UniProt ID | CHS3_YEAST | |
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UniProt AC | P29465 | |
Protein Name | Chitin synthase 3 {ECO:0000303|PubMed:2050737} | |
Gene Name | CHS3 {ECO:0000303|PubMed:2050738} | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 1165 | |
Subcellular Localization |
Cell membrane Multi-pass membrane protein . Bud neck . Cytoplasmic vesicle membrane Multi-pass membrane protein . Localizes to a ring on the surface of cells about to undergo bud emergence and in the mother-bud neck of small-budded cells (PubMed: |
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Protein Description | Appears to be responsible for the synthesis of the majority of the chitin found in the cell wall periphery. It is involved in the synthesis of the chitin ring that forms in the cell wall just before bud emergence. This ring remains at the base of the bud as the bud grows and ultimately forms part of the bud scar marking the division site on the mother cell. Also catalyzes the synthesis of chitin laid down during mating and spore cell-wall synthesis.. | |
Protein Sequence | MTGLNGDDPDDYYLNLNQDEESLLRSRHSVGSGAPHRQGSLVRPERSRLNNPDNPHFYYAQKTQEQMNHLDVLPSSTGVNPNATRRSGSLRSKGSVRSKFSGRETDSYLLQDMNTTDKKASVKISDEGVAEDEFDKDGDVDNFEESSTQPINKSIKPLRKETNDTLSFWQMYCYFITFWAPAPILAFCGMPKKERQMAWREKVALISVILYIGAIVAFLTFGFTKTVCSSSKLRLKNNEVSTEFVVINGKAYELDTSSRSGIQDVEVDSDTLYGPWSDAGKDASFLFQNVNGNCHNLITPKSNSSIPHDDDNNLAWYFPCKLKNQDGSSKPNFTVENYAGWNCHTSKEDRDAFYGLKSKADVYFTWDGIKNSSRNLIVYNGDVLDLDLLDWLEKDDVDYPVVFDDLKTSNLQGYDLSLVLSNGHERKIARCLSEIIKVGEVDSKTVGCIASDVVLYVSLVFILSVVIIKFIIACYFRWTVARKQGAYIVDNKTMDKHTNDIEDWSNNIQTKAPLKEVDPHLRPKKYSKKSLGHKRASTFDLLKKHSSKMFQFNESVIDLDTSMSSSLQSSGSYRGMTTMTTQNAWKLSNENKAVHSRNPSTLLPTSSMFWNKATSSPVPGSSLIQSLDSTIIHPDIVQQPPLDFMPYGFPLIHTICFVTCYSEDEEGLRTTLDSLSTTDYPNSHKLLMVVCDGLIKGSGNDKTTPEIALGMMDDFVTPPDEVKPYSYVAVASGSKRHNMAKIYAGFYKYDDSTIPPENQQRVPIITIVKCGTPAEQGAAKPGNRGKRDSQIILMSFLEKITFDERMTQLEFQLLKNIWQITGLMADFYETVLMVDADTKVFPDALTHMVAEMVKDPLIMGLCGETKIANKAQSWVTAIQVFEYYISHHQAKAFESVFGSVTCLPGCFSMYRIKSPKGSDGYWVPVLANPDIVERYSDNVTNTLHKKNLLLLGEDRFLSSLMLKTFPKRKQVFVPKAACKTIAPDKFKVLLSQRRRWINSTVHNLFELVLIRDLCGTFCFSMQFVIGIELIGTMVLPLAICFTIYVIIFAIVSKPTPVITLVLLAIILGLPGLIVVITATRWSYLWWMCVYICALPIWNFVLPSYAYWKFDDFSWGDTRTIAGGNKKAQDENEGEFDHSKIKMRTWREFEREDILNRKEESDSFVA | |
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 |
---|---|---|---|---|---|
22 | Phosphorylation | NLNQDEESLLRSRHS CCCCCHHHHHHHHCC | 30.56 | 30377154 | |
