| UniProt ID | ASK1_YEAST | |
|---|---|---|
| UniProt AC | P35734 | |
| Protein Name | DASH complex subunit ASK1 | |
| Gene Name | ASK1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 292 | |
| 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 | MDSASKEETLEKLDQEITVNLQKIDSNLSFCFHKITQDIIPHVATYSEICERIMDSTEWLGTMFQETGLVNLQANAAAPVGNAPVKSLVSNNVGIFPTSAEEASRQSQTDNGPNEADSAVHVNRDVHSMFNNDSIDDFHTANITSTGQILKLPDSSDEDTGSEAVPSREQTDLTGEGHGGADDEQDESTIQRQSRKRKISLLLQQQYGSSSSMVPSPIVPNKMRKQLAHEEHINNDGDNDDENSNNIESSPLKQGHHHPKGQADDNNEGPDEEESTKEVPKPGTIIHFSTNR | |
| 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 |
|---|---|---|---|---|---|
| 26 | Phosphorylation | VNLQKIDSNLSFCFH HCHHHHCCCCHHHHH | 43.05 | 21440633 | |
| 90 | Phosphorylation | APVKSLVSNNVGIFP CCHHHHHCCCCCCCC | 28.16 | 19779198 | |
| 98 | Phosphorylation | NNVGIFPTSAEEASR CCCCCCCCCHHHHHH | 29.80 | 27738172 | |
| 99 | Phosphorylation | NVGIFPTSAEEASRQ CCCCCCCCHHHHHHH | 33.64 | 28889911 | |
| 107 | Phosphorylation | AEEASRQSQTDNGPN HHHHHHHHCCCCCCC | 33.66 | 23749301 | |
| 109 | Phosphorylation | EASRQSQTDNGPNEA HHHHHHCCCCCCCHH | 36.36 | 19779198 | |
| 118 | Phosphorylation | NGPNEADSAVHVNRD CCCCHHHHHHCCCCC | 38.96 | 23749301 | |
| 128 | Phosphorylation | HVNRDVHSMFNNDSI CCCCCHHHHHCCCCC | 25.56 | 22369663 | |
| 134 | Phosphorylation | HSMFNNDSIDDFHTA HHHHCCCCCCCCCCC | 30.00 | 22369663 | |
| 140 | Phosphorylation | DSIDDFHTANITSTG CCCCCCCCCCCCCCC | 22.76 | 22369663 | |
| 144 | Phosphorylation | DFHTANITSTGQILK CCCCCCCCCCCCEEE | 21.75 | 22369663 | |
| 145 | Phosphorylation | FHTANITSTGQILKL CCCCCCCCCCCEEEC | 27.09 | 22369663 | |
| 146 | Phosphorylation | HTANITSTGQILKLP CCCCCCCCCCEEECC | 25.18 | 22369663 | |
| 155 | Phosphorylation | QILKLPDSSDEDTGS CEEECCCCCCCCCCC | 37.44 | 22369663 | |
| 156 | Phosphorylation | ILKLPDSSDEDTGSE EEECCCCCCCCCCCC | 53.02 | 22369663 | |
| 160 | Phosphorylation | PDSSDEDTGSEAVPS CCCCCCCCCCCCCCC | 40.33 | 22890988 | |
| 162 | Phosphorylation | SSDEDTGSEAVPSRE CCCCCCCCCCCCCHH | 25.19 | 22890988 | |
| 167 | Phosphorylation | TGSEAVPSREQTDLT CCCCCCCCHHHCCCC | 41.68 | 22890988 | |
| 171 | Phosphorylation | AVPSREQTDLTGEGH CCCCHHHCCCCCCCC | 28.37 | 22369663 | |
| 174 | Phosphorylation | SREQTDLTGEGHGGA CHHHCCCCCCCCCCC | 35.68 | 22369663 | |
| 188 | Phosphorylation | ADDEQDESTIQRQSR CCCCCCHHHHHHHHH | 38.82 | 22369663 | |
| 189 | Phosphorylation | DDEQDESTIQRQSRK CCCCCHHHHHHHHHH | 21.05 | 24909858 | |
| 200 | Phosphorylation | QSRKRKISLLLQQQY HHHHHHHHHHHHHHH | 18.92 | 17330950 | |
| 207 | Phosphorylation | SLLLQQQYGSSSSMV HHHHHHHHCCCCCCC | 18.03 | 19779198 | |
| 209 | Phosphorylation | LLQQQYGSSSSMVPS HHHHHHCCCCCCCCC | 23.32 | 21551504 | |
| 210 | Phosphorylation | LQQQYGSSSSMVPSP HHHHHCCCCCCCCCC | 23.28 | 19823750 | |
| 211 | Phosphorylation | QQQYGSSSSMVPSPI HHHHCCCCCCCCCCC | 24.93 | 19823750 | |
| 212 | Phosphorylation | QQYGSSSSMVPSPIV HHHCCCCCCCCCCCC | 26.25 | 21551504 | |
| 216 | Phosphorylation | SSSSMVPSPIVPNKM CCCCCCCCCCCCHHH | 18.82 | 19823750 | |
| 244 | Phosphorylation | GDNDDENSNNIESSP CCCCCCCCCCCCCCC | 29.25 | 22369663 | |
| 249 | Phosphorylation | ENSNNIESSPLKQGH CCCCCCCCCCCCCCC | 33.20 | 22369663 | |
| 250 | Phosphorylation | NSNNIESSPLKQGHH CCCCCCCCCCCCCCC | 22.82 | 22369663 | |
| 275 | Phosphorylation | EGPDEEESTKEVPKP CCCCHHHCCCCCCCC | 48.32 | 28889911 | |
| 276 | Phosphorylation | GPDEEESTKEVPKPG CCCHHHCCCCCCCCC | 34.21 | 21440633 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ASK1_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 ASK1_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-26; SER-107; SER-155;SER-156 AND SER-200, 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-174 AND SER-188, ANDMASS 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-134; SER-155; SER-156AND SER-200, AND MASS SPECTROMETRY. | |
| "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-26; SER-118; SER-134; THR-140; SER-200 ANDSER-250. | |
