Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome (Q22010540)

7 February 2023

H Hiyama

1

H

Hiyama

1 reference

7 February 2023

M Yokoi

2

M

Yokoi

1 reference

7 February 2023

C Masutani

3

C

Masutani

1 reference

7 February 2023

K Sugasawa

4

K

Sugasawa

1 reference

7 February 2023

T Maekawa

5

T

Maekawa

1 reference

7 February 2023

K Tanaka

6

K

Tanaka

1 reference

7 February 2023

F Hanaoka

8

F

Hanaoka

1 reference

Journal of Biological Chemistry

7 February 2023

publication date

24 September 1999

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language of work or name

English

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published in

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volume

274

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issue

39

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page(s)

28019-25

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The Saccharomyces cerevisiae DNA repair gene RAD23 encodes a nuclear protein containing a ubiquitin-like domain required for biological function

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HHR23B, a human Rad23 homolog, stimulates XPC protein in nucleotide excision repair in vitro

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The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover.

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Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26 S proteasome subunit Mcb1.

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Characterization of Two Polyubiquitin Binding Sites in the 26 S Protease Subunit 5a

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Purification and cloning of a nucleotide excision repair complex involving the xeroderma pigmentosum group C protein and a human homologue of yeast RAD23

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inferred from DOI database lookup

7 January 2021

based on heuristic

Nin1p, a regulatory subunit of the 26S proteasome, is necessary for activation of Cdc28p kinase of Saccharomyces cerevisiae

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