| UniProt ID | BIK1_YEAST | |
|---|---|---|
| UniProt AC | P11709 | |
| Protein Name | Nuclear fusion protein BIK1 | |
| Gene Name | BIK1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 440 | |
| Subcellular Localization | Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Cytoplasm, cytoskeleton, spindle. Cytoplasm. And mitotic spindle. | |
| Protein Description | Required for nuclear fusion, chromosome disjunction, and nuclear segregation during mitosis. Probably required for the formation or stabilization of microtubules during mitosis and for spindle pole body fusion during conjugation.. | |
| Protein Sequence | MDRYQRKIGCFIQIPNLGRGQLKYVGPVDTKAGMFAGVDLLANIGKNDGSFMGKKYFQTEYPQSGLFIQLQKVASLIEKASISQTSRRTTMEPLSIPKNRSIVRLTNQFSPMDDPKSPTPMRSFRITSRHSGNQQSMDQEASDHHQQQEFGYDNREDRMEVDSILSSDRKANHNTTSDWKPDNGHMNDLNSSEVTIELREAQLTIEKLQRKQLHYKRLLDDQRMVLEEVQPTFDRYEATIQEREKEIDHLKQQLELERRQQAKQKQFFDAENEQLLAVVSQLHEEIKENEERNLSHNQPTGANEDVELLKKQLEQLRNIEDQFELHKTKWAKEREQLKMHNDSLSKEYQNLSKELFLTKPQDSSSEEVASLTKKLEEANEKIKQLEQAQAQTAVESLPIFDPPAPVDTTAGRQQWCEHCDTMGHNTAECPHHNPDNQQFF | |
| 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 |
|---|---|---|---|---|---|
| 75 | Phosphorylation | IQLQKVASLIEKASI HHHHHHHHHHHHHCC | 32.63 | 30377154 | |
| 81 | Phosphorylation | ASLIEKASISQTSRR HHHHHHHCCCCCCCC | 33.56 | 20377248 | |
| 83 | Phosphorylation | LIEKASISQTSRRTT HHHHHCCCCCCCCCC | 25.55 | 19823750 | |
| 85 | Phosphorylation | EKASISQTSRRTTME HHHCCCCCCCCCCCC | 19.87 | 20377248 | |
| 86 | Phosphorylation | KASISQTSRRTTMEP HHCCCCCCCCCCCCC | 16.48 | 20377248 | |
| 89 | Phosphorylation | ISQTSRRTTMEPLSI CCCCCCCCCCCCCCC | 29.41 