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A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domain
scientific article
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instance of
scholarly article
1 reference
stated in
PubMed
PubMed ID
12628920
retrieved
1 December 2016
title
A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domain
(English)
1 reference
stated in
PubMed
PubMed ID
12628920
retrieved
1 December 2016
main subject
Cue2p YKL090W
1 reference
stated in
GOA release 2020-03-11
Guanine nucleotide exchange factor VPS9 YML097C
1 reference
stated in
GOA release 2020-03-11
Cue3p YGL110C
1 reference
stated in
GOA release 2020-03-11
Ubiquitin-binding protein CUE5 YOR042W
1 reference
stated in
GOA release 2020-03-11
author name string
Susan C Shih
series ordinal
1
0 references
Gali Prag
series ordinal
2
0 references
Smitha A Francis
series ordinal
3
0 references
Myra A Sutanto
series ordinal
4
0 references
James H Hurley
series ordinal
5
0 references
Linda Hicke
series ordinal
6
0 references
language of work or name
English
0 references
publication date
17 March 2003
0 references
published in
The EMBO Journal
1 reference
stated in
PubMed
PubMed ID
12628920
retrieved
1 December 2016
volume
22
0 references
page(s)
1273-81
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issue
6
0 references
cites work
Solution structures of UBA domains reveal a conserved hydrophobic surface for protein-protein interactions
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Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome
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The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum
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20 March 2017
Ubiquitin-associated (UBA) domains in Rad23 bind ubiquitin and promote inhibition of multi-ubiquitin chain assembly
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20 March 2017
UBA domains of DNA damage-inducible proteins interact with ubiquitin
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PubMed Central
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20 March 2017
Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function prediction
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DOT4 links silencing and cell growth in Saccharomyces cerevisiae
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A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisiae
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20 March 2017
Vps9p is a guanine nucleotide exchange factor involved in vesicle-mediated vacuolar protein transport
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PubMed Central
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20 March 2017
The ubiquitin system
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PubMed Central
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20 March 2017
Role of Cue1p in ubiquitination and degradation at the ER surface
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PubMed Central
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20 March 2017
A yeast protein related to a mammalian Ras-binding protein, Vps9p, is required for localization of vacuolar proteins
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PubMed Central
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20 March 2017
New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
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20 March 2017
Getting started with yeast
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PubMed Central
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20 March 2017
Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast
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PubMed Central
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20 March 2017
Hrs sorts ubiquitinated proteins into clathrin-coated microdomains of early endosomes
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PubMed Central
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7 April 2017
A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins
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PubMed Central
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7 April 2017
Proteins containing the UBA domain are able to bind to multi-ubiquitin chains
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PubMed Central
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7 April 2017
Protein regulation by monoubiquitin
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PubMed Central
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7 April 2017
Overcoming expression and purification problems of RhoGDI using a family of "parallel" expression vectors
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7 April 2017
Evolution and function of ubiquitin-like protein-conjugation systems
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PubMed Central
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9 May 2017
Novel domains and orthologues of eukaryotic transcription elongation factors.
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29 September 2017
The ubiquitin-interacting motifs target the endocytic adaptor protein epsin for ubiquitination
1 reference
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PubMed Central
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29 September 2017
A ubiquitin-interacting motif (UIM) is essential for Eps15 and Eps15R ubiquitination
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=151082
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29 September 2017
Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis
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PubMed Central
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29 September 2017
A ubiquitin-interacting motif conserved in components of the proteasomal and lysosomal protein degradation systems
1 reference
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PubMed Central
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29 September 2017
Ubiquitin and its kin: how close are the family ties?
1 reference
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PubMed Central
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=151082
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29 September 2017
Monoubiquitin carries a novel internalization signal that is appended to activated receptors
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PubMed Central
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=151082
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29 September 2017
Structure of a human DNA repair protein UBA domain that interacts with HIV-1 Vpr.
1 reference
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PubMed Central
reference URL
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29 September 2017
MDP1, a Saccharomyces cerevisiae gene involved in mitochondrial/cytoplasmic protein distribution, is identical to the ubiquitin-protein ligase gene RSP5.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=151082
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29 September 2017
The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitination pathway
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=151082
retrieved
29 September 2017
Surface hydrophobic residues of multiubiquitin chains essential for proteolytic targeting
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=151082
retrieved
29 September 2017
Distinct functional surface regions on ubiquitin
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=151082
retrieved
27 November 2018
Identifiers
DOI
10.1093/EMBOJ/CDG140
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3160446
OpenCitations bibliographic resource ID
3160446
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3160446
PMCID
151082
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3160446
PubMed ID
12628920
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3160446
ResearchGate publication ID
10863197
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