26 | Phosphorylation | DEESLLRSRHSVGSG CHHHHHHHHCCCCCC | 34.02 | 19684113 | |
29 | Phosphorylation | SLLRSRHSVGSGAPH HHHHHHCCCCCCCCC | 27.36 | 19684113 | |
32 | Phosphorylation | RSRHSVGSGAPHRQG HHHCCCCCCCCCCCC | 29.62 | 23749301 | |
40 | Phosphorylation | GAPHRQGSLVRPERS CCCCCCCCCCCCCHH | 18.49 | 28132839 | |
62 | Ubiquitination | PHFYYAQKTQEQMNH CCCHHCHHHHHHHCC | 43.96 | 17644757 | |
75 | Phosphorylation | NHLDVLPSSTGVNPN CCCCCCCCCCCCCCC | 36.05 | 27017623 | |
84 | Phosphorylation | TGVNPNATRRSGSLR CCCCCCCCCCCCCCC | 33.00 | 21551504 | |
87 | Phosphorylation | NPNATRRSGSLRSKG CCCCCCCCCCCCCCC | 29.46 | 21440633 | |
89 | Phosphorylation | NATRRSGSLRSKGSV CCCCCCCCCCCCCCC | 23.12 | 21440633 | |
92 | Phosphorylation | RRSGSLRSKGSVRSK CCCCCCCCCCCCCCC | 46.81 | 21440633 | |
101 | Phosphorylation | GSVRSKFSGRETDSY CCCCCCCCCCCCCCE | 40.45 | 20377248 | |
105 | Phosphorylation | SKFSGRETDSYLLQD CCCCCCCCCCEEECC | 28.96 | 20377248 | |
107 | Phosphorylation | FSGRETDSYLLQDMN CCCCCCCCEEECCCC | 25.71 | 28889911 | |
108 | Phosphorylation | SGRETDSYLLQDMNT CCCCCCCEEECCCCC | 17.78 | 19823750 | |
115 | Phosphorylation | YLLQDMNTTDKKASV EEECCCCCCCCCCCC | 29.72 | 19823750 | |
116 | Phosphorylation | LLQDMNTTDKKASVK EECCCCCCCCCCCCE | 40.60 | 19823750 | |
118 | Ubiquitination | QDMNTTDKKASVKIS CCCCCCCCCCCCEEC | 48.42 | 23749301 | |
119 | Ubiquitination | DMNTTDKKASVKISD CCCCCCCCCCCEECC | 49.02 | 24961812 | |
123 | Ubiquitination | TDKKASVKISDEGVA CCCCCCCEECCCCCC | 33.72 | 24961812 | |
125 | Phosphorylation | KKASVKISDEGVAED CCCCCEECCCCCCCC | 24.72 | 28889911 | |
136 | Ubiquitination | VAEDEFDKDGDVDNF CCCCCCCCCCCCCCC | 69.77 | 23749301 | |
146 | Phosphorylation | DVDNFEESSTQPINK CCCCCCCCCCCCCCC | 31.33 | 22369663 | |
147 | Phosphorylation | VDNFEESSTQPINKS CCCCCCCCCCCCCCC | 34.05 | 22369663 | |
148 | Phosphorylation | DNFEESSTQPINKSI CCCCCCCCCCCCCCC | 47.87 | 22369663 | |
153 | Ubiquitination | SSTQPINKSIKPLRK CCCCCCCCCCCCCCH | 55.03 | 17644757 | |
236 | Ubiquitination | SSSKLRLKNNEVSTE CCCCEEECCCCCCEE | 51.82 | 17644757 | |
250 | Ubiquitination | EFVVINGKAYELDTS EEEEECCEEEEEECC | 43.22 | 17644757 | |
281 | Ubiquitination | GPWSDAGKDASFLFQ CCHHHCCCCHHHEEE | 52.41 | 17644757 | |
301 | Ubiquitination | CHNLITPKSNSSIPH CCCCCCCCCCCCCCC | 54.33 | 17644757 | |
303 | N-linked_Glycosylation | NLITPKSNSSIPHDD CCCCCCCCCCCCCCC | 46.00 | - | |
321 | Ubiquitination | LAWYFPCKLKNQDGS EEEEEEEEEECCCCC | 63.83 | 17644757 | |
332 | N-linked_Glycosylation | QDGSSKPNFTVENYA CCCCCCCCEEEEECC | 49.29 | - | |
