Caspase-2 - Revision history

Wu3857: /* Protein Function */

2020-01-04T05:28:50Z

‎Protein Function

Wu3857 at 05:28, 4 January 2020

2020-01-04T05:28:40Z

Wu3857 at 05:28, 4 January 2020

2020-01-04T05:28:17Z

Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|CASP2|[https://www.uniprot.org/uniprot/P42575 P42575]|Homo sapiens|Cys320|[http://pfam.xfam.org/family/PF00656..."

2020-01-04T05:28:00Z

Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|CASP2|[https://www.uniprot.org/uniprot/P42575 P42575]|Homo sapiens|Cys320|[http://pfam.xfam.org/family/PF00656..."

New page

{| align="left"
| __TOC__
|}
{{#invoke:InfoboxforTarget|run|CASP2|[https://www.uniprot.org/uniprot/P42575 P42575]|Homo sapiens|Cys320|[http://pfam.xfam.org/family/PF00656 Peptidase C14A family]|[[:Category:Caspase-2|Ligand list]]|Protease}}
==Summary==

===Protein Function ===
Caspase-2 proteolytically cleaves other proteins. It belongs to a family of cysteine proteases called caspases that cleave proteins only at an amino acid following an aspartic acid residue. Within this family, caspase-2 is part of the Ich-1 subfamily. It is one of the most conserved caspases in different species of animal. Caspase-2 has a similar amino acid sequence to initiator caspases, including caspase 1, caspase-4, caspase-5, and caspase-9. It is produced as a zymogen, which contains a long pro-domain that is similar to that of caspase-9 and contains a protein interaction domain known as a CARD domain. Pro-caspase-2 contains two subunits, p19 and p12. (From Wikipedia) 

Caspase-2 was discovered as the first mammalian apoptotic caspase. Caspase-2 is engaged as an initiator in both the extrinsic and the intrinsic pathways of apoptosis. Additionally, Caspase-2 serves in neuronal cells both as the default initiator and the default executioner caspase. (PMID: 12920126) 

===Cys Function & Property===
The catalytic triad in Caspase-3 comprises Cys320, His277 and the backbone carbonyl oxygen atom of Arg219, which points towards the Nϵ atom of His277. 

* Hydrophobic property:
:[[File:595-hydro.png||600px]]
* SASA:
:Cys320: 11.39 A^2 

==Protein Sequence==

MAAPSAGSWS TFQHKELMAA DRGRRILGVC GMHPHHQETL KKNRVVLAKQ 
LLLSELLEHL LEKDIITLEM RELIQAKVGS FSQNVELLNL LPKRGPQAFD 
AFCEALRETK QGHLEDMLLT TLSGLQHVLP PLSCDYDLSL PFPVCESCPL 
YKKLRLSTDT VEHSLDNKDG PVCLQVKPCT PEFYQTHFQL AYRLQSRPRG 
LALVLSNVHF TGEKELEFRS GGDVDHSTLV TLFKLLGYDV HVLCDQTAQE 
MQEKLQNFAQ LPAHRVTDSC IVALLSHGVE GAIYGVDGKL LQLQEVFQLF 
DNANCPSLQN KPKMFFIQA'''C''' RGDETDRGVD QQDGKNHAGS PGCEESDAGK 
EKLPKMRLPT RSDMICGYAC LKGTAAMRNT KRGSWYIEAL AQVFSERACD 
MHVADMLVKV NALIKDREGY APGTEFHRCK EMSEYCSTLC RHLYLFPGHP 
PT 


==Structural Information==
*Known structure with covalent ligand: 
:[https://www.rcsb.org/structure/1PYO 1PYO] 

*Protein structure:
[[File:595.png|center|800px]]

==Related Pathway==
*[https://www.genome.jp/kegg-bin/show_pathway?ko04210 Apoptosis] 

==Experimental Evidence==
:Crystallography

==Reference==
# Schweizer A, Briand C, Grütter M G. '''Crystal structure of caspase-2, apical initiator of the intrinsic apoptotic pathway[J].''' Journal of Biological Chemistry, 2003, 278(43): 42441-42447. [https://www.ncbi.nlm.nih.gov/pubmed/?term=12920126 12920126] 

