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Search results 101 to 167 out of 167 for Clpp

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Type Details Score
Publication
- | J:211773
     
First Author: Mouse Genome Informatics and the International Mouse Phenotyping Consortium (IMPC)
Year: 2014
Journal: Database Release
Title: Obtaining and Loading Phenotype Annotations from the International Mouse Phenotyping Consortium (IMPC) Database
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Publication
- | J:342605
       
First Author: GOA curators
Year: 2016
Title: Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
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Publication
- | J:155856
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Title: Rat to Mouse ISO GO annotation transfer
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Publication
16141072 | J:99680
First Author: Carninci P
Year: 2005
Journal: Science
Title: The transcriptional landscape of the mammalian genome.
Volume: 309
Issue: 5740
Pages: 1559-63
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Publication
11217851 | J:65060
First Author: Kawai J
Year: 2001
Journal: Nature
Title: Functional annotation of a full-length mouse cDNA collection.
Volume: 409
Issue: 6821
Pages: 685-90
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Publication
14610273 | J:86696
First Author: Zambrowicz BP
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: Wnk1 kinase deficiency lowers blood pressure in mice: a gene-trap screen to identify potential targets for therapeutic intervention.
Volume: 100
Issue: 24
Pages: 14109-14
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Publication
- | J:141210
     
First Author: Mouse Genome Informatics (MGI) and National Center for Biotechnology Information (NCBI)
Year: 2008
Journal: Database Download
Title: Mouse Gene Trap Data Load from dbGSS
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Publication
21677750 | J:173534
First Author: Skarnes WC
Year: 2011
Journal: Nature
Title: A conditional knockout resource for the genome-wide study of mouse gene function.
Volume: 474
Issue: 7351
Pages: 337-42
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Publication
- | J:293217
       
First Author: GemPharmatech
Year: 2020
Title: GemPharmatech Website.
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Publication
- | J:342587
       
First Author: AgBase, BHF-UCL, Parkinson's UK-UCL, dictyBase, HGNC, Roslin Institute, FlyBase and UniProtKB curators
Year: 2011
Title: Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
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Publication
- | J:68900
     
First Author: The Jackson Laboratory Mouse Radiation Hybrid Database
Year: 2004
Journal: Database Release
Title: Mouse T31 Radiation Hybrid Data Load
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Publication
12466851 | J:80000
First Author: Okazaki Y
Year: 2002
Journal: Nature
Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume: 420
Issue: 6915
Pages: 563-73
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Publication
- | J:164563
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Title: Human to Mouse ISO GO annotation transfer
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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:157972
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
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Publication
- | J:57747
     
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
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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: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: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: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: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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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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HT Experiment
E-GEOD-40207 | Expression data from mitochondrial protease ClpP knock-out mice
Series Id: GSE40207
Experiment Type: transcription profiling by array
Study Type: WT vs. Mutant
Source: ArrayExpress
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Publication
37033217 | J:345679
 
First Author: Li G
Year: 2023
Journal: Front Endocrinol (Lausanne)
Title: Mitochondrial stress response gene Clpp deficiency impairs oocyte competence and deteriorate cyclophosphamide-induced ovarian damage in young mice.
Volume: 14
Pages: 1122012
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Interaction Experiment
Hu D (2019)
Description: Alpha-synuclein suppresses mitochondrial protease ClpP to trigger mitochondrial oxidative damage and neurotoxicity.
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Publication
33374937 | J:307532
 
