UniProt ID | CHS5_YEAST | |
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UniProt AC | Q12114 | |
Protein Name | Chitin biosynthesis protein CHS5 | |
Gene Name | CHS5 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 671 | |
Subcellular Localization |
Golgi apparatus, trans-Golgi network membrane Peripheral membrane protein . Trans-Golgi network location requires interaction with myristoylated GTP-bound ARF1 for the recruitment to the membranes. |
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Protein Description | Component of the CHS5/6 complex which mediates export of specific cargo proteins, including chitin synthase CHS3. Also involved in targeting FUS1 to sites of polarized growth.. | |
Protein Sequence | MSSVDVLLTVGKLDASLALLTTQDHHVIEFPTVLLPENVKAGSIIKMQVSQNLEEEKKQRNHFKSIQAKILEKYGTHKPESPVLKIVNVTQTSCVLAWDPLKLGSAKLKSLILYRKGIRSMVIPNPFKVTTTKISGLSVDTPYEFQLKLITTSGTLWSEKVILRTHKMTDMSGITVCLGPLDPLKEISDLQISQCLSHIGARPLQRHVAIDTTHFVCNDLDNEESNEELIRAKHNNIPIVRPEWVRACEVEKRIVGVRGFYLDADQSILKNYTFPPVNEEELSYSKENEPVAEVADENKMPEDTTDVEQVASPNDNESNPSEAKEQGEKSGHETAPVSPVEDPLHASTALENETTIETVNPSVRSLKSEPVGTPNIEENKADSSAEAVVEEPNEAVAESSPNEEATGQKSEDTDTHSNEQADNGFVQTEEVAENNITTESAGENNEPADDAAMEFGRPEAEIETPEVNESIEDANEPAEDSNEPVEDSNKPVKDSNKPVEDSNKPVEDSNKPVEDSNKPVEDANEPVEDTSEPVEDAGEPVQETNEFTTDIASPRHQEEDIELEAEPKDATESVAVEPSNEDVKPEEKGSEAEDDINNVSKEAASGESTTHQKTEASASLESSAVTEEQETTEAEVNTDDVLSTKEAKKNTGNSNSNKKKNKKNKKKGKKK | |
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 |
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73 | Acetylation | IQAKILEKYGTHKPE HHHHHHHHHCCCCCC | 45.60 | 24489116 | |
74 | Phosphorylation | QAKILEKYGTHKPES HHHHHHHHCCCCCCC | 20.20 | 22369663 | |
76 | Phosphorylation | KILEKYGTHKPESPV HHHHHHCCCCCCCCE | 24.52 | 22369663 | |
81 | Phosphorylation | YGTHKPESPVLKIVN HCCCCCCCCEEEEEE | 28.92 | 21440633 | |
120 | Phosphorylation | LYRKGIRSMVIPNPF HHHCCCCCEECCCCC | 18.58 | 21440633 | |
283 | Phosphorylation | PVNEEELSYSKENEP CCCHHHHCCCCCCCC | 30.55 | 28152593 | |
284 | Phosphorylation | VNEEELSYSKENEPV CCHHHHCCCCCCCCH | 36.06 | 21440633 | |
299 | Ubiquitination | AEVADENKMPEDTTD HHHCCCCCCCCCCCC | 54.51 | 23749301 | |
304 | Phosphorylation | ENKMPEDTTDVEQVA CCCCCCCCCCHHHHC | 24.19 | 20377248 | |
305 | Phosphorylation | NKMPEDTTDVEQVAS CCCCCCCCCHHHHCC | 50.82 | 21440633 | |
312 | Phosphorylation | TDVEQVASPNDNESN CCHHHHCCCCCCCCC | 25.94 | 20377248 | |
318 | Phosphorylation | ASPNDNESNPSEAKE CCCCCCCCCHHHHHH | 61.36 | 25521595 | |
321 | Phosphorylation | NDNESNPSEAKEQGE CCCCCCHHHHHHHHH | 55.21 | 28152593 | |
330 | Phosphorylation | AKEQGEKSGHETAPV HHHHHHHCCCCCCCC | 40.87 | 20377248 | |
334 | Phosphorylation | GEKSGHETAPVSPVE HHHCCCCCCCCCCCC | 30.50 | 22369663 | |
338 | Phosphorylation | GHETAPVSPVEDPLH CCCCCCCCCCCCCCC | 23.36 | 22369663 | |
347 | Phosphorylation | VEDPLHASTALENET CCCCCCCCHHCCCCC | 11.94 | 20377248 | |
348 | Phosphorylation | EDPLHASTALENETT CCCCCCCHHCCCCCE | 35.72 | 20377248 | |
