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Search results 8001 to 8100 out of 8285 for C2

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0.022s

Categories

Hits by Pathway

Hits by Category

Hits by Strain

Type Details Score
Protein
Q62089
Organism: Mus musculus/domesticus
Length: 78  
Fragment?: true
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Protein
Q6BCW8
Organism: Mus musculus/domesticus
Length: 177  
Fragment?: true
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Protein
V9GXR5
Organism: Mus musculus/domesticus
Length: 601  
Fragment?: true
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Protein
H3BKH3
Organism: Mus musculus/domesticus
Length: 615  
Fragment?: false
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Protein
Q6BCV7
Organism: Mus musculus/domesticus
Length: 219  
Fragment?: true
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Protein
Q80ZL3
Organism: Mus musculus/domesticus
Length: 897  
Fragment?: false
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Protein
F6TRN1
Organism: Mus musculus/domesticus
Length: 69  
Fragment?: true
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Protein
F6W2Q5
Organism: Mus musculus/domesticus
Length: 764  
Fragment?: false
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Protein
Q62091
Organism: Mus musculus/domesticus
Length: 88  
Fragment?: true
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Protein
Q810B2
Organism: Mus musculus/domesticus
Length: 722  
Fragment?: true
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Protein
F6ZW42
Organism: Mus musculus/domesticus
Length: 637  
Fragment?: true
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Protein
Q546B3
Organism: Mus musculus/domesticus
Length: 733  
Fragment?: false
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Publication
11854009 | -
First Author: Glading A
Year: 2002
Journal: Trends Cell Biol
Title: Cutting to the chase: calpain proteases in cell motility.
Volume: 12
Issue: 1
Pages: 46-54
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Publication
11950589 | -
First Author: Perrin BJ
Year: 2002
Journal: Int J Biochem Cell Biol
Title: Calpain.
Volume: 34
Issue: 7
Pages: 722-5
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Publication
10601010 | -
First Author: Hosfield CM
Year: 1999
Journal: EMBO J
Title: Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation.
Volume: 18
Issue: 24
Pages: 6880-9
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Publication
11893336 | J:75369
First Author: Moldoveanu T
Year: 2002
Journal: Cell
Title: A Ca(2+) switch aligns the active site of calpain.
Volume: 108
Issue: 5
Pages: 649-60
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Publication
20420449 | -
First Author: Seebeck FP
Year: 2010
Journal: J Am Chem Soc
Title: In vitro reconstitution of Mycobacterial ergothioneine biosynthesis.
Volume: 132
Issue: 19
Pages: 6632-3
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Publication
27626371 | -
First Author: Stroud DA
Year: 2016
Journal: Nature
Title: Accessory subunits are integral for assembly and function of human mitochondrial complex I.
Volume: 538
Issue: 7623
Pages: 123-126
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Publication
15140260 | -
 