First Author: Esencan E
Year: 2020
Journal: Antioxidants (Basel)
Title: Mitochondrial Stress Response Gene Clpp Is Not Required for Granulosa Cell Function.
Volume: 10
Issue: 1
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GO Term
GO:0009368 | endopeptidase Clp complex
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Publication
8393068 | -
First Author: Giffard PM
Year: 1993
Journal: J Gen Microbiol
Title: The ftf gene encoding the cell-bound fructosyltransferase of Streptococcus salivarius ATCC 25975 is preceded by an insertion sequence and followed by FUR1 and clpP homologues.
Volume: 139
Issue: 5
Pages: 913-20
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Protein Domain
IPR041473 | CtsR_C
Type: Domain
Description: This entry corresponds to the C-terminal dimerization domain of CtsR. CtsR of L. monocytogenes negatively regulates the clpC, clpP and clpE genes belonging to the CtsR regulon [].
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Protein Domain
IPR040465 | CtsR_N
Type: Domain
Description: This family consists of several Firmicute transcriptional repressor of class III stress genes (CtsR) proteins. CtsR of L. monocytogenes negatively regulates the clpC, clpP and clpE genes belonging to the CtsR regulon []. This entry is the N-terminal HTH domain.
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Protein Domain
IPR008463 | CtsR
Type: Family
Description: This family consists of several transcriptional repressor of class III stress gene (CtsR) proteins, mainly from Firmicute species. CtsR of Listeria monocytogenes negatively regulates the clpC, clpP and clpE genes belonging to the CtsR regulon [].
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Publication
18421152 | -
First Author: Yokoyama H
Year: 2008
Journal: J Synchrotron Radiat
Title: Novel dimer structure of a membrane-bound protease with a catalytic Ser-Lys dyad and its linkage to stomatin.
Volume: 15
Issue: Pt 3
Pages: 254-7
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Publication
15752073 | -
First Author: Pandit SB
Year: 2004
Journal: In Silico Biol
Title: Identification and analysis of a new family of bacterial serine proteinases.
Volume: 4
Issue: 4
Pages: 563-72
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Protein Domain
IPR002825 | Pept_S49_ser-pept_pro
Type: Family
Description: This family of archaebacterial proteins, formerly known as DUF114, has been found to be a serine dehydrogenase proteinase distantly related to ClpP proteinases that belong to the serine proteinase superfamily. The family belong to MEROPS peptidase family S49; they are mostly unassigned peptidases but include the archaean signal peptide peptidase 1 []. The family has a catalytic triad of Ser, Asp, His residues, which shows an altered residue ordering compared with the ClpP proteinases but similar to that of the carboxypeptidase clan [].
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Publication
10692157 | -
First Author: Nair S
Year: 2000
Journal: Mol Microbiol
Title: CtsR controls class III heat shock gene expression in the human pathogen Listeria monocytogenes.
Volume: 35
Issue: 4
Pages: 800-11
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Publication
2197276 | -
First Author: Maurizi MR
Year: 1990
Journal: J Biol Chem
Title: Clp P represents a unique family of serine proteases.
Volume: 265
Issue: 21
Pages: 12546-52
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Publication
1480111 | -
First Author: Gottesman S
Year: 1992
Journal: Microbiol Rev
Title: Regulation by proteolysis: energy-dependent proteases and their targets.
Volume: 56
Issue: 4
Pages: 592-621
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Protein Domain
IPR023562 | ClpP/TepA
Type: Family
Description: This entry includes peptidases from the MEROPS peptidase family S14, including ClpP endopeptidase and translocation-enhancing protein TepA.ClpP is an ATP-dependent protease that cleaves a number of proteins, such as casein and albumin []. It exists as a heterodimer of ATP-binding regulatory A and catalytic P subunits, both of which are required for effective levels of protease activity in the presence ofATP [], although the P subunit alone does possess some catalytic activity. Proteases highly similar to ClpP have been found to be encoded in the genome of bacteria, metazoa, some viruses and in the chloroplast of plants. A number of the proteins in this family are classified as non-peptidase homologues as they have been found experimentally to be without peptidase activity, or lack amino acid residues that are believed to be essential for catalytic activity. Translocation-enhancing protein TepA displays sequence similarity to ClpP. It is required for efficient translocation of pre-proteins across the membrane [].
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Protein Domain
IPR033135 | ClpP_His_AS
Type: Active_site
Description: The endopeptidase Clp () from Escherichia coli cleaves peptides invarious proteins in a process that requires ATP hydrolysis [, ]. Clp is adimeric protein which consists of a proteolytic subunit (gene clpP) and eitherof two related ATP-binding regulatory subunits (genes clpA and clpX). ClpP isa serine protease which has a chymotrypsin-like activity. Its catalyticactivity seems to be provided by a charge relay system similar to that of thetrypsin family of serine proteases, but which evolved by independentconvergent evolution.Proteases highly similar to ClpP have been found to be encoded in the genomeof the chloroplast of plants and seem to be also present in other eukaryotes.This entry represents a conserved region containing a histidine that is involved in the catalytic triad.
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Protein Domain
IPR041902 | CtsR_N_sf
Type: Homologous_superfamily
Description: This superfamily represents the N-terminal winged HTH domain of CtsR, a dimeric repressor. The members include several Firmicute transcriptional repressor of class III stress genes (CtsR) proteins. CtsR of L. monocytogenes negatively regulates the clpC, clpP and clpE genes belonging to the CtsR regulon [].CtsR consists of an N-terminal domain, a DNA binding domain with a helix-turn-helix motif (HTH) and a C-terminal dimerisation domain organised in a four helix bundle, with an unknown function. CtsR has a role in forming a complex with DNA, binding to promoter regions of heat-shock genes. It is mainly involved in the regulatory network of the bacterial heat-shock response. The phosphorylation sites reside in the winged HTH domain [].
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Protein Domain
IPR013461 | ClpA
Type: Family
Description: Proteins in this entry are related to ClpA () from Escherichia coli. ClpA is an ATP-dependent chaperone and part of the ClpAP protease that participates in regulatory protein degradation and the dissolution and degradation of protein aggregates []. ClpA functions as the regulatory component of the ATP dependent protease complex ClpAP []. ClpA recognises sequences in specific proteins, which it then unfolds in an ATP-dependent manner and transports into the degradation chamber of the associated ClpP protease [, ]. A small adaptor-like protein, ClpS, modulates the activity of ClpA and is an important regulatory factor for this protein []. It protects ClpA from autodegradation and appears to redirect its activity away from soluble proteins and toward aggregated proteins.
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Protein Domain
IPR018215 | ClpP_Ser_AS
Type: Active_site
Description: Clp is an ATP-dependent protease that cleaves a number of proteins, such as casein and albumin []. It exists as a heterodimer of ATP-binding regulatory A and catalytic P subunits, both of which are required for effective levels of protease activity in the presence ofATP [], although the P subunit alone does possess some catalytic activity.Proteases highly similar to ClpP have been found to be encoded in the genomeof bacteria, metazoa, some viruses and in the chloroplast of plants. A number of the proteins in this family are classified as non-peptidase homologues as they have been found experimentally to be without peptidase activity, or lack amino acid residues that are believed to be essential for catalytic activity.This entry represents a conserved region containing a serine that is involved in the catalytic triad.
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Publication
35653190 | J:332383
 
