UniProt ID | DSN1_YEAST | |
---|---|---|
UniProt AC | P40568 | |
Protein Name | Kinetochore-associated protein DSN1 | |
Gene Name | DSN1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 576 | |
Subcellular Localization | Nucleus. Chromosome, centromere, kinetochore. Associated with the kinetochore. | |
Protein Description | Acts as essential component of the kinetochore MIND complex, which is required for the spindle checkpoint and kinetochore integrity. MIND plays a role in establishing a bipolar spindle-kinetochore interaction by joining kinetochore subunits contacting DNA to those contacting microtubules.. | |
Protein Sequence | MSLEPTQTVSGTPPMLHQRTHKQVYPLRMETIPILESDSKATLQSNEPTQKDEEETEYFENKQSVSNLSPDLKFKRHKNKHIQGFPTLGERLDNLQDIKKAKRVENFNSSAPIADDNHSGDATANATANATANATANVNASAMPAPYMPYYYYYHPMNAPTPAMIPYPGSPMHSIMPNSSLQPFYSQPTAAGGPDMTTPQNISSSQQLLPAPQLFPYGSFHQQQLQQPHYIQRTRERKKSIGSQRGRRLSMLASQANGGSTIISPHKDIPEEDFYTVVGNASFGKNLQIRQLFNWCLMRSLHKLELKAKNQEEEGELEHLTKKSKLESTKAETDYVDPKRLAMVIIKEFVDDLKKDHIAIDWEDEEKYEDEDEEKILDNTENYDDTELRQLFQENDDDDDDDDEVDYSEIQRSRRKFSERRKALPKEPKKLLPNSKNVENTKNLSILTSKVNAIKNEVKEWAVTLDTSRPDLEWQELTSFSSQPLEPLSDTEEPDLAIADVETKLETKVDELRYQSHILNSHSLALNEITNSKVNKLNIETMRKISSETDDDHSQVINPQQLLKGLSLSFSKKLDL | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSLEPTQTV ------CCCCCCCCC | 41.25 | 28152593 | |
6 | Phosphorylation | --MSLEPTQTVSGTP --CCCCCCCCCCCCC | 27.74 | 30377154 | |
8 | Phosphorylation | MSLEPTQTVSGTPPM CCCCCCCCCCCCCCC | 21.08 | 28132839 | |
10 | Phosphorylation | LEPTQTVSGTPPMLH CCCCCCCCCCCCCCC | 40.09 | 28152593 | |
12 | Phosphorylation | PTQTVSGTPPMLHQR CCCCCCCCCCCCCCC | 19.40 | 15665377 | |
15 | Oxidation | TVSGTPPMLHQRTHK CCCCCCCCCCCCCCC | 5.70 | 15665377 | |
56 | Phosphorylation | TQKDEEETEYFENKQ CCCCHHHHHHHHCHH | 38.99 | 28889911 | |
64 | Phosphorylation | EYFENKQSVSNLSPD HHHHCHHHHHCCCCC | 29.17 | 22369663 | |
66 | Phosphorylation | FENKQSVSNLSPDLK HHCHHHHHCCCCCCH | 36.98 | 22369663 | |
69 | Phosphorylation | KQSVSNLSPDLKFKR HHHHHCCCCCCHHHH | 22.18 | 22369663 | |
240 | Phosphorylation | RTRERKKSIGSQRGR HHHHHHHHHCCHHHH | 34.91 | 21440633 | |
243 | Phosphorylation | ERKKSIGSQRGRRLS HHHHHHCCHHHHHHH | 18.29 | 24961812 | |
250 | Phosphorylation | SQRGRRLSMLASQAN CHHHHHHHHHHHHCC | 15.22 | 19823750 | |
254 | Phosphorylation | RRLSMLASQANGGST HHHHHHHHHCCCCCE | 26.34 | 24961812 | |
260 | Phosphorylation | ASQANGGSTIISPHK HHHCCCCCEEECCCC | 20.17 | 24961812 | |
261 | Phosphorylation | SQANGGSTIISPHKD HHCCCCCEEECCCCC | 26.13 | 24961812 | |
264 | Phosphorylation | NGGSTIISPHKDIPE CCCCEEECCCCCCCH | 19.66 | 28889911 | |
282 | Phosphorylation | YTVVGNASFGKNLQI EEEECCCCCCCCHHH | 38.23 | 21551504 | |
380 | Phosphorylation | EEKILDNTENYDDTE HHHHHHCCCCCCHHH | 25.85 | 27214570 | |
383 | Phosphorylation | ILDNTENYDDTELRQ HHHCCCCCCHHHHHH | 14.68 | 29688323 | |
386 | Phosphorylation | NTENYDDTELRQLFQ CCCCCCHHHHHHHHH | 33.74 | 28889911 | |
514 | Phosphorylation | TKVDELRYQSHILNS HHHHHHHHHHHHHHH | 27.30 | 27017623 | |
516 | Phosphorylation | VDELRYQSHILNSHS HHHHHHHHHHHHHHH | 11.99 | 27017623 | |
521 | Phosphorylation | YQSHILNSHSLALNE HHHHHHHHHHHHHHH | 15.82 | 19779198 | |
523 | Phosphorylation | SHILNSHSLALNEIT HHHHHHHHHHHHHHC | 18.37 | 19779198 | |
532 | Phosphorylation | ALNEITNSKVNKLNI HHHHHCCHHHHHCCH | 29.36 | 19779198 | |
554 | Phosphorylation | SETDDDHSQVINPQQ CCCCCCCHHCCCHHH | 32.89 | 28152593 |
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 DSN1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DSN1_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 DSN1_YEAST !! |
Kegg Drug | ||||||
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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-69, AND MASSSPECTROMETRY. |