| UniProt ID | VPS54_YEAST | |
|---|---|---|
| UniProt AC | Q12071 | |
| Protein Name | Vacuolar protein sorting-associated protein 54 | |
| Gene Name | VPS54 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 889 | |
| Subcellular Localization |
Golgi apparatus, trans-Golgi network membrane Peripheral membrane protein. Endosome membrane Peripheral membrane protein. Mitochondrion membrane Peripheral membrane protein . May also be mitochondrial. |
|
| Protein Description | Involved in retrograde transport from early and late endosomes to late Golgi by linking the vesicle through the t-SNARE TGL1 to the Golgi, leading to the membrane fusion between late Golgi and endosomal vesicles. Seems also to be involved in protein transport from Golgi to the plasma membrane and is required for the integrity of the actin cytoskeleton.. | |
| Protein Sequence | MSISETPHNKSQGLQKAAGRPKIVVPEGSPSRNSDSGSFTIEGDTSLNDDLLSISGSVTPRARRSSRLSLDSITPRRSFDSRTLSVANSRSFGFENETHSGSMDFSPLGNNSIYEIVMNTRRKNWLNYPTVADIPQVSLSKNDLDDHWKTHVIEYVKNIKSDYQIFQSTNNIRNMNQMEQLKELREGENMHEESFEANLRQGDAELINSIPDFYFSDKFQLDNPRTFHKVLDAIDLFLTKLDMKRQAERDEAFSELRDRLNDFLDIVETLLVTEISKSSHKFFHALSEVDNIQKRALDTMSELKELAQNIKTIDAENIRKKISHLEMIFKRKNVEKLEQGLLQAKLVLNKTDECKSMYEENKLDNCLELIKSIDYLIKGDDSINEDVQSWTRCWPYKLSNLRTIPALSATREFLTNMKIEIGGKFSLQLSILLIDDLRSFCKSIKPKETLHRIQTGSNDKKQTIFTDNFSSKITELIVRLNRCEELTSAFDLYREKSITELKSIIKIYLPTENAHADNNHDEKHLNNGSTSGSKLSRLIKEQTPAEFQSMLVNIFTHALEALRRLYGHQKLLLDISLNELASVKSPNENQHNMITQLDIRTGINEIIRIIQLRTGKIIAVRRELNLSLRYDYFLKFYAICVIFIQECEVLSGEFLTKYLSNVLASQIKHYANAQSSKNYRNIKKKIDAEEWIPYIVDSSIQSDVNDIVSSIDIDPLSWTTILDMVGGSHDCENGRSEDKEKDEGNETYQGHRKSVVVGDKTFVASSSLLATIEVIKELMVLSINLPSIYLSNFEKLCYDALQYYNSSAMASVTQPGNSLLKTGRNLSIMGESLDCLAEFVIIVQRFYQRLSNSNRDFEPFDASHYTTLLGQFQASSNKIYMANAPPPPV | |
| 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 | Phosphorylation | ------MSISETPHN ------CCCCCCCCC | 34.52 | 22369663 | |
| 4 | Phosphorylation | ----MSISETPHNKS ----CCCCCCCCCHH | 28.27 | 22369663 | |
| 6 | Phosphorylation | --MSISETPHNKSQG --CCCCCCCCCHHHH | 24.05 | 22369663 | |
| 29 | Phosphorylation | KIVVPEGSPSRNSDS CEECCCCCCCCCCCC | 20.31 | 22369663 | |
| 31 | Phosphorylation | VVPEGSPSRNSDSGS ECCCCCCCCCCCCCC | 45.88 | 22369663 | |
| 65 | Phosphorylation | VTPRARRSSRLSLDS CCHHHHHCCCCCCCC | 17.79 | 22369663 | |
| 66 | Phosphorylation | TPRARRSSRLSLDSI CHHHHHCCCCCCCCC | 35.11 | 22369663 | |
| 69 | Phosphorylation | ARRSSRLSLDSITPR HHHCCCCCCCCCCCC | 29.08 | 22369663 | |
| 72 | Phosphorylation | SSRLSLDSITPRRSF CCCCCCCCCCCCCCC | 33.39 | 22369663 | |
| 74 | Phosphorylation | RLSLDSITPRRSFDS CCCCCCCCCCCCCCC | 18.07 | 22369663 | |
| 78 | Phosphorylation | DSITPRRSFDSRTLS CCCCCCCCCCCCCEE | 34.38 | 21440633 | |
| 83 | Phosphorylation | RRSFDSRTLSVANSR CCCCCCCCEEEECCC | 27.60 | 22369663 | |
| 85 | Phosphorylation | SFDSRTLSVANSRSF CCCCCCEEEECCCCC | 20.69 | 22369663 | |
| 89 | Phosphorylation | RTLSVANSRSFGFEN CCEEEECCCCCCCCC | 21.40 | 22369663 | |
| 194 | Phosphorylation | GENMHEESFEANLRQ CCCCCHHHHHHHHHH | 25.96 | 30377154 | |
| 463 | Phosphorylation | GSNDKKQTIFTDNFS CCCCCCCEEECCCHH | 27.26 | 21440633 | |
| 470 | Phosphorylation | TIFTDNFSSKITELI EEECCCHHHHHHHHH | 36.66 | 21440633 | |
| 497 | Phosphorylation | FDLYREKSITELKSI HHHHHHCCHHHHHHH | 29.95 | 19823750 | |
| 499 | Phosphorylation | LYREKSITELKSIIK HHHHCCHHHHHHHEE | 42.21 | 19823750 | |
| 502 | Acetylation | EKSITELKSIIKIYL HCCHHHHHHHEEEEC | 33.12 | 24489116 | |
| 503 | Phosphorylation | KSITELKSIIKIYLP CCHHHHHHHEEEECC | 42.02 | 19823750 | |
| 523 | Acetylation | ADNNHDEKHLNNGST CCCCCCHHCCCCCCC | 60.49 | 24489116 | |
| 601 | Phosphorylation | ITQLDIRTGINEIIR HHHHHHHHCHHHHHH | 42.63 | 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 VPS54_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of VPS54_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 VPS54_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-29; SER-69 AND THR-74,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-69, AND MASSSPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69 AND SER-72, AND MASSSPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-69, AND MASSSPECTROMETRY. | |
