Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|TGM2, TGC, TGase H, TGase-2|[https://www.uniprot.org/uniprot/P21980 P21980]|Homo sapiens|Cys277|[http://pfam.xf..."

2020-04-30T01:53:56Z

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{{#invoke:InfoboxforTarget|run|TGM2, TGC, TGase H, TGase-2|[https://www.uniprot.org/uniprot/P21980 P21980]|Homo sapiens|Cys277|[http://pfam.xfam.org/family/PF00656 Transglutaminase-like superfamily]|[[:Category:Protein-glutamine gamma-glutamyltransferase 2|Ligand list]]|Metabolic enzyme}}
==Summary==

===Protein Function ===
Transglutaminases play important roles in diverse biological functions by selectively crosslinking proteins. They catalyze, in a Ca2+dependent manner, the transamidation of glutamine residues to lysine residues, resulting in proteolytically resistant NƐ(ƴ-glutamyl)lysyl isopeptide bonds. 
Transglutaminase 2 (TG2, also known as tissue transglutaminase) s structurally and mechanistically complex, and has both intracellular and extracellular functions. The catalytic mechanism, related to that of cysteine Metabolic enzymes, involves an active site thiol that reacts with a glutamine side chain of a protein or peptide substrate to form a thioester intermediate from which the acyl group is transferred to an amine substrate. In the absence of a suitable amine, water can act as an alternative nucleophile, leading to deamidation of the glutamine residue to glutamate. (PMID: 18092889)
 
[[File:603-function.png|center|600px]]

===Cys Function & Property===
Cys227 is one of the active site of TGM2. 

* Hydrophobic property:
:[[File:603-hydro.png||600px]]
* SASA:
:Cys277: 1.107 A^2 

==Protein Sequence==

MAEELVLERC DLELETNGRD HHTADLCREK LVVRRGQPFW LTLHFEGRNY 
EASVDSLTFS VVTGPAPSQE AGTKARFPLR DAVEEGDWTA TVVDQQDCTL 
SLQLTTPANA PIGLYRLSLE ASTGYQGSSF VLGHFILLFN AWCPADAVYL 
DSEEERQEYV LTQQGFIYQG SAKFIKNIPW NFGQFEDGIL DICLILLDVN 
PKFLKNAGRD CSRRSSPVYV GRVVSGMVNC NDDQGVLLGR WDNNYGDGVS 
PMSWIGSVDI LRRWKNHGCQ RVKYGQ'''C'''WVF AAVACTVLRC LGIPTRVVTN 
YNSAHDQNSN LLIEYFRNEF GEIQGDKSEM IWNFHCWVES WMTRPDLQPG 
YEGWQALDPT PQEKSEGTYC CGPVPVRAIK EGDLSTKYDA PFVFAEVNAD 
VVDWIQQDDG SVHKSINRSL IVGLKISTKS VGRDEREDIT HTYKYPEGSS 
EEREAFTRAN HLNKLAEKEE TGMAMRIRVG QSMNMGSDFD VFAHITNNTA 
EEYVCRLLLC ARTVSYNGIL GPECGTKYLL NLNLEPFSEK SVPLCILYEK 
YRDCLTESNL IKVRALLVEP VINSYLLAER DLYLENPEIK IRILGEPKQK 
RKLVAEVSLQ NPLPVALEGC TFTVEGAGLT EEQKTVEIPD PVEAGEEVKV 
RMDLLPLHMG LHKLVVNFES DKLKAVKGFR NVIIGPA 


==Structural Information==
*Known structure with covalent ligand: 
:[https://www.rcsb.org/structure/3S3S 3S3S] 
:[https://www.rcsb.org/structure/3S3P 3S3P] 
:[https://www.rcsb.org/structure/3S3J 3S3J] 

*Protein structure:
[[File:603.png|center|800px]]

==Related Pathway==
*[https://www.genome.jp/kegg-bin/show_pathway?ko05016 Huntington disease] 

==Experimental Evidence==
:Crystallography

==Reference==
# Pinkas D M, Strop P, Brunger A T, et al. Transglutaminase 2 undergoes a large conformational change upon activation[J]. PLoS biology, 2007, 5(12). [https://www.ncbi.nlm.nih.gov/pubmed/?term=18092889 18092889] 

[[Category:Targets]]
[[Category:Homo sapiens]]
[[Category:Metabolic enzyme]]
[[Category:Transglutaminase-like superfamily]]
[[Category:Huntington disease]]

Protein-glutamine gamma-glutamyltransferase 2 - Revision history

Wu3857: Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|TGM2, TGC, TGase H, TGase-2|[https://www.uniprot.org/uniprot/P21980 P21980]|Homo sapiens|Cys277|[http://pfam.xf..."

Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|TGM2, TGC, TGase H, TGase-2|[https://www.uniprot.org/uniprot/P21980 P21980]|Homo sapiens|Cys277|[http://pfam.xf..."