140
PPMPGALGAS
150
GSSGHELSAL
160
GGEGGLQSLL
170
GNMSHSQLMQ
180
LIGPAGLGGL
190
GGLGALTGPG
200
LASLLGSSGP
210
PGSSSSSSSR
220
SQSAAVTPSS
230
TTSSTRATPA
240
PSAPAAASAT
250
SPSPAPSSGN
260
GASTAASPTQ
270
PIQLSDLQSI
280
LATMNVPAGP
290
AGGQQVDLAS
300
VLTPEIMAPI
310
LANADVQERL
320
LPYLPSGESL
330
PQTADEIQNT
340
LTSPQFQQAL
350
GMFSAALASG
360
QLGPLMCQFG
370
LPAEAVEAAN
380
KGDVEAFAKA
390
MQNNAKPEQK
400
EGDTKDKKDE
EEDMSLD
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0000502 |
proteasome complex |
| Cellular Component |
GO:0008541 |
proteasome regulatory particle, lid subcomplex |
| Cellular Component |
GO:0008021 |
synaptic vesicle |
| Molecular Function |
GO:0061133 |
endopeptidase activator activity |
| Molecular Function |
GO:0140678 |
molecular function inhibitor activity |
| Molecular Function |
GO:0002020 |
protease binding |
| Molecular Function |
GO:0070628 |
proteasome binding |
| Biological Process |
GO:0071357 |
cellular response to type I interferon |
| Biological Process |
GO:0010498 |
proteasomal protein catabolic process |
| Biological Process |
GO:0043248 |
proteasome assembly |
| 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:0006368 |
transcription elongation by RNA polymerase II |
Reference
[1] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.