357 | Ubiquitination | RDAFYGLKSKADVYF HHHHHCCCCCCCEEE | 45.61 | 17644757 | |
359 | Ubiquitination | AFYGLKSKADVYFTW HHHCCCCCCCEEEEE | 47.20 | 17644757 | |
370 | Ubiquitination | YFTWDGIKNSSRNLI EEEECCCCCCCCCEE | 57.20 | 17644757 | |
394 | Ubiquitination | DLLDWLEKDDVDYPV HHHHHHHHCCCCCCE | 57.99 | 17644757 | |
407 | Ubiquitination | PVVFDDLKTSNLQGY CEEECCCCCCCCCCC | 57.83 | 17644757 | |
427 | Ubiquitination | LSNGHERKIARCLSE CCCCCHHHHHHHHHH | 37.42 | 17644757 | |
496 | Ubiquitination | VDNKTMDKHTNDIED ECCCCCCCCCCCHHH | 41.32 | 23749301 | |
505 | Phosphorylation | TNDIEDWSNNIQTKA CCCHHHHHHCCCCCC | 32.11 | 21440633 | |
511 | Ubiquitination | WSNNIQTKAPLKEVD HHHCCCCCCCHHHCC | 31.47 | 17644757 | |
515 | Ubiquitination | IQTKAPLKEVDPHLR CCCCCCHHHCCCCCC | 55.41 | 17644757 | |
524 | Ubiquitination | VDPHLRPKKYSKKSL CCCCCCCCCCCCHHC | 58.89 | 17644757 | |
525 | Ubiquitination | DPHLRPKKYSKKSLG CCCCCCCCCCCHHCC | 58.39 | 17644757 | |
537 | Phosphorylation | SLGHKRASTFDLLKK HCCCCCHHHHHHHHH | 33.37 | 22369663 | |
538 | Phosphorylation | LGHKRASTFDLLKKH CCCCCHHHHHHHHHH | 21.86 | 22369663 | |
586 | Ubiquitination | MTTQNAWKLSNENKA EECCCCCCCCCCCCC | 39.36 | 23749301 | |
592 | Ubiquitination | WKLSNENKAVHSRNP CCCCCCCCCCCCCCC | 45.68 | 23749301 | |
596 | Phosphorylation | NENKAVHSRNPSTLL CCCCCCCCCCCCCCC | 27.44 | 21440633 | |
600 | Phosphorylation | AVHSRNPSTLLPTSS CCCCCCCCCCCCCCH | 34.92 | 25704821 | |
601 | Phosphorylation | VHSRNPSTLLPTSSM CCCCCCCCCCCCCHH | 33.30 | 21440633 | |
605 | Phosphorylation | NPSTLLPTSSMFWNK CCCCCCCCCHHHCCC | 33.14 | 24961812 | |
606 | Phosphorylation | PSTLLPTSSMFWNKA CCCCCCCCHHHCCCC | 20.19 | 21440633 | |
607 | Phosphorylation | STLLPTSSMFWNKAT CCCCCCCHHHCCCCC | 22.07 | 21440633 | |
612 | Ubiquitination | TSSMFWNKATSSPVP CCHHHCCCCCCCCCC | 43.57 | 17644757 | |
741 | Ubiquitination | SKRHNMAKIYAGFYK CCCCCCHHEEEEEEE | 26.02 | 17644757 | |
748 | Ubiquitination | KIYAGFYKYDDSTIP HEEEEEEECCCCCCC | 39.69 | 17644757 | |
749 | Phosphorylation | IYAGFYKYDDSTIPP EEEEEEECCCCCCCC | 17.38 | 21551504 | |
753 | Phosphorylation | FYKYDDSTIPPENQQ EEECCCCCCCCCCCC | 44.49 | 21551504 | |
766 | Phosphorylation | QQRVPIITIVKCGTP CCCCCEEEEEECCCC | 22.04 | 21551504 | |
769 | Ubiquitination | VPIITIVKCGTPAEQ CCEEEEEECCCCHHH | 24.09 | 17644757 | |
780 | Ubiquitination | PAEQGAAKPGNRGKR CHHHCCCCCCCCCCC | 53.58 | 23749301 | |
807 | Phosphorylation | ITFDERMTQLEFQLL CCCCHHHHHHHHHHH | 35.90 | 29136822 | |
