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Cue1p is an activator of Ubc7p E2 activity in vitro and in vivo
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scholarly article
1 reference
stated in
PubMed
PubMed ID
18321851
retrieved
1 December 2016
title
Cue1p is an activator of Ubc7p E2 activity in vitro and in vivo
(English)
1 reference
stated in
PubMed
PubMed ID
18321851
retrieved
1 December 2016
main subject
cell biology
0 references
ubiquitin-protein transferase activator activity
1 reference
stated in
Gene Ontology release 2020-05-02
Gene Ontology ID
GO:0097027
Cue1p YMR264W
1 reference
stated in
GOA release 2020-03-11
author name string
Omar A Bazirgan
series ordinal
1
0 references
Randolph Y Hampton
series ordinal
2
0 references
language of work or name
English
0 references
publication date
9 May 2008
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published in
Journal of Biological Chemistry
1 reference
stated in
PubMed
PubMed ID
18321851
retrieved
1 December 2016
volume
283
0 references
issue
19
0 references
page(s)
12797-810
0 references
cites work
A ubiquitin ligase transfers preformed polyubiquitin chains from a conjugating enzyme to a substrate
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Determinants of RING-E2 fidelity for Hrd1p, a membrane-anchored ubiquitin ligase
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Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins
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A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation
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The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding site
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Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A
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Mechanism of ubiquitin recognition by the CUE domain of Vps9p
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A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domain
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The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction
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A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation
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Crystal structure of the human ubiquitin conjugating enzyme complex, hMms2-hUbc13
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Molecular insights into polyubiquitin chain assembly: crystal structure of the Mms2/Ubc13 heterodimer
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In vivo action of the HRD ubiquitin ligase complex: mechanisms of endoplasmic reticulum quality control and sterol regulation
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Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation.
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Recognition of the polyubiquitin proteolytic signal
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RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination
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Pex22p of Pichia pastoris, essential for peroxisomal matrix protein import, anchors the ubiquitin-conjugating enzyme, Pex4p, on the peroxisomal membrane
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Cdc53/cullin and the essential Hrt1 RING-H2 subunit of SCF define a ubiquitin ligase module that activates the E2 enzyme Cdc34
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Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair
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The ubiquitin system
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Role of Cue1p in ubiquitination and degradation at the ER surface
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ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
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Inhibition of proteolysis and cell cycle progression in a multiubiquitination-deficient yeast mutant
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Site-directed mutagenesis by overlap extension using the polymerase chain reaction
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The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase
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Sec61p-independent degradation of the tail-anchored ER membrane protein Ubc6p
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29 September 2017
Structural basis of ubiquitylation.
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29 September 2017
ER-associated degradation in protein quality control and cellular regulation
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29 September 2017
Creation of a pluripotent ubiquitin-conjugating enzyme
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29 September 2017
Endoplasmic reticulum degradation requires lumen to cytosol signaling. Transmembrane control of Hrd1p by Hrd3p.
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29 September 2017
HRD gene dependence of endoplasmic reticulum-associated degradation
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29 September 2017
Regulation of HMG-CoA reductase degradation requires the P-type ATPase Cod1p/Spf1p
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29 September 2017
Retrograde protein translocation: ERADication of secretory proteins in health and disease
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29 September 2017
Sequence determinants for regulated degradation of yeast 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein
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29 September 2017
Ubiquitin-mediated regulation of 3-hydroxy-3-methylglutaryl-CoA reductase
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29 September 2017
Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein
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29 September 2017
Regulated degradation of HMG-CoA reductase, an integral membrane protein of the endoplasmic reticulum, in yeast
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29 September 2017
Redirecting the specificity of ubiquitination by modifying ubiquitin-conjugating enzymes
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29 September 2017
A chimeric ubiquitin conjugating enzyme that combines the cell cycle properties of CDC34 (UBC3) and the DNA repair properties of RAD6 (UBC2): implications for the structure, function and evolution of the E2s
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29 September 2017
Genome analysis and functional characterization of the E2 and RING-type E3 ligase ubiquitination enzymes of Arabidopsis
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2 June 2018
Measuring protein degradation with green fluorescent protein
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2 June 2018
Endoplasmic reticulum degradation: reverse protein flow of no return
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2 June 2018
Identification of a portable determinant of cell cycle function within the carboxyl-terminal domain of the yeast CDC34 (UBC3) ubiquitin conjugating (E2) enzyme
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2 June 2018
Autoregulation of an E2 enzyme by ubiquitin-chain assembly on its catalytic residue.
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21 January 2018
Mechanism of lysine 48-linked ubiquitin-chain synthesis by the cullin-RING ubiquitin-ligase complex SCF-Cdc34.
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Crossref
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21 January 2018
Evaluation of a diffusion-driven mechanism for substrate ubiquitination by the SCF-Cdc34 ubiquitin ligase complex
1 reference
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Crossref
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21 January 2018
Identification of an ubiquitin-ligation system for the epidermal-growth-factor receptor--herbimycin A induces in vitro ubiquitination in rabbit-reticulocyte lysate
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/18321851
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1074/JBC.M801122200
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
5106361
OpenCitations bibliographic resource ID
5106361
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
5106361
PMCID
2442330
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
5106361
PubMed ID
18321851
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
5106361
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