| UniProt ID | MTC1_YEAST | |
|---|---|---|
| UniProt AC | P47018 | |
| Protein Name | Maintenance of telomere capping protein 1 | |
| Gene Name | MTC1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 478 | |
| Subcellular Localization | Cytoplasm . Cytoplasmic vesicle, COPI-coated vesicle . | |
| Protein Description | Involved in telomere capping.. | |
| Protein Sequence | MSENKNSEAEDVFEFLDSLPEAKNGGKMVNTDVKGSQEGVKGGSNSVAGKTGNDGKKGDDDIFEFLEELEKSNLSLTDKKGVEKKAPSESVNNKAQDEKVEESKENKNSEQDAHGKEKEPQQQEKEEEEEEEEEEEEEEEETPLHDPIASISNWWSSSGSAKVSSIWNKTAEQASQIKNRLAQEQLDLTSKINTSTITEIARNLQKIVVGETEEVLRIHLVHDLVNYPSLQYNIESKFDQVLSSQVEGGIRIFVDEWGHPNNNGITPVEKKPSVADGELGNSKKKLQFNLFDGKVTDGEKLAFANLENAVKLFNTAHEEYQKQQKEADATPDDDRSSISSNSNKISDLFISILPIAIPQKQKDADGDFQVTDSNTPGNFNFTLVLKDITNDITTITRSQGFPVKWVNWLEGSVEKTGSTASEERNKSYDQKKQKESEDEDEDDEIIDPSEWVKEWIEDGLSLSFGVMAQNYVIDRMGL | |
| 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 | ------MSENKNSEA ------CCCCCCCCH | 50.29 | 22369663 | |
| 5 | Ubiquitination | ---MSENKNSEAEDV ---CCCCCCCCHHHH | 58.77 | 24961812 | |
| 7 | Phosphorylation | -MSENKNSEAEDVFE -CCCCCCCCHHHHHH | 39.53 | 22369663 | |
| 18 | Phosphorylation | DVFEFLDSLPEAKNG HHHHHHHCCCHHHCC | 48.23 | 22369663 | |
| 31 | Phosphorylation | NGGKMVNTDVKGSQE CCCEEEECCCCCCCC | 30.66 | 22369663 | |
| 34 | Ubiquitination | KMVNTDVKGSQEGVK EEEECCCCCCCCCCC | 56.51 | 23749301 | |
| 36 | Phosphorylation | VNTDVKGSQEGVKGG EECCCCCCCCCCCCC | 21.24 | 20377248 | |
| 41 | Ubiquitination | KGSQEGVKGGSNSVA CCCCCCCCCCCCCCC | 69.30 | 23749301 | |
| 44 | Phosphorylation | QEGVKGGSNSVAGKT CCCCCCCCCCCCCCC | 34.30 | 23749301 | |
| 46 | Phosphorylation | GVKGGSNSVAGKTGN CCCCCCCCCCCCCCC | 18.29 | 25752575 | |
| 72 | Phosphorylation | FLEELEKSNLSLTDK HHHHHHHCCCCCCCC | 33.36 | 22369663 | |
| 75 | Phosphorylation | ELEKSNLSLTDKKGV HHHHCCCCCCCCCCC | 33.21 | 22369663 | |
| 77 | Phosphorylation | EKSNLSLTDKKGVEK HHCCCCCCCCCCCCC | 42.25 | 22369663 | |
| 88 | Phosphorylation | GVEKKAPSESVNNKA CCCCCCCCHHHCHHH | 47.57 | 21082442 | |
| 90 | Phosphorylation | EKKAPSESVNNKAQD CCCCCCHHHCHHHHH | 34.19 | 28889911 | |
| 164 | Phosphorylation | SSGSAKVSSIWNKTA CCCCHHHHHHHHHHH | 18.52 | 28889911 | |
| 165 | Phosphorylation | SGSAKVSSIWNKTAE CCCHHHHHHHHHHHH | 34.31 | 21440633 | |
| 169 | Acetylation | KVSSIWNKTAEQASQ HHHHHHHHHHHHHHH | 33.83 | 24489116 | |
| 178 | Ubiquitination | AEQASQIKNRLAQEQ HHHHHHHHHHHHHHH | 28.51 | 23749301 | |
| 191 | Ubiquitination | EQLDLTSKINTSTIT HHHHHHHHCCHHHHH | 34.44 | 23749301 | |
| 194 | Phosphorylation | DLTSKINTSTITEIA HHHHHCCHHHHHHHH | 30.62 | 22369663 | |
| 195 | Phosphorylation | LTSKINTSTITEIAR HHHHCCHHHHHHHHH | 17.21 | 22369663 | |
