| UniProt ID | VID30_YEAST | |
|---|---|---|
| UniProt AC | P53076 | |
| Protein Name | Vacuolar import and degradation protein 30 | |
| Gene Name | VID30 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 958 | |
| Subcellular Localization | Nucleus . Cytoplasm . | |
| Protein Description | Has a role in the negative regulation of gluconeogenesis. Required for both proteasome-dependent and vacuolar catabolite degradation of fructose-1,6-bisphosphatase (FBPase).. | |
| Protein Sequence | MSEYMDDVDREFINCLFPSYLLQQPVAYDLWILYLQHRKLFHKLKNTNLINADENPTGVGMGRTKLTALTRKEIWSKLMNLGVLGTISFEAVNDDYLIQVYKYFYPDVNDFTLRFGVKDSNKNSVRVMKASSDMRKNAQELLEPVLSEREMALNSNTSLENDRNDDDDDDDDDDDDDDDDDDDDDESDLESLEGEVDTDTDDNNEGDGSDNHEEGGEEGSRGADADVSSAQQRAERVADPWIYQRSRSAINIETESRNLWDTSDKNSGLQYYPPDQSPSSSFSSPRVSSGNDKNDNEATNVLSNSGSKKKNSMIPDIYKILGYFLPSRWQAQPNNSLQLSQDGITHLQPNPDYHSYMTYERSSASSASTRNRLRTSFENSGKVDFAVTWANKSLPDNKLTIFYYEIKVLSVTSTESAENSNIVIGYKLVENELMEATTKKSVSRSSVAGSSSSLGGSNNMSSNRVPSTSFTMEGTQRRDYIYEGGVSAMSLNVDGSINKCQKYGFDLNVFGYCGFDGLITNSTEQSKEYAKPFGRDDVIGCGINFIDGSIFFTKNGIHLGNAFTDLNDLEFVPYVALRPGNSIKTNFGLNEDFVFDIIGYQDKWKSLAYEHICRGRQMDVSIEEFDSDESEEDETENGPEENKSTNVNEDLMDIDQEDGAAGNKDTKKLNDEKDNNLKFLLGEDNRFIDGKLVRPDVNNINNLSVDDGSLPNTLNVMINDYLIHEGLVDVAKGFLKDLQKDAVNVNGQHSESKDVIRHNERQIMKEERMVKIRQELRYLINKGQISKCINYIDNEIPDLLKNNLELVFELKLANYLVMIKKSSSKDDDEIENLILKGQELSNEFIYDTKIPQSLRDRFSGQLSNVSALLAYSNPLVEAPKEISGYLSDEYLQERLFQVSNNTILTFLHKDSECALENVISNTRAMLSTLLEYNAFGSTNSSDPRYYKAINFDEDVLNL | |
| 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 | ------MSEYMDDVD ------CCCCHHHCC | 37.12 | 22814378 | |
| 64 | Phosphorylation | TGVGMGRTKLTALTR CCCCCCHHHHHHHHH | 25.36 | 26447709 | |
| 67 | Phosphorylation | GMGRTKLTALTRKEI CCCHHHHHHHHHHHH | 22.60 | 21551504 | |
| 70 | Phosphorylation | RTKLTALTRKEIWSK HHHHHHHHHHHHHHH | 36.91 | 21551504 | |
| 76 | Phosphorylation | LTRKEIWSKLMNLGV HHHHHHHHHHHHCCC | 22.90 | 21551504 | |
| 147 | Phosphorylation | ELLEPVLSEREMALN HHHHHHHCHHHHHHC | 34.54 | 22369663 | |
| 157 | Phosphorylation | EMALNSNTSLENDRN HHHHCCCCCCCCCCC | 34.21 | 29688323 | |
| 158 | Phosphorylation | MALNSNTSLENDRND HHHCCCCCCCCCCCC | 37.63 | 29688323 | |
| 228 | Phosphorylation | RGADADVSSAQQRAE CCCCCCCCHHHHHHH | 22.09 | 28889911 | |
| 229 | Phosphorylation | GADADVSSAQQRAER CCCCCCCHHHHHHHH | 29.91 | 25752575 | |
| 246 | Phosphorylation | DPWIYQRSRSAINIE CHHHHHHHHCCCCCE | 18.30 | 22369663 | |
| 248 | Phosphorylation | WIYQRSRSAINIETE HHHHHHHCCCCCEEC | 34.44 | 22369663 | |
| 277 | Phosphorylation | QYYPPDQSPSSSFSS CCCCCCCCCCCCCCC | 33.84 | 21551504 | |
| 279 | Phosphorylation | YPPDQSPSSSFSSPR CCCCCCCCCCCCCCC | 43.81 | 21440633 | |
| 280 | Phosphorylation | PPDQSPSSSFSSPRV CCCCCCCCCCCCCCC | 38.49 | 19779198 | |
| 281 | Phosphorylation | PDQSPSSSFSSPRVS CCCCCCCCCCCCCCC | 33.22 | 25752575 | |
| 283 | Phosphorylation | QSPSSSFSSPRVSSG CCCCCCCCCCCCCCC | 41.18 | 21440633 | |
