| UniProt ID | PRS4_YEAST | |
|---|---|---|
| UniProt AC | P40327 | |
| Protein Name | 26S proteasome regulatory subunit 4 homolog | |
| Gene Name | RPT2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 437 | |
| Subcellular Localization | Cytoplasm . Nucleus . | |
| Protein Description | The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity). Has ATPase activity.. | |
| Protein Sequence | MGQGVSSGQDKKKKKGSNQKPKYEPPVQSKFGRKKRKGGPATAEKLPNIYPSTRCKLKLLRMERIKDHLLLEEEFVSNSEILKPFEKKQEEEKKQLEEIRGNPLSIGTLEEIIDDDHAIVTSPTMPDYYVSILSFVDKELLEPGCSVLLHHKTMSIVGVLQDDADPMVSVMKMDKSPTESYSDIGGLESQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPRLCRQIFKVAGENAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDDRGDVKVIMATNKIETLDPALIRPGRIDRKILFENPDLSTKKKILGIHTSKMNLSEDVNLETLVTTKDDLSGADIQAMCTEAGLLALRERRMQVTAEDFKQAKERVMKNKVEENLEGLYL | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
|
|
||
* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | N-myristoyl glycine | ------MGQGVSSGQ ------CCCCCCCCC | 32.71 | - | |
| 2 | Myristoylation | ------MGQGVSSGQ ------CCCCCCCCC | 32.71 | 12504901 | |
| 6 | Phosphorylation | --MGQGVSSGQDKKK --CCCCCCCCCCCCC | 35.26 | 30377154 | |
| 15 | Ubiquitination | GQDKKKKKGSNQKPK CCCCCCCCCCCCCCC | 76.17 | 22817900 | |
| 20 | Ubiquitination | KKKGSNQKPKYEPPV CCCCCCCCCCCCCCC | 47.96 | 22817900 | |
| 22 | Acetylation | KGSNQKPKYEPPVQS CCCCCCCCCCCCCHH | 70.09 | 22865919 | |
| 22 | Ubiquitination | KGSNQKPKYEPPVQS CCCCCCCCCCCCCHH | 70.09 | 22817900 | |
| 30 | Ubiquitination | YEPPVQSKFGRKKRK CCCCCHHCCCCCCCC | 34.44 | 17644757 | |
| 30 | Acetylation | YEPPVQSKFGRKKRK CCCCCHHCCCCCCCC | 34.44 | 24489116 | |
| 37 | Ubiquitination | KFGRKKRKGGPATAE CCCCCCCCCCCCCHH | 76.68 | 17644757 | |
| 45 | Acetylation | GGPATAEKLPNIYPS CCCCCHHHCCCCCCC | 67.77 | 24489116 | |
| 45 | Ubiquitination | GGPATAEKLPNIYPS CCCCCHHHCCCCCCC | 67.77 | 24961812 | |
| 66 | Ubiquitination | LLRMERIKDHLLLEE HHHHHHHHHHHHCCC | 45.37 | 23749301 | |
| 83 | Ubiquitination | VSNSEILKPFEKKQE CCCHHHCHHHHHHHH | 54.01 | 17644757 | |
| 87 | Ubiquitination | EILKPFEKKQEEEKK HHCHHHHHHHHHHHH | 61.20 | 17644757 | |
| 88 | Ubiquitination | ILKPFEKKQEEEKKQ HCHHHHHHHHHHHHH | 56.60 | 17644757 | |
| 138 | Ubiquitination | SILSFVDKELLEPGC HHHHHCCHHHCCCCC | 44.98 | 17644757 | |
| 152 | Ubiquitination | CSVLLHHKTMSIVGV CEEEEECCCCEEEEE | 34.86 | 17644757 | |
| 175 | Acetylation | VSVMKMDKSPTESYS CEEEECCCCCCCCHH | 55.63 | 24489116 | |
| 175 | Ubiquitination | VSVMKMDKSPTESYS CEEEECCCCCCCCHH | 55.63 | 23749301 | |
| 176 | Phosphorylation | SVMKMDKSPTESYSD EEEECCCCCCCCHHH | 32.56 | 22369663 | |
| 178 | Phosphorylation | MKMDKSPTESYSDIG EECCCCCCCCHHHCC | 44.66 | 22369663 | |
| 180 | Phosphorylation | MDKSPTESYSDIGGL CCCCCCCCHHHCCCH | 32.20 | 22369663 | |
| 181 | Phosphorylation | DKSPTESYSDIGGLE CCCCCCCHHHCCCHH | 12.25 | 22369663 | |
