Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome
about
Identification of a functional docking site in the Rpn1 LRR domain for the UBA-UBL domain protein Ddi13-Methyladenine-DNA glycosylase (MPG protein) interacts with human RAD23 proteinsCentrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repairRad23 ubiquitin-associated domains (UBA) inhibit 26 S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chainsA complex between peptide:N-glycanase and two proteasome-linked proteins suggests a mechanism for the degradation of misfolded glycoproteinsUbiquitin receptor proteins hHR23a and hPLIC2 interactAccumulation of polyubiquitinated proteins by overexpression of RBCC protein interacting with protein kinase C2, a splice variant of ubiquitin ligase RBCC protein interacting with protein kinase C1HIV-1 replication through hHR23A-mediated interaction of Vpr with 26S proteasomeRole of the UBL-UBA protein KPC2 in degradation of p27 at G1 phase of the cell cycle.Involvement of rhp23, a Schizosaccharomyces pombe homolog of the human HHR23A and Saccharomyces cerevisiae RAD23 nucleotide excision repair genes, in cell cycle control and protein ubiquitinationIdentification of proteins that interact with mammalian peptide:N-glycanase and implicate this hydrolase in the proteasome-dependent pathway for protein degradationInvolvement of the DNA repair protein hHR23 in p53 degradationAPOBEC3G-UBA2 fusion as a potential strategy for stable expression of APOBEC3G and inhibition of HIV-1 replicationUbiquitin-like and ubiquitin-associated domain proteins: significance in proteasomal degradationThe ubiquitin-associated domain of hPLIC-2 interacts with the proteasomeA novel regulation mechanism of DNA repair by damage-induced and RAD23-dependent stabilization of xeroderma pigmentosum group C proteinAtaxin-3 interactions with rad23 and valosin-containing protein and its associations with ubiquitin chains and the proteasome are consistent with a role in ubiquitin-mediated proteolysisStructural determinants for the binding of ubiquitin-like domains to the proteasomeRegulation of repair by the 26SproteasomeThe life cycle of the 26S proteasome: from birth, through regulation and function, and onto its deathFunctions of the 19S complex in proteasomal degradationParkin binds the Rpn10 subunit of 26S proteasomes through its ubiquitin-like domainStructure and ubiquitin binding of the ubiquitin-interacting motifBinding surface mapping of intra- and interdomain interactions among hHR23B, ubiquitin, and polyubiquitin binding site 2 of S5aSolution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor downregulationDNA-repair protein hHR23a alters its protein structure upon binding proteasomal subunit S5aStructure of the ubiquitin-interacting motif of S5a bound to the ubiquitin-like domain of HR23BProteasome subunit Rpn13 is a novel ubiquitin receptorStructure of the S5a:K48-Linked Diubiquitin Complex and Its Interactions with Rpn13Solution structure of the E3 ligase HOIL-1 Ubl domainProteasome subunit Rpn1 binds ubiquitin-like protein domains.Proteasomes can degrade a significant proportion of cellular proteins independent of ubiquitination.Proteasome nuclear activity affects chromosome stability by controlling the turnover of Mms22, a protein important for DNA repair.Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome.Rad23 interaction with the proteasome is regulated by phosphorylation of its ubiquitin-like (UbL) domainPhysical association of ubiquitin ligases and the 26S proteasome.The NEF4 complex regulates Rad4 levels and utilizes Snf2/Swi2-related ATPase activity for nucleotide excision repair.Targeting of NEDD8 and its conjugates for proteasomal degradation by NUB1Cleaning up in the endoplasmic reticulum: ubiquitin in chargeTargeting proteins for degradation
P2860
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P2860
Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome
description
1999 nî lūn-bûn
@nan
1999 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
name
Interaction of hHR23 with S5a. ...... S5a subunit of 26 S proteasome
@ast
Interaction of hHR23 with S5a. ...... S5a subunit of 26 S proteasome
@en
Interaction of hHR23 with S5a. ...... S5a subunit of 26 S proteasome
@en-gb
Interaction of hHR23 with S5a. ...... S5a subunit of 26 S proteasome
@nl
type
label
Interaction of hHR23 with S5a. ...... S5a subunit of 26 S proteasome
@ast
Interaction of hHR23 with S5a. ...... S5a subunit of 26 S proteasome
@en
Interaction of hHR23 with S5a. ...... S5a subunit of 26 S proteasome
@en-gb
Interaction of hHR23 with S5a. ...... S5a subunit of 26 S proteasome
@nl
prefLabel
Interaction of hHR23 with S5a. ...... S5a subunit of 26 S proteasome
@ast
Interaction of hHR23 with S5a. ...... S5a subunit of 26 S proteasome
@en
Interaction of hHR23 with S5a. ...... S5a subunit of 26 S proteasome
@en-gb
Interaction of hHR23 with S5a. ...... S5a subunit of 26 S proteasome
@nl
P2093
P2860
P3181
P356
P1476
Interaction of hHR23 with S5a. ...... S5a subunit of 26 S proteasome
@en
P2093
C Masutani
J H Hoeijmakers
K Sugasawa
P2860
P304
P3181
P356
10.1074/JBC.274.39.28019
P407
P577
1999-09-24T00:00:00Z