Searches of the MEROPS database

Display Known Cleavages for a Protein

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Accession:

Sequence P03366

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Peptide and protein substrates that are thought to be physiologically relevant are indicated by P. Peptide and protein substrates that are not physiologically relevant are indicated by N. 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 peptidase, click on the peptidase name.

Cleavage Site	Peptidase	Residue range	Cleavage type	Description	Evidence	Reference
1	unknown peptidase	1-1447	P		NT	<%Agarwal et al., 2012[]%>
76	endoplasmic reticulum aminopeptidase 1	76-85	P			Saveanu et al., 2005
132	HIV-1 retropepsin	128-135	P			Dunn, 2004
167	HIV-2 retropepsin	163-172	P	pathological turnover		Dunn, 2004
209	HIV-1 retropepsin	133-363	P			Tözsér et al., 2003
321	HIV-1 retropepsin	133-363	P			Tözsér et al., 2003
363	HIV-1 retropepsin	2-1447	P			Dunn, 2004
377	HIV-1 retropepsin	2-1447	P	pathological turnover		Dunn, 2004
432	HIV-1 retropepsin	2-1447	P	pathological turnover		Dunn, 2004
440	unknown peptidase	1-1447	P		NT	<%Agarwal et al., 2012[]%>
448	HIV-1 retropepsin	2-1447	P	pathological turnover		Dunn, 2004
500	unknown peptidase	1-1447	P		NT	<%Agarwal et al., 2012[]%>
599	HIV-1 retropepsin	2-1447	P	pathological turnover		Dunn, 2004
1039	HIV-1 retropepsin	2-1447	P	pathological turnover		Dunn, 2004
1159	HIV-1 retropepsin	2-1447	P	pathological turnover		Dunn, 2004