| 182 | Phosphorylation | KSPTESYSDIGGLES CCCCCCHHHCCCHHH | 31.84 | 22369663 | |
| 189 | Phosphorylation | SDIGGLESQIQEIKE HHCCCHHHHHHHHHH | 37.31 | 22369663 | |
| 195 | Ubiquitination | ESQIQEIKESVELPL HHHHHHHHHHCCCCC | 43.09 | 17644757 | |
| 217 | Ubiquitination | EMGIKPPKGVILYGA HHCCCCCCEEEEEEC | 74.47 | 17644757 | |
| 229 | Ubiquitination | YGAPGTGKTLLAKAV EECCCCCHHHHHHHH | 35.52 | 23749301 | |
| 234 | Ubiquitination | TGKTLLAKAVANQTS CCHHHHHHHHHCCCC | 43.28 | 23749301 | |
| 250 | Phosphorylation | TFLRIVGSELIQKYL HHHHHHCHHHHHHHH | 20.52 | 26447709 | |
| 255 | Ubiquitination | VGSELIQKYLGDGPR HCHHHHHHHHCCCHH | 35.13 | 23749301 | |
| 255 | Acetylation | VGSELIQKYLGDGPR HCHHHHHHHHCCCHH | 35.13 | 24489116 | |
| 256 | Phosphorylation | GSELIQKYLGDGPRL CHHHHHHHHCCCHHH | 10.27 | 26447709 | |
| 269 | Ubiquitination | RLCRQIFKVAGENAP HHHHHHHHHHCCCCC | 32.57 | 23749301 | |
| 290 | Ubiquitination | EIDAIGTKRYDSNSG ECCCCCCCCCCCCCC | 43.69 | 23749301 | |
| 323 | Ubiquitination | FDDRGDVKVIMATNK CCCCCCEEEEEECCC | 30.68 | 17644757 | |
| 330 | Acetylation | KVIMATNKIETLDPA EEEEECCCCCCCCHH | 37.25 | 24489116 | |
| 330 | Ubiquitination | KVIMATNKIETLDPA EEEEECCCCCCCCHH | 37.25 | 23749301 | |
| 347 | Ubiquitination | RPGRIDRKILFENPD CCCCCCCCHHCCCCC | 39.76 | 23749301 | |
| 356 | Phosphorylation | LFENPDLSTKKKILG HCCCCCCCCCCCEEC | 45.63 | 28152593 | |
| 357 | Phosphorylation | FENPDLSTKKKILGI CCCCCCCCCCCEECE | 54.93 | 28889911 | |
| 358 | Ubiquitination | ENPDLSTKKKILGIH CCCCCCCCCCEECEE | 49.01 | 17644757 | |
| 359 | Ubiquitination | NPDLSTKKKILGIHT CCCCCCCCCEECEEC | 45.17 | 17644757 | |
| 360 | Ubiquitination | PDLSTKKKILGIHTS CCCCCCCCEECEECC | 44.73 | 17644757 | |
| 368 | Ubiquitination | ILGIHTSKMNLSEDV EECEECCCCCCCCCC | 32.72 | 17644757 | |
| 417 | Ubiquitination | QVTAEDFKQAKERVM CCCHHHHHHHHHHHH | 62.76 | 23749301 | |
| 417 | Acetylation | QVTAEDFKQAKERVM CCCHHHHHHHHHHHH | 62.76 | 24489116 | |
| 420 | Ubiquitination | AEDFKQAKERVMKNK HHHHHHHHHHHHHHH | 43.49 | 22817900 | |
| 425 | Ubiquitination | QAKERVMKNKVEENL HHHHHHHHHHHHHHC | 51.24 | 23749301 | |
| 427 | Ubiquitination | KERVMKNKVEENLEG HHHHHHHHHHHHCCC | 45.57 | 23749301 |
| 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 PRS4_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PRS4_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 PRS4_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| Myristoylation | |
| Reference | PubMed |
| "N-terminal modifications of the 19S regulatory particle subunits ofthe yeast proteasome."; Kimura Y., Saeki Y., Yokosawa H., Polevoda B., Sherman F., Hirano H.; Arch. Biochem. Biophys. 409:341-348(2003). Cited for: PROTEIN SEQUENCE OF 2-11, AND MYRISTOYLATION AT GLY-2. | |
| 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-176; THR-178; SER-180;TYR-181; SER-182; SER-356 AND THR-357, 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-180, AND MASSSPECTROMETRY. | |
