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Search results 1 to 100 out of 450 for Cipc

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Type Details Score
Gene
85457 | CIPC
Type: gene
Organism: human
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Gene
506130 | CIPC
Type: gene
Organism: cattle
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Gene
771996 | CIPC
Type: gene
Organism: chicken
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Gene
704679 | CIPC
Type: gene
Organism: macaque, rhesus
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Gene
100145786 | cipc
Type: gene
Organism: frog, western clawed
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Gene
314330 | Cipc
Type: gene
Organism: rat
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Gene
490802 | CIPC
Type: gene
Organism: dog, domestic
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Gene
467516 | CIPC
Type: gene
Organism: chimpanzee
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Protein Coding Gene
MGI:1919185 | Cipc
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Domain
IPR031602 | CIPC
Type: Family
Description: Clock-interacting pacemaker or clock-interacting circadian protein (CIPC) is an additional negative-feedback regulator of the circadian clock, through inhibition of CLOCK-BMAL1 activity [, , ]. Studies in knockout mice suggest that it may not be critically required for basic clock function [].
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Publication
17310242 | J:204645
First Author: Zhao WN
Year: 2007
Journal: Nat Cell Biol
Title: CIPC is a mammalian circadian clock protein without invertebrate homologues.
Volume: 9
Issue: 3
Pages: 268-75
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Publication
25862660 | J:244550
First Author: Qu Z
Year: 2015
Journal: Sci China Life Sci
Title: Inactivation of Cipc alters the expression of Per1 but not circadian rhythms in mice.
Volume: 58
Issue: 4
Pages: 368-72
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Publication
19414601 | J:150025
First Author: Yoshitane H
Year: 2009
Journal: Mol Cell Biol
Title: Roles of CLOCK phosphorylation in suppression of E-box-dependent transcription.
Volume: 29
Issue: 13
Pages: 3675-86
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Publication
35705041 | J:328244
First Author: Zheng J
Year: 2022
Journal: Cell Rep
Title: Satellite cell-specific deletion of Cipc alleviates myopathy in mdx mice.
Volume: 39
Issue: 11
Pages: 110939
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Protein
Q8R0W1
Organism: Mus musculus/domesticus
Length: 432  
Fragment?: false
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Protein
A0A087WRF0
Organism: Mus musculus/domesticus
Length: 82  
Fragment?: false
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Protein
A0A087WPE5
Organism: Mus musculus/domesticus
Length: 81  
Fragment?: false
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Protein
A0A087WRZ3
Organism: Mus musculus/domesticus
Length: 79  
Fragment?: true
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Protein
A0A087WNZ2
Organism: Mus musculus/domesticus
Length: 131  
Fragment?: true
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Protein
A0A087WQ97
Organism: Mus musculus/domesticus
Length: 60  
Fragment?: false
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Protein
Z4YJJ0
Organism: Mus musculus/domesticus
Length: 411  
Fragment?: false
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Publication
19341811 | -
First Author: Dardente H
Year: 2009
Journal: Comp Biochem Physiol A Mol Integr Physiol
Title: Transcriptional feedback loops in the ovine circadian clock.
Volume: 153
Issue: 4
Pages: 391-8
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Protein Coding Gene
MGP_CAROLIEiJ_G0017981 | -
Type: protein_coding_gene
Organism: Mus caroli
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Protein Coding Gene
MGP_129S1SvImJ_G0019974 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AJ_G0019932 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AKRJ_G0019907 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_BALBcJ_G0019911 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C3HHeJ_G0019717 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI_C57BL6J_1919185 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C57BL6NJ_G0020363 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CASTEiJ_G0019267 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CBAJ_G0019689 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_DBA2J_G0019802 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_FVBNJ_G0019789 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_LPJ_G0019876 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NODShiLtJ_G0019828 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NZOHlLtJ_G0020395 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PWKPhJ_G0019031 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_WSBEiJ_G0019320 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PahariEiJ_G0029740 | -
Type: protein_coding_gene
Organism: Mus pahari
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Protein Coding Gene
MGP_SPRETEiJ_G0018826 | -
Type: protein_coding_gene
Organism: Mus spretus
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Publication
12693553 | J:83413
First Author: Okazaki N
Year: 2003
Journal: DNA Res
Title: Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries.