354 | Phosphorylation | STALENETTIETVNP CHHCCCCCEEEECCH | 44.66 | 23749301 | |
355 | Phosphorylation | TALENETTIETVNPS HHCCCCCEEEECCHH | 15.61 | 20377248 | |
358 | Phosphorylation | ENETTIETVNPSVRS CCCCEEEECCHHHHH | 23.02 | 22369663 | |
362 | Phosphorylation | TIETVNPSVRSLKSE EEEECCHHHHHHCCC | 25.59 | 22369663 | |
365 | Phosphorylation | TVNPSVRSLKSEPVG ECCHHHHHHCCCCCC | 37.68 | 22369663 | |
368 | Phosphorylation | PSVRSLKSEPVGTPN HHHHHHCCCCCCCCC | 53.04 | 22369663 | |
373 | Phosphorylation | LKSEPVGTPNIEENK HCCCCCCCCCCCCCC | 17.25 | 22369663 | |
383 | Phosphorylation | IEENKADSSAEAVVE CCCCCCCCCCCHHHC | 35.99 | 22369663 | |
384 | Phosphorylation | EENKADSSAEAVVEE CCCCCCCCCCHHHCC | 30.58 | 22369663 | |
399 | Phosphorylation | PNEAVAESSPNEEAT CCHHHHHCCCCCCCC | 41.16 | 22369663 | |
400 | Phosphorylation | NEAVAESSPNEEATG CHHHHHCCCCCCCCC | 24.21 | 24961812 | |
406 | Phosphorylation | SSPNEEATGQKSEDT CCCCCCCCCCCCCCC | 43.34 | 24961812 | |
553 | Phosphorylation | EFTTDIASPRHQEED CEECCCCCCCCCCCC | 23.85 | 27214570 | |
571 | Phosphorylation | EAEPKDATESVAVEP ECCCCCCCCCEECCC | 38.64 | 22890988 | |
573 | Phosphorylation | EPKDATESVAVEPSN CCCCCCCCEECCCCC | 15.83 | 22369663 | |
579 | Phosphorylation | ESVAVEPSNEDVKPE CCEECCCCCCCCCHH | 39.07 | 22369663 | |
584 | Ubiquitination | EPSNEDVKPEEKGSE CCCCCCCCHHHCCCC | 60.06 | 23749301 | |
584 | Acetylation | EPSNEDVKPEEKGSE CCCCCCCCHHHCCCC | 60.06 | 24489116 | |
588 | Ubiquitination | EDVKPEEKGSEAEDD CCCCHHHCCCCCHHH | 67.10 | 23749301 | |
590 | Phosphorylation | VKPEEKGSEAEDDIN CCHHHCCCCCHHHHH | 44.71 | 22369663 | |
600 | Phosphorylation | EDDINNVSKEAASGE HHHHHHHCHHHHCCC | 27.23 | 22890988 | |
601 | Acetylation | DDINNVSKEAASGES HHHHHHCHHHHCCCC | 47.27 | 24489116 | |
605 | Phosphorylation | NVSKEAASGESTTHQ HHCHHHHCCCCCHHH | 50.57 | 28889911 | |
608 | Phosphorylation | KEAASGESTTHQKTE HHHHCCCCCHHHHHH | 41.97 | 28889911 | |
609 | Phosphorylation | EAASGESTTHQKTEA HHHCCCCCHHHHHHH | 24.80 | 28889911 | |
610 | Phosphorylation | AASGESTTHQKTEAS HHCCCCCHHHHHHHH | 31.43 | 27717283 | |
631 | Phosphorylation | AVTEEQETTEAEVNT CCCCHHHHCEEEECH | 29.63 | 24961812 | |
632 | Phosphorylation | VTEEQETTEAEVNTD CCCHHHHCEEEECHH | 32.23 | 24961812 | |
638 | Phosphorylation | TTEAEVNTDDVLSTK HCEEEECHHHHCCHH | 38.46 | 27214570 | |
643 | Phosphorylation | VNTDDVLSTKEAKKN ECHHHHCCHHHHHHH | 36.96 | 24961812 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of CHS5_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CHS5_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 CHS5_YEAST !! |
Kegg Drug | ||||||
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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-338; SER-362; SER-383;SER-553; SER-573; SER-579 AND SER-590, 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 THR-334; SER-338; SER-347;SER-573 AND SER-590, AND MASS SPECTROMETRY. | |
"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-590, AND MASSSPECTROMETRY. |