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Search results 101 to 140 out of 140 for Dph1

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Type Details Score
Publication
- | J:75000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
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Publication
- | J:161428
       
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
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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:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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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: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
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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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.
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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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DO Term
DOID:0070477 | diphthamide deficiency syndrome 1
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Genotype
Genotype
Symbol: Dph1/Dph1
Background: C57BL/6J-Dph1 Dph1
Zygosity: ht
Has Mutant Allele: true
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Protein Domain
IPR035435 | DPH1/DPH2_euk_archaea
Type: Family
Description: This entry includes diphthamide synthesis DPH1 from eukaryotes and archaea and DPH2 from archaea.Archaeal and eukaryotic translation elongation factor 2 (EF-2) contain a unique posttranslationally modified histidine residue called diphthamide, which become the target for ADP-ribosylation by diphtheria toxin []. DPH1 catalyzes the first step of diphthamide biosynthesis and is required for the modification of EF-2 []. The human DPH1 is also known as OVCA1 (for ovarian cancer gene 1), a tumour suppressor gene that plays a crucial role in the regulation of cell proliferation, embryonic development, and tumorigenesis [].
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Publication
31463593 | -
First Author: Dong M
Year: 2019
Journal: J Biol Inorg Chem
Title: The asymmetric function of Dph1-Dph2 heterodimer in diphthamide biosynthesis.
Volume: 24
Issue: 6
Pages: 777-782
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Protein Domain
IPR016435 | DPH1/DPH2
Type: Family
Description: Archaeal and eukaryotic translation elongation factor 2 contain a unique posttranslationally modified histidine residue called diphthamide, the target of the diphtheria toxin. Diphtheria toxin inhibits eukaryotic protein synthesis by ADP-ribosylating diphthamide in EF2 [].Members of this family include 2-(3-amino-3-carboxypropyl)histidine synthase subunit 1/2 (also known as Diphtheria toxin resistance protein 1/2, DPH 1/2), which are involved in the first step of diphthamide synthesis [, ]. Archaeal DPHs are more similar to eukaryotic DPH1 than to DPH2 [].
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Protein Domain
IPR044248 | DPH3/4-like
Type: Family
Description: Diphthamide is a unique post-translationally modified histidine residue found only in translation elongation factor 2 (eEF-2). It is conserved from archaea to humans and serves as the target for diphteria toxin and Pseudomonas exotoxin A. These two toxins catalyse the transfer of ADP-ribose to diphtamide on eEF-2, thus inactivating eEF-2, halting cellular protein synthesis, and causing cell death []. The biosynthesis of diphtamide is dependent on at least five proteins, DPH1 to -5, and a still unidentified amidating enzyme. DPH3 and DPH4 share a conserved region, which encode a putative zinc finger, the DPH-type or CSL-type (after the the final conserved cysteine of the zinc finger and the next two residues) MB domain contains a Cys-X-Cys...Cys-X2-Cys motif which tetrahedrically coordinates both Fe and Zn. The Fe containing DPH-type MBD has an electron transfer activity [, , , , , ].This entry includes DPH3, DPH4 and their homologues.
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Protein
B1ARH1
Organism: Mus musculus/domesticus
Length: 275  
Fragment?: true
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Publication
16648478 | J:109066
First Author: Liu S
Year: 2006
Journal: Mol Cell Biol
Title: Dph3, a small protein required for diphthamide biosynthesis, is essential in mouse development.
Volume: 26
Issue: 10
Pages: 3835-41
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Publication
18765564 | J:139665
First Author: Webb TR
Year: 2008
Journal: J Cell Sci
Title: Diphthamide modification of eEF2 requires a J-domain protein and is essential for normal development.
Volume: 121
Issue: Pt 19
Pages: 3140-5
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Publication
24422557 | J:354406
First Author: Dong M
Year: 2014
Journal: J Am Chem Soc
Title: Dph3 is an electron donor for Dph1-Dph2 in the first step of eukaryotic diphthamide biosynthesis.
Volume: 136
Issue: 5
Pages: 1754-7
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Protein
Q9CR25
Organism: Mus musculus/domesticus
Length: 489  
Fragment?: false
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Publication
14527407 | -
First Author: Liu S
Year: 2003
Journal: Mol Cell
Title: Retroviral insertional mutagenesis identifies a small protein required for synthesis of diphthamide, the target of bacterial ADP-ribosylating toxins.