First Author: Kumar R
Year: 2022
Journal: J Clin Invest
Title: A mitochondrial unfolded protein response inhibitor suppresses prostate cancer growth in mice via HSP60.
Volume: 132
Issue: 13
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Publication
15375180 | J:94142
First Author: Ito J
Year: 2004
Journal: J Lipid Res
Title: Apolipoprotein A-I induces translocation of protein kinase C[alpha] to a cytosolic lipid-protein particle in astrocytes.
Volume: 45
Issue: 12
Pages: 2269-76
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Publication
26142927 | J:231201
First Author: Al-Furoukh N
Year: 2015
Journal: Biochim Biophys Acta
Title: ClpX stimulates the mitochondrial unfolded protein response (UPRmt) in mammalian cells.
Volume: 1853
Issue: 10 Pt A
Pages: 2580-91
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Publication
10485712 | -
First Author: Weber-Ban EU
Year: 1999
Journal: Nature
Title: Global unfolding of a substrate protein by the Hsp100 chaperone ClpA.
Volume: 401
Issue: 6748
Pages: 90-3
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Publication
2186030 | -
First Author: Gottesman S
Year: 1990
Journal: J Biol Chem
Title: The ATP-dependent Clp protease of Escherichia coli. Sequence of clpA and identification of a Clp-specific substrate.
Volume: 265
Issue: 14
Pages: 7886-93
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Publication
11287666 | -
First Author: Ishikawa T
Year: 2001
Journal: Proc Natl Acad Sci U S A
Title: Translocation pathway of protein substrates in ClpAP protease.
Volume: 98
Issue: 8
Pages: 4328-33
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Publication
28824920 | -
 
