UniProt ID | VPS27_YEAST | |
---|---|---|
UniProt AC | P40343 | |
Protein Name | Vacuolar protein sorting-associated protein 27 | |
Gene Name | VPS27 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 622 | |
Subcellular Localization |
Endosome membrane Peripheral membrane protein Cytoplasmic side . |
|
Protein Description | Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane. Controls exit from the prevacuolar compartment (PVC) in both the forward direction to the vacuole and the return to the Golgi. Allows VPS10 to return to the (trans-Golgi network) TGN from the PVC. Might also function as an alternate adapter in the COPIb clathrin-like coat.. | |
Protein Sequence | MSVSTPSELDALIEQATSESIPNGDLDLPIALEISDVLRSRRVNPKDSMRCIKKRILNTADNPNTQLSSWKLTNICVKNGGTPFIKEICSREFMDTMEHVILREDSNEELSELVKTILYELYVAFKNDSQLNYVAKVYDKLISRGIKFPEKLTLSNSPTAMFDSKTPADWIDSDACMICSKKFSLLNRKHHCRSCGGVFCQEHSSNSIPLPDLGIYEPVRVCDSCFEDYDLKRHDDSKKSKKHRHKRKKDRDYSTPEDEEELIRKAIELSLKESRNSASSEPIVPVVESKNEVKRQEIEEEEDPDLKAAIQESLREAEEAKLRSERQKASRQMQPQQPSPQPQPIHSVDLSDEEKDSIYMFASLVEKMKSRPLNEILEDSKLQNLAQRVFASKARLNYALNDKAQKYNTLIEMNGKISEIMNIYDRLLEQQLQSINLSQQYTLPQVPSDPYNYLTENVQNPAESYQTPPLQQLSSHQYKPQQDVSRQQSVKANSSPTTNIDHLKTIDVTPHAQQKPQSHVELAPSDPPYPKEEAEDEGTQAVQDEESSTQESRERPYPVETENGETSINKRPQGITRYDFPTVPARKFVQPESTVPLPASSSEIPIKEERPPSPQEELLIEL | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
71 | Ubiquitination | NTQLSSWKLTNICVK CCCCCCEEEECEEHH | 47.59 | 17644757 | |
133 | Phosphorylation | KNDSQLNYVAKVYDK CCHHHHHHHHHHHHH | 15.46 | 28889911 | |
136 | Acetylation | SQLNYVAKVYDKLIS HHHHHHHHHHHHHHH | 31.14 | 24489116 | |
147 | Ubiquitination | KLISRGIKFPEKLTL HHHHCCCCCCCCCCC | 58.66 | 23749301 | |
151 | Ubiquitination | RGIKFPEKLTLSNSP CCCCCCCCCCCCCCC | 47.19 | 23749301 | |
153 | Phosphorylation | IKFPEKLTLSNSPTA CCCCCCCCCCCCCCC | 38.93 | 22369663 | |
155 | Phosphorylation | FPEKLTLSNSPTAMF CCCCCCCCCCCCCCC | 29.99 | 22369663 | |
157 | Phosphorylation | EKLTLSNSPTAMFDS CCCCCCCCCCCCCCC | 21.91 | 22369663 | |
159 | Phosphorylation | LTLSNSPTAMFDSKT CCCCCCCCCCCCCCC | 30.49 | 25521595 | |
164 | Phosphorylation | SPTAMFDSKTPADWI CCCCCCCCCCCCHHC | 27.45 | 19823750 | |
232 | Ubiquitination | CFEDYDLKRHDDSKK CCCCCCCCCCCCCHH | 44.80 | 23749301 | |
253 | Phosphorylation | KRKKDRDYSTPEDEE HHHHCCCCCCCHHHH | 18.48 | 20377248 | |
254 | Phosphorylation | RKKDRDYSTPEDEEE HHHCCCCCCCHHHHH | 41.60 | 24961812 | |
255 | Phosphorylation | KKDRDYSTPEDEEEL HHCCCCCCCHHHHHH | 25.19 | 21440633 | |
272 | Ubiquitination | KAIELSLKESRNSAS HHHHHHHHHHHCCCC | 50.71 | 23749301 | |
274 | Phosphorylation | IELSLKESRNSASSE HHHHHHHHHCCCCCC | 34.86 | 22369663 | |
277 | Phosphorylation | SLKESRNSASSEPIV HHHHHHCCCCCCCCE | 28.55 | 22369663 | |
279 | Phosphorylation | KESRNSASSEPIVPV HHHHCCCCCCCCEEE | 34.75 | 20377248 | |
