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Search results 101 to 177 out of 177 for Clpx

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Type Details Score
GXD Expression
GXD Expression
   
Assay Type: In situ reporter (knock in)
Annotation Date: 2021-04-16
Strength: Present
Sex: Male
Emaps: EMAPS:1689428
Pattern: Not Specified
Stage: TS28
Assay Id: MGI:6691462
Age: postnatal adult
Image: JAX_1373309
Specimen Label: JAX_1373309
Detected: true
Specimen Num: 53
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GXD Expression
GXD Expression
   
Assay Type: In situ reporter (knock in)
Annotation Date: 2021-04-16
Strength: Present
Sex: Female
Emaps: EMAPS:1796228
Pattern: Not Specified
Stage: TS28
Assay Id: MGI:6691462
Age: postnatal adult
Image: JAX_1373270
Specimen Label: JAX_1373270
Detected: true
Specimen Num: 14
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GXD Expression
GXD Expression
   
Assay Type: In situ reporter (knock in)
Annotation Date: 2021-04-16
Strength: Present
Sex: Male
Emaps: EMAPS:1881228
Pattern: Not Specified
Stage: TS28
Assay Id: MGI:6691462
Age: postnatal adult
Image: JAX_1373279
Specimen Label: JAX_1373279
Detected: true
Specimen Num: 23
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Publication
32376682 | J:290315
 
First Author: Cheong A
Year: 2020
Journal: Development
Title: Nuclear-encoded mitochondrial ribosomal proteins are required to initiate gastrulation.
Volume: 147
Issue: 10
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Publication
12865426 | J:100953
First Author: Da Cruz S
Year: 2003
Journal: J Biol Chem
Title: Proteomic analysis of the mouse liver mitochondrial inner membrane.
Volume: 278
Issue: 42
Pages: 41566-71
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Publication
- | J:279207
     
First Author: Mager J
Year: 2019
Journal: MGI Direct Data Submission
Title: A Catalog of Early Lethal KOMP Phenotypes
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Publication
14651853 | J:86816
First Author: Mootha VK
Year: 2003
Journal: Cell
Title: Integrated analysis of protein composition, tissue diversity, and gene regulation in mouse mitochondria.
Volume: 115
Issue: 5
Pages: 629-40
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Publication
18614015 | J:151002
First Author: Pagliarini DJ
Year: 2008
Journal: Cell
Title: A mitochondrial protein compendium elucidates complex I disease biology.
Volume: 134
Issue: 1
Pages: 112-23
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Publication
10725249 | J:60984
First Author: Ko MS
Year: 2000
Journal: Development
Title: Large-scale cDNA analysis reveals phased gene expression patterns during preimplantation mouse development.
Volume: 127
Issue: 8
Pages: 1737-49
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Publication
- | J:81858
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Title: Data Curation Using Mouse Genome Assembly
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Publication
12904583 | J:85162
First Author: Hansen J
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: A large-scale, gene-driven mutagenesis approach for the functional analysis of the mouse genome.
Volume: 100
Issue: 17
Pages: 9918-22
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Publication
- | J:188991
     
First Author: The Jackson Laboratory
Year: 2012
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by The Jackson Laboratory
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Publication
24194600 | J:228563
First Author: Koscielny G
Year: 2014
Journal: Nucleic Acids Res
Title: The International Mouse Phenotyping Consortium Web Portal, a unified point of access for knockout mice and related phenotyping data.
Volume: 42
Issue: Database issue
Pages: D802-9
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Publication
- | J:136110
     
First Author: Velocigene
Year: 2008
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by Velocigene (Regeneron Pharmaceuticals)
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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:342604
       
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
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Publication
- | J:72247
       
First Author: DDB, FB, MGI, GOA, ZFIN curators
Year: 2001
Title: Gene Ontology annotation through association of InterPro records with GO terms
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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
38355793 | J:345621
First Author: Adams DJ
Year: 2024
Journal: Nature
Title: Genetic determinants of micronucleus formation in vivo.
Volume: 627
Issue: 8002
Pages: 130-136
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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:293217
       
First Author: GemPharmatech
Year: 2020
Title: GemPharmatech Website.
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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
- | J:326541
       
