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EC Number
Posttranslational Modification
Commentary
Reference
3.4.21.122
glycoprotein
sequence conatins potential N-glycosylation sites N213 and N249
753752
3.4.21.122
proteolytic modification
autocleavage of TMPRSS2 releases a 24-kDa peptide from the C-terminal active domain
753762
3.4.21.122
proteolytic modification
enzyme is autocatalytically activitated
755102
3.4.21.122
proteolytic modification
the amino-terminal Ile of the protease domain is preceded by Arg in the context of a peptide sequence Arg-Ile-Val-Gly-Gly typical for the proteolytic activator site of serine protease zymogens
753752
3.4.21.122
proteolytic modification
TMPRSS2-encoded serine protease is expressed as a 70000 MW full-length form and a cleaved 32000 MW protease domain. The proteolytic cleavage is dependent on catalytic activity, suggesting that it occurs as a result of autocleavage. The cleavage site is at Arg255
764399
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