[[Category:Targets]]
[[Category:Homo sapiens]]
[[Category:Protease]]
[[Category:Peptidase C14A family]]
[[Category:Apoptosis]]

@@ Line 7: / Line 7: @@
 ===Protein Function ===
 Caspase-2 proteolytically cleaves other proteins. It belongs to a family of cysteine proteases called caspases that cleave proteins only at an amino acid following an aspartic acid residue. Within this family, caspase-2 is part of the Ich-1 subfamily. It is one of the most conserved caspases in different species of animal. Caspase-2 has a similar amino acid sequence to initiator caspases, including caspase 1, caspase-4, caspase-5, and caspase-9. It is produced as a zymogen, which contains a long pro-domain that is similar to that of caspase-9 and contains a protein interaction domain known as a CARD domain. Pro-caspase-2 contains two subunits, p19 and p12. (From Wikipedia) <br/>
 Caspase-2 was discovered as the first mammalian apoptotic caspase. It is engaged as an initiator in both the extrinsic and the intrinsic pathways of apoptosis. Additionally, Caspase-2 serves in neuronal cells both as the default initiator and the default executioner caspase. (PMID: 12920126) <br/>
 ===Cys Function & Property===

@@ Line 7: / Line 7: @@
 ===Protein Function ===
 Caspase-2 proteolytically cleaves other proteins. It belongs to a family of cysteine proteases called caspases that cleave proteins only at an amino acid following an aspartic acid residue. Within this family, caspase-2 is part of the Ich-1 subfamily. It is one of the most conserved caspases in different species of animal. Caspase-2 has a similar amino acid sequence to initiator caspases, including caspase 1, caspase-4, caspase-5, and caspase-9. It is produced as a zymogen, which contains a long pro-domain that is similar to that of caspase-9 and contains a protein interaction domain known as a CARD domain. Pro-caspase-2 contains two subunits, p19 and p12. (From Wikipedia) <br/>
-Caspase-2 was discovered as the first mammalian apoptotic caspase. Caspase-2 is engaged as an initiator in both the extrinsic and the intrinsic pathways of apoptosis. Additionally, Caspase-2 serves in neuronal cells both as the default initiator and the default executioner caspase. (PMID: 12920126) <br/>
+Caspase-2 was discovered as the first mammalian apoptotic caspase. It is engaged as an initiator in both the extrinsic and the intrinsic pathways of apoptosis. Additionally, Caspase-2 serves in neuronal cells both as the default initiator and the default executioner caspase. (PMID: 12920126) <br/>
 ===Cys Function & Property===

@@ Line 7: / Line 7: @@
 ===Protein Function ===
 Caspase-2 proteolytically cleaves other proteins. It belongs to a family of cysteine proteases called caspases that cleave proteins only at an amino acid following an aspartic acid residue. Within this family, caspase-2 is part of the Ich-1 subfamily. It is one of the most conserved caspases in different species of animal. Caspase-2 has a similar amino acid sequence to initiator caspases, including caspase 1, caspase-4, caspase-5, and caspase-9. It is produced as a zymogen, which contains a long pro-domain that is similar to that of caspase-9 and contains a protein interaction domain known as a CARD domain. Pro-caspase-2 contains two subunits, p19 and p12. (From Wikipedia) <br/>
 Caspase-2 was discovered as the first mammalian apoptotic caspase. Caspase-2 is engaged as an initiator in both the extrinsic and the intrinsic pathways of apoptosis. Additionally, Caspase-2 serves in neuronal cells both as the default initiator and the default executioner caspase. (PMID: 12920126) <br/>

Caspase-2 - Revision history

Wu3857: /* Protein Function */

Wu3857 at 05:28, 4 January 2020

Wu3857 at 05:28, 4 January 2020

Wu3857: Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|CASP2|[https://www.uniprot.org/uniprot/P42575 P42575]|Homo sapiens|Cys320|[http://pfam.xfam.org/family/PF00656..."

Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|CASP2|[https://www.uniprot.org/uniprot/P42575 P42575]|Homo sapiens|Cys320|[http://pfam.xfam.org/family/PF00656..."