First Author: Cyagen Biosciences Inc.
Year: 2022
Title: Cyagen Biosciences 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: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: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: The Gene Ontology Consortium
Year: 2010
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs
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Publication
21267068 | J:153498
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
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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: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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Publication
11278349 | -
First Author: Banecki B
Year: 2001
Journal: J Biol Chem
Title: Structure-function analysis of the zinc-binding region of the Clpx molecular chaperone.
Volume: 276
Issue: 22
Pages: 18843-8
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Publication
12925799 | -
First Author: Kim DY
Year: 2003
Journal: Acta Crystallogr D Biol Crystallogr
Title: Purification, crystallization and preliminary X-ray studies of ClpX from Helicobacter pylori.
Volume: 59
Issue: Pt 9
Pages: 1642-4
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Publication
12937164 | -
First Author: Wojtyra UA
Year: 2003
Journal: J Biol Chem
Title: The N-terminal zinc binding domain of ClpX is a dimerization domain that modulates the chaperone function.
Volume: 278
Issue: 49
Pages: 48981-90
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Protein Domain
IPR038366 | Znf_CppX_C4_sf
Type: Homologous_superfamily
Description: The ClpX heat shock protein of Escherichia coli is a member of the universally conserved Hsp100 family of proteins, and possesses a putative zinc finger motif of the C4 type []. This presumed zinc binding domain (ZBD) is found at the N terminus of the ClpX protein. ClpX is an ATPase which functions both as a substrate specificity component of the ClpXP protease and as a molecular chaperone. ZBD is a member of the treble clef zinc finger family, a motif known to facilitate protein-ligand, protein-DNA, and protein-protein interactions and forms a constitutive dimer that is essential for the degradation of some, but not all, ClpX substrates [].
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Protein
Q3TNL0
Organism: Mus musculus/domesticus
Length: 192  
Fragment?: false
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Protein
Q8C4Z5
Organism: Mus musculus/domesticus
Length: 143  
Fragment?: true
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Protein
Q8BRZ3
Organism: Mus musculus/domesticus
Length: 170  
Fragment?: true
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Protein Domain
IPR010603 | Znf_CppX_C4
Type: Domain
Description: Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [, , , , ]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few []. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target. The ClpX heat shock protein of Escherichia coli is a member of the universally conserved Hsp100 family of proteins, and possesses a putative zinc finger motif of the C4 type []. This presumed zinc binding domain (ZBD) is found at the N terminus of the ClpX protein. ClpX is an ATPase which functions both as a substrate specificity component of the ClpXP protease and as a molecular chaperone. ZBD is a member of the treble clef zinc finger family, a motif known to facilitate protein-ligand, protein-DNA, and protein-protein interactions and forms a constitutive dimer that is essential for the degradation of some, but not all, ClpX substrates [].
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Protein Domain
IPR004487 | Clp_protease_ATP-bd_su_ClpX
Type: Family
Description: ClpX is a member of the HSP (heat-shock protein) 100 family. Gel filtration and electron microscopy showed that ClpX subunits associate to form a six-membered ring that is stabilised by binding of ATP or nonhydrolysable analogs of ATP []. It functions as an ATP-dependent []molecular chaperone and is the regulatory subunit of the ClpXP protease [].ClpXP is involved in DNA damage repair, stationary-phase gene expression, and ssrA-mediated protein quality control. To date more than 50 proteins include transcription factors, metabolic enzymes, and proteins involved in the starvation and oxidative stress responses have been identified as substrates []. The N-terminal domain of ClpX is a C4-type zinc binding domain (ZBD) involved in substrate recognition. ZBD forms a very stable dimer that is essential for promoting the degradation of some typical ClpXP substrates such as lO and MuA [].
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Publication
14525985 | -
First Author: Donaldson LW
Year: 2003
Journal: J Biol Chem
Title: Solution structure of the dimeric zinc binding domain of the chaperone ClpX.
Volume: 278
Issue: 49
Pages: 48991-6
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Publication
12667450 | -
First Author: Flynn JM
Year: 2003
Journal: Mol Cell
Title: Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals.
Volume: 11
Issue: 3
Pages: 671-83
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Publication
9575205 | -
First Author: Grimaud R
Year: 1998
Journal: J Biol Chem
Title: Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP.
Volume: 273
Issue: 20
Pages: 12476-81
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Publication
12761164 | -
First Author: Nanamiya H
Year: 2003
Journal: J Biochem
Title: Involvement of ClpX protein in the post-transcriptional regulation of a competence specific transcription factor, ComK protein, of Bacillus subtilis.
Volume: 133
Issue: 3
Pages: 295-302
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Protein
Q6P8N8
Organism: Mus musculus/domesticus
Length: 620  
Fragment?: false
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Protein
Q9JHS4
Organism: Mus musculus/domesticus
Length: 634  
Fragment?: false
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Publication
10411757 | -
First Author: Liu J
Year: 1999
Journal: Mol Microbiol
Title: Role of lon and ClpX in the post-translational regulation of a sigma subunit of RNA polymerase required for cellular differentiation in Bacillus subtilis.
Volume: 33
Issue: 2
Pages: 415-28
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GO Term
GO:0009368 | endopeptidase Clp complex
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GO Term
GO:0009376 | HslUV protease complex
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Protein Domain
IPR046425 | ClpX_bact
Type: Family
Description: ClpX is a member of the HSP (heat-shock protein) 100 family. Gel filtration and electron microscopy showed that ClpX subunits associate to form a six-membered ring that is stabilised by binding of ATP or nonhydrolysable analogs of ATP []. It functions as an ATP-dependent []molecular chaperone and is the regulatory subunit of the ClpXP protease [].ClpXP is involved in DNA damage repair, stationary-phase gene expression, and ssrA-mediated protein quality control. To date more than 50 proteins include transcription factors, metabolic enzymes, and proteins involved in the starvation and oxidative stress responses have been identified as substrates []. The N-terminal domain of ClpX is a C4-type zinc binding domain (ZBD) involved in substrate recognition. ZBD forms a very stable dimer that is essential for promoting the degradation of some typical ClpXP substrates such as lO and MuA []. This entry represents ClpX subunit from bacteria.
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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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Protein Domain
IPR004491 | HslU
Type: Family
Description: This family of proteins represent HslU, a bacterial clpX homologue, which is an ATPase and chaperone belonging to the AAA Clp/Hsp100 family and a component of the eubacterial proteasome. ATP-dependent protease complexes are present in all three kingdoms of life, where they rid the cell of misfolded or damaged proteins and control the level of certain regulatory proteins. They include the proteasome in Eukaryotes, Archaea, and Actinomycetales and the HslVU (ClpQY, ClpXP) complex in other eubacteria. Genes homologous to eubacterial HslV, , (ClpQ,) and HslU (ClpY, ClpX) have also been demonstrated in to be present in the genome of trypanosomatid protozoa. They are expressed as precursors, with a propeptidethat is removed to produce the active protease. The protease is probably located in the kinetoplast (mitochondrion). Phylogenetic analysis shows that HslV and HslU from trypanosomatids form a single clad with other eubacterial homologues [].
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Publication
38139332 | J:343763
 