| 196 | Phosphorylation | TSKINTSTITEIARN HHHCCHHHHHHHHHH | 29.85 | 22369663 | |
| 198 | Phosphorylation | KINTSTITEIARNLQ HCCHHHHHHHHHHHH | 22.79 | 22369663 | |
| 266 | Phosphorylation | HPNNNGITPVEKKPS CCCCCCCCCCCCCCC | 23.76 | 22369663 | |
| 273 | Phosphorylation | TPVEKKPSVADGELG CCCCCCCCCCCCCCC | 38.52 | 17330950 | |
| 282 | Phosphorylation | ADGELGNSKKKLQFN CCCCCCCCCCEEEEE | 44.01 | 27017623 | |
| 285 | Acetylation | ELGNSKKKLQFNLFD CCCCCCCEEEEEEEC | 51.78 | 24489116 | |
| 294 | Acetylation | QFNLFDGKVTDGEKL EEEEECCCCCCCHHE | 43.75 | 24489116 | |
| 300 | Acetylation | GKVTDGEKLAFANLE CCCCCCHHEEECCHH | 51.12 | 24489116 | |
| 330 | Phosphorylation | QQKEADATPDDDRSS HHHHCCCCCCCCHHH | 28.00 | 22890988 | |
| 336 | Phosphorylation | ATPDDDRSSISSNSN CCCCCCHHHHCCCCC | 38.73 | 22369663 | |
| 337 | Phosphorylation | TPDDDRSSISSNSNK CCCCCHHHHCCCCCH | 27.64 | 25521595 | |
| 339 | Phosphorylation | DDDRSSISSNSNKIS CCCHHHHCCCCCHHH | 25.97 | 22369663 | |
| 340 | Phosphorylation | DDRSSISSNSNKISD CCHHHHCCCCCHHHH | 42.48 | 25521595 | |
| 342 | Phosphorylation | RSSISSNSNKISDLF HHHHCCCCCHHHHHH | 41.26 | 22369663 | |
| 346 | Phosphorylation | SSNSNKISDLFISIL CCCCCHHHHHHHHHH | 29.85 | 24961812 | |
| 371 | Phosphorylation | ADGDFQVTDSNTPGN CCCCEEECCCCCCCC | 23.95 | 28889911 | |
| 373 | Phosphorylation | GDFQVTDSNTPGNFN CCEEECCCCCCCCEE | 32.98 | 28889911 | |
| 375 | Phosphorylation | FQVTDSNTPGNFNFT EEECCCCCCCCEEEE | 36.20 | 28889911 | |
| 393 | Phosphorylation | KDITNDITTITRSQG EECCCCCCEEECCCC | 18.27 | 30377154 | |
| 394 | Phosphorylation | DITNDITTITRSQGF ECCCCCCEEECCCCC | 22.23 | 30377154 | |
| 396 | Phosphorylation | TNDITTITRSQGFPV CCCCCEEECCCCCCE | 23.36 | 30377154 | |
| 398 | Phosphorylation | DITTITRSQGFPVKW CCCEEECCCCCCEEE | 26.46 | 30377154 | |
| 412 | Phosphorylation | WVNWLEGSVEKTGST EEEEHHCCCHHCCCC | 20.09 | 22369663 | |
| 419 | Phosphorylation | SVEKTGSTASEERNK CCHHCCCCHHHHHHH | 35.23 | 25752575 | |
| 421 | Phosphorylation | EKTGSTASEERNKSY HHCCCCHHHHHHHCH | 39.83 | 27214570 | |
| 436 | Phosphorylation | DQKKQKESEDEDEDD HHHHHHHCCCCCCCC | 58.33 | 22369663 | |
| 449 | Phosphorylation | DDEIIDPSEWVKEWI CCCCCCHHHHHHHHH | 40.10 | 25521595 |
| 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 MTC1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MTC1_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 MTC1_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-18; SER-88; THR-194;THR-266; SER-273; SER-337; SER-339; SER-340 AND SER-436, 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-75; SER-336; SER-337;SER-339 AND SER-340, 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-273 AND SER-436, ANDMASS SPECTROMETRY. | |
