Substrates for peptidase C02.015: calpain B

Summary Gene structure Alignment Tree Sequences Sequence features Distribution Literature Substrates

Peptide and protein substrates that are thought to be physiologically relevant are indicated by P. Peptide and protein substrates that are thought to be pathologically relevant are indicated by D. Peptide and protein substrates that are not physiologically relevant are indicated by N. Synthetic substrates are indicated by S. Click on the symbol to show only physiological, non-physiological or synthetic substrates, or here to display all substrates. How cleavage sites have been identified are indicated by the following evidence codes: NT = N-terminal sequencing, MS = mass spectroscopy, MU = mutation, CS = consensus sequence, LC = liquid chromatography. To see all annotated cleavages for a protein substrate, click on the UniProt Accession.

Substrate Uniprot Residue range Cleavage Site Cleavage type Evidence P4 P3 P2 P1 P1' P2' P3' P4' Reference CutDB MERNUM
calpain B Q9VT65 1-925 peptide-Asn74+Ala-peptide N His Ala Gln Asn Ala Ser Tyr Ala 16119
calpain B Q9VT65 1-925 peptide-Gln224+Asn-peptide N Pro Glu Asn Gln Asn Met Phe Trp Jekely & Friedrich, 1999 16120
DABCYL-TPLKSPPPSPR-EDANS Dabcyl-Thr-Pro-Leu-Lys+Ser-Pro-Pro-Pro-Ser-Pro-Arg-EDANS S Thr Pro Leu Lys Ser Pro Pro Pro Tompa et al., 2004
Suc-Leu-Tyr-NHMec Suc-Leu-Tyr+NHMec S - Suc Leu Tyr AMC - - - Jekely & Friedrich, 1999