First Author: Leung DW
Year: 2004
Journal: Mol Cancer
Title: Phospholipase C delta-4 overexpression upregulates ErbB1/2 expression, Erk signaling pathway, and proliferation in MCF-7 cells.
Volume: 3
Pages: 15
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Protein Domain
IPR001300 | Peptidase_C2_calpain_cat
Type: Domain
Description: This group of cysteine peptidases belong to the MEROPS peptidase family C2 (calpain family, clan CA). A type example is calpain, which is an intracellular protease involved in many important cellular functions that are regulated by calcium [, ]. The protein is a complex of 2 polypeptide chains (light and heavy), with eleven known active peptidases in humans and two non-peptidase homologues known as calpamodulin and androglobin []. These include a highly calcium-sensitive (i.e., micro-molar range) form known as mu-calpain, mu-CANP or calpain I; a form sensitive to calcium in the milli-molar range, known as m-calpain, m-CANP or calpain II; and a third form, known as p94, which is found in skeletal muscle only [].All forms have identical light but different heavy chains. Both mu- and m-calpain are heterodimers containing an identical 28kDa subunit and an 80kDa subunit that shares 55-65% sequence homology between the two proteases [, ]. The crystallographic structure of m-calpain reveals six "domains"in the 80kDa subunit [, ]: A 19-amino acid NH2-terminal sequence;Active site domain IIa;Active site domain IIb. Domain 2 showslow levels of sequence similarity to papain; although the catalytic His hasnot been located by biochemical means, it is likely that calpain and papainare related [].Domain III;An 18-amino acid extended sequence linking domain III to domain IV;Domain IV, which resembles the penta EF-hand family of polypeptides, binds calcium and regulates activity []. Ca2+-binding causes a rearrangement of the protein backbone, the net effect of which is that a Trp side chain, which acts as a wedge between catalytic domains IIa and IIb in the apo state, moves away from the active site cleft allowing for the proper formation of the catalytic triad []. Calpain-like mRNAs have been identified in other organisms including bacteria, but the molecules encoded by these mRNAs have not been isolated, so little is known about their properties. How calpain activity is regulated in these organisms cells is still unclear In metazoans, the activity of calpain is controlled by a single proteinase inhibitor, calpastatin (). The calpastatin gene can produce eight or more calpastatin polypeptides ranging from 17 to 85kDa by use of different promoters and alternative splicing events. The physiological significance of these different calpastatins is unclear, although all bind to three different places on the calpain molecule; binding to at least two of the sites is Ca2+ dependent. The calpains ostensibly participate in a variety of cellular processes including remodelling of cytoskeletal/membrane attachments, different signal transduction pathways, and apoptosis. Deregulated calpain activity following loss of Ca2+ homeostasis results in tissue damage in response to events such as myocardial infarcts, stroke, and brain trauma []. Calpains are a family of cytosolic cysteine proteinases (see ). Members of the calpain family are believed to function in various biological processes, including integrin-mediated cell migration, cytoskeletal remodeling, cell differentiation and apoptosis [, ].The calpain family includes numerous members from C. elegans to mammals and with homologues in yeast and bacteria. The best characterised members are the m- and mu-calpains, both proteins are heterodimer composed of a large catalytic subunit and a small regulatory subunit. The large subunit comprises four domains (dI-dIV) while the small subunit has two domains (dV-dVI). Domain dI is a short region cleaved by autolysis, dII is the catalytic core, dIII is a C2-like domain, dIV consists of five calcium binding EF-hand motifs [].The crystal structure of calpain has been solved [, ]. The catalytic region consists of two distinct structural domains (dIIa and dIIb). dIIa contains a central helix flanked on three faces by a cluster of α-helices and is entirely unrelated to the corresponding domain in the typical thiol proteinases. The fold of dIIb is similar to the corresponding domain in other cysteine proteinases and contains two three-stranded anti-parallel β-sheets. The catalytic triad residues (C,H,N) are located in dIIa and dIIb. The activation of the domain is dependent on the binding of two calcium atoms in two non EF-hand calcium binding sites located in the catalytic core, one close to the Cys active site in dIIa and one at the end of dIIb. Calcium-binding induced conformational changes in the catalytic domain which align the active site [][].The profile covers the whole catalytic domain.A cysteine peptidase is a proteolytic enzyme that hydrolyses a peptide bond using the thiol group of a cysteine residue as a nucleophile. Hydrolysis involves usually a catalytic triad consisting of the thiol group of the cysteine, the