| UniProt ID | VPS72_YEAST | |
|---|---|---|
| UniProt AC | Q03388 | |
| Protein Name | Vacuolar protein sorting-associated protein 72 | |
| Gene Name | VPS72 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 795 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Participates in the catalytic exchange of histone H2A for the H2A variant HTZ1, an euchromatin-specific factor, leading to chromatin remodeling and changes in transcription of targeted genes. Indirectly involved in vacuolar protein sorting.. | |
| Protein Sequence | MSDEGADKSLDTNTEFIIQTRSRRSNAGNKLQKLLEQELRDIESTKRQISSYKNGNDDEEDEIGLLFQEDEDDEDFEMMAKDDDDEGEEKEDETQSIRKEPSQASSEQAADDLMFSSSESEDSSNENDEDAEEKEIRRQELLSRKKRNKRLQKGPVVIKKQKPKPKSGEAIPRSHHTHEQLNAETLLLNTRRTSKRSSVMENTMKVYEKLSKAEKKRKIIQERIRKHKEQESQHMLTQEERLRIAKETEKLNILSLDKFKEQEVWKKENRLALQKRQKQKFQPNETILQFLSTAWLMTPAMELEDRKYWQEQLNKRDKKKKKYPRKPKKNLNLGKQDASDDKKRESEESIKNDGDVNSLGENSSSVHNQKRIEETSTNDTVEGESSPDAAVSRVNSDELKPTALPDVTLDAIANKQSTVDEAPNSQPQKNIITNEQKITNVGEPIQNLHNEEIKDEMVSALESRENTFENSSPAAQVVSQRDNSATPTPSNSTGTEDTILISPDTDIKGEPEPCLKTEGIENLSHNVPQETKSNTDVSFLKQVTFTDHPQVAIIDTEESPSKKDTANVDESSAENSLSTQTYEGPEQLTSRNFVTLYDFPNAPPNLKDFNTNLFGDRWSYTNGLSATQRPQDMKTVFHSILPSPPQSSVPSPTVDISLDLSALANFPSFGEYDKKIVHQINTEINKDLEIKIKTQPPTGVFLANGIRKKCLITNKECQYFDPRTGVPYSDVEAYKIIQRIQDPISKEEGRSDIKRDETTNEDSDDQVRFKWFGFKNGGIYLDLSQRPAKGVPEGF | |
| 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 |
|---|---|---|---|---|---|
| 33 | Acetylation | NAGNKLQKLLEQELR CHHHHHHHHHHHHHH | 66.53 | 24489116 | |
| 94 | Phosphorylation | GEEKEDETQSIRKEP CCCCHHHHHHHHHCC | 39.68 | 21551504 | |
| 96 | Phosphorylation | EKEDETQSIRKEPSQ CCHHHHHHHHHCCCH | 31.61 | 27717283 | |
| 198 | Phosphorylation | RRTSKRSSVMENTMK CCHHCCHHHHHHHHH | 29.53 | 23749301 | |
| 207 | Phosphorylation | MENTMKVYEKLSKAE HHHHHHHHHHHHHHH | 11.22 | 27017623 | |
| 211 | Phosphorylation | MKVYEKLSKAEKKRK HHHHHHHHHHHHHHH | 40.67 | 27017623 | |
| 358 | Phosphorylation | KNDGDVNSLGENSSS CCCCCCCCCCCCCCH | 37.28 | 21551504 | |
| 385 | Phosphorylation | NDTVEGESSPDAAVS CCCCCCCCCCCHHHH | 59.01 | 23749301 | |
| 386 | Phosphorylation | DTVEGESSPDAAVSR CCCCCCCCCCHHHHC | 23.61 | 22369663 | |
| 396 | Phosphorylation | AAVSRVNSDELKPTA HHHHCCCCCCCCCCC | 29.61 | 17563356 | |
| 417 | Phosphorylation | DAIANKQSTVDEAPN HHHHCCCCCCCCCCC | 31.82 | 30377154 | |
| 425 | Phosphorylation | TVDEAPNSQPQKNII CCCCCCCCCCCCCCC | 42.02 | 25752575 | |
| 429 | Ubiquitination | APNSQPQKNIITNEQ CCCCCCCCCCCCCCH | 57.72 | 15699485 | |
| 437 | Ubiquitination | NIITNEQKITNVGEP CCCCCCHHHCCCCHH | 45.37 | 15699485 | |
| 463 | Phosphorylation | EMVSALESRENTFEN HHHHHHHHCCCCCCC | 45.83 | 28889911 | |
| 467 | Phosphorylation | ALESRENTFENSSPA HHHHCCCCCCCCCCH | 27.81 | 28889911 | |
| 471 | Phosphorylation | RENTFENSSPAAQVV CCCCCCCCCCHHHHH | 30.42 | 23749301 | |
| 472 | Phosphorylation | ENTFENSSPAAQVVS CCCCCCCCCHHHHHC | 30.09 | 21082442 | |
| 502 | Phosphorylation | TEDTILISPDTDIKG CCCEEEECCCCCCCC | 17.18 | 28889911 | |
| 533 | Phosphorylation | NVPQETKSNTDVSFL CCCCCCCCCCCCHHH | 53.00 | 22369663 | |
| 535 | Phosphorylation | PQETKSNTDVSFLKQ CCCCCCCCCCHHHHC | 44.89 | 22369663 | |
| 538 | Phosphorylation | TKSNTDVSFLKQVTF CCCCCCCHHHHCCCC | 27.89 | 21440633 | |
| 556 | Phosphorylation | PQVAIIDTEESPSKK CCEEEEECCCCCCCC | 31.10 | 24961812 | |
| 559 | Phosphorylation | AIIDTEESPSKKDTA EEEECCCCCCCCCCC | 28.39 | 20377248 | |
| 561 | Phosphorylation | IDTEESPSKKDTANV EECCCCCCCCCCCCC | 62.71 | 24961812 | |
| 565 | Phosphorylation | ESPSKKDTANVDESS CCCCCCCCCCCCHHH | 29.07 | 27017623 | |
| 581 | Phosphorylation | ENSLSTQTYEGPEQL HHCCCCCCCCCHHHH | 24.51 | 27017623 | |
| 715 | Ubiquitination | KKCLITNKECQYFDP EEEEECCCCCCCCCC | 51.74 | 15699485 | |
| 770 | Acetylation | SDDQVRFKWFGFKNG CCCCEEEEEEEECCC | 30.92 | 24489116 |
| 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 VPS72_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of VPS72_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 VPS72_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-396; SER-425; SER-471;SER-472; SER-502 AND SER-538, 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-396, AND MASSSPECTROMETRY. | |
