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Search results 7901 to 8000 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
Q3TT45
Organism: Mus musculus/domesticus
Length: 259  
Fragment?: false
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Protein
Q62090
Organism: Mus musculus/domesticus
Length: 64  
Fragment?: true
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Protein
Q69ZS5
Organism: Mus musculus/domesticus
Length: 658  
Fragment?: true
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Protein
Q6ZPG8
Organism: Mus musculus/domesticus
Length: 774  
Fragment?: true
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Protein
A0A0R4J073
Organism: Mus musculus/domesticus
Length: 727  
Fragment?: false
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Protein
Q8K4M3
Organism: Mus musculus/domesticus
Length: 61  
Fragment?: true
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Protein
Q8R4U3
Organism: Mus musculus/domesticus
Length: 923  
Fragment?: false
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Protein
A0A0A0MQH4
Organism: Mus musculus/domesticus
Length: 56  
Fragment?: true
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Protein
G5E8N4
Organism: Mus musculus/domesticus
Length: 923  
Fragment?: false
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Protein
Q91Y36
Organism: Mus musculus/domesticus
Length: 963  
Fragment?: false
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Protein
A0A0R4J183
Organism: Mus musculus/domesticus
Length: 446  
Fragment?: false
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Protein
Q2M4H1
Organism: Mus musculus/domesticus
Length: 441  
Fragment?: true
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Protein
H3BLS0
Organism: Mus musculus/domesticus
Length: 1509  
Fragment?: false
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Protein
E0CYJ1
Organism: Mus musculus/domesticus
Length: 141  
Fragment?: false
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Protein
E0CZE7
Organism: Mus musculus/domesticus
Length: 136  
Fragment?: true
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Protein
Q3ULG4
Organism: Mus musculus/domesticus
Length: 379  
Fragment?: false
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Protein
F6QQP6
Organism: Mus musculus/domesticus
Length: 713  
Fragment?: true
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Protein
A2ARJ0
Organism: Mus musculus/domesticus
Length: 207  
Fragment?: true
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Protein
Q3TU06
Organism: Mus musculus/domesticus
Length: 777  
Fragment?: true
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Protein
H3BKF6
Organism: Mus musculus/domesticus
Length: 1389  
Fragment?: true
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Protein
Q5NCM5
Organism: Mus musculus/domesticus
Length: 634  
Fragment?: false
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Protein
Q52KF5
Organism: Mus musculus/domesticus
Length: 712  
Fragment?: true
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Protein
E9PXV1
Organism: Mus musculus/domesticus
Length: 179  
Fragment?: false
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Protein
O89067
Organism: Mus musculus/domesticus
Length: 77  
Fragment?: true
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Protein
Q3U0P9
Organism: Mus musculus/domesticus
Length: 162  
Fragment?: true
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Protein
H3BJY3
Organism: Mus musculus/domesticus
Length: 146  
Fragment?: true
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Protein
H3BJQ9
Organism: Mus musculus/domesticus
Length: 1517  
Fragment?: false
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Protein
Q3ZAT5
Organism: Mus musculus/domesticus
Length: 438  
Fragment?: false
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Protein
F8WHG0
Organism: Mus musculus/domesticus
Length: 178  
Fragment?: false
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Protein
Q3TZ84
Organism: Mus musculus/domesticus
Length: 609  
Fragment?: false
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Protein
Q5NCM7
Organism: Mus musculus/domesticus
Length: 583  
Fragment?: false
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Protein
Q496P6
Organism: Mus musculus/domesticus
Length: 342  
Fragment?: true
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Publication
10802189 | -
First Author: Stubbs S
Year: 2000
Journal: FEMS Microbiol Lett
Title: Production of actin-specific ADP-ribosyltransferase (binary toxin) by strains of Clostridium difficile.
Volume: 186
Issue: 2
Pages: 307-12
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Publication
18485873 | -
First Author: Jin L
Year: 2008
Journal: Cell
Title: Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex.
Volume: 133
Issue: 4
Pages: 653-65
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Publication
31485716 | -
First Author: Rhooms SK
Year: 2020
Journal: Cell Mol Life Sci
Title: Insights from Drosophila on mitochondrial complex I.
