Q02724 · ULP1_YEAST
- ProteinUbiquitin-like-specific protease 1
- GeneULP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids621 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
Miscellaneous
Present with 377 molecules/cell in log phase SD medium.
Catalytic activity
- 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.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 514 | |||||
Sequence: H | ||||||
Active site | 531 | |||||
Sequence: D | ||||||
Active site | 580 | |||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nuclear envelope | |
Cellular Component | nucleolus | |
Cellular Component | nucleus | |
Molecular Function | cysteine-type peptidase activity | |
Molecular Function | deSUMOylase activity | |
Biological Process | G2/M transition of mitotic cell cycle | |
Biological Process | protein desumoylation | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameUbiquitin-like-specific protease 1
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionQ02724
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine | ||||
Sequence: S | ||||||
Chain | PRO_0000101731 | 2-621 | Ubiquitin-like-specific protease 1 | |||
Sequence: SVEVDKHRNTLQYHKKNPYSPLFSPISTYRCYPRVLNNPSESRRSASFSGIYKKRTNTSRFNYLNDRRVLSMEESMKDGSDRASKAGFIGGIRETLWNSGKYLWHTFVKNEPRNFDGSEVEASGNSDVESRSSGSRSSDVPYGLRENYSSDTRKHKFDTSTWALPNKRRRIESEGVGTPSTSPISSLASQKSNCDSDNSITFSRDPFGWNKWKTSAIGSNSENNTSDQKNSYDRRQYGTAFIRKKKVAKQNINNTKLVSRAQSEEVTYLRQIFNGEYKVPKILKEERERQLKLMDMDKEKDTGLKKSIIDLTEKIKTILIENNKNRLQTRNENDDDLVFVKEKKISSLERKHKDYLNQKLKFDRSILEFEKDFKRYNEILNERKKIQEDLKKKKEQLAKKKLVPELNEKDDDQVQKALASRENTQLMNRDNIEITVRDFKTLAPRRWLNDTIIEFFMKYIEKSTPNTVAFNSFFYTNLSERGYQGVRRWMKRKKTQIDKLDKIFTPINLNQSHWALGIIDLKKKTIGYVDSLSNGPNAMSFAILTDLQKYVMEESKHTIGEDFDLIHLDCPQQPNGYDCGIYVCMNTLYGSADAPLDFDYKDAIRMRRFIAHLILTDALK | ||||||
Modified residue | 21 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 25 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 179 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 264 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 116-150 | Disordered | ||||
Sequence: FDGSEVEASGNSDVESRSSGSRSSDVPYGLRENYS | ||||||
Compositional bias | 120-146 | Polar residues | ||||
Sequence: EVEASGNSDVESRSSGSRSSDVPYGLR | ||||||
Region | 169-196 | Disordered | ||||
Sequence: RRRIESEGVGTPSTSPISSLASQKSNCD | ||||||
Compositional bias | 176-196 | Polar residues | ||||
Sequence: GVGTPSTSPISSLASQKSNCD | ||||||
Region | 432-621 | Protease | ||||
Sequence: NIEITVRDFKTLAPRRWLNDTIIEFFMKYIEKSTPNTVAFNSFFYTNLSERGYQGVRRWMKRKKTQIDKLDKIFTPINLNQSHWALGIIDLKKKTIGYVDSLSNGPNAMSFAILTDLQKYVMEESKHTIGEDFDLIHLDCPQQPNGYDCGIYVCMNTLYGSADAPLDFDYKDAIRMRRFIAHLILTDALK |
Sequence similarities
Belongs to the peptidase C48 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length621
- Mass (Da)72,378
- Last updated1996-11-01 v1
- ChecksumF71132817FAF0B41
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 120-146 | Polar residues | ||||
Sequence: EVEASGNSDVESRSSGSRSSDVPYGLR | ||||||
Compositional bias | 176-196 | Polar residues | ||||
Sequence: GVGTPSTSPISSLASQKSNCD |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U36624 EMBL· GenBank· DDBJ | AAB68167.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006949 EMBL· GenBank· DDBJ | DAA11408.1 EMBL· GenBank· DDBJ | Genomic DNA |