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Search results 101 to 122 out of 122 for Dsc1

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0.027s

Type

Details

Score

Publication

- | J:144086

First Author:	Mouse Genome Informatics Scientific Curators
Year:	2009
Journal:	Database Download
Title:	Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform

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Publication

- | J:155721

First Author:	Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year:	2010
Journal:	Database Download
Title:	Consensus CDS project

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Publication

- | J:85324

First Author:	Mouse Genome Informatics Group
Year:	2003
Journal:	Database Procedure
Title:	Automatic Encodes (AutoE) Reference

•

Publication

- | J:53168

First Author:	Bairoch A
Year:	1999
Journal:	Database Release
Title:	SWISS-PROT Annotated protein sequence database

•

Publication

- | J:91388

First Author:	Mouse Genome Informatics Scientific Curators
Year:	2005

Title:	Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations

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Publication

- | J:155221

First Author:	Mouse Genome Informatics
Year:	2010
Journal:	Database Release
Title:	Protein Ontology Association Load.

•

Publication

- | J:90438

First Author:	Mouse Genome Informatics Scientific Curators
Year:	2005

Title:	Obtaining and loading genome assembly coordinates from NCBI annotations

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Publication

- | J:144087

First Author:	Mouse Genome Informatics Scientific Curators
Year:	2009
Journal:	Database Download
Title:	Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform

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GO Term

GO:0030907 | MBF transcription complex

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Allele

Dsc1<em1Smoc> | MGI:7289401

Name:	desmocollin 1; endonuclease-mediated mutation 1, Shanghai Model Organisms Center
Allele Type:	Endonuclease-mediated
Attribute String:	Null/knockout

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GO Term

GO:0120185 | MBF transcription complex assembly

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Strain

MGI:6475159 | C57BL/6JSmoc-Dsc1<em1Smoc>/Smoc

Attribute String:

coisogenic, endonuclease-mediated mutation, mutant strain

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Publication

25078903 | -

First Author:	Tong Z
Year:	2014
Journal:	Mol Cell Proteomics
Title:	Identification of candidate substrates for the Golgi Tul1 E3 ligase using quantitative diGly proteomics in yeast.
Volume:	13
Issue:	11
Pages:	2871-82

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Publication

31368600 | -

First Author:	Schmidt O
Year:	2019
Journal:	EMBO J
Title:	Endosome and Golgi-associated degradation (EGAD) of membrane proteins regulates sphingolipid metabolism.
Volume:	38
Issue:	15
Pages:	e101433

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Protein Domain

IPR019413 | Dsc3_ub-like_dom

Type:

Domain

Description:

This is the N-terminal ubiquitin-like domain of DSC E3 ubiquitin ligase complex subunit 3 (Dsc3). Dsc3 is a component of the DSC E3 ubiquitin ligase complex (a Golgi-specific protein ubiquitination system) that functions in protein homeostasis under non-stress conditions, playing a role in protein quality control through endosome and Golgi-associated degradation pathway (EGAD) which targets membrane proteins at Golgi and endosomes for degradation by cytosolic proteasomes [, , ]. Dsc3 is also involved in endocytic protein trafficking [].Yeast DSC E3 ubiquitin ligase complex is the homologue of Hrd1 E3 ligase complex from mammals, in which Dsc1, Dsc2 and Dsc3 corresponds to Hrd1, Der1, and Usa1, respectively. Dsc3 is a Herp-like protein that acts as a bridge between Dsc1 and Dsc2 for their interaction [].

•

Protein Domain

IPR025390 | Dsc3_C

Type:

Domain

Description:

This is the C-terminal domain of DSC E3 ubiquitin ligase complex subunit 3 (Dsc3), which contains two transmembrane helices and a characteristic GFDRL sequence motif. Dsc3 is a component of the DSC E3 ubiquitin ligase complex (a Golgi-specific protein ubiquitination system) that functions in protein homeostasis under non-stress conditions, playing a role in protein quality control through endosome and Golgi-associated degradation pathway (EGAD) which targets membrane proteins at Golgi and endosomes for degradation by cytosolic proteasomes [, , ]. Dsc3 is also involved in endocytic protein trafficking [].Yeast DSC E3 ubiquitin ligase complex is the homologue of Hrd1 E3 ligase complex from mammals, in which Dsc1, Dsc2 and Dsc3 corresponds to Hrd1, Der1, and Usa1, respectively. Dsc3 is a Herp-like protein that acts as a bridge between Dsc1 and Dsc2 for their interaction [].

•

Protein Domain

IPR045226 | Dsc3

Type:

Family

Description:

This entry represents DSC E3 ubiquitin ligase complex subunit 3 (Dsc3), a component of the DSC E3 ubiquitin ligase complex (a Golgi-specific protein ubquitination system) that functions in protein homeostasis under non-stress conditions, playing a role in protein quality control through endosome and Golgi-associated degradation pathway (EGAD) which targets membrane proteins at Golgi and endosomes for degradation by cytosolic proteasomes [, , ]. Dsc3 is also involved in endocytic protein trafficking []. Dsc3 has an ubiquitin-like domain and two C-terminal transmembrane regions.Yeast DSC E3 ubiquitin ligase complex is the homologue of Hrd1 E3 ligase complex from mammals, in which Dsc1, Dsc2 and Dsc3 corresponds to Hrd1, Der1, and Usa1, respectively. Dsc3 is a Herp-like protein that acts as a bridge between Dsc1 and Dsc2 for their interaction [].

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Publication

21777356 | -

First Author:	Arlt H
Year:	2011
Journal:	Traffic
Title:	An overexpression screen in Saccharomyces cerevisiae identifies novel genes that affect endocytic protein trafficking.
Volume:	12
Issue:	11
Pages:	1592-603

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Publication

21504829 | -

First Author:	Stewart EV
Year:	2011
Journal:	Mol Cell
Title:	Yeast SREBP cleavage activation requires the Golgi Dsc E3 ligase complex.
Volume:	42
Issue:	2
Pages:	160-71

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Publication

29355480 | -

First Author:	Yang X
Year:	2018
Journal:	Elife
Title:	Sorting of a multi-subunit ubiquitin ligase complex in the endolysosome system.
Volume:	7

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Publication

24280725 | J:208078

First Author:	Omori-Miyake M
Year:	2014
Journal:	J Invest Dermatol
Title:	In vitro assessment of IL-4- or IL-13-mediated changes in the structural components of keratinocytes in mice and humans.
Volume:	134
Issue:	5
Pages:	1342-1350

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Publication

15489334 | -

First Author:	Gerhard DS
Year:	2004
Journal:	Genome Res
Title:	The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume:	14
Issue:	10B
Pages:	2121-7

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