First Author: Key J
Year: 2023
Journal: Int J Mol Sci
Title: Translation Fidelity and Respiration Deficits in CLPP-Deficient Tissues: Mechanistic Insights from Mitochondrial Complexome Profiling.
Volume: 24
Issue: 24
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Protein Coding Gene
MGI:1858213 | Clpp
Type: protein_coding_gene
Organism: mouse, laboratory
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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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Publication
7783616 | -
First Author: van Sinderen D
Year: 1995
Journal: Mol Microbiol
Title: comK encodes the competence transcription factor, the key regulatory protein for competence development in Bacillus subtilis.
Volume: 15
Issue: 3
Pages: 455-62
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Protein Domain
IPR010461 | ComK
Type: Family
Description: Competence is the ability of a cell to take up exogenous DNA from its environment, resulting in transformation. It is widespread among bacteria and is probably an important mechanism for the horizontal transfer of genes. DNA usually becomes available by the death and lysis of other cells. Competent bacteria use components of extracellular filaments called type 4 pili to create pores in their membranes and pull DNA through the pores into the cytoplasm. This process, including the development of competence and the expression of the uptake machinery, is regulated in response to cell-cell signalling and/or nutritional conditions [].This family consists of several bacterial ComK proteins. ComK of Bacillus subtilis is a positive autoregulatory protein occupying a central position in the competence-signal-transduction network. It positively regulates the transcription of late competence genes, which specify morphogenetic and structural proteins necessary for construction of the DNA-binding and uptake apparatus, as well as the transcription of comK itself [, ]. ComK specifically binds to the promoters of the genes that it affects. It has been found that ClpX plays an important role in the regulation of ComK at the post-transcriptional level [].
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Publication
12665246 | -
First Author: Matthews JM
Year: 2002
Journal: IUBMB Life
Title: Zinc fingers--folds for many occasions.
Volume: 54
Issue: 6
Pages: 351-5
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Publication
17210253 | -
First Author: Gamsjaeger R
Year: 2007
Journal: Trends Biochem Sci
Title: Sticky fingers: zinc-fingers as protein-recognition motifs.
Volume: 32
Issue: 2
Pages: 63-70
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Publication
15963892 | -
First Author: Hall TM
Year: 2005
Journal: Curr Opin Struct Biol
Title: Multiple modes of RNA recognition by zinc finger proteins.
Volume: 15
Issue: 3
Pages: 367-73
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Publication
15718139 | -
First Author: Brown RS
Year: 2005
Journal: Curr Opin Struct Biol
Title: Zinc finger proteins: getting a grip on RNA.
Volume: 15
Issue: 1
Pages: 94-8
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Publication
10529348 | -
First Author: Klug A
Year: 1999
Journal: J Mol Biol
Title: Zinc finger peptides for the regulation of gene expression.
Volume: 293
Issue: 2
Pages: 215-8
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Publication
11179890 | -
First Author: Laity JH
Year: 2001
Journal: Curr Opin Struct Biol
Title: Zinc finger proteins: new insights into structural and functional diversity.
Volume: 11
Issue: 1
Pages: 39-46
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Publication
12446803 | -
First Author: Couvreur B
Year: 2002
Journal: Mol Biol Evol
Title: Eubacterial HslV and HslU subunits homologs in primordial eukaryotes.
Volume: 19
Issue: 12
Pages: 2110-7
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Publication
8901420 | -
First Author: Solomon JM
Year: 1996
Journal: Trends Genet
Title: Who's competent and when: regulation of natural genetic competence in bacteria.
Volume: 12
Issue: 4
Pages: 150-5
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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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