Volume: 77
Issue: 4
Pages: 607-618
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Publication
9799632 | -
First Author: Lewis RJ
Year: 1998
Journal: J Mol Biol
Title: An evolutionary link between sporulation and prophage induction in the structure of a repressor:anti-repressor complex.
Volume: 283
Issue: 5
Pages: 907-12
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Publication
10892750 | -
First Author: Bell CE
Year: 2000
Journal: Cell
Title: Crystal structure of the lambda repressor C-terminal domain provides a model for cooperative operator binding.
Volume: 101
Issue: 7
Pages: 801-11
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Publication
12453420 | -
First Author: Chi YI
Year: 2002
Journal: Mol Cell
Title: Diabetes mutations delineate an atypical POU domain in HNF-1alpha.
Volume: 10
Issue: 5
Pages: 1129-37
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Publication
22933801 | J:187689
First Author: tom Dieck S
Year: 2012
Journal: J Neurosci
Title: Deletion of the presynaptic scaffold CAST reduces active zone size in rod photoreceptors and impairs visual processing.
Volume: 32
Issue: 35
Pages: 12192-203
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Publication
24348337 | -
 
First Author: Lazarevic V
Year: 2013
Journal: Front Cell Neurosci
Title: Molecular mechanisms driving homeostatic plasticity of neurotransmitter release.
Volume: 7
Pages: 244
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Protein Domain
IPR022683 | Calpain_III
Type: Domain
Description: 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.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 [].
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Protein
Q762C4
Organism: Mus musculus/domesticus
Length: 421  
Fragment?: false
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Publication
12843408 | -
First Author: Goll DE
Year: 2003
Journal: Physiol Rev
Title: The calpain system.
Volume: 83
Issue: 3
Pages: 731-801
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Protein
Q9D805
Organism: Mus musculus/domesticus
Length: 690  
Fragment?: false
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Protein
Q9ER56
Organism: Mus musculus/domesticus
Length: 720  
Fragment?: false
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Protein
O08529
Organism: Mus musculus/domesticus
Length: 700  
Fragment?: false
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Protein
Q64691
Organism: Mus musculus/domesticus
Length: 821  
Fragment?: false
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Protein
O35350
Organism: Mus musculus/domesticus
Length: 713  
Fragment?: false
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Protein
Q0VGP9
Organism: Mus musculus/domesticus
Length: 709  
Fragment?: false
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Protein
Q3U8S5
Organism: Mus musculus/domesticus
Length: 700  
Fragment?: false
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Protein
A0A668KLF1
Organism: Mus musculus/domesticus
Length: 815  
Fragment?: false
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Protein
Q3TB79
Organism: Mus musculus/domesticus
Length: 699  
Fragment?: true
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Protein
E9QL26
Organism: Mus musculus/domesticus
Length: 720  
Fragment?: false
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Protein
A2AVV6
Organism: Mus musculus/domesticus
Length: 785  
Fragment?: false
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Protein
Q762C5
Organism: Mus musculus/domesticus
Length: 653  
Fragment?: false
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Protein
A2AVV5
Organism: Mus musculus/domesticus
Length: 737  
Fragment?: false
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Protein
O88977
Organism: Mus musculus/domesticus
Length: 709  
Fragment?: false
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Protein
A4QPE6
Organism: Mus musculus/domesticus
Length: 821  
Fragment?: false
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Protein
Q6PDE6
Organism: Mus musculus/domesticus
Length: 690  
Fragment?: false
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Protein
Q80Y25
Organism: Mus musculus/domesticus
Length: 713  
Fragment?: false
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Protein
Q3UDG8
Organism: Mus musculus/domesticus
Length: 713  
Fragment?: false
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Protein
Q3U3A8
Organism: Mus musculus/domesticus
Length: 700  
Fragment?: false
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Protein
Q8C2J1
Organism: Mus musculus/domesticus
Length: 713  
Fragment?: false
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Protein
A2AVV7
Organism: Mus musculus/domesticus
Length: 757  
Fragment?: false
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Protein
Q3TI07
Organism: Mus musculus/domesticus
Length: 713  
Fragment?: false
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Protein
F2Z3X0
Organism: Mus musculus/domesticus
Length: 508  
Fragment?: false
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Protein
F6XQ00
Organism: Mus musculus/domesticus
Length: 711  
Fragment?: false
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Protein
B8JJM6
Organism: Mus musculus/domesticus
Length: 713  
Fragment?: false
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Protein
H3BK95
Organism: Mus musculus/domesticus
Length: 296  
Fragment?: true
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Protein
Q1MX41
Organism: Mus musculus/domesticus
Length: 545  
Fragment?: false
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Protein
Q1MX42
Organism: Mus musculus/domesticus
Length: 585  
Fragment?: false
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Protein
Q1MX40
Organism: Mus musculus/domesticus
Length: 571  
Fragment?: false
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Protein
Q1MX43
Organism: Mus musculus/domesticus
Length: 559  
Fragment?: false
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Publication
21633816 | -
First Author: Capdevila M
Year: 2011
Journal: J Biol Inorg Chem
Title: Metallothionein protein evolution: a miniassay.
