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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Carboxypeptidase Y

UniprotKB/SwissProt ID: P00729 (P00729)

Gene Name: PRC1

Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Function: Vacuolar serine-type carboxypeptidase involved in degradation of small peptides (PubMed:8679540). Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate (PubMed:8679540). Also plays a role in breakdown of the autophagic body and the autophagosome-dependent protein synthesis (PubMed:29514932). Plays a key role in phytochelatin (PC) synthesis from glutathione (GSH) by cleaving the Gly from GSH and form the PC-peptides of the structure (gamma-Glu-Cys)2-Gly (PubMed:17408619). Also involved in resistance to xenobiotics via the degradation of glutathione-S-conjugates (PubMed:19897216)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Vacuole lumen

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR029058 AB_hydrolase_fold
IPR001563 Peptidase_S10
IPR008442 Propeptide_carboxypepY
IPR033124 Ser_caboxypep_his_AS
IPR018202 Ser_caboxypep_ser_AS