Type |
Details |
Score |
Allele |
Name: |
CWC27 spliceosome-associated protein; gene trap OST59365, Lexicon Genetics |
Allele Type: |
Gene trapped |
|
|
•
•
•
•
•
|
Allele |
Name: |
CWC27 spliceosome-associated protein; gene trap AX0074, Wellcome Trust Sanger Institute |
Allele Type: |
Gene trapped |
|
|
•
•
•
•
•
|
Allele |
Name: |
CWC27 spliceosome-associated protein; gene trap BC0101, Wellcome Trust Sanger Institute |
Allele Type: |
Gene trapped |
|
|
•
•
•
•
•
|
Allele |
Name: |
CWC27 spliceosome-associated protein; gene trap A071B05, German Gene Trap Consortium |
Allele Type: |
Gene trapped |
|
|
•
•
•
•
•
|
Allele |
Name: |
CWC27 spliceosome-associated protein; gene trap DD0035, Wellcome Trust Sanger Institute |
Allele Type: |
Gene trapped |
|
|
•
•
•
•
•
|
Allele |
Name: |
CWC27 spliceosome-associated protein; gene trap W014D08, German Gene Trap Consortium |
Allele Type: |
Gene trapped |
|
|
•
•
•
•
•
|
Allele |
Name: |
CWC27 spliceosome-associated protein; gene trap OST30008, Lexicon Genetics |
Allele Type: |
Gene trapped |
|
|
•
•
•
•
•
|
Allele |
Name: |
CWC27 spliceosome-associated protein; gene trap W061B05, German Gene Trap Consortium |
Allele Type: |
Gene trapped |
|
|
•
•
•
•
•
|
Allele |
Name: |
CWC27 spliceosome-associated protein; gene trap A060C03, German Gene Trap Consortium |
Allele Type: |
Gene trapped |
|
|
•
•
•
•
•
|
Allele |
Name: |
CWC27 spliceosome-associated protein; gene trap A060D03, German Gene Trap Consortium |
Allele Type: |
Gene trapped |
|
|
•
•
•
•
•
|
Allele |
Name: |
CWC27 spliceosome-associated protein; targeted mutation 1a, Wellcome Trust Sanger Institute |
Allele Type: |
Targeted |
Attribute String: |
Conditional ready, Null/knockout, Reporter |
|
•
•
•
•
•
|
Allele |
Name: |
CWC27 spliceosome-associated protein; targeted mutation 1e, Wellcome Trust Sanger Institute |
Allele Type: |
Targeted |
Attribute String: |
Null/knockout, Reporter |
|
•
•
•
•
•
|
Allele |
Name: |
CWC27 spliceosome-associated protein; targeted mutation 1, Mammalian Functional Genomics Centre |
Allele Type: |
Targeted |
Attribute String: |
Null/knockout, Reporter |
|
•
•
•
•
•
|
Allele |
Name: |
CWC27 spliceosome-associated protein; targeted mutation 1, Lexicon Pharmaceuticals |
Allele Type: |
Targeted |
Attribute String: |
Null/knockout |
|
•
•
•
•
•
|
Allele |
Name: |
CWC27 spliceosome-associated protein; targeted mutation 2e, Wellcome Trust Sanger Institute |
Allele Type: |
Targeted |
Attribute String: |
Null/knockout, Reporter |
|
•
•
•
•
•
|
Allele |
Name: |
CWC27 spliceosome-associated protein; targeted mutation 2a, Wellcome Trust Sanger Institute |
Allele Type: |
Targeted |
Attribute String: |
Conditional ready, Null/knockout, Reporter |
|
•
•
•
•
•
|
Allele |
Name: |
CWC27 spliceosome-associated protein; targeted mutation 1b, Wellcome Trust Sanger Institute |
Allele Type: |
Targeted |
Attribute String: |
Null/knockout, Reporter |
|
•
•
•
•
•
|
Allele |
Name: |
CWC27 spliceosome-associated protein; endonuclease-mediated mutation 14, GemPharmatech Co., Ltd |
Allele Type: |
Endonuclease-mediated |
Attribute String: |
Null/knockout |
|
•
•
•
•
•
|
Allele |
Name: |
CWC27 spliceosome-associated protein; endonuclease-mediated mutation 1, GemPharmatech Co., Ltd |
Allele Type: |
Endonuclease-mediated |
Attribute String: |
Conditional ready, No functional change |
|
•
•
•
•
•
|
Strain |
Attribute String: |
mutant strain, targeted mutation |
|
•
•
•
•
•
|
Strain |
Attribute String: |
mutant stock, targeted mutation |
|
•
•
•
•
•
|
Allele |
Name: |
CWC27 spliceosome-associated protein; gene trap IST10030G6, Texas A&M Institute for Genomic Medicine |
Allele Type: |
Gene trapped |
|
|
•
•
•
•
•
|
Allele |
Name: |
CWC27 spliceosome-associated protein; gene trap IST14265E10, Texas A&M Institute for Genomic Medicine |
Allele Type: |
Gene trapped |
|
|
•
•
•
•
•
|
Strain |
Attribute String: |
mutant strain, targeted mutation |
|
•
•
•
•
•
|
Strain |
Attribute String: |
coisogenic, mutant strain, endonuclease-mediated mutation |
|
•
•
•
•
•
|
Strain |
Attribute String: |
coisogenic, mutant strain, endonuclease-mediated mutation |
|
•
•
•
•
•
|
Genotype |
Symbol: |
Cwc27/Cwc27 |
Background: |
B6;129S5-Cwc27/Mmucd |
Zygosity: |
hm |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
Genotype |
Symbol: |
Cwc27/Cwc27 |
Background: |
B6N(Cg)-Cwc27/J |
Zygosity: |
hm |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
Strain |
Attribute String: |
mutant strain, coisogenic, targeted mutation |
|
•
•
•
•
•
|
Strain |
