Proteasomal ubiquitin receptor ADRM1

UniProt Q16186 Organism Homo sapiens Gene ADRM1, GP110

Also known as: ADRM1, GP110

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. Within the complex, functions as a proteasomal ubiquitin receptor. Engages and activates 19S-associated deubiquitinases UCHL5 and PSMD14 during protein degradation. UCHL5 reversibly associate with the 19S regulatory particle whereas PSMD14 is an intrinsic subunit of the proteasome lid subcomplex.

Classification

Family (Pfam): PF04683 Rpn13_ADRM1_Pru, PF16550 RPN13_C
InterPro: DEUBAD_dom, Rpn13/ADRM1, Rpn13/ADRM1_Pru, Rpn13/ADRM1_Pru_sf, RPN13_DEUBAD, RPN13_DEUBAD_sf
Functional cluster: RNA-Polymerase II Transcription Factors

Experimental structures · PDB · 21

2KQZ NMR
2KR0 NMR
2L5V NMR
2MKZ NMR
2NBV NMR
4UEL X-ray 2.30A
4UEM X-ray 2.82A
4WLQ X-ray 2.85A
4WLR X-ray 2.00A
5IRS X-ray 1.80A
5V1Y X-ray 1.42A
5V1Z X-ray 2.00A
… and 9 more

A predicted model is available from AlphaFold.

Gene Ontology · 16

Drugs targeting this protein · 6

OPROZOMIB inhibitor
IXAZOMIB inhibitor
BORTEZOMIB inhibitor
IXAZOMIB CITRATE inhibitor
CARFILZOMIB inhibitor
BORTEZOMIB D-MANNITOL inhibitor

Related proteins · sequence + function similarity

Co-cited proteins · studied together in the literature

Proteasomal ubiquitin receptor ADRM1 2 shared papers
Ubiquitin carboxyl-terminal hydrolase isozyme L5 3 shared papers
Ubiquitin-protein ligase E3C 2 shared papers
26S proteasome non-ATPase regulatory subunit 1 2 shared papers
Ubiquitin carboxyl-terminal hydrolase isozyme L5 1 shared papers
E3 ubiquitin-protein ligase RNF181 1 shared papers
26S proteasome regulatory subunit 7 1 shared papers

Literature · 24 cited papers

Acute unfolding of a single protein immediately stimulates recruitment of ubiquitin protein ligase E3C (UBE3C) to 26S proteasomes. J. Biol. Chem. · 2019
Structures of Rpn1 T1:Rad23 and hRpn13:hPLIC2 reveal distinct binding mechanisms between substrate receptors and shuttle factors of the proteasome. Structure · 2016
Structural basis for the activation and inhibition of the UCH37 deubiquitylase. Mol. Cell · 2015
Mechanism of UCH-L5 activation and inhibition by DEUBAD domains in RPN13 and INO80G. Mol. Cell · 2015
Autoubiquitination of the 26S proteasome on Rpn13 regulates breakdown of ubiquitin conjugates. EMBO J. · 2014
Mechanism of the Rpn13-induced activation of Uch37. Protein Cell · 2014
An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J. Proteomics · 2014
Toward a comprehensive characterization of a human cancer cell phosphoproteome. J. Proteome Res. · 2013
N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. Proc. Natl. Acad. Sci. U.S.A. · 2012
Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features. Mol. Cell. Proteomics · 2012
Initial characterization of the human central proteome. BMC Syst. Biol. · 2011
Structure of proteasome ubiquitin receptor hRpn13 and its activation by the scaffolding protein hRpn2. Mol. Cell · 2010
… and 12 more in the literature graph

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