| UniProt ID | SP110_YEAST | |
|---|---|---|
| UniProt AC | P32380 | |
| Protein Name | Spindle pole body component 110 | |
| Gene Name | SPC110 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 944 | |
| Subcellular Localization | Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Tightly associated with the nucleus. It is present in a granular pattern that excludes the nucleolus. | |
| Protein Description | Component of the spindle pole body (SPB) required for the proper execution of spindle pole body (SPB) duplication. Potential role in cross-linking filaments or anchoring other molecules. It is essential for growth.. | |
| Protein Sequence | MDEASHLPNGSLKNMEFTPVGFIKSKRNTTQTQVVSPTKVPNANNGDENEGPVKKRQRRSIDDTIDSTRLFSEASQFDDSFPEIKANIPPSPRSGNVDKSRKRNLIDDLKKDVPMSQPLKEQEVREHQMKKERFDRALESKLLGKRHITYANSDISNKELYINEIKSLKHEIKELRKEKNDTLNNYDTLEEETDDLKNRLQALEKELDAKNKIVNSRKVDDHSGCIEEREQMERKLAELERKLKTVKDQVLELENNSDVQSLKLRSKEDELKNLMNELNELKSNAEEKDTQLEFKKNELRKRTNELNELKIKSDEMDLQLKQKQNESKRLKDELNELETKFSENGSQSSAKENELKMLKNKIAELEEEISTKNSQLIAKEGKLASLMAQLTQLESKLNQRDSQLGSREEELKKTNDKLQKDIRIAREETVSKDERIIDLQKKVKQLENDLFVIKKTHSESKTITDNELESKDKLIKILENDLKVAQEKYSKMEKELKEREFNYKISESKLEDEKTTLNEKISNLAAENSQLKNKIEDNSTATHHMKENYEKQLESLRKDIEEYKESAKDSEDKIEELKIRIAENSAKVSEKRSKDIKQKDEQISDLTQNLKLQEDEISSLKSIIDRYKKDFNQLKSEQSNIQHDLNLQILNLENKLIESEDELKSLRDSQKIEIENWKRKYNNLSLENDRLLTEKESASDKEREISILNRKLDEMDKEKWNLQESKEKYKRELQKVITANDRLRREKEELNENSNNIRIMEDKMTRIKKNYLSEITSLQEENRRLEERLILNERRKDNDSTMQLNDIISYYKLKYHSEVRHNNDLKVINDYLNKVLALGTRRLRLDTRKGEHSLNISLPDDDELDRDYYNSHVYTRYHDYEYPLRFNLNRRGPYFERRLSFKTVALLVLACVRMKRIAFYRRSDDNRLRILRDRIESSSGRISW | |
| 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 |
|---|---|---|---|---|---|
| 5 | Phosphorylation | ---MDEASHLPNGSL ---CCCCCCCCCCCC | 24.41 | 30377154 | |
| 11 | Phosphorylation | ASHLPNGSLKNMEFT CCCCCCCCCCCCEEE | 42.69 | 28889911 | |
| 18 | Phosphorylation | SLKNMEFTPVGFIKS CCCCCEEECEEEEEE | 12.08 | 21551504 | |
| 29 | Phosphorylation | FIKSKRNTTQTQVVS EEEECCCCCCEEEEC | 25.06 | 22890988 | |
| 30 | Phosphorylation | IKSKRNTTQTQVVSP EEECCCCCCEEEECC | 32.92 | 22890988 | |
| 32 | Phosphorylation | SKRNTTQTQVVSPTK ECCCCCCEEEECCCC | 22.65 | 22890988 | |
| 36 | Phosphorylation | TTQTQVVSPTKVPNA CCCEEEECCCCCCCC | 28.17 | 22369663 | |
| 38 | Phosphorylation | QTQVVSPTKVPNANN CEEEECCCCCCCCCC | 36.85 | 22369663 | |
| 60 | Phosphorylation | VKKRQRRSIDDTIDS CCCCHHHCHHHHHHH | 32.34 | 22369663 | |
| 64 | Phosphorylation | QRRSIDDTIDSTRLF HHHCHHHHHHHHHHH | 23.96 | 22890988 | |
| 67 | Phosphorylation | SIDDTIDSTRLFSEA CHHHHHHHHHHHHHH | 16.15 | 22890988 | |
| 68 | Phosphorylation | IDDTIDSTRLFSEAS HHHHHHHHHHHHHHH | 27.87 | 22890988 | |
| 72 | Phosphorylation | IDSTRLFSEASQFDD HHHHHHHHHHHHCCC | 36.52 | 28889911 | |
| 75 | Phosphorylation | TRLFSEASQFDDSFP HHHHHHHHHCCCCCH | 27.59 | 28152593 | |
| 80 | Phosphorylation | EASQFDDSFPEIKAN HHHHCCCCCHHHHCC | 44.54 | 22369663 | |
| 91 | Phosphorylation | IKANIPPSPRSGNVD HHCCCCCCCCCCCCC | 27.82 | 19823750 | |
| 94 | Phosphorylation | NIPPSPRSGNVDKSR CCCCCCCCCCCCHHH | 37.80 | 25521595 | |
| 141 | Acetylation | FDRALESKLLGKRHI HHHHHHHHHHCCCCC | 38.05 | 24489116 | |
| 150 | Phosphorylation | LGKRHITYANSDISN HCCCCCEECCCCCCC | 11.81 | 21700874 | |
| 153 | Phosphorylation | RHITYANSDISNKEL CCCEECCCCCCCCCH | 28.31 | 23749301 | |
| 156 | Phosphorylation | TYANSDISNKELYIN EECCCCCCCCCHHHH | 47.00 | 21700874 | |
| 158 | Acetylation | ANSDISNKELYINEI CCCCCCCCCHHHHHH | 42.16 | 24489116 | |
| 161 | Phosphorylation | DISNKELYINEIKSL CCCCCCHHHHHHHHH | 11.64 | 21700874 | |
| 166 | Acetylation | ELYINEIKSLKHEIK CHHHHHHHHHHHHHH | 43.48 | 24489116 | |
| 188 | Phosphorylation | DTLNNYDTLEEETDD CCCCCCHHHHHHHHH | 26.21 | 21700874 | |
| 205 | Acetylation | NRLQALEKELDAKNK HHHHHHHHHHHHCCC | 65.51 | 24489116 | |
| 261 | Phosphorylation | ENNSDVQSLKLRSKE CCCCCHHHHHHCCHH | 27.59 | 21700874 | |
| 283 | Phosphorylation | NELNELKSNAEEKDT HHHHHHHHCHHHHHH | 54.63 | 21440633 | |
| 331 | Acetylation | QNESKRLKDELNELE HHHHHHHHHHHHHHH | 53.87 | 23572591 | |
| 339 | Phosphorylation | DELNELETKFSENGS HHHHHHHHHHCCCCC | 50.44 | 28889911 | |
| 346 | Phosphorylation | TKFSENGSQSSAKEN HHHCCCCCCCCHHHH | 38.17 | 24603354 | |
| 348 | Phosphorylation | FSENGSQSSAKENEL HCCCCCCCCHHHHHH | 33.68 | 21700874 | |
| 349 | Phosphorylation | SENGSQSSAKENELK CCCCCCCCHHHHHHH | 35.41 | 28889911 | |
| 406 | Phosphorylation | QRDSQLGSREEELKK HHHHHHCCHHHHHHH | 45.15 | 27214570 | |
| 460 | Phosphorylation | IKKTHSESKTITDNE EEECCCCCCCCCCCH | 37.81 | 21700874 | |
| 470 | Phosphorylation | ITDNELESKDKLIKI CCCCHHCCHHHHHHH | 59.80 | 30377154 | |
| 509 | Acetylation | NYKISESKLEDEKTT CHHCCHHHHCCCCCH | 52.42 | 24489116 | |
| 515 | Phosphorylation | SKLEDEKTTLNEKIS HHHCCCCCHHHHHHH | 34.17 | 28132839 | |
| 516 | Phosphorylation | KLEDEKTTLNEKISN HHCCCCCHHHHHHHH | 38.36 | 28889911 | |
| 529 | Phosphorylation | SNLAAENSQLKNKIE HHHHHHCHHHCHHHC | 28.53 | 28889911 | |
| 607 | Phosphorylation | DEQISDLTQNLKLQE HHHHHHHHHHHHCCH | 22.02 | 28889911 | |
| 639 | Phosphorylation | NQLKSEQSNIQHDLN HHHHHHHHHHCHHHH | 31.67 | 21700874 | |
| 659 | Phosphorylation | LENKLIESEDELKSL HHHHHCCCHHHHHHH | 43.27 | 27017623 | |
| 665 | Phosphorylation | ESEDELKSLRDSQKI CCHHHHHHHHHHHCH | 41.06 | 21700874 | |
| 669 | Phosphorylation | ELKSLRDSQKIEIEN HHHHHHHHHCHHHHH | 27.26 | 21700874 | |
| 754 | Phosphorylation | KEELNENSNNIRIME HHHHHHCCCCCCCCH | 25.69 | 23749301 | |
| 853 | Phosphorylation | DTRKGEHSLNISLPD CCCCCCCCCCCCCCC | 20.86 | 21700874 | |
| 869 | Phosphorylation | DELDRDYYNSHVYTR CCCCHHHHHHCCCCE | 17.93 | 21700874 | |
| 871 | Phosphorylation | LDRDYYNSHVYTRYH CCHHHHHHCCCCEEC | 9.75 | 21700874 | |
| 937 | Phosphorylation | ILRDRIESSSGRISW HHHHHHHHCCCCCCC | 27.68 | 21700874 | |
| 938 | Phosphorylation | LRDRIESSSGRISW- HHHHHHHCCCCCCC- | 24.83 | 21700874 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SP110_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 SP110_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-36; SER-60; SER-91 ANDSER-529, 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-36, 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-60, AND MASSSPECTROMETRY. | |
| "Yeast Mps1p phosphorylates the spindle pole component Spc110p in theN-terminal domain."; Friedman D.B., Kern J.W., Huneycutt B.J., Vinh D.B., Crawford D.K.,Steiner E., Scheiltz D., Yates J. III, Resing K.A., Ahn N.G.,Winey M., Davis T.N.; J. Biol. Chem. 276:17958-17967(2001). Cited for: PHOSPHORYLATION AT SER-60; THR-64 AND THR68, AND FUNCTION. | |
