Basic Information
Name | Saccharopepsin (EC 3.4.23.25) (Aspartate protease) (PrA) (Proteinase A) (Carboxypeptidase Y-deficient protein 4) (Proteinase YSCA) |
Uniprot ID | P07267 |
Systematic gene name | YPL154C |
Standard gene name | PEP4 |
Gene names | PEP4 PHO9 PRA1 YPL154C P2585 |
Description from SGD | YPL154C PEP4 SGDID:S000006075, Chr XVI from 260931-259714, Genome Release 64-3-1, reverse complement, Verified ORF, "Vacuolar aspartyl protease (proteinase A); required for posttranslational precursor maturation of vacuolar proteinases; important for protein turnover after oxidative damage; plays a protective role in acetic acid induced apoptosis; synthesized as a zymogen, self-activates" |
Protein length | 405 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MFSLKALLPL ALLLVSANQV AAKVHKAKIY KHELSDEMKE VTFEQHLAHL
GQKYLTQFEK ANPEVVFSRE HPFFTEGGHD VPLTNYLNAQ YYTDITLGTP
PQNFKVILDT GSSNLWVPSN ECGSLACFLH SKYDHEASSS YKANGTEFAI
QYGTGSLEGY ISQDTLSIGD LTIPKQDFAE ATSEPGLTFA FGKFDGILGL
GYDTISVDKV VPPFYNAIQQ DLLDEKRFAF YLGDTSKDTE NGGEATFGGI
DESKFKGDIT WLPVRRKAYW EVKFEGIGLG DEYAELESHG AAIDTGTSLI
TLPSGLAEMI NAEIGAKKGW TGQYTLDCNT RDNLPDLIFN FNGYNFTIGP
YDYTLEVSGS CISAITPMDF PEPVGPLAIV GDAFLRKYYS IYDLGNNAVG
LAKAI
GQKYLTQFEK ANPEVVFSRE HPFFTEGGHD VPLTNYLNAQ YYTDITLGTP
PQNFKVILDT GSSNLWVPSN ECGSLACFLH SKYDHEASSS YKANGTEFAI
QYGTGSLEGY ISQDTLSIGD LTIPKQDFAE ATSEPGLTFA FGKFDGILGL
GYDTISVDKV VPPFYNAIQQ DLLDEKRFAF YLGDTSKDTE NGGEATFGGI
DESKFKGDIT WLPVRRKAYW EVKFEGIGLG DEYAELESHG AAIDTGTSLI
TLPSGLAEMI NAEIGAKKGW TGQYTLDCNT RDNLPDLIFN FNGYNFTIGP
YDYTLEVSGS CISAITPMDF PEPVGPLAIV GDAFLRKYYS IYDLGNNAVG
LAKAI
Legend
- X Ubiquitination
- X Phoshorylation
- X Glycosylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[60, Ubi] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |
[138, Phos] | Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications) |
[139, Phos] | Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications) |
[144, Glyc] | Zielinska, D.F., Gnad, F., Schropp, K., Wiśniewski, J.R., Mann, M. (2012). Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542-548. (Publication) (All modifications) |
[318, Ubi] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |
[387, Ubi] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |