Calpain-2 - Revision history

Wu3857 at 21:39, 19 August 2019

2019-08-19T21:39:33Z

Wu3857 at 20:28, 29 July 2019

2019-07-29T20:28:05Z

Wu3857 at 20:23, 28 July 2019

2019-07-28T20:23:47Z

Wu3857: /* Reference */

2019-07-28T20:12:39Z

‎Reference

Wu3857: /* Protein Function */

2019-07-28T20:09:25Z

‎Protein Function

Wu3857: /* Protein Function */

2019-07-28T20:09:18Z

‎Protein Function

Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|CAPN2|[https://www.uniprot.org/uniprot/P17655 P17655]|Homo sapiens|Cys105|[http://pfam.xfam.org/family/PF00648..."

2019-07-28T20:08:52Z

Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|CAPN2|[https://www.uniprot.org/uniprot/P17655 P17655]|Homo sapiens|Cys105|[http://pfam.xfam.org/family/PF00648..."

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{| align="left"
| __TOC__
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{{#invoke:InfoboxforTarget|run|CAPN2|[https://www.uniprot.org/uniprot/P17655 P17655]|Homo sapiens|Cys105|[http://pfam.xfam.org/family/PF00648 Peptidase C2 family]|[[:Category:Calpain-2|Ligand list]]}}
==Summary==

===Protein Function ===
Calpain-2 catalytic subunit is a protein that in humans is encoded by the CAPN2 gene. The calpains, calcium-activated neutral proteases, are nonlysosomal, intracellular cysteine proteases. The mammalian calpains include ubiquitous, stomach-specific, and muscle-specific proteins. The ubiquitous enzymes consist of heterodimers with distinct large, catalytic subunits associated with a common small, regulatory subunit. This gene encodes the large subunit of the ubiquitous enzyme, calpain 2. Multiple heterogeneous transcriptional start sites in the 5' UTR have been reported. (From Wikipedia) 
Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves MYOC at 'Arg-226'. (From Uniprot) 
Calpains are active participants in fundamental mammalian cellular processes such as cell migration and associated-cytoskeletal remodeling, apoptosis and cell cycle progression. Abnormal calpain activation is also linked to Alzheimer's disease (AD). In AD, calpain relays the toxic effect of extracellular amyloid peptides on neurons to intracellular tau aggregation and neuronal cell death. (PMID: 15491615)
 

===Cys Function & Property===
Cys105 is one of the active sites of Cathepsin H, which is very close to His262 and Asn286 in space. These three residues formed a typical catalytic triad motif. 

* Hydrophobic property:
:[[File:490-hydro.png||600px]]
* SASA：
:Cys105: 43.83 A^2

==Protein Sequence==

MAGIAAKLAK DREAAEGLGS HDRAIKYLNQ DYEALRNECL EAGTLFQDPS 
FPAIPSALGF KELGPYSSKT RGIEWKRPTE ICADPQFIIG GATRTDICQG 
ALGD'''C'''WLLAA IASLTLNEEI LARVVPLNQS FQENYAGIFH FQFWQYGEWV 
EVVVDDRLPT KDGELLFVHS AEGSEFWSAL LEKAYAKING CYEALSGGAT 
TEGFEDFTGG IAEWYELKKP PPNLFKIIQK ALQKGSLLGC SIDITSAADS 
EAITFQKLVK GHAYSVTGAE EVESNGSLQK LIRIRNPWGE VEWTGRWNDN 
CPSWNTIDPE ERERLTRRHE DGEFWMSFSD FLRHYSRLEI CNLTPDTLTS 
DTYKKWKLTK MDGNWRRGST AGGCRNYPNT FWMNPQYLIK LEEEDEDEED 
GESGCTFLVG LIQKHRRRQR KMGEDMHTIG FGIYEVPEEL SGQTNIHLSK 
NFFLTNRARE RSDTFINLRE VLNRFKLPPG EYILVPSTFE PNKDGDFCIR 
VFSEKKADYQ AVDDEIEANL EEFDISEDDI DDGFRRLFAQ LAGEDAEISA 
FELQTILRRV LAKRQDIKSD GFSIETCKIM VDMLDSDGSG KLGLKEFYIL 
WTKIQKYQKI YREIDVDRSG TMNSYEMRKA LEEAGFKMPC QLHQVIVARF 
ADDQLIIDFD NFVRCLVRLE TLFKIFKQLD PENTGTIELD LISWLCFSVL 


==Structural Information==
*Known structures with covalent ligands: 
:[https://www.rcsb.org/structure/2NQA 2NQA] 

*Protein structure:
[[File:490.png|center|800px]]

==Related Pathway==
*[https://www.genome.jp/kegg-bin/show_pathway?ko04141 Protein processing in endoplasmic reticulum] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko04210 Apoptosis] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko04217 Necroptosis] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko04218 Cellular senescence] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko04510 Focal adhesion] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko05010 Alzheimer disease] 

==Experimental Evidence==
:Crystallography

==Reference==
# Moldoveanu T, Campbell R L, Cuerrier D, et al. '''Crystal structures of calpain–E64 and–leupeptin inhibitor complexes reveal mobile loops gating the active site[J].''' Journal of molecular biology, 2004, 343(5): 1313-1326. [https://www.ncbi.nlm.nih.gov/pubmed/?term=15491615 15491615] 

