| UniProt ID | UBP6_YEAST | |
|---|---|---|
| UniProt AC | P43593 | |
| Protein Name | Ubiquitin carboxyl-terminal hydrolase 6 | |
| Gene Name | UBP6 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 499 | |
| Subcellular Localization | ||
| Protein Description | Predominant proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. Ensures the regeneration of ubiquitin at the proteasome. Has proteasome-inhibitory activity and delays the degradation of ubiquitinated proteins to provide a time window allowing gradual deubiquitination of the substrate. Stabilizes the association of HUL5 with proteasomes and works in opposition to polyubiquitin elongation activity of HUL5.. | |
| Protein Sequence | MSGETFEFNIRHSGKVYPITLSTDATSADLKSKAEELTQVPSARQKYMVKGGLSGEESIKIYPLIKPGSTVMLLGTPDANLISKPAKKNNFIEDLAPEQQVQQFAQLPVGFKNMGNTCYLNATLQALYRVNDLRDMILNYNPSQGVSNSGAQDEEIHKQIVIEMKRCFENLQNKSFKSVLPIVLLNTLRKCYPQFAERDSQGGFYKQQDAEELFTQLFHSMSIVFGDKFSEDFRIQFKTTIKDTANDNDITVKENESDSKLQCHISGTTNFMRNGLLEGLNEKIEKRSDLTGANSIYSVEKKISRLPKFLTVQYVRFFWKRSTNKKSKILRKVVFPFQLDVADMLTPEYAAEKVKVRDELRKVEKEKNEKEREIKRRKFDPSSSENVMTPREQYETQVALNESEKDQWLEEYKKHFPPNLEKGENPSCVYNLIGVITHQGANSESGHYQAFIRDELDENKWYKFNDDKVSVVEKEKIESLAGGGESDSALILMYKGFGL | |
| 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 |
|---|---|---|---|---|---|
| 15 | Ubiquitination | FNIRHSGKVYPITLS EEEEECCEEEEEEEE | 41.43 | 17644757 | |
| 31 | Ubiquitination | DATSADLKSKAEELT CCCCHHHHHHHHHHH | 50.92 | 17644757 | |
| 33 | Ubiquitination | TSADLKSKAEELTQV CCHHHHHHHHHHHCC | 59.22 | 17644757 | |
| 60 | Ubiquitination | LSGEESIKIYPLIKP CCCCCEEEEEECCCC | 45.53 | 17644757 | |
| 66 | Ubiquitination | IKIYPLIKPGSTVML EEEEECCCCCCEEEE | 51.51 | 17644757 | |
| 84 | Ubiquitination | PDANLISKPAKKNNF CCHHHCCCCCCCCCC | 41.84 | 17644757 | |
| 87 | Ubiquitination | NLISKPAKKNNFIED HHCCCCCCCCCCHHH | 65.64 | 17644757 | |
| 88 | Ubiquitination | LISKPAKKNNFIEDL HCCCCCCCCCCHHHC | 60.26 | 17644757 | |
| 112 | Ubiquitination | AQLPVGFKNMGNTCY HCCCCCCCCCCCCHH | 39.84 | 17644757 | |
| 140 | Phosphorylation | LRDMILNYNPSQGVS HHHHHHHCCCCCCCC | 25.63 | 22369663 | |
| 143 | Phosphorylation | MILNYNPSQGVSNSG HHHHCCCCCCCCCCC | 35.61 | 22369663 | |
| 147 | Phosphorylation | YNPSQGVSNSGAQDE CCCCCCCCCCCCCCH | 31.91 | 22369663 | |
| 149 | Phosphorylation | PSQGVSNSGAQDEEI CCCCCCCCCCCCHHH | 28.18 | 22369663 | |
| 165 | Ubiquitination | KQIVIEMKRCFENLQ HHHHHHHHHHHHHHC | 32.97 | 17644757 | |
| 174 | Ubiquitination | CFENLQNKSFKSVLP HHHHHCCCCHHHHHH | 44.29 | 17644757 | |
| 177 | Acetylation | NLQNKSFKSVLPIVL HHCCCCHHHHHHHHH | 46.90 | 24489116 | |
| 177 | Ubiquitination | NLQNKSFKSVLPIVL HHCCCCHHHHHHHHH | 46.90 | 17644757 | |
| 178 | Phosphorylation | LQNKSFKSVLPIVLL HCCCCHHHHHHHHHH | 27.20 | 21440633 | |
| 190 | Ubiquitination | VLLNTLRKCYPQFAE HHHHHHHHHCHHHHH | 41.03 | 23749301 | |
| 238 | Ubiquitination | EDFRIQFKTTIKDTA CCEEEEEEEEEECCC | 28.51 | 17644757 | |
| 242 | Succinylation | IQFKTTIKDTANDND EEEEEEEECCCCCCC | 47.11 | 23954790 | |