Volume: 10
Issue: 1
Pages: 35-48
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Publication
- | J:265051
     
First Author: MGI and IMPC
Year: 2018
Journal: Database Release
Title: MGI Load of Endonuclease-Mediated Alleles (CRISPR) from the International Mouse Phenotyping Consortium (IMPC)
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Publication
12520002 | J:91812
First Author: Stryke D
Year: 2003
Journal: Nucleic Acids Res
Title: BayGenomics: a resource of insertional mutations in mouse embryonic stem cells.
Volume: 31
Issue: 1
Pages: 278-81
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Publication
- | J:326541
       
First Author: Cyagen Biosciences Inc.
Year: 2022
Title: Cyagen Biosciences Website.
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Publication
18799693 | J:142754
First Author: Hansen GM
Year: 2008
Journal: Genome Res
Title: Large-scale gene trapping in C57BL/6N mouse embryonic stem cells.
Volume: 18
Issue: 10
Pages: 1670-9
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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: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
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
- | J:23000
       
First Author: MGD Nomenclature Committee
Year: 1995
Title: Nomenclature Committee Use
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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
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:60000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2000
Title: Gene Ontology Annotation by electronic association of SwissProt Keywords with GO terms
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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: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: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: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: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: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: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:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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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
11080456 | -
First Author: Mosbah A
Year: 2000
Journal: J Mol Biol
Title: Solution structure of the module X2 1 of unknown function of the cellulosomal scaffolding protein CipC of Clostridium cellulolyticum.
Volume: 304
Issue: 2
Pages: 201-17
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Publication
8918451 | -
First Author: Tormo J
Year: 1996
Journal: EMBO J
Title: Crystal structure of a bacterial family-III cellulose-binding domain: a general mechanism for attachment to cellulose.
Volume: 15
Issue: 21
Pages: 5739-51
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Publication
1490597 | -
First Author: Poole DM
Year: 1992
Journal: FEMS Microbiol Lett
Title: Identification of the cellulose-binding domain of the cellulosome subunit S1 from Clostridium thermocellum YS.
Volume: 78
Issue: 2-3
Pages: 181-6
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Publication
11092922 | -
First Author: Shimon LJ
Year: 2000
Journal: Acta Crystallogr D Biol Crystallogr
Title: Structure of a family IIIa scaffoldin CBD from the cellulosome of Clostridium cellulolyticum at 2.2 A resolution.
Volume: 56
Issue: Pt 12
Pages: 1560-8
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Publication
9537366 | -
First Author: Irwin D
Year: 1998
Journal: J Bacteriol
Title: Roles of the catalytic domain and two cellulose binding domains of Thermomonospora fusca E4 in cellulose hydrolysis.
Volume: 180
Issue: 7
Pages: 1709-14
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Publication
9055408 | -
First Author: Gal L
Year: 1997
Journal: Appl Environ Microbiol
Title: Characterization of the cellulolytic complex (cellulosome) produced by Clostridium cellulolyticum.
Volume: 63
Issue: 3
Pages: 903-9
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Protein Domain
IPR036966 | CBM3_sf
Type: Homologous_superfamily
Description: Carbohydrate-binding modules (CBM) have been classified into more than 40families according to sequence homology. Several cellulolytic enzymesshare a conserved region of about 150 amino acid residues, the CBM3 domain[]. It has been classified in three different subtypes, termed family IIIa, IIIb and IIIc. The family IIIa (scaffoldin) and IIIb (mainly free enzymes) are closely similar in their primary structures and both types bind strongly to crystalline cellulose [, ]. Members of the family IIIc, fail to bind crystalline cellulose, but serve in a 'helper' capacity by feeding a single incoming cellulose chain into the active site of the neighbouring catalytic module pending hydrolysis [, ].The CBM3 domain is mainly found C-terminal to the catalytic domain, whichcorrespond to a wide range of bacterial glycosyl hydrolases like family 9, family 5 and family 10.The crystal structure of CBM3 has been solved []. Itconsists of nine β-strands which form a compact domain that has an overallprismatic shape. It is arranged in two antiparallel β-sheets that stackface-to-face to form a beta sandwich with jelly roll topology. Two definedsurfaces, located on opposite sides of the molecule, contain conserved polarand aromatic residues which are probably involved in the binding of the CBM tocellulose [, ]. The first one forms a planar strip whereas the second one forms a shallow groove.Some proteins known to contain a CBM3 domain are listed below:Clostridial cellulosomal scaffolding proteins cipA, cipC and cbpA. Theypromote the binding of cellulose to the catalytic domains of thecellulolytic enzymes.Bacterial cellulases A, B, F, G, I, N, Y, Z (Endo-1,4-beta-glucanase, ).This entry represents the CBM3 domain, which is also known as cellulose-binding domain family III (CBD III).
