UniProt ID | MAD1_YEAST | |
---|---|---|
UniProt AC | P40957 | |
Protein Name | Spindle assembly checkpoint component MAD1 | |
Gene Name | MAD1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 749 | |
Subcellular Localization | Nucleus. | |
Protein Description | Central component of the spindle assembly checkpoint. Thought to recruit MAD2 to unattached kinetochores. During checkpoint activity, MAD2 is relayed from the MAD1-MAD2 complex to the mitotic checkpoint complex (MCC). The formation of a MAD1-BUB1-BUB3 complex seems to be required for the spindle checkpoint mechanism.. | |
Protein Sequence | MDVRAALQCFFSALSGRFTGKKLGLEIYSIQYKMSNSGGSSPFLESPGGSPDVGSTNGQSNRQIQALQFKLNTLQNEYEIEKLQLQKQTNILEKKYKATIDELEKALNDTKYLYESNDKLEQELKSLKERSANSMNDKDKCIEELRTTLQNKDLEMETLRQQYDSKLSKVTNQCDHFKLEAESSHSLLMKYEKEIKRQSVDIKDLQHQVMEKDDELSSVKASKMINSHPNYSTEEFNELTEMNKMIQDQVQYTKELELANMQQANELKKLKQSQDTSTFWKLENEKLQNKLSQLHVLESQYENLQLENIDLKSKLTKWEIYNDSDDDDDNNVNNNDNNNNNKNDNNNDNNNDTSNNNNINNNNRTKNNIRNNPEEIIRDWKLTKKECLILTDMNDKLRLDNNNLKLLNDEMALERNQILDLNKNYENNIVNLKRLNHELEQQKSLSFEECRLLREQLDGLYSAQNNALLEVENSETHASNKNVNEDMNNLIDTYKNKTEDLTNELKKLNDQLLSNSNDVETQRKKRKLTSDQIGLNYSQRLNELQLENVSVSRELSKAQTTIQLLQEKLEKLTKLKEKKIRILQLRDGPFIKDQFIKKNKLLLLEKENADLLNELKKNNPAVETVPISVYDSLNFELKQFEQEVFKSNKRFSRLKQVFNNKSLEFIDVVNSLLGFKLEFQQDSRVKIFSCFKPEKYLIADLNENTLKSNLDADIEGWDDLMNLWVEDRGQLPCFLATITLRLWEQRQAK | |
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 |
---|---|---|---|---|---|
41 | Phosphorylation | MSNSGGSSPFLESPG ECCCCCCCCCCCCCC | 23.97 | 19779198 | |
134 | Phosphorylation | LKERSANSMNDKDKC HHHHHHHCCCCHHHH | 20.76 | 27017623 | |
199 | Phosphorylation | EKEIKRQSVDIKDLQ HHHHHHCCCCHHHHH | 26.28 | 30377154 | |
316 | Phosphorylation | IDLKSKLTKWEIYND CCCCCCCCEEEECCC | 37.54 | 22369663 | |
321 | Phosphorylation | KLTKWEIYNDSDDDD CCCEEEECCCCCCCC | 11.03 | 22369663 | |
324 | Phosphorylation | KWEIYNDSDDDDDNN EEEECCCCCCCCCCC | 39.02 | 22369663 | |
381 | Acetylation | EEIIRDWKLTKKECL HHHHHHHHCCCCEEE | 51.04 | 24489116 | |
391 | Phosphorylation | KKECLILTDMNDKLR CCEEEEEECCCCCCC | 26.63 | 25704821 | |
433 | Acetylation | ENNIVNLKRLNHELE CCCCCCHHHHHHHHH | 50.03 | 24489116 | |
446 | Phosphorylation | LEQQKSLSFEECRLL HHHHHCCCHHHHHHH | 37.39 | 30377154 | |
498 | Phosphorylation | IDTYKNKTEDLTNEL HHHHHHHHHHHHHHH | 44.09 | 21440633 | |
502 | Phosphorylation | KNKTEDLTNELKKLN HHHHHHHHHHHHHHH | 38.68 | 20377248 | |
552 | Phosphorylation | QLENVSVSRELSKAQ HCCCCHHHHHHHHHH | 16.72 | 30377154 | |
568 | Acetylation | TIQLLQEKLEKLTKL HHHHHHHHHHHHHHH | 49.32 | 24489116 | |
655 | Acetylation | NKRFSRLKQVFNNKS CCHHHHHHHHHCCCC | 43.22 | 25381059 |
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 MAD1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MAD1_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 MAD1_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 THR-502, AND MASSSPECTROMETRY. |