EC Number | Cloned (Comment) | Organism |
---|---|---|
3.4.21.B4 | - |
Homo sapiens |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.21.B4 | Homo sapiens | P49863 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.21.B4 | actin + H2O | - |
Homo sapiens | ? | - |
? | |
3.4.21.B4 | beta-tubulin + H2O | cleaves beta-tubulin after Arg62 (YVPR-/-AV) and Arg282 (QQYR-/-AL) | Homo sapiens | ? | - |
? | |
3.4.21.B4 | endoplasmic reticulum-associated SET complex + H2O | - |
Homo sapiens | ? | - |
? | |
3.4.21.B4 | heterogeneous nuclear ribonucleoprotein K + H2O | granzyme K and granzyme A cleave with different kinetics at distinct sites | Homo sapiens | ? | - |
? | |
3.4.21.B4 | additional information | granzyme K prefers Arg over Lys at P1 position. Granzyme K and granzyme A display highly restricted substrate specificities that overlapp only partially. Whereas granzyme K and granzyme A cleave SET with similar efficiencies likely at the same sites, both granzymes cleave the pre-mRNA-binding protein heterogeneous ribonuclear protein K with different kinetics at distinct sites. Granzyme K is markedly more efficient in cleaving heterogeneous ribonuclear protein K than granzyme A. Granzyme K, but not granzyme A, cleaves the microtubule network protein beta-tubulin after two distinct Arg residues. Neither GrK cleavage sites in beta-tubulin nor a peptide based proteomic screen reveal a clear granzyme K consensus sequence around the P1 residue, suggesting that GrK specificity depends on electrostatic interactions between exosites of the substrate and the enzyme | Homo sapiens | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.4.21.B4 | GRK | - |
Homo sapiens |