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Protein Domain
IPR001956 | CBM3
Type: Domain
Description: Carbohydrate-binding modules (CBM) have been classified into more than 40families according to sequence homology. Several cellulolytic enzymesshare a conserved region of about 150 amino acid residues, the CBM3 domain[]. It has been classified in three different subtypes, termed family IIIa, IIIb and IIIc. The family IIIa (scaffoldin) and IIIb (mainly free enzymes) are closely similar in their primary structures and both types bind strongly to crystalline cellulose [, ]. Members of the family IIIc, fail to bind crystalline cellulose, but serve in a 'helper' capacity by feeding a single incoming cellulose chain into the active site of the neighbouring catalytic module pending hydrolysis [, ].The CBM3 domain is mainly found C-terminal to the catalytic domain, whichcorrespond to a wide range of bacterial glycosyl hydrolases like family 9, family 5 and family 10.The crystal structure of CBM3 has been solved []. Itconsists of nine β-strands which form a compact domain that has an overallprismatic shape. It is arranged in two antiparallel β-sheets that stackface-to-face to form a beta sandwich with jelly roll topology. Two definedsurfaces, located on opposite sides of the molecule, contain conserved polarand aromatic residues which are probably involved in the binding of the CBM tocellulose [, ]. The first one forms a planar strip whereas the second one forms a shallow groove.Some proteins known to contain a CBM3 domain are listed below:Clostridial cellulosomal scaffolding proteins cipA, cipC and cbpA. Theypromote the binding of cellulose to the catalytic domains of thecellulolytic enzymes.Bacterial cellulases A, B, F, G, I, N, Y, Z (Endo-1,4-beta-glucanase, ).This entry represents the CBM3 domain, which is also known as cellulose-binding domain family III (CBD III).
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Publication
12651950 | -
First Author: Arnesano F
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: A redox switch in CopC: an intriguing copper trafficking protein that binds copper(I) and copper(II) at different sites.
Volume: 100
Issue: 7
Pages: 3814-9
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Publication
15380510 | -
First Author: Aggarwal BB
Year: 2004
Journal: Cancer Cell
Title: Nuclear factor-kappaB: the enemy within.
Volume: 6
Issue: 3
Pages: 203-8
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Publication
14671122 | -
First Author: Misaghi S
Year: 2004
Journal: J Virol
Title: Structural and functional analysis of human cytomegalovirus US3 protein.
Volume: 78
Issue: 1
Pages: 413-23
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Publication
15513926 | -
First Author: Dransart E
Year: 2005
Journal: J Biol Chem
Title: Uncoupling of inhibitory and shuttling functions of rho GDP dissociation inhibitors.
Volume: 280
Issue: 6
Pages: 4674-83
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Publication
15290350 | -
First Author: Pepe I
Year: 2004
Journal: Amino Acids
Title: Biochemical mechanisms for a possible involvement of the transglutaminase activity in the pathogenesis of the polyglutamine diseases: minireview article.
Volume: 26
Issue: 4
Pages: 431-4
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Publication
15102497 | -
First Author: Gurevich VV
Year: 2004
Journal: Trends Pharmacol Sci
Title: The molecular acrobatics of arrestin activation.
Volume: 25
Issue: 2
Pages: 105-11
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Publication
14756796 | -
First Author: Maamar H
Year: 2004
Journal: Mol Microbiol
Title: Cellulolysis is severely affected in Clostridium cellulolyticum strain cipCMut1.
