| UniProt ID | ULP1_YEAST | |
|---|---|---|
| UniProt AC | Q02724 | |
| Protein Name | Ubiquitin-like-specific protease 1 | |
| Gene Name | ULP1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 621 | |
| Subcellular Localization | ||
| Protein Description | 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.. | |
| Protein Sequence | MSVEVDKHRNTLQYHKKNPYSPLFSPISTYRCYPRVLNNPSESRRSASFSGIYKKRTNTSRFNYLNDRRVLSMEESMKDGSDRASKAGFIGGIRETLWNSGKYLWHTFVKNEPRNFDGSEVEASGNSDVESRSSGSRSSDVPYGLRENYSSDTRKHKFDTSTWALPNKRRRIESEGVGTPSTSPISSLASQKSNCDSDNSITFSRDPFGWNKWKTSAIGSNSENNTSDQKNSYDRRQYGTAFIRKKKVAKQNINNTKLVSRAQSEEVTYLRQIFNGEYKVPKILKEERERQLKLMDMDKEKDTGLKKSIIDLTEKIKTILIENNKNRLQTRNENDDDLVFVKEKKISSLERKHKDYLNQKLKFDRSILEFEKDFKRYNEILNERKKIQEDLKKKKEQLAKKKLVPELNEKDDDQVQKALASRENTQLMNRDNIEITVRDFKTLAPRRWLNDTIIEFFMKYIEKSTPNTVAFNSFFYTNLSERGYQGVRRWMKRKKTQIDKLDKIFTPINLNQSHWALGIIDLKKKTIGYVDSLSNGPNAMSFAILTDLQKYVMEESKHTIGEDFDLIHLDCPQQPNGYDCGIYVCMNTLYGSADAPLDFDYKDAIRMRRFIAHLILTDALK | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MSVEVDKHR ------CCCCCCCCC | 27.30 | 22814378 | |
| 21 | Phosphorylation | YHKKNPYSPLFSPIS HHCCCCCCCCCCCCC | 19.18 | 17330950 | |
| 25 | Phosphorylation | NPYSPLFSPISTYRC CCCCCCCCCCCHHCC | 29.07 | 17330950 | |
| 48 | Phosphorylation | SESRRSASFSGIYKK CHHCCCCCCCCEEEC | 22.61 | 25533186 | |
| 72 | Phosphorylation | LNDRRVLSMEESMKD CCHHCEECHHHHCCC | 22.69 | 28152593 | |
| 119 | Phosphorylation | EPRNFDGSEVEASGN CCCCCCCCCEECCCC | 40.07 | 28889911 | |
| 124 | Phosphorylation | DGSEVEASGNSDVES CCCCEECCCCCCCCC | 25.63 | 22890988 | |
| 127 | Phosphorylation | EVEASGNSDVESRSS CEECCCCCCCCCCCC | 46.70 | 22369663 | |
| 131 | Phosphorylation | SGNSDVESRSSGSRS CCCCCCCCCCCCCCC | 36.99 | 22890988 | |
| 134 | Phosphorylation | SDVESRSSGSRSSDV CCCCCCCCCCCCCCC | 39.41 | 23749301 | |
| 138 | Phosphorylation | SRSSGSRSSDVPYGL CCCCCCCCCCCCCCC | 32.37 | 28889911 | |
| 157 | Acetylation | SSDTRKHKFDTSTWA CCCCCCCCCCCCCCC | 48.23 | 22865919 | |
| 160 | Phosphorylation | TRKHKFDTSTWALPN CCCCCCCCCCCCCCC | 31.05 | 30377154 | |
| 174 | Phosphorylation | NKRRRIESEGVGTPS CCCCCCCCCCCCCCC | 36.96 | 22369663 | |
| 179 | Phosphorylation | IESEGVGTPSTSPIS CCCCCCCCCCCCCHH | 16.20 | 22369663 | |
| 181 | Phosphorylation | SEGVGTPSTSPISSL CCCCCCCCCCCHHHH | 41.16 | 22369663 | |
| 182 | Phosphorylation | EGVGTPSTSPISSLA CCCCCCCCCCHHHHH | 39.46 | 22369663 | |
| 183 | Phosphorylation | GVGTPSTSPISSLAS CCCCCCCCCHHHHHH | 25.27 | 22369663 | |
| 186 | Phosphorylation | TPSTSPISSLASQKS CCCCCCHHHHHHCCC | 23.76 | 22369663 | |
| 187 | Phosphorylation | PSTSPISSLASQKSN CCCCCHHHHHHCCCC | 28.77 | 22369663 | |
| 190 | Phosphorylation | SPISSLASQKSNCDS CCHHHHHHCCCCCCC | 43.35 | 22369663 | |
| 193 | Phosphorylation | SSLASQKSNCDSDNS HHHHHCCCCCCCCCC | 34.74 | 21440633 | |
| 200 | Phosphorylation | SNCDSDNSITFSRDP CCCCCCCCCEEECCC | 28.17 | 21440633 | |
| 215 | Phosphorylation | FGWNKWKTSAIGSNS CCCCCCCCCCCCCCC | 23.44 | 28889911 | |
| 220 | Phosphorylation | WKTSAIGSNSENNTS CCCCCCCCCCCCCCC | 30.94 | 30377154 | |
| 222 | Phosphorylation | TSAIGSNSENNTSDQ CCCCCCCCCCCCCCC | 43.32 | 23749301 | |
| 264 | Phosphorylation | KLVSRAQSEEVTYLR CCCHHHHHHHHHHHH | 34.44 | 25752575 | |
| 268 | Phosphorylation | RAQSEEVTYLRQIFN HHHHHHHHHHHHHHC | 21.81 | 27017623 | |
| 308 | Phosphorylation | KDTGLKKSIIDLTEK CCCCCHHHHHHHHHH | 24.16 | 28889911 | |
| 551 | Phosphorylation | ILTDLQKYVMEESKH HHHHHHHHHHHHHCC | 7.65 | 28889911 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of ULP1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ULP1_YEAST !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of ULP1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-48; SER-124;THR-179; SER-183; SER-264; SER-308 AND TYR-551, AND MASS SPECTROMETRY. | |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-179 AND SER-183, ANDMASS SPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-25 AND THR-179,AND MASS SPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND MASSSPECTROMETRY. | |