Volume: 16
Issue: 7
Pages: 977-89
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Publication
1646017 | -
First Author: Ambler RP
Year: 1991
Journal: Biochim Biophys Acta
Title: Sequence variability in bacterial cytochromes c.
Volume: 1058
Issue: 1
Pages: 42-7
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Protein
Q60902
Organism: Mus musculus/domesticus
Length: 907  
Fragment?: false
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Protein
Q9QYI5
Organism: Mus musculus/domesticus
Length: 324  
Fragment?: false
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Protein
P42567
Organism: Mus musculus/domesticus
Length: 897  
Fragment?: false
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Protein
Q8VI24
Organism: Mus musculus/domesticus
Length: 733  
Fragment?: false
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Protein
Q60611
Organism: Mus musculus/domesticus
Length: 764  
Fragment?: false
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Protein
Q9Z123
Organism: Mus musculus/domesticus
Length: 777  
Fragment?: false
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Protein
Q8BJI4
Organism: Mus musculus/domesticus
Length: 691  
Fragment?: false
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Protein
Q91X58
Organism: Mus musculus/domesticus
Length: 257  
Fragment?: false
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Protein
B2RQZ8
Organism: Mus musculus/domesticus
Length: 692  
Fragment?: false
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Protein
Q3UEK1
Organism: Mus musculus/domesticus
Length: 244  
Fragment?: false
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Protein
Q5U4D4
Organism: Mus musculus/domesticus
Length: 576  
Fragment?: false
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Protein
E2JL35
Organism: Mus musculus/domesticus
Length: 179  
Fragment?: true
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Protein
Q6BCX0
Organism: Mus musculus/domesticus
Length: 227  
Fragment?: true
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Protein
H3BK65
Organism: Mus musculus/domesticus
Length: 933  
Fragment?: false
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Protein
A0A087WPF5
Organism: Mus musculus/domesticus
Length: 255  
Fragment?: true
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Protein
P70260
Organism: Mus musculus/domesticus
Length: 119  
Fragment?: true
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Protein
Q3TYV9
Organism: Mus musculus/domesticus
Length: 329  
Fragment?: true
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Protein
E0CY18
Organism: Mus musculus/domesticus
Length: 218  
Fragment?: true
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Protein
Q6BCV9
Organism: Mus musculus/domesticus
Length: 215  
Fragment?: true
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Protein
F6XBL0
Organism: Mus musculus/domesticus
Length: 199  
Fragment?: true
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Protein
A0A2Z6DUK5
Organism: Mus musculus/domesticus
Length: 70  
Fragment?: false
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Protein
Q6BCW1
Organism: Mus musculus/domesticus
Length: 179  
Fragment?: true
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Protein
E9PVB7
Organism: Mus musculus/domesticus
Length: 795  
Fragment?: false
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Protein
Q6BCW5
Organism: Mus musculus/domesticus
Length: 204  
Fragment?: true
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Protein
Q6X2S0
Organism: Mus musculus/domesticus
Length: 578  
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