Volume: 12
Issue: 3
Pages: 603-13
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Publication
11595641 | -
First Author: Collier RJ
Year: 2001
Journal: Toxicon
Title: Understanding the mode of action of diphtheria toxin: a perspective on progress during the 20th century.
Volume: 39
Issue: 11
Pages: 1793-803
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Protein
Q5NCQ5
Organism: Mus musculus/domesticus
Length: 438  
Fragment?: false
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Publication
20559380 | -
First Author: Zhang Y
Year: 2010
Journal: Nature
Title: Diphthamide biosynthesis requires an organic radical generated by an iron-sulphur enzyme.
Volume: 465
Issue: 7300
Pages: 891-6
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Protein Domain
IPR007872 | DPH_MB_dom
Type: Domain
Description: Diphthamide is a unique post-translationallymodified histidine residue found only in translation elongation factor 2 (eEF-2). It is conserved from archaea to humans and serves as the target for diphteria toxin and Pseudomonas exotoxin A. These two toxins catalyse the transfer of ADP-ribose to diphtamide on eEF-2, thus inactivating eEF-2, halting cellular protein synthesis, and causing cell death []. The biosynthesis of diphtamide is dependent on at least five proteins, DPH1 to -5, and a still unidentified amidating enzyme. DPH3 and DPH4 share a conserved region, which encode a putative zinc finger, the DPH-type or CSL-type (after the the final conserved cysteine of the zinc finger and the next two residues) MB domain contains a Cys-X-Cys...Cys-X2-Cys motif which tetrahedrically coordinates both Fe and Zn. The Fe containing DPH-type MBD has an electron transfer activity [, , , , , ].This entry represents the DPH-type metal binding domain consists of a three-stranded β-sandwich with one sheet comprising two parallel strands: (i) β1 and (ii) β6 and one antiparallel strand: β5. The second sheet in the β-sandwich is comprised of strands β2, β3, and β4 running anti-parallel to each other. The two β-sheets are separated by a short stretch α-helix. It can be found in proteins such as DPH3 and DPH4. This domain is also found associated with N-terminal domain of heat shock protein DnaJ domain [, , ].
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Protein Domain
IPR042264 | DPH1/DPH2_2
Type: Homologous_superfamily
Description: Diphthamide is the name given to a unique post-translationally modified histidine residue in archaeal and eukaryotic translation elongation factor 2. Thismodified histidine is target of diphtheria toxin, which inhibits eukaryotic protein synthesis by ADP-ribosylating diphthamide in EF2 [].The diphthamide synthesis DPH1/DPH2 enzymes which catalyse the first step in diphthamide biosynthesis. Archaeal DPHs are more similar to eukaryotic DPH1 than to DPH2 [].Available structural information on PhDph2 reveals that this enzyme is a homodimer and that each monomer comprises three domains which share the same overall fold. The basic domain fold is a four-stranded parallel β-sheet with three flanking α-helices (or two α-helices and one 3(10) helix in the case of domain 2). The two β-sheets in domain 1 and 2 each contain an additional β-strand that is antiparallel to the rest of the β-sheet. Domains 2 and 3 have two additional α-helices. Domain 1 of one monomer and domain 3 of the adjacent monomer form the dimer interface, creating an extended nine-stranded β-sheet. The domain folds and their arrangement resemble the structure of quinolinate synthase but the orientations of the domains with respect to each other are different in the two enzymes. Three conserved cysteine residues (Cys59, Cys163 and Cys287), each coming from a different structural domain, are clustered together in the centre of the PhDph2 monomers. All three cysteine residues are conserved in eukaryotic DPH1s. The first and third cysteine residues are conserved in eukaryotic DPH2s [].This superfamily represents the domain 2 found in diphthamide synthesis DPH1/DPH2 enzymes.
