Detail Information for IndEnz0002011501
IED ID IndEnz0002011501
Enzyme Type ID protease011501
Protein Name Ubiquitin-like-specific protease 1
EC 3.4.22.68
Gene Name ULP1 YPL020C LPB11C
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Enzyme Sequence MSVEVDKHRNTLQYHKKNPYSPLFSPISTYRCYPRVLNNPSESRRSASFSGIYKKRTNTSRFNYLNDRRVLSMEESMKDGSDRASKAGFIGGIRETLWNSGKYLWHTFVKNEPRNFDGSEVEASGNSDVESRSSGSRSSDVPYGLRENYSSDTRKHKFDTSTWALPNKRRRIESEGVGTPSTSPISSLASQKSNCDSDNSITFSRDPFGWNKWKTSAIGSNSENNTSDQKNSYDRRQYGTAFIRKKKVAKQNINNTKLVSRAQSEEVTYLRQIFNGEYKVPKILKEERERQLKLMDMDKEKDTGLKKSIIDLTEKIKTILIENNKNRLQTRNENDDDLVFVKEKKISSLERKHKDYLNQKLKFDRSILEFEKDFKRYNEILNERKKIQEDLKKKKEQLAKKKLVPELNEKDDDQVQKALASRENTQLMNRDNIEITVRDFKTLAPRRWLNDTIIEFFMKYIEKSTPNTVAFNSFFYTNLSERGYQGVRRWMKRKKTQIDKLDKIFTPINLNQSHWALGIIDLKKKTIGYVDSLSNGPNAMSFAILTDLQKYVMEESKHTIGEDFDLIHLDCPQQPNGYDCGIYVCMNTLYGSADAPLDFDYKDAIRMRRFIAHLILTDALK
Enzyme Length 621
Uniprot Accession Number Q02724
Absorption
Active Site ACT_SITE 514; /evidence=ECO:0000269|PubMed:10882122; ACT_SITE 531; /evidence=ECO:0000269|PubMed:10882122; ACT_SITE 580; /evidence=ECO:0000269|PubMed:10882122
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolysis of the alpha-linked peptide bond in the sequence Gly-Gly-|-Ala-Thr-Tyr at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptide, Smt3, leading to the mature form of the protein. A second reaction involves the cleavage of an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein.; EC=3.4.22.68; Evidence={ECO:0000269|PubMed:10882122};
DNA Binding
EC Number 3.4.22.68
Enzyme Function FUNCTION: Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SMT3 to its mature form and deconjugation of SMT3 from targeted proteins. Has an essential role in the G2/M phase of the cell cycle. {ECO:0000269|PubMed:10094048}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Beta strand (9); Chain (1); Compositional bias (2); Helix (11); Initiator methionine (1); Modified residue (5); Region (3); Turn (4)
Keywords 3D-structure;Acetylation;Hydrolase;Phosphoprotein;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway
Interact With
Induction
Subcellular Location
Modified Residue MOD_RES 2; /note="N-acetylserine"; /evidence="ECO:0007744|PubMed:22814378"; MOD_RES 21; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17330950"; MOD_RES 25; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17330950"; MOD_RES 179; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956"; MOD_RES 264; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18407956"
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (7)
Cross Reference PDB 1EUV; 2HKP; 2HL8; 2HL9; 5H2V; 5H2W; 5H2X;
Mapped Pubmed ID 10713161; 11056382; 11274415; 11283351; 11574060; 11595179; 11805826; 12429940; 12471376; 12654900; 14607092; 15169880; 15263846; 15557117; 15596868; 15781853; 15808504; 15870298; 16198156; 16429126; 16554755; 17031663; 17234788; 17403926; 17428805; 17467257; 17499995; 17509569; 17538013; 17704192; 17724121; 17768054; 18031227; 18467498; 18499666; 18719252; 19008217; 19107407; 19107421; 19107423; 19162180; 19536198; 20351217; 20580716; 20647537; 21222284; 21602906; 21892772; 22025676; 22034919; 22964839; 23175280; 23403034; 23550137; 23712011; 23731471; 23812602; 24074957; 24500206; 24705649; 25171917; 25184662; 25231978; 25833950; 25845599; 26004856; 26633173; 26709543; 26783300; 26837752; 26921322; 26960810; 27134164; 27683094; 27939291; 29351565; 29695777; 30357586; 6752695;
Motif
Gene Encoded By
Mass 72,378
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.22.68;