Attribute String: |
mutant strain, coisogenic, targeted mutation |
|
•
•
•
•
•
|
Genotype |
Symbol: |
Cwc27/Cwc27<+> |
Background: |
B6N(Cg)-Cwc27/J |
Zygosity: |
ht |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Mikol V |
Year: |
1993 |
Journal: |
J Mol Biol |
Title: |
X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal complex at 2.1 A resolution. |
Volume: |
234 |
Issue: |
4 |
Pages: |
1119-30 |
|
•
•
•
•
•
|
Publication |
First Author: |
Zhao Y |
Year: |
1996 |
Journal: |
Biochemistry |
Title: |
Crystal structure implies that cyclophilin predominantly catalyzes the trans to cis isomerization. |
Volume: |
35 |
Issue: |
23 |
Pages: |
7356-61 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Cyclophilins exhibit peptidyl-prolyl cis-trans isomerase (PPIase) activity (), accelerating protein folding by catalysing the cis-trans isomerisation of proline imidic peptide bonds in oligopeptides [, ]. They also have protein chaperone-like functions []and are the major high-affinity binding proteins for the immunosuppressive drug cyclosporin A (CSA) in vertebrates [].Cyclophilins are found in all prokaryotes and eukaryotes, and have been structurally conserved throughout evolution, implying their importance in cellular function []. They share a common 109 amino acid cyclophilin-like domain (CLD) and additional domains unique to each member of the family. The CLD domain contains the PPIase activity, while the unique domains are important for selection of protein substrates and subcellular compartmentalisation [].This entry includes eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the immunosuppressive drug cyclosporin (CsA). Immunosuppression in vertebrates is believed to be the result of the cyclophilin A-cyclosporin protein drug complex binding to and inhibiting the protein-phosphatase calcineurin [, ]. This entry also includes proteins that do not have the peptidyl-prolyl cis-trans isomerase activity, such as CWC27 from humans []. |
|
•
•
•
•
•
|
Publication |
First Author: |
Davis TL |
Year: |
2010 |
Journal: |
PLoS Biol |
Title: |
Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases. |
Volume: |
8 |
Issue: |
7 |
Pages: |
e1000439 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
147
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
166
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
161
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
166
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
91
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
90
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
166
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
83
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
646
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
196
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
207
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
188
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Stamnes MA |
Year: |
1992 |
Journal: |
Trends Cell Biol |
Title: |
Cyclophilins: a new family of proteins involved in intracellular folding. |
Volume: |
2 |
Issue: |
9 |
Pages: |
272-6 |
|
•
•
•
•
•
|
Publication |
First Author: |
Wang P |
Year: |
2005 |
Journal: |
Genome Biol |
Title: |
The cyclophilins. |
Volume: |
6 |
Issue: |
7 |
Pages: |
226 |
|
•
•
•
•
•
|
Publication |
First Author: |
Lee J |
Year: |
2010 |
Journal: |
J Int Med Res |
Title: |
An overview of cyclophilins in human cancers. |
Volume: |
38 |
Issue: |
5 |
Pages: |
1561-74 |
|
•
•
•
•
•
|
Publication |
First Author: |
Nagy PD |
Year: |
2011 |
Journal: |
Virology |
Title: |
Emerging picture of host chaperone and cyclophilin roles in RNA virus replication. |
Volume: |
411 |
Issue: |
2 |
Pages: |
374-82 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
521
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
531
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Fischer G |
Year: |
1990 |
Journal: |
Biochemistry |
Title: |
The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cell. |
Volume: |
29 |
Issue: |
9 |
Pages: |
2205-12 |
|
•
•
•
•
•
|
Publication |
First Author: |
Gerhard DS |
Year: |
2004 |
Journal: |
Genome Res |
Title: |
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |
Volume: |
14 |
Issue: |
10B |
Pages: |
2121-7 |
|
•
•
•
•
•
|
Publication |
First Author: |
Huttlin EL |
Year: |
2010 |
Journal: |
Cell |
Title: |
A tissue-specific atlas of mouse protein phosphorylation and expression. |
Volume: |
143 |
Issue: |
7 |
Pages: |
1174-89 |
|
•
•
•
•
•
|