imidazolium ring of a histidine, and a third residue, usually asparagine or aspartic acid, to orientate and activate the imidazolium ring. In only one family of cysteine peptidases, is the role of the general base assigned to a residue other than a histidine: in peptidases from family C89 (acid ceramidase) an arginine is the general base. Cysteine peptidases can be grouped into fourteen different clans, with members of each clan possessing a tertiary fold unique to the clan. Four clans of cysteine peptidases share structural similarities with serine and threonine peptidases and asparagine lyases. From sequence similarities, cysteine peptidases can be clustered into over 80 different families []. Clans CF, CM, CN, CO, CP and PD contain only one family.Cysteine peptidases are often active at acidic pH and are therefore confined to acidic environments, such as the animal lysosome or plant vacuole. Cysteine peptidases can be endopeptidases, aminopeptidases, carboxypeptidases, dipeptidyl-peptidases or omega-peptidases. They are inhibited by thiol chelators such as iodoacetate, iodoacetic acid, N-ethylmaleimide or p-chloromercuribenzoate.Clan CA includes proteins with a papain-like fold. There is a catalytic triad which occurs in the order: Cys/His/Asn (or Asp). A fourth residue, usually Gln, is important for stabilising the acyl intermediate that forms during catalysis, and this precedes the active site Cys. The fold consists of two subdomains with the active site between them. One subdomain consists of a bundle of helices, with the catalytic Cys at the end of one of them, and the other subdomain is a β-barrel with the active site His and Asn (or Asp). There are over thirty families in the clan, and tertiary structures have been solved for members of most of these. Peptidases in clan CA are usually sensitive to the small molecule inhibitor E64, which is ineffective against peptidases from other clans of cysteine peptidases [].Clan CD includes proteins with a caspase-like fold. Proteins in the clan have an α/β/α sandwich structure. There is a catalytic dyad which occurs in the order His/Cys. The active site His occurs in a His-Gly motif and the active site Cys occurs in an Ala-Cys motif; both motifs are preceded by a block of hydrophobic residues []. Specificity is predominantly directed towards residues that occupy the S1 binding pocket, so that caspases cleave aspartyl bonds, legumains cleave asparaginyl bonds, and gingipains cleave lysyl or arginyl bonds.Clan CE includes proteins with an adenain-like fold. The fold consists of two subdomains with the active site between them. One domain is a bundle of helices, and the other a β-barrell. The subdomains are in the opposite order to those found in peptidases from clan CA, and this is reflected in the order of active site residues: His/Asn/Gln/Cys. This has prompted speculation that proteins in clans CA and CE are related, and that members of one clan are derived from a circular permutation of the structure of the other.Clan CL includes proteins with a sortase B-like fold. Peptidases in the clan hydrolyse and transfer bacterial cell wall peptides. The fold shows a closed β-barrel decorated with helices with the active site at one end of the barrel []. The active site consists of a His/Cys catalytic dyad.Cysteine peptidases with a chymotrypsin-like fold are included in clan PA, which also includes serine peptidases. Cysteine peptidases that are N-terminal nucleophile hydrolases are included in clan PB. Cysteine peptidases with a tertiary structure similar to that of the serine-type aspartyl dipeptidase are included in clan PC. Cysteine peptidases with an intein-like fold are included in clan PD, which also includes asparagine lyases.
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Publication
31260032 | J:277122
First Author: Buenaventura DF
Year: 2019
Journal: Invest Ophthalmol Vis Sci
Title: Identification of Genes With Enriched Expression in Early Developing Mouse Cone Photoreceptors.
Volume: 60
Issue: 8
Pages: 2787-2799
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Protein
Q8CG14
Organism: Mus musculus/domesticus
Length: 688  
Fragment?: false
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Protein
Q14DT6
Organism: Mus musculus/domesticus
Length: 694  
Fragment?: false
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Protein
A0A1W2P7F1
Organism: Mus musculus/domesticus
Length: 694  
Fragment?: false
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Protein
Q3T9K7
Organism: Mus musculus/domesticus
Length: 688  
Fragment?: false
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Protein
E9Q6C2
Organism: Mus musculus/domesticus
Length: 694  
Fragment?: false
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Publication
22560297 | J:184521
First Author: Koss M
Year: 2012
Journal: Dev Cell
Title: Congenital asplenia in mice and humans with mutations in a Pbx/Nkx2-5/p15 module.
Volume: 22
Issue: 5
Pages: 913-26
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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
30186101 | J:266522
 