| 284 | Phosphorylation | SPSSSFSSPRVSSGN CCCCCCCCCCCCCCC | 18.08 | 28889911 | |
| 288 | Phosphorylation | SFSSPRVSSGNDKND CCCCCCCCCCCCCCC | 33.53 | 23749301 | |
| 289 | Phosphorylation | FSSPRVSSGNDKNDN CCCCCCCCCCCCCCC | 38.47 | 21440633 | |
| 293 | Ubiquitination | RVSSGNDKNDNEATN CCCCCCCCCCCHHHH | 70.92 | 23749301 | |
| 303 | Phosphorylation | NEATNVLSNSGSKKK CHHHHHHCCCCCCCC | 25.35 | 23749301 | |
| 375 | Phosphorylation | STRNRLRTSFENSGK HHHHHHHHHHHCCCC | 42.22 | 28889911 | |
| 376 | Phosphorylation | TRNRLRTSFENSGKV HHHHHHHHHHCCCCE | 24.91 | 23749301 | |
| 438 | Phosphorylation | NELMEATTKKSVSRS HHHHHHHCCCCCCHH | 43.45 | 27017623 | |
| 441 | Phosphorylation | MEATTKKSVSRSSVA HHHHCCCCCCHHHCC | 27.21 | 27017623 | |
| 443 | Phosphorylation | ATTKKSVSRSSVAGS HHCCCCCCHHHCCCC | 33.27 | 28889911 | |
| 445 | Phosphorylation | TKKSVSRSSVAGSSS CCCCCCHHHCCCCCC | 22.97 | 19779198 | |
| 446 | Phosphorylation | KKSVSRSSVAGSSSS CCCCCHHHCCCCCCC | 18.18 | 19779198 | |
| 450 | Phosphorylation | SRSSVAGSSSSLGGS CHHHCCCCCCCCCCC | 19.80 | 28889911 | |
| 451 | Phosphorylation | RSSVAGSSSSLGGSN HHHCCCCCCCCCCCC | 24.03 | 30377154 | |
| 452 | Phosphorylation | SSVAGSSSSLGGSNN HHCCCCCCCCCCCCC | 31.14 | 30377154 | |
| 453 | Phosphorylation | SVAGSSSSLGGSNNM HCCCCCCCCCCCCCC | 32.74 | 28889911 | |
| 461 | Phosphorylation | LGGSNNMSSNRVPST CCCCCCCCCCCCCCC | 26.95 | 21440633 | |
| 467 | Phosphorylation | MSSNRVPSTSFTMEG CCCCCCCCCCEEECC | 33.55 | 23749301 | |
| 468 | Phosphorylation | SSNRVPSTSFTMEGT CCCCCCCCCEEECCC | 23.07 | 30377154 | |
| 469 | Phosphorylation | SNRVPSTSFTMEGTQ CCCCCCCCEEECCCC | 24.06 | 28889911 | |
| 471 | Phosphorylation | RVPSTSFTMEGTQRR CCCCCCEEECCCCCC | 17.68 | 23749301 | |
| 475 | Phosphorylation | TSFTMEGTQRRDYIY CCEEECCCCCCEEEE | 12.95 | 27017623 | |
| 480 | Phosphorylation | EGTQRRDYIYEGGVS CCCCCCEEEEECCEE | 12.00 | 26447709 | |
| 482 | Phosphorylation | TQRRDYIYEGGVSAM CCCCEEEEECCEEEE | 11.42 | 26447709 | |
| 487 | Phosphorylation | YIYEGGVSAMSLNVD EEEECCEEEEEEECC | 22.87 | 26447709 | |
| 490 | Phosphorylation | EGGVSAMSLNVDGSI ECCEEEEEEECCCCH | 19.26 | 26447709 | |
| 496 | Phosphorylation | MSLNVDGSINKCQKY EEEECCCCHHHHHHC | 20.65 | 26447709 | |
| 529 | Phosphorylation | STEQSKEYAKPFGRD CHHHHHHHHCCCCCC | 24.54 | 29688323 | |
| 627 | Phosphorylation | VSIEEFDSDESEEDE EEHHHCCCCCCCCCC | 48.90 | 19795423 | |
| 630 | Phosphorylation | EEFDSDESEEDETEN HHCCCCCCCCCCCCC | 51.80 | 19795423 | |
| 920 | Phosphorylation | CALENVISNTRAMLS HHHHHHHHHHHHHHH | 28.06 | 27214570 |
| 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 VID30_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of VID30_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 VID30_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-147; SER-246; SER-248;SER-277; SER-453 AND SER-469, 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-147 AND SER-248, ANDMASS SPECTROMETRY. | |