[[Category:Targets|Targets]]
[[Category:Peptidase C2 family|Peptidase C2 family]]
[[Category:Protein processing in endoplasmic reticulum|Protein processing in endoplasmic reticulum]]
[[Category:Apoptosis|Apoptosis]]
[[Category:Necroptosis|Necroptosis]]
[[Category:Cellular senescence|Cellular senescence]]
[[Category:Focal adhesion|Focal adhesion]]
[[Category:Alzheimer disease|Alzheimer disease]]

@@ Line 58: / Line 58: @@
 # Moldoveanu T, Campbell R L, Cuerrier D, et al. '''Crystal structures of calpain–E64 and–leupeptin inhibitor complexes reveal mobile loops gating the active site[J].''' Journal of Molecular Biology, 2004, 343(5): 1313-1326. [https://www.ncbi.nlm.nih.gov/pubmed/?term=15491615 15491615]<br/>
-[[Category:Targets|Targets]]
+[[Category:Targets]]
-[[Category:Homo sapiens|Homo sapiens]]
+[[Category:Homo sapiens]]
-[[Category:Protease|Protease]]
+[[Category:Protease]]
-[[Category:Peptidase C2 family|Peptidase C2 family]]
+[[Category:Peptidase C2 family]]
-[[Category:Protein processing in endoplasmic reticulum|Protein processing in endoplasmic reticulum]]
+[[Category:Protein processing in endoplasmic reticulum]]
-[[Category:Apoptosis|Apoptosis]]
+[[Category:Apoptosis]]
-[[Category:Necroptosis|Necroptosis]]
+[[Category:Necroptosis]]
-[[Category:Cellular senescence|Cellular senescence]]
+[[Category:Cellular senescence]]
-[[Category:Focal adhesion|Focal adhesion]]
+[[Category:Focal adhesion]]
-[[Category:Alzheimer disease|Alzheimer disease]]
+[[Category:Alzheimer disease]]

@@ Line 56: / Line 56: @@
 ==Reference==
-# Moldoveanu T, Campbell R L, Cuerrier D, et al. '''Crystal structures of calpain–E64 and–leupeptin inhibitor complexes reveal mobile loops gating the active site[J].''' Journal of molecular biology, 2004, 343(5): 1313-1326. [https://www.ncbi.nlm.nih.gov/pubmed/?term=15491615 15491615]<br/>
+# Moldoveanu T, Campbell R L, Cuerrier D, et al. '''Crystal structures of calpain–E64 and–leupeptin inhibitor complexes reveal mobile loops gating the active site[J].''' Journal of Molecular Biology, 2004, 343(5): 1313-1326. [https://www.ncbi.nlm.nih.gov/pubmed/?term=15491615 15491615]<br/>
 [[Category:Targets|Targets]]

@@ Line 7: / Line 7: @@
 ===Protein Function ===
 Calpain-2 catalytic subunit is a protein that in humans is encoded by the CAPN2 gene. The calpains, calcium-activated neutral proteases, are nonlysosomal, intracellular cysteine proteases. The mammalian calpains include ubiquitous, stomach-specific, and muscle-specific proteins. The ubiquitous enzymes consist of heterodimers with distinct large, catalytic subunits associated with a common small, regulatory subunit. This gene encodes the large subunit of the ubiquitous enzyme, calpain 2. Multiple heterogeneous transcriptional start sites in the 5' UTR have been reported. (From Wikipedia)<br/>
-Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves MYOC at Arg-226. (From Uniprot)<br/>
+Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves MYOC at Arg226. (From Uniprot)<br/>
 Calpains are active participants in fundamental mammalian cellular processes such as cell migration and associated-cytoskeletal remodeling, apoptosis and cell cycle progression. Abnormal calpain activation is also linked to Alzheimer's disease (AD). In AD, calpain relays the toxic effect of extracellular amyloid peptides on neurons to intracellular tau aggregation and neuronal cell death. (PMID: 15491615)
 <br/>

@@ Line 7: / Line 7: @@
 ===Protein Function ===
 Calpain-2 catalytic subunit is a protein that in humans is encoded by the CAPN2 gene. The calpains, calcium-activated neutral proteases, are nonlysosomal, intracellular cysteine proteases. The mammalian calpains include ubiquitous, stomach-specific, and muscle-specific proteins. The ubiquitous enzymes consist of heterodimers with distinct large, catalytic subunits associated with a common small, regulatory subunit. This gene encodes the large subunit of the ubiquitous enzyme, calpain 2. Multiple heterogeneous transcriptional start sites in the 5' UTR have been reported. (From Wikipedia)<br/>
-Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves MYOC at 'Arg-226'. (From Uniprot)<br/>
+Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves MYOC at Arg-226. (From Uniprot)<br/>
 Calpains are active participants in fundamental mammalian cellular processes such as cell migration and associated-cytoskeletal remodeling, apoptosis and cell cycle progression. Abnormal calpain activation is also linked to Alzheimer's disease (AD). In AD, calpain relays the toxic effect of extracellular amyloid peptides on neurons to intracellular tau aggregation and neuronal cell death. (PMID: 15491615)
 <br/>

Calpain-2 - Revision history

Wu3857 at 21:39, 19 August 2019

Wu3857 at 20:28, 29 July 2019

Wu3857 at 20:23, 28 July 2019

Wu3857: /* Reference */

Wu3857: /* Protein Function */

Wu3857: /* Protein Function */

Wu3857: Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|CAPN2|[https://www.uniprot.org/uniprot/P17655 P17655]|Homo sapiens|Cys105|[http://pfam.xfam.org/family/PF00648..."

Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|CAPN2|[https://www.uniprot.org/uniprot/P17655 P17655]|Homo sapiens|Cys105|[http://pfam.xfam.org/family/PF00648..."