| UniProt ID | DUO1_YEAST | |
|---|---|---|
| UniProt AC | P53168 | |
| Protein Name | DASH complex subunit DUO1 | |
| Gene Name | DUO1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 247 | |
| Subcellular Localization | Nucleus . Cytoplasm, cytoskeleton, spindle pole . 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 | MSEQSQLDDSTIDKLIPQIFNEMRSNLNNTTNKFPKSTGGGASDNISANSNSIRSFNSITTQSLLKESESLDKITAMIKNVTAALKNNLPVYVNQVHEVCKSTNSILDSWINIHSQAGYIHKLMSDQTYLKLINDRLHNENVNTNDEDGSTLHNVIALKKKEILDLRQKLENRKGEKDAAPAKPPNQGLNPRYGVQSGRRPVPSAGISNNGRVRKTHVPASKRPSGIPRVTNRWTKPTASSSRKMFR | |
| 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 | ------MSEQSQLDD ------CCCHHHCCH | 44.32 | 22814378 | |
| 2 | Phosphorylation | ------MSEQSQLDD ------CCCHHHCCH | 44.32 | 22369663 | |
| 5 | Phosphorylation | ---MSEQSQLDDSTI ---CCCHHHCCHHHH | 28.76 | 19795423 | |
| 10 | Phosphorylation | EQSQLDDSTIDKLIP CHHHCCHHHHHHHHH | 27.25 | 28132839 | |
| 11 | Phosphorylation | QSQLDDSTIDKLIPQ HHHCCHHHHHHHHHH | 39.94 | 28132839 | |
| 25 | Phosphorylation | QIFNEMRSNLNNTTN HHHHHHHHHCCCCCC | 44.34 | 24961812 | |
| 30 | Phosphorylation | MRSNLNNTTNKFPKS HHHHCCCCCCCCCCC | 30.58 | 24961812 | |
| 31 | Phosphorylation | RSNLNNTTNKFPKST HHHCCCCCCCCCCCC | 38.24 | 24961812 | |
| 33 | Acetylation | NLNNTTNKFPKSTGG HCCCCCCCCCCCCCC | 62.03 | 24489116 | |
| 43 | Phosphorylation | KSTGGGASDNISANS CCCCCCCCCCCCCCC | 34.17 | 27017623 | |
| 55 | Phosphorylation | ANSNSIRSFNSITTQ CCCCCCHHCCHHHHH | 27.40 | 28889911 | |
| 102 | Phosphorylation | QVHEVCKSTNSILDS HHHHHHHCCCHHHHH | 27.91 | 28889911 | |
| 103 | Phosphorylation | VHEVCKSTNSILDSW HHHHHHCCCHHHHHH | 20.62 | 28889911 | |
| 105 | Phosphorylation | EVCKSTNSILDSWIN HHHHCCCHHHHHHHH | 25.31 | 28889911 | |
| 109 | Phosphorylation | STNSILDSWINIHSQ CCCHHHHHHHHHHHC | 26.81 | 26447709 | |
| 115 | Phosphorylation | DSWINIHSQAGYIHK HHHHHHHHCCCHHHH | 20.23 | 28889911 | |
| 119 | Phosphorylation | NIHSQAGYIHKLMSD HHHHCCCHHHHHHCC | 11.67 | 26447709 | |
| 222 | Acetylation | KTHVPASKRPSGIPR ECCCCHHHCCCCCCC | 71.13 | 25381059 | |
| 225 | Phosphorylation | VPASKRPSGIPRVTN CCHHHCCCCCCCCCC | 54.08 | 27017623 |
| 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 DUO1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DUO1_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 DUO1_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-55, AND MASSSPECTROMETRY. | |
