Literature summary for 3.4.21.B2 extracted from

Khurshid, R.; Saleem, M.; Akhtar, M.S.; Salim, A.
Granzyme M: Characterization with sites of post-translational modification and specific sites of interaction with substrates and inhibitors (2010), Mol. Biol. Rep., 392, 199-207.

Search for more literature for 3.4.21.B2

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	inhibitors bound to the granzyme active site show that the dimer also contributes to substrate specificity in a unique manner by extending the active-site cleft	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
additional information	in Gzm M there are cationic sites, cs1 and cs2, that may participate in binding of Gzm M to the cell surface, thereby promoting its uptake and eventual release into the cytoplasm	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P51124	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
additional information	post-translational modification, including O-glycosylation of serine, phosphorylation of serine and threonine and myristoylation of glycine, play an important role in the interaction of enzyme with the cell surface membrane and regulate protein trafficking and stability. Phosphorylated serine and threonine also plays a role in tumor elimination, viral clearance and tissue repair	Homo sapiens

Synonyms

Synonyms	Comment	Organism
Granzyme M	-	Homo sapiens
Gzm M	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	Gzm M shows apoptotic activity both by caspase dependent and independent pathways	Homo sapiens

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Release 2023.1 (January 2023)