First Author: Elsen GE
Year: 2018
Journal: Front Neurosci
Title: The Epigenetic Factor Landscape of Developing Neocortex Is Regulated by Transcription Factors Pax6→ Tbr2→ Tbr1.
Volume: 12
Pages: 571
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Publication
9811942 | J:50869
First Author: Ko MS
Year: 1998
Journal: Hum Mol Genet
Title: Genome-wide mapping of unselected transcripts from extraembryonic tissue of 7.5-day mouse embryos reveals enrichment in the t-complex and under-representation on the X chromosome.
Volume: 7
Issue: 12
Pages: 1967-78
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Publication
12466855 | J:80501
First Author: Gitton Y
Year: 2002
Journal: Nature
Title: A gene expression map of human chromosome 21 orthologues in the mouse.
Volume: 420
Issue: 6915
Pages: 586-90
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Publication
12466854 | J:80502
First Author: Reymond A
Year: 2002
Journal: Nature
Title: Human chromosome 21 gene expression atlas in the mouse.
Volume: 420
Issue: 6915
Pages: 582-6
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Publication
22967998 | J:190524
First Author: Shalom-Barak T
Year: 2012
Journal: Dev Biol
Title: Placental PPARγ regulates spatiotemporally diverse genes and a unique metabolic network.
Volume: 372
Issue: 1
Pages: 143-55
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Publication
24146773 | J:209112
First Author: Shimizu H
Year: 2013
Journal: PLoS One
Title: The AERO system: a 3D-like approach for recording gene expression patterns in the whole mouse embryo.
Volume: 8
Issue: 10
Pages: e75754
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Publication
- | J:29126
     