Volume: 51
Issue: 2
Pages: 589-98
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Protein Domain
IPR014756 | Ig_E-set
Type: Homologous_superfamily
Description: The immunoglobulin (Ig) like fold, which consists of a β-sandwich of seven or more strands in two sheets with a greek-key topology, is one of the most common protein modules found in animals. Many different unrelated proteins share an Ig-like fold, which is often involved in interactions, commonly with other Ig-like domains via their β-sheets []. Of these, the "early"set (E set) domains are possibly related to the immunoglobulin () and/or fibronectin type III () Ig-like protein superfamilies. Ig-like E set domains include:C-terminal domain of certain transcription factors, such as the pro-inflammatory transcription factor NF-kappaB, and the T-cell transcription factors NFAT1 and NFAT5 [].Ig-like domains of sugar-utilising enzymes, such as galactose oxidase (C-terminal domain), sialidase (linker domain), and maltogenic amylase (N-terminal domain).C-terminal domain of arthropod haemocyanin, where many loops are inserted into the fold. These proteins act as dioxygen-transporting proteins.C-terminal domain of class II viral fusion proteins. These envelope glycoproteins are responsible for membrane fusion with target cells during viral invasion.Cytomegaloviral US (unique short) proteins. These type I membrane proteins help suppress the host immune response by modulating surface expression of MHC class I molecules [].Molybdenium-containing oxidoreductase-like dimerisation domain found in enzymes such as sulphite reductase.ML domains found in cholesterol-binding epididymal secretory protein E1, and in a major house-dust mite allergen; ML domains are implicated in lipid recognition, particularly the recognition of pathogen-related products.Rho-GDI-like signalling proteins, which regulate the activity of small G proteins [].Cytoplasmic domain of inward rectifier potassium channels such as Girk1 and Kirbac1.1. These channels act as regulators of excitability in eukaryotic cells.N-terminal domain of transglutaminases, including coagulation factor XIII; many loops are inserted into the fold in these proteins. These proteins act to catalyse the cross-linking of various protein substrates [].Filamin repeat rod domain found in proteins such as the F-actin cross-linking gelation factor ABP-120. These proteins interact with a variety of cellular proteins, acting as signalling scaffolds [].Arrestin family of proteins, which contain a tandem repeat of two elaborated Ig-like domains contacting each other head-to-head. These proteins are key to the redirection of GPCR signals to alternative pathways [].C-terminal domain of arginine-specific cysteine proteases, such as Gingipain-R, which act as major virulence factors of Porphyromonas gingivalis (Bacteroides gingivalis).Copper-resistance proteins, such as CopC, which act as copper-trafficking proteins [].Cellulosomal scaffoldin proteins, such as CipC module x2.1. These proteins act as scaffolding proteins of cellulosomes, which contain cellulose-degrading enzymes [].Quinohaemoprotein amine dehydrogenases (A chain), which contain a tandem repeat of two Ig-like domains. These proteins function in electron transfer reactions.Internalin Ig-like domains, which are truncated and fused to a leucine-rich repeat domain. These proteins are required for host cell invasion of Listeria species.
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Protein
O88188
Organism: Mus musculus/domesticus
Length: 162  
Fragment?: false
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Protein
Q9JHF9
Organism: Mus musculus/domesticus
Length: 160  
Fragment?: false
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Protein
Q8C4B4
Organism: Mus musculus/domesticus
Length: 251  
Fragment?: false
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Protein
O35075
Organism: Mus musculus/domesticus
Length: 297  
Fragment?: false
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Protein
M0QWG6
Organism: Mus musculus/domesticus
Length: 124  
Fragment?: false
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Protein
A0A087WQZ9
Organism: Mus musculus/domesticus
Length: 142  
Fragment?: false
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Protein
M0QWR1
Organism: Mus musculus/domesticus
Length: 70  
Fragment?: false
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Protein
F7BA91
Organism: Mus musculus/domesticus
Length: 140  
Fragment?: true
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Protein
Q64HC9
Organism: Mus musculus/domesticus
Length: 142  
Fragment?: false
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Protein
Q14AM4
Organism: Mus musculus/domesticus
Length: 160  
Fragment?: false
•
•
•
•
•
Protein
Q921U5
Organism: Mus musculus/domesticus
Length: 217  
Fragment?: true
•
•
•
•
•
Protein
Q3TBA1
Organism: Mus musculus/domesticus
Length: 152  
Fragment?: true
•
•
•
•
•




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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