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Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome
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scholarly article
1 reference
stated in
PubMed
PubMed ID
11805328
retrieved
1 December 2016
title
Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome
(English)
1 reference
stated in
PubMed
PubMed ID
11805328
retrieved
1 December 2016
main subject
Ubiquitin domain-containing protein DSK2 YMR276W
1 reference
stated in
GOA release 2020-03-11
author name string
Minoru Funakoshi
series ordinal
1
0 references
Toru Sasaki
series ordinal
2
0 references
Takeharu Nishimoto
series ordinal
3
0 references
Hideki Kobayashi
series ordinal
4
0 references
language of work or name
English
0 references
publication date
22 January 2002
0 references
published in
Proceedings of the National Academy of Sciences of the United States of America
1 reference
stated in
PubMed
PubMed ID
11805328
retrieved
1 December 2016
volume
99
0 references
issue
2
0 references
page(s)
745-50
0 references
cites work
UBA domains of DNA damage-inducible proteins interact with ubiquitin
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Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes
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Physical association of ubiquitin ligases and the 26S proteasome
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Recognition of the polyubiquitin proteolytic signal
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Rpn9 is required for efficient assembly of the yeast 26S proteasome
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Saccharomyces cerevisiae putative G protein, Gtr1p, which forms complexes with itself and a novel protein designated as Gtr2p, negatively regulates the Ran/Gsp1p G protein cycle through Gtr2p
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A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly.
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The ubiquitin system
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PubMed Central
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A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3.
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Yeast counterparts of subunits S5a and p58 (S3) of the human 26S proteasome are encoded by two multicopy suppressors of nin1-1
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The N-end rule: functions, mysteries, uses
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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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A proteolytic pathway that recognizes ubiquitin as a degradation signal
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The yeast ubiquitin genes: a family of natural gene fusions
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A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
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20 March 2017
Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain
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The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome
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20 March 2017
Ubiquitin-related proteins regulate interaction of vimentin intermediate filaments with the plasma membrane
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Characterization of two polyubiquitin binding sites in the 26 S protease subunit 5a
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20 March 2017
Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome
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20 March 2017
In vivo half-life of a protein is a function of its amino-terminal residue
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Proteins containing the UBA domain are able to bind to multi-ubiquitin chains
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PubMed Central
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Rad23 links DNA repair to the ubiquitin/proteasome pathway
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The proteasome: paradigm of a self-compartmentalizing protease
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Dosage suppressors of pds1 implicate ubiquitin-associated domains in checkpoint control
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Ubiquitin in chains
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Cell cycle-regulated modification of the ribosome by a variant multiubiquitin chain
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29 September 2017
Cdc28 activates exit from mitosis in budding yeast.
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29 September 2017
A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch
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29 September 2017
Identification of XDRP1; a Xenopus protein related to yeast Dsk2p binds to the N-terminus of cyclin A and inhibits its degradation
1 reference
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PubMed Central
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29 September 2017
Pleiotropic defects caused by loss of the proteasome-interacting factors Rad23 and Rpn10 of Saccharomyces cerevisiae.
1 reference
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PubMed Central
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29 September 2017
The Doa4 deubiquitinating enzyme is required for ubiquitin homeostasis in yeast
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29 September 2017
Scythe: a novel reaper-binding apoptotic regulator.
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29 September 2017
Yeast ubiquitin-like genes are involved in duplication of the microtubule organizing center
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29 September 2017
The Saccharomyces cerevisiae DNA repair gene RAD23 encodes a nuclear protein containing a ubiquitin-like domain required for biological function
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PubMed Central
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29 September 2017
Mph1, a member of the Mps1-like family of dual specificity protein kinases, is required for the spindle checkpoint in S. pombe.
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2 June 2018
Roles of ubiquitin-mediated proteolysis in cell cycle control
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2 June 2018
Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain
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2 June 2018
A genetic interaction between a ubiquitin-like protein and ubiquitin-mediated proteolysis in Dictyostelium discoideum(1).
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21 January 2018
Analysis of a gene encoding Rpn10 of the fission yeast proteasome reveals that the polyubiquitin-binding site of this subunit is essential when Rpn12/Mts3 activity is compromised.
1 reference
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Crossref
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https://api.crossref.org/works/10.1073%2FPNAS.012585199
retrieved
21 January 2018
The DNA repair protein rad23 is a negative regulator of multi-ubiquitin chain assembly
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1073%2FPNAS.012585199
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21 January 2018
E2/E3-mediated assembly of lysine 29-linked polyubiquitin chains
1 reference
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Crossref
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https://api.crossref.org/works/10.1073%2FPNAS.012585199
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21 January 2018
Xenopus cyclin A1 can associate with Cdc28 in budding yeast, causing cell-cycle arrest with an abnormal distribution of nuclear DNA
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1073%2FPNAS.012585199
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21 January 2018
Identifiers
DOI
10.1073/PNAS.012585199
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4277601
ADS bibcode
2002PNAS...99..745F
0 references
OpenCitations bibliographic resource ID
4277601
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4277601
PMCID
117376
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4277601
PubMed ID
11805328
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4277601
ResearchGate publication ID
11554452
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