| 242 | Ubiquitination | IQFKTTIKDTANDND EEEEEEEECCCCCCC | 47.11 | 17644757 | |
| 244 | Phosphorylation | FKTTIKDTANDNDIT EEEEEECCCCCCCEE | 23.51 | 21126336 | |
| 253 | Ubiquitination | NDNDITVKENESDSK CCCCEEEEECCCCCC | 46.29 | 23749301 | |
| 283 | Ubiquitination | LLEGLNEKIEKRSDL HHHHHHHHHHHHHCC | 55.91 | 17644757 | |
| 283 | Acetylation | LLEGLNEKIEKRSDL HHHHHHHHHHHHHCC | 55.91 | 24489116 | |
| 286 | Ubiquitination | GLNEKIEKRSDLTGA HHHHHHHHHHCCCCC | 61.75 | 17644757 | |
| 286 | Acetylation | GLNEKIEKRSDLTGA HHHHHHHHHHCCCCC | 61.75 | 24489116 | |
| 297 | Phosphorylation | LTGANSIYSVEKKIS CCCCCHHHCHHHHHH | 13.39 | 28889911 | |
| 298 | Phosphorylation | TGANSIYSVEKKISR CCCCHHHCHHHHHHC | 23.33 | 21440633 | |
| 301 | Ubiquitination | NSIYSVEKKISRLPK CHHHCHHHHHHCCCC | 53.93 | 17644757 | |
| 302 | Ubiquitination | SIYSVEKKISRLPKF HHHCHHHHHHCCCCC | 32.20 | 17644757 | |
| 308 | Ubiquitination | KKISRLPKFLTVQYV HHHHCCCCCHHHHHH | 58.56 | 23749301 | |
| 308 | Acetylation | KKISRLPKFLTVQYV HHHHCCCCCHHHHHH | 58.56 | 24489116 | |
| 332 | Ubiquitination | KKSKILRKVVFPFQL CCCHHHHHHHCCEEC | 39.03 | 17644757 | |
| 346 | Phosphorylation | LDVADMLTPEYAAEK CCHHHHCCHHHHHHH | 13.87 | 22369663 | |
| 349 | Phosphorylation | ADMLTPEYAAEKVKV HHHCCHHHHHHHHHH | 16.59 | 22369663 | |
| 353 | Ubiquitination | TPEYAAEKVKVRDEL CHHHHHHHHHHHHHH | 42.50 | 17644757 | |
| 355 | Ubiquitination | EYAAEKVKVRDELRK HHHHHHHHHHHHHHH | 42.49 | 17644757 | |
| 378 | Acetylation | EREIKRRKFDPSSSE HHHHHHHCCCCCCCC | 59.14 | 25381059 | |
| 378 | Ubiquitination | EREIKRRKFDPSSSE HHHHHHHCCCCCCCC | 59.14 | 23749301 | |
| 382 | Phosphorylation | KRRKFDPSSSENVMT HHHCCCCCCCCCCCC | 48.63 | 22890988 | |
| 383 | Phosphorylation | RRKFDPSSSENVMTP HHCCCCCCCCCCCCH | 47.24 | 22890988 | |
| 384 | Phosphorylation | RKFDPSSSENVMTPR HCCCCCCCCCCCCHH | 37.21 | 22890988 | |
| 389 | Phosphorylation | SSSENVMTPREQYET CCCCCCCCHHHHHHH | 18.21 | 22369663 | |
| 405 | Acetylation | VALNESEKDQWLEEY HHCCHHHHHHHHHHH | 65.58 | 24489116 | |
| 405 | Ubiquitination | VALNESEKDQWLEEY HHCCHHHHHHHHHHH | 65.58 | 17644757 | |
| 413 | Ubiquitination | DQWLEEYKKHFPPNL HHHHHHHHHHCCCCC | 42.95 | 17644757 | |
| 414 | Ubiquitination | QWLEEYKKHFPPNLE HHHHHHHHHCCCCCC | 49.96 | 17644757 | |
| 468 | Acetylation | WYKFNDDKVSVVEKE CEECCCCCEEEEEHH | 38.99 | 24489116 | |
| 470 | Phosphorylation | KFNDDKVSVVEKEKI ECCCCCEEEEEHHHH | 26.62 | 22369663 | |
| 486 | Phosphorylation | SLAGGGESDSALILM HHCCCCCCHHEEEEE | 39.89 | 21440633 | |
| 488 | Phosphorylation | AGGGESDSALILMYK CCCCCCHHEEEEEEE | 33.96 | 21440633 |
| 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 UBP6_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of UBP6_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 UBP6_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-298; SER-383; THR-389AND SER-470, 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 SER-383; THR-389 ANDSER-470, AND MASS 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 THR-389, AND MASSSPECTROMETRY. | |