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Protein Domain
IPR042263 | DPH1/DPH2_1
Type: Homologous_superfamily
Description: Diphthamide is the name given to a unique post-translationally modified histidine residue in archaeal and eukaryotic translation elongation factor 2. This modified histidine is target of diphtheria toxin, which inhibits eukaryotic protein synthesis by ADP-ribosylating diphthamide in EF2 [].The diphthamide synthesis DPH1/DPH2 enzymes which catalyse the first step in diphthamide biosynthesis. Archaeal DPHs are more similar to eukaryotic DPH1 than to DPH2 [].Available structural information on PhDph2 reveals that this enzyme is a homodimer and that each monomer comprises three domains which share the same overall fold. The basic domain fold is a four-stranded parallel β-sheet with three flanking α-helices (or two α-helices and one 3(10) helix in the case of domain 2). The two β-sheets in domain 1 and 2 each contain an additional β-strand that is antiparallel to the rest of the β-sheet. Domains 2 and 3 have two additional α-helices. Domain 1 of one monomer and domain 3 of the adjacent monomer form the dimer interface, creating an extended nine-stranded β-sheet. The domain folds and their arrangement resemble the structure of quinolinate synthase but the orientations of the domains with respect to each other are different in the two enzymes. Three conserved cysteine residues (Cys59, Cys163 and Cys287), each coming from a different structural domain, are clustered together in the centre of the PhDph2 monomers. All three cysteine residues are conserved in eukaryotic DPH1s. The first and third cysteine residues are conserved in eukaryotic DPH2s [].This superfamily represents the domain 1 found in diphthamide synthesis DPH1/DPH2 enzymes.
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Protein Domain
IPR042265 | DPH1/DPH2_3
Type: Homologous_superfamily
Description: Diphthamide is the name given to a unique post-translationally modified histidine residue in archaeal and eukaryotic translation elongation factor 2. This modified histidine is target of diphtheria toxin, which inhibits eukaryotic protein synthesis by ADP-ribosylating diphthamide in EF2 [].The diphthamide synthesis DPH1/DPH2 enzymes which catalyse the first step in diphthamide biosynthesis. Archaeal DPHs are more similar to eukaryotic DPH1 than to DPH2 [].Available structural information on PhDph2 reveals that this enzyme is a homodimer and that each monomer comprises three domains which share the same overall fold. The basic domain fold is a four-stranded parallel β-sheet with three flanking α-helices (or two α-helices and one 3(10) helix in the case of domain 2). The two β-sheets in domain 1 and 2 each contain an additional β-strand that is antiparallel to the rest of the β-sheet. Domains 2 and 3 have two additional α-helices. Domain 1 of one monomer and domain 3 of the adjacent monomer form the dimer interface, creating an extended nine-stranded β-sheet. The domain folds and their arrangementresemble the structure of quinolinate synthase but the orientations of the domains with respect to each other are different in the two enzymes. Three conserved cysteine residues (Cys59, Cys163 and Cys287), each coming from a different structural domain, are clustered together in the centre of the PhDph2 monomers. All three cysteine residues are conserved in eukaryotic DPH1s. The first and third cysteine residues are conserved in eukaryotic DPH2s [].This superfamily represents the domain 3 found in diphthamide synthesis DPH1/DPH2 enzymes.
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Publication
18021800 | -
First Author: Proudfoot M
Year: 2008
Journal: J Mol Biol
Title: Biochemical and structural characterization of a novel family of cystathionine beta-synthase domain proteins fused to a Zn ribbon-like domain.
Volume: 375
Issue: 1
Pages: 301-15
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Protein
Q8K0W9
Organism: Mus musculus/domesticus
Length: 82  
Fragment?: false
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Protein
D3YXV3
Organism: Mus musculus/domesticus
Length: 57  
Fragment?: false
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Protein
E9PZC5
Organism: Mus musculus/domesticus
Length: 54  
Fragment?: false
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Publication
15952786 | -
First Author: Sun J
Year: 2005
Journal: Biochemistry
Title: Solution structure of Kti11p from Saccharomyces cerevisiae reveals a novel zinc-binding module.
Volume: 44
Issue: 24
Pages: 8801-9
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Publication
22367199 | -
First Author: Thakur A
Year: 2012
Journal: J Biol Chem
Title: Structure and mechanistic insights into novel iron-mediated moonlighting functions of human J-protein cochaperone, Dph4.
Volume: 287
Issue: 16
Pages: 13194-205
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Publication
25543256 | -
First Author: Glatt S
Year: 2015
Journal: Structure
Title: Structure of the Kti11/Kti13 heterodimer and its double role in modifications of tRNA and eukaryotic elongation factor 2.
Volume: 23
Issue: 1
Pages: 149-160
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Protein
Q91ZF0
Organism: Mus musculus/domesticus
Length: 148  
Fragment?: false
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Protein
F7CGC9
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: true
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