First Author: Duran EC
Year: 2017
Journal: Front Mol Biosci
Title: Comparative Analysis of the Structure and Function of AAA+ Motors ClpA, ClpB, and Hsp104: Common Threads and Disparate Functions.
Volume: 4
Pages: 54
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Publication
11292737 | J:69042
First Author: Yamamoto T
Year: 2001
Journal: Infect Immun
Title: Disruption of the genes for ClpXP protease in Salmonella enterica serovar Typhimurium results in persistent infection in mice, and development of persistence requires endogenous gamma interferon and tumor necrosis factor alpha.
Volume: 69
Issue: 5
Pages: 3164-74
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Protein Domain
IPR036628 | Clp_N_dom_sf
Type: Homologous_superfamily
Description: ClpA is an ATP-dependent chaperone and part of the ClpAP protease that participates in regulatory protein degradation and the dissolution and degradation of protein aggregates []. ClpA recognises sequences in specific proteins, which it then unfolds in an ATP-dependent manner and transports into the degradation chamber of the associated ClpP protein [, ]. A small adaptor-like protein, ClpS, modulates the activity of ClpA and is an important regulatory factor for this protein []. It protects ClpA from autodegradation and appears to redirect its activity away from soluble proteins and toward aggregated proteins.Molecular chaperones recognize unfolded or misfolded proteins by binding to hydrophobic surface patches not normally exposed in the native proteins. Members of the Clp/Hsp100 family of chaperones are present in eubacteria and within organelles of all eukaryotes, promoting disaggregation and disassembly of protein complexes and participating in energy-dependent protein degradation. The ClpA, ClpB, and ClpC subfamilies of the Clp/Hsp100 ATPases contain a conserved N-terminal domain of ~150 amino acids, which in turn consists of two repeats of ~75 residues. Although the Clp repeat (R) domain contains two approximate sequence repeats, it behaves as a single cooperatively folded unit. The Clp R domain is thought to provide a means for regulating the specificity of and to enlarge the substrate pool available to Clp/Hsp100 chaperone or protease complexes. These roles can be assisted through the binding of an adaptor protein. Adaptor proteins bind to the Clp R domain, modulate the target specificity of the Clp/Hsp100 complex to a particular substrate of interest, and may also regulate the activity of the complex [, , , , , ].The Clp R domain is monomeric and partially alpha helical. It is a single folding unit with pseudo 2-fold symmetry. The Clp R domain structure consists of two four-helix bundles connected by a flexible loop [, , ]. This entry represents the Clp repeat (R) domain [].
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Protein Coding Gene
MGI:1346017 | Clpx
Type: protein_coding_gene
Organism: mouse, laboratory
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Publication
19498169 | -
First Author: Fuhrmann J
Year: 2009
Journal: Science
Title: McsB is a protein arginine kinase that phosphorylates and inhibits the heat-shock regulator CtsR.
Volume: 324
Issue: 5932
Pages: 1323-7
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Publication
10455123 | -
First Author: Bolhuis A
Year: 1999
Journal: J Biol Chem
Title: Signal peptide peptidase- and ClpP-like proteins of Bacillus subtilis required for efficient translocation and processing of secretory proteins.
Volume: 274
Issue: 35
Pages: 24585-92
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Publication
12235156 | -
First Author: Guo F
Year: 2002
Journal: J Biol Chem
Title: Crystal structure of the heterodimeric complex of the adaptor, ClpS, with the N-domain of the AAA+ chaperone, ClpA.
Volume: 277
Issue: 48
Pages: 46753-62
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Publication
12205096 | -
First Author: Guo F
Year: 2002
Journal: J Biol Chem
Title: Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease.
Volume: 277
Issue: 48
Pages: 46743-52
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Publication
15037248 | -
First Author: Xia D
Year: 2004
Journal: J Struct Biol
Title: Crystallographic investigation of peptide binding sites in the N-domain of the ClpA chaperone.
Volume: 146
Issue: 1-2
Pages: 166-79
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Publication
19361434 | -
First Author: Kojetin DJ
Year: 2009
Journal: J Mol Biol
Title: Structural and motional contributions of the Bacillus subtilis ClpC N-domain to adaptor protein interactions.
Volume: 387
Issue: 3
Pages: 639-52
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Publication
25921872 | -
First Author: Kim J
Year: 2015
Journal: Plant Cell
Title: Structures, Functions, and Interactions of ClpT1 and ClpT2 in the Clp Protease System of Arabidopsis Chloroplasts.
Volume: 27
Issue: 5
Pages: 1477-96
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Publication
11344323 | -
First Author: Lo JH
Year: 2001
Journal: Protein Sci
Title: Characterization of the N-terminal repeat domain of Escherichia coli ClpA-A class I Clp/HSP100 ATPase.
Volume: 10
Issue: 3
Pages: 551-9
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Publication
28375147 | -
First Author: Wang P
Year: 2017
Journal: Acta Crystallogr D Struct Biol
Title: Crystal structures of Hsp104 N-terminal domains from Saccharomyces cerevisiae and Candida albicans suggest the mechanism for the function of Hsp104 in dissolving prions.
Volume: 73
Issue: Pt 4
Pages: 365-372
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Publication
27317673 | -
First Author: Liang Y
Year: 2016
Journal: Plant Cell
Title: SMAX1-LIKE7 Signals from the Nucleus to Regulate Shoot Development in Arabidopsis via Partially EAR Motif-Independent Mechanisms.
Volume: 28
Issue: 7
Pages: 1581-601
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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