821 | Phosphorylation | LKNIWQITGLMADFY HHHHHHHHHHHHHHH | 14.79 | 29136822 | |
828 | Phosphorylation | TGLMADFYETVLMVD HHHHHHHHHEEEEEC | 15.96 | 29136822 | |
830 | Phosphorylation | LMADFYETVLMVDAD HHHHHHHEEEEECCC | 13.94 | 29136822 | |
838 | Phosphorylation | VLMVDADTKVFPDAL EEEECCCCCCCHHHH | 30.72 | 29136822 | |
865 | Phosphorylation | IMGLCGETKIANKAQ HHHHCCCCCHHHHHH | 17.03 | 28889911 | |
891 | Ubiquitination | YISHHQAKAFESVFG HHHHHHHHHHHHHHC | 47.22 | 17644757 | |
916 | Ubiquitination | MYRIKSPKGSDGYWV EEEECCCCCCCCCEE | 77.47 | 17644757 | |
935 | Phosphorylation | NPDIVERYSDNVTNT CHHHHHHCCCCCCHH | 13.58 | 25005228 | |
940 | Phosphorylation | ERYSDNVTNTLHKKN HHCCCCCCHHHHHCC | 28.83 | 25005228 | |
945 | Ubiquitination | NVTNTLHKKNLLLLG CCCHHHHHCCEEEEC | 46.61 | 17644757 | |
946 | Ubiquitination | VTNTLHKKNLLLLGE CCHHHHHCCEEEECC | 41.92 | 17644757 | |
963 | Acetylation | FLSSLMLKTFPKRKQ HHHHHHHHHCCCCCC | 33.87 | 24489116 | |
987 | Acetylation | TIAPDKFKVLLSQRR CCCCHHHHHHHHHHH | 37.40 | 24489116 | |
1126 | Ubiquitination | TIAGGNKKAQDENEG EECCCCCCCCCCCCC | 56.11 | 17644757 | |
1139 | Ubiquitination | EGEFDHSKIKMRTWR CCCCCHHHHHHHHHH | 42.81 | 17644757 | |
1141 | Ubiquitination | EFDHSKIKMRTWREF CCCHHHHHHHHHHHH | 26.51 | 17644757 | |
1157 | Ubiquitination | REDILNRKEESDSFV HHHHHCCHHHCCCCC | 65.83 | 23749301 | |
1162 | Phosphorylation | NRKEESDSFVA---- CCHHHCCCCCC---- | 30.79 | 23749301 |
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 CHS3_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of CHS3_YEAST !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
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Oops, there are no SNP-PTM records of CHS3_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-147, AND MASSSPECTROMETRY. | |
"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-147, 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-537 AND THR-538, ANDMASS SPECTROMETRY. | |
"A proteomics approach to understanding protein ubiquitination."; Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.; Nat. Biotechnol. 21:921-926(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-606, UBIQUITINATION ATLYS-136, AND MASS SPECTROMETRY. | |
Ubiquitylation | |
Reference | PubMed |
"A proteomics approach to understanding protein ubiquitination."; Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.; Nat. Biotechnol. 21:921-926(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-606, UBIQUITINATION ATLYS-136, AND MASS SPECTROMETRY. |