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 | ||
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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 | ||||||
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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. |