280 | Phosphorylation | ESRNSASSEPIVPVV HHHCCCCCCCCEEEE | 47.29 | 22369663 | |
289 | Phosphorylation | PIVPVVESKNEVKRQ CCEEEECCCCHHHHH | 29.22 | 22369663 | |
290 | Ubiquitination | IVPVVESKNEVKRQE CEEEECCCCHHHHHH | 43.55 | 23749301 | |
294 | Ubiquitination | VESKNEVKRQEIEEE ECCCCHHHHHHHHHH | 42.03 | 22817900 | |
313 | Phosphorylation | LKAAIQESLREAEEA HHHHHHHHHHHHHHH | 19.15 | 24961812 | |
321 | Ubiquitination | LREAEEAKLRSERQK HHHHHHHHHHHHHHH | 47.95 | 23749301 | |
339 | Phosphorylation | QMQPQQPSPQPQPIH HCCCCCCCCCCCCCC | 31.65 | 22369663 | |
347 | Phosphorylation | PQPQPIHSVDLSDEE CCCCCCCCCCCCHHH | 20.32 | 22369663 | |
351 | Phosphorylation | PIHSVDLSDEEKDSI CCCCCCCCHHHHCHH | 38.21 | 22369663 | |
369 | Ubiquitination | ASLVEKMKSRPLNEI HHHHHHHHCCCHHHH | 55.15 | 17644757 | |
381 | Ubiquitination | NEILEDSKLQNLAQR HHHCCCHHHHHHHHH | 67.43 | 17644757 | |
381 | Acetylation | NEILEDSKLQNLAQR HHHCCCHHHHHHHHH | 67.43 | 24489116 | |
403 | Ubiquitination | LNYALNDKAQKYNTL HHHHHCHHHHHHHHH | 52.20 | 23749301 | |
489 | Phosphorylation | QDVSRQQSVKANSSP HCCCHHHHHHCCCCC | 19.76 | 21551504 | |
494 | Phosphorylation | QQSVKANSSPTTNID HHHHHCCCCCCCCCC | 42.42 | 22369663 | |
495 | Phosphorylation | QSVKANSSPTTNIDH HHHHCCCCCCCCCCC | 26.52 | 22369663 | |
497 | Phosphorylation | VKANSSPTTNIDHLK HHCCCCCCCCCCCEE | 34.13 | 22369663 | |
498 | Phosphorylation | KANSSPTTNIDHLKT HCCCCCCCCCCCEEE | 33.29 | 22369663 | |
509 | Phosphorylation | HLKTIDVTPHAQQKP CEEEEECCCCCCCCC | 12.95 | 29734811 | |
547 | Phosphorylation | QAVQDEESSTQESRE CCCCCCCCCCCCHHC | 36.32 | 29734811 | |
548 | Phosphorylation | AVQDEESSTQESRER CCCCCCCCCCCHHCC | 37.07 | 28889911 | |
549 | Phosphorylation | VQDEESSTQESRERP CCCCCCCCCCHHCCC | 45.71 | 29734811 | |
552 | Phosphorylation | EESSTQESRERPYPV CCCCCCCHHCCCCCC | 29.62 | 20377248 | |
587 | Ubiquitination | FPTVPARKFVQPEST CCCCCCHHCCCCCCC | 52.58 | 15699485 | |
600 | Phosphorylation | STVPLPASSSEIPIK CCCCCCCCCCCCCCC | 32.24 | 23607784 | |
601 | Phosphorylation | TVPLPASSSEIPIKE CCCCCCCCCCCCCCC | 33.81 | 21440633 | |
602 | Phosphorylation | VPLPASSSEIPIKEE CCCCCCCCCCCCCCC | 36.73 | 23607784 | |
613 | Phosphorylation | IKEERPPSPQEELLI CCCCCCCCCCHHHHC | 41.73 | 19823750 |
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 VPS27_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of VPS27_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 VPS27_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-155; SER-157; SER-274;SER-279; SER-280; SER-495; THR-497 AND SER-613, 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-495, 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-157 AND SER-495, ANDMASS SPECTROMETRY. | |
"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-157 AND SER-495, ANDMASS SPECTROMETRY. |