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Search results 101 to 125 out of 125 for Hgh1

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0.019s

Type

Details

Score

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:63103

First Author:	Mouse Genome Database and National Center for Biotechnology Information
Year:	2000
Journal:	Database Release
Title:	Entrez Gene Load

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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:85324

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

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UniProt Feature

Begin:	1
Description:	Protein HGH1 homolog
Type:	chain
End:	393

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Protein Domain

IPR007206 | Protein_HGH1_C

Type:	Domain
Description:	This entry represents a domain within Protein HGH1, of unknown function. It is found C-terminal to another domain of unknown function ().

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Protein Domain

IPR007205 | Protein_HGH1_N

Type:	Domain
Description:	This entry represents a domain within Protein HGH1, of unknown function. It is found N-terminal to another domain of unknown function ().

•

Allele

Hgh1<+> | MGI:2441396

Name:	HGH1 homolog; wild type

•

Allele

Hgh1<Gt(OST232852)Lex> | MGI:4243198

Name:	HGH1 homolog; gene trap OST232852, Lexicon Genetics
Allele Type:	Gene trapped

•

Allele

Hgh1<tm1(KOMP)Vlcg> | MGI:4452874

Name:	HGH1 homolog; targeted mutation 1, Velocigene
Allele Type:	Targeted
Attribute String:	Null/knockout, Reporter

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Allele

Hgh1<tm1a(EUCOMM)Hmgu> | MGI:5472647

Name:	HGH1 homolog; targeted mutation 1a, Helmholtz Zentrum Muenchen GmbH
Allele Type:	Targeted
Attribute String:	Conditional ready, Null/knockout, Reporter

•

Publication

30876805 | -

First Author:	Schopf FH
Year:	2019
Journal:	Mol Cell
Title:	The Co-chaperone Cns1 and the Recruiter Protein Hgh1 Link Hsp90 to Translation Elongation via Chaperoning Elongation Factor 2.
Volume:	74
Issue:	1
Pages:	73-87.e8

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Allele

Hgh1<Gt(IST13352C5)Tigm> | MGI:5158825

Name:	HGH1 homolog; gene trap IST13352C5, Texas A&M Institute for Genomic Medicine
Allele Type:	Gene trapped

•

Publication

21777655 | J:184111

First Author:	Vakili H
Year:	2011
Journal:	Mol Cell Endocrinol
Title:	Transgenic mice expressing the human growth hormone gene provide a model system to study human growth hormone synthesis and secretion in non-tumor-derived pituitary cells: differential effects of dexamethasone and thyroid hormone.
Volume:	345
Issue:	1-2
Pages:	48-57

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Publication

27151213 | J:235007

First Author:	Vakili H
Year:	2016
Journal:	J Biol Chem
Title:	Evidence for a Circadian Effect on the Reduction of Human Growth Hormone Gene Expression in Response to Excess Caloric Intake.
Volume:	291
Issue:	26
Pages:	13823-33

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Publication

22833680 | J:317754

First Author:	Vakili H
Year:	2012
Journal:	J Biol Chem
Title:	Negative regulation of human growth hormone gene expression by insulin is dependent on hypoxia-inducible factor binding in primary non-tumor pituitary cells.
Volume:	287
Issue:	40
Pages:	33282-92

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Protein

Q05AH4

Organism:	Mus musculus/domesticus
Length:	187
Fragment?:	false

•

Publication

11493638 | -

First Author:	Crevel G
Year:	2001
Journal:	J Cell Sci
Title:	The Drosophila Dpit47 protein is a nuclear Hsp90 co-chaperone that interacts with DNA polymerase alpha.
Volume:	114
Issue:	Pt 11
Pages:	2015-25

•

Publication

18320024 | -

First Author:	Crevel G
Year:	2008
Journal:	PLoS One
Title:	The human TPR protein TTC4 is a putative Hsp90 co-chaperone which interacts with CDC6 and shows alterations in transformed cells.
Volume:	3
Issue:	3
Pages:	e0001737

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Protein Domain

IPR044059 | Csn1/TTC4_wheel

Type:

Domain

Description:

Co-chaperones are helper interacting proteins that modulate the chaperone cycle, being involved in substrate specificity and stimulation of chaperone activity of HSP90/70 and include other heat shock proteins, TPR containing proteins, cyclophilins and others. The TPR containing proteins possess an N-terminal TPR domain, which are more closely related to each other than to TPR domains from other proteins with different functionality [, ], which is involved in HSP90/70 direct interaction. The first N-terminal residues prior to the TRP domain and the C-terminal domain are involved and important for domain interplay and stabilisation of its interactions []. The Hsp90 chaperone machinery in eukaryotes comprises a number of distinct accessory factors, among them TTC4 from human and its homologues Cns1 from yeast and Dpit47 from Drosophila, structurally and functionally conserved from yeast to human. Cns1 is one of the few essential co-chaperones in yeast, important for maintaining translation elongation, specifically chaperoning the elongation factor eEF2. Cns1 interacts with Hgh1 and forms a quaternary complex together with eEF2 and Hsp90 mediating the proper folding and solubility of eEF2. Recently, the C-terminal structure has been solved and is called the "wheel"domain according to its 2D projection. It shows an overall fold consisting of a twisted five-stranded beta sheet surrounded by several alpha helices [].This entry represents the wheel domain found at the C terminus of yeast Cns1, human TTC4 and Drosophila Dpit47 proteins.

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Protein

Q8R3H9

Organism:	Mus musculus/domesticus
Length:	386
Fragment?:	false

•

Protein

Q8C2G3

Organism:	Mus musculus/domesticus
Length:	386
Fragment?:	false

•

Protein

Q3UZC4

Organism:	Mus musculus/domesticus
Length:	386
Fragment?:	false

•

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

•

Publication

21183079 | J:292518

First Author:	Huttlin EL
Year:	2010
Journal:	Cell
Title:	A tissue-specific atlas of mouse protein phosphorylation and expression.
Volume:	143
Issue:	7
Pages:	1174-89

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