| UniProt ID | VID22_YEAST | |
|---|---|---|
| UniProt AC | Q05934 | |
| Protein Name | Vacuolar import and degradation protein 22 | |
| Gene Name | VID22 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 901 | |
| Subcellular Localization |
Cell membrane Single-pass membrane protein. Nucleus. |
|
| Protein Description | Has a role in the negative regulation of gluconeogenesis. Imports fructose-1,6-bisphosphatase (FBPase) into the intermediate vacuole import and degradation (Vid) vesicles. This is an indirect role and requires cyclophilin A.. | |
| Protein Sequence | MRAMDTQVQSAERGLVLPPMNSTVSSATAATTATNTDTDTDGDRDEERESLAEDGSEWVPAYMLTRDRSRYLGHFLGVDKMLEAVKCKYCGVIIRRQGNSISMAEASQTHLWSTHKIDPNANYYSGWTGVEAGSTFMVRPPLKNHQGGSATTNSIANLLEIDEDFLKRTREKEMALPLVQSLAIIIASENLPLSFVDNTAVRLLINQNANSLSFIDHDLILNAIRSIAYNLDRIIQRTALRNNSDLSLIIDKNYLLMDPTDRSNQLSNRLKNQLFEMQKINFFSLSHSVWNNTISILSIQYYDDFHSQVKTLPLIIQNLHEYNNDPKLSIPAQLLKISQELPGLQNTVISITLPRSQIVDLLNVMDSQPFFPNTYTNAKNYYHNCIISIINSAILPLFGTPKSADITHPRQSSFSKEPLTLLDSLIDLSNIDISNSIFSRINSFLDDLQSNSWQLDKFRSLCEKFGFEFVCSKFDLSRYSTATVSLQTFLNLRPIIEEYQSSIQIEKFNEIDFQIIDYLLITLNSINRILKFFTSSKSLNFTYVLFAIMSIEKHLLSTLGSLQFQRLIAPFETFLSKIQEFKTILFSDDMNLLAMFLCPAILFEREVLEYSFHTISLSEIVDKLSTSIFSLLKRFLNLHTIGNVNNSHNTSNHSNMNIHTDNQTNNINNRSGNNSDNNDNEHDNDNDNHSNSNTPASRIDIDPTGGENSVLPEQQPQNSNNNLSFGSLSDTHHLSDSTISKEIDSIFLQIIQEDLYDYLSTVNSIVPISYRSYCEQSNFIRDSGRFKKRIITEDSIIGELEQPMNFIEELLDIHVPVCNAFWSQYLDNDAGPIIRILFKIMQCQSSSSIRGEYSFLNDFIPRVHPDLTQEIIKIKLFNDQFVASKVDYDLDTLQTASQYLP | |
| 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 |
|---|---|---|---|---|---|
| 10 | Phosphorylation | AMDTQVQSAERGLVL CCHHHHHHHHCCCCC | 32.99 | 30377154 | |
| 21 | N-linked_Glycosylation | GLVLPPMNSTVSSAT CCCCCCCCCCCCCCC | 40.06 | - | |
| 22 | Phosphorylation | LVLPPMNSTVSSATA CCCCCCCCCCCCCCC | 24.76 | 19779198 | |
| 32 | Phosphorylation | SSATAATTATNTDTD CCCCCCCCCCCCCCC | 27.10 | 19779198 | |
| 34 | Phosphorylation | ATAATTATNTDTDTD CCCCCCCCCCCCCCC | 36.24 | 19779198 | |
| 36 | Phosphorylation | AATTATNTDTDTDGD CCCCCCCCCCCCCCC | 35.60 | 19779198 | |
| 38 | Phosphorylation | TTATNTDTDTDGDRD CCCCCCCCCCCCCCH | 38.47 | 19779198 | |
| 40 | Phosphorylation | ATNTDTDTDGDRDEE CCCCCCCCCCCCHHH | 43.93 | 19779198 | |
| 149 | Phosphorylation | LKNHQGGSATTNSIA CCCCCCCCCCHHHHH | 29.30 | 30377154 | |
| 151 | Phosphorylation | NHQGGSATTNSIANL CCCCCCCCHHHHHHH | 28.36 | 21440633 | |
| 242 | N-linked_Glycosylation | IQRTALRNNSDLSLI HHHHHHHCCCCCEEE | 53.89 | - | |
| 244 | Phosphorylation | RTALRNNSDLSLIID HHHHHCCCCCEEEEC | 43.40 | 30377154 | |
| 291 | N-linked_Glycosylation | SLSHSVWNNTISILS EECHHHHCCCEEEEE | 33.34 | - | |
| 538 | Phosphorylation | KFFTSSKSLNFTYVL HHHHCCCCCCHHHHH | 30.41 | 21126336 | |
| 540 | N-linked_Glycosylation | FTSSKSLNFTYVLFA HHCCCCCCHHHHHHH | 34.01 | - | |
| 645 | N-linked_Glycosylation | LHTIGNVNNSHNTSN CCCCCCCCCCCCCCC | 48.57 | - | |
| 649 | N-linked_Glycosylation | GNVNNSHNTSNHSNM CCCCCCCCCCCCCCE | 45.05 | - | |
| 652 | N-linked_Glycosylation | NNSHNTSNHSNMNIH CCCCCCCCCCCEEEE | 40.34 | - | |
| 662 | N-linked_Glycosylation | NMNIHTDNQTNNINN CEEEECCCCCCCCCC | 52.29 | - | |
| 669 | N-linked_Glycosylation | NQTNNINNRSGNNSD CCCCCCCCCCCCCCC | 35.38 | - | |
| 671 | Phosphorylation | TNNINNRSGNNSDNN CCCCCCCCCCCCCCC | 48.25 | 17563356 | |
| 673 | N-linked_Glycosylation | NINNRSGNNSDNNDN CCCCCCCCCCCCCCC | 46.18 | - | |
| 675 | Phosphorylation | NNRSGNNSDNNDNEH CCCCCCCCCCCCCCC | 45.79 | 17563356 | |
| 688 | N-linked_Glycosylation | EHDNDNDNHSNSNTP CCCCCCCCCCCCCCC | 46.90 | - | |
| 690 | Phosphorylation | DNDNDNHSNSNTPAS CCCCCCCCCCCCCHH | 48.48 | 17563356 | |
| 719 | Phosphorylation | PEQQPQNSNNNLSFG CCCCCCCCCCCCCCC | 35.37 | 30377154 | |
| 722 | N-linked_Glycosylation | QPQNSNNNLSFGSLS CCCCCCCCCCCCCCC | 41.11 | - | |
| 724 | Phosphorylation | QNSNNNLSFGSLSDT CCCCCCCCCCCCCCC | 29.68 | 30377154 | |
| 727 | Phosphorylation | NNNLSFGSLSDTHHL CCCCCCCCCCCCCCC | 23.77 | 30377154 | |
| 845 | Phosphorylation | FKIMQCQSSSSIRGE HHHHHCCCCCCCCCC | 39.55 | 29136822 | |
| 846 | Phosphorylation | KIMQCQSSSSIRGEY HHHHCCCCCCCCCCH | 11.39 | 29136822 | |
| 847 | Phosphorylation | IMQCQSSSSIRGEYS HHHCCCCCCCCCCHH | 34.72 | 29136822 | |
| 848 | Phosphorylation | MQCQSSSSIRGEYSF HHCCCCCCCCCCHHH | 20.46 | 27017623 |
| 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 VID22_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of VID22_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 VID22_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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-671; SER-675 ANDSER-690, AND MASS SPECTROMETRY. | |