First Author: The Jackson Laboratory DNA Panel Mapping Resource
Year: 1999
Journal: Database Release
Title: JAX Interspecific Backcross BSS and BSB Public Mapping Data
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Publication
14621295 | J:86686
First Author: Okazaki N
Year: 2003
Journal: DNA Res
Title: Prediction of the coding sequences of mouse homologues of KIAA gene: III. the complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries.
Volume: 10
Issue: 4
Pages: 167-80
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Publication
15935055 | J:99424
First Author: Toonen RF
Year: 2005
Journal: J Neurochem
Title: Munc18-1 stabilizes syntaxin 1, but is not essential for syntaxin 1 targeting and SNARE complex formation.
Volume: 93
Issue: 6
Pages: 1393-400
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Publication
- | J:104881
     
First Author: The RIKEN BioResource Center
Year: 2006
Journal: Unpublished
Title: Information obtained from The RIKEN BioResource Center
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Publication
15368895 | J:92575
First Author: Okazaki N
Year: 2004
Journal: DNA Res
Title: Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries.
Volume: 11
Issue: 3
Pages: 205-18
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Publication
- | J:157064
     
First Author: University of California, Davis
Year: 2010
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by the University of California, Davis
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Protein
Q61137
Organism: Mus musculus/domesticus
Length: 1302  
Fragment?: false
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Protein
Q80Z10
Organism: Mus musculus/domesticus
Length: 1352  
Fragment?: false
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Protein
P31362
Organism: Mus musculus/domesticus
Length: 431  
Fragment?: false
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Protein
Q9DAC9
Organism: Mus musculus/domesticus
Length: 329  
Fragment?: false
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Protein
P31361
Organism: Mus musculus/domesticus
Length: 497  
Fragment?: false
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Protein
Q9CVD2
Organism: Mus musculus/domesticus
Length: 355  
Fragment?: false
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Protein
Q63955
Organism: Mus musculus/domesticus
Length: 338  
Fragment?: false
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Protein
Q63934
Organism: Mus musculus/domesticus
Length: 411  
Fragment?: false
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Protein
P22361
Organism: Mus musculus/domesticus
Length: 628  
Fragment?: false
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Protein
P25425
Organism: Mus musculus/domesticus
Length: 770  
Fragment?: false
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Protein
P21952
Organism: Mus musculus/domesticus
Length: 449  
Fragment?: false
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Protein
P62515
Organism: Mus musculus/domesticus
Length: 361  
Fragment?: false
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Protein
Q8BJA3
Organism: Mus musculus/domesticus
Length: 419  
Fragment?: false
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Protein
P27889
Organism: Mus musculus/domesticus
Length: 558  
Fragment?: false
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Protein
P31360
Organism: Mus musculus/domesticus
Length: 445  
Fragment?: false
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Protein
Q00196
Organism: Mus musculus/domesticus
Length: 463  
Fragment?: false
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Protein
O88811
Organism: Mus musculus/domesticus
Length: 523  
Fragment?: false
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Protein
P70297
Organism: Mus musculus/domesticus
Length: 548  
Fragment?: false
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Protein
A0A0A0MQM6
Organism: Mus musculus/domesticus
Length: 580  
Fragment?: true
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Protein
A0A0A0MQE0
Organism: Mus musculus/domesticus
Length: 758  
Fragment?: false
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Protein
H3BK13
Organism: Mus musculus/domesticus
Length: 408  
Fragment?: false
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Protein
Q3U5D1
Organism: Mus musculus/domesticus
Length: 419  
Fragment?: false
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Protein
Q3TQ49
Organism: Mus musculus/domesticus
Length: 548  
Fragment?: false
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Protein
Q3UGN9
Organism: Mus musculus/domesticus
Length: 462  
Fragment?: false
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Protein
Q9DBT6
Organism: Mus musculus/domesticus
Length: 624  
Fragment?: false
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Protein
G3UZG9
Organism: Mus musculus/domesticus
Length: 157  
Fragment?: true
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Protein
A0A0R4J273
Organism: Mus musculus/domesticus
Length: 329  
Fragment?: false
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Protein
H3BKF8
Organism: Mus musculus/domesticus
Length: 445  
Fragment?: true
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Protein
Q66JY7
Organism: Mus musculus/domesticus
Length: 628  
Fragment?: false
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Protein
E9Q6Z8
Organism: Mus musculus/domesticus
Length: 769  
Fragment?: false
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Protein
E2JL33
Organism: Mus musculus/domesticus
Length: 74  
Fragment?: true
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Protein
F8VQL7
Organism: Mus musculus/domesticus
Length: 782  
Fragment?: false
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Protein
Q9QY74
Organism: Mus musculus/domesticus
Length: 891  
Fragment?: false
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Protein
Q2M4H2
Organism: Mus musculus/domesticus
Length: 558  
Fragment?: false
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Protein
Q546X9
Organism: Mus musculus/domesticus
Length: 355  
Fragment?: false
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Protein
F6T5L3
Organism: Mus musculus/domesticus
Length: 287  
Fragment?: true
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Protein
H3BL55
Organism: Mus musculus/domesticus
Length: 416  
Fragment?: false
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Protein
Q810M8
Organism: Mus musculus/domesticus
Length: 319  
Fragment?: true
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Protein
H3BL72
Organism: Mus musculus/domesticus
Length: 247  
Fragment?: false
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Protein
F6X4A2
Organism: Mus musculus/domesticus
Length: 126  
Fragment?: true
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Protein
Q3UMC8
Organism: Mus musculus/domesticus
Length: 553  
Fragment?: false
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Protein
Q7TSC9
Organism: Mus musculus/domesticus
Length: 568  
Fragment?: false
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Protein
Q80ZA2
Organism: Mus musculus/domesticus
Length: 337  
Fragment?: false
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Protein
D3YZ77
Organism: Mus musculus/domesticus
Length: 752  
Fragment?: true
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Protein
E2JL30
Organism: Mus musculus/domesticus
Length: 132  
Fragment?: true
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Protein
Q3TAS0
Organism: Mus musculus/domesticus
Length: 168  
Fragment?: false
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Protein
I1E4X2
Organism: Mus musculus/domesticus
Length: 706  
Fragment?: false
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Protein
H3BKM3
Organism: Mus musculus/domesticus
Length: 420  
Fragment?: false
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Protein
H3BK67
Organism: Mus musculus/domesticus
Length: 405  
Fragment?: false
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Protein
Q920N8
Organism: Mus musculus/domesticus
Length: 464  
Fragment?: false
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Protein
A0A494BAF0
Organism: Mus musculus/domesticus
Length: 256  
Fragment?: false
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Protein
H3BJ31
Organism: Mus musculus/domesticus
Length: 364  
Fragment?: true
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Protein
E9Q717
Organism: Mus musculus/domesticus
Length: 291  
Fragment?: false
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Protein
Q7TSV1
Organism: Mus musculus/domesticus
Length: 806  
Fragment?: true
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Protein
Q3UHD7
Organism: Mus musculus/domesticus
Length: 1294  
Fragment?: false
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Protein
A0A0A6YWE6
Organism: Mus musculus/domesticus
Length: 1172  
Fragment?: false
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Protein
H3BJT4
Organism: Mus musculus/domesticus
Length: 431  
Fragment?: false
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Protein
A0A0R4J1Z4
Organism: Mus musculus/domesticus
Length: 793  
Fragment?: false
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Protein
H3BKB7
Organism: Mus musculus/domesticus
Length: 467  
Fragment?: false
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Protein
Q8BRX1
Organism: Mus musculus/domesticus
Length: 891  
Fragment?: false
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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.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

© 2002 - 2017 Department of Genetics, University of Cambridge, Downing Street,
Cambridge CB2 3EH, United Kingdom