Search Results

Overview

Uniprot IDQ16186
Protein NameProteasomal ubiquitin receptor ADRM1
Gene NameADRM1
OrganismHomo 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.