| UniProt ID | DAM1_YEAST | |
|---|---|---|
| UniProt AC | P53267 | |
| Protein Name | DASH complex subunit DAM1 | |
| Gene Name | DAM1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 343 | |
| Subcellular Localization | Nucleus. Cytoplasm, cytoskeleton, spindle. Chromosome, centromere, kinetochore. Associates with the mitotic spindle and the kinetochore. | |
| Protein Description | Component of the DASH complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore. The DASH ring complex may both stabilize microtubules during chromosome attachment in anaphase A, and allow the chromosome to remain attached to the depolymerizing microtubule in anaphase B. Microtubule depolymerization proceeds by protofilament splaying and induces the kinetochore-attached ring to slide longitudinally, thereby helping to transduce depolymerization energy into pulling forces to disjoin chromatids.. | |
| Protein Sequence | MSEDKAKLGTTRSATEYRLSIGSAPTSRRSSMGESSSLMKFADQEGLTSSVGEYNENTIQQLLLPKIRELSDSIITLDSNFTRLNFIHESLADLNESLGSLLYGIMSNSWCVEFSQAPHDIQDDLIAIKQLKSLEDEKNNLVMELSNMERGIKRKKDEQGENDLAKASQNKQFNQPLFPSSQVRKYRSYDNRDKRKPSKIGNNLQVENEEDYEDDTSSEASFVLNPTNIGMSKSSQGHVTKTTRLNNNTNSKLRRKSILHTIRNSIASGADLPIENDNVVNLGDLHPNNRISLGSGAARVVNGPVTKNRNSMFSGRAERKPTESRHSVAKKTEKKINTRPPFR | |
| 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 | Acetylation | ------MSEDKAKLG ------CCHHHHHHC | 55.28 | 22814378 | |
| 13 | Phosphorylation | AKLGTTRSATEYRLS HHHCCCCCCCEEEEE | 37.13 | 22369663 | |
| 15 | Phosphorylation | LGTTRSATEYRLSIG HCCCCCCCEEEEECC | 34.49 | 22369663 | |
| 17 | Phosphorylation | TTRSATEYRLSIGSA CCCCCCEEEEECCCC | 16.70 | 22369663 | |
| 20 | Phosphorylation | SATEYRLSIGSAPTS CCCEEEEECCCCCCC | 18.86 | 22369663 | |
| 23 | Phosphorylation | EYRLSIGSAPTSRRS EEEEECCCCCCCCCC | 29.43 | 22369663 | |
| 26 | Phosphorylation | LSIGSAPTSRRSSMG EECCCCCCCCCCCCC | 34.28 | 22369663 | |
| 27 | Phosphorylation | SIGSAPTSRRSSMGE ECCCCCCCCCCCCCC | 25.33 | 22369663 | |
| 30 | Phosphorylation | SAPTSRRSSMGESSS CCCCCCCCCCCCCCH | 24.46 | 22369663 | |
| 31 | Phosphorylation | APTSRRSSMGESSSL CCCCCCCCCCCCCHH | 29.06 | 22369663 | |
| 35 | Phosphorylation | RRSSMGESSSLMKFA CCCCCCCCCHHHHHC | 21.35 | 23749301 | |
| 36 | Phosphorylation | RSSMGESSSLMKFAD CCCCCCCCHHHHHCC | 24.16 | 22369663 | |
| 37 | Phosphorylation | SSMGESSSLMKFADQ CCCCCCCHHHHHCCC | 41.59 | 22369663 | |
| 48 | Phosphorylation | FADQEGLTSSVGEYN HCCCCCCCCCCCCCC | 29.79 | 30377154 | |
| 188 | Phosphorylation | SQVRKYRSYDNRDKR HHHHHHHCCCCCCCC | 33.47 | 17287358 | |
| 217 | Phosphorylation | EDYEDDTSSEASFVL CCCCCCCCCCCEEEE | 32.93 | 19779198 | |
| 218 | Phosphorylation | DYEDDTSSEASFVLN CCCCCCCCCCEEEEC | 39.00 | 19779198 | |
| 221 | Phosphorylation | DDTSSEASFVLNPTN CCCCCCCEEEECCCC | 16.31 | 19779198 | |
| 233 | Methylation | PTNIGMSKSSQGHVT CCCCCCCCCCCCCCC | 45.28 | 16143104 | |
| 241 | Acetylation | SSQGHVTKTTRLNNN CCCCCCCEEEECCCC | 46.97 | 25381059 | |
| 252 | Acetylation | LNNNTNSKLRRKSIL CCCCCCCHHHHHHHH | 48.35 | 25381059 | |
| 257 | Phosphorylation | NSKLRRKSILHTIRN CCHHHHHHHHHHHHH | 28.68 | 25533186 | |
| 265 | Phosphorylation | ILHTIRNSIASGADL HHHHHHHHHHCCCCC | 15.07 | 22369663 | |
| 268 | Phosphorylation | TIRNSIASGADLPIE HHHHHHHCCCCCCCC | 32.61 | 22369663 | |
| 292 | Phosphorylation | LHPNNRISLGSGAAR CCCCCCEECCCCCCE | 24.36 | 22369663 | |
| 295 | Phosphorylation | NNRISLGSGAARVVN CCCEECCCCCCEEEC | 30.47 | 22369663 | |
| 307 | Acetylation | VVNGPVTKNRNSMFS EECCCCCCCCCCCCC | 54.89 | 25381059 | |
| 311 | Phosphorylation | PVTKNRNSMFSGRAE CCCCCCCCCCCCCCC | 20.26 | 24909858 | |
| 322 | Phosphorylation | GRAERKPTESRHSVA CCCCCCCCHHHHHHH | 50.02 | 27017623 | |
| 324 | Phosphorylation | AERKPTESRHSVAKK CCCCCCHHHHHHHHH | 37.46 | 27017623 | |
| 327 | Phosphorylation | KPTESRHSVAKKTEK CCCHHHHHHHHHHHH | 23.74 | 27017623 | |
| 330 | Acetylation | ESRHSVAKKTEKKIN HHHHHHHHHHHHHHC | 59.06 | 25381059 | |
| 331 | Acetylation | SRHSVAKKTEKKINT HHHHHHHHHHHHHCC | 52.78 | 25381059 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 20 | S | Phosphorylation | Kinase | IPL1 | P38991 | Uniprot |
| 257 | S | Phosphorylation | Kinase | IPL1 | P38991 | Uniprot |
| 265 | S | Phosphorylation | Kinase | IPL1 | P38991 | Uniprot |
| 292 | S | Phosphorylation | Kinase | IPL1 | P38991 | Uniprot |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DAM1_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 DAM1_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-23; SER-27; SER-30 ANDSER-31, 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-31, AND MASSSPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, 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-31, AND MASSSPECTROMETRY. | |
| "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-23, AND MASSSPECTROMETRY. | |
| "Phospho-regulation of kinetochore-microtubule attachments by theAurora kinase Ipl1p."; Cheeseman I.M., Anderson S., Jwa M., Green E.M., Kang J.-S.,Yates J.R. III, Chan C.S.M., Drubin D.G., Barnes G.; Cell 111:163-172(2002). Cited for: PHOSPHORYLATION AT SER-20; SER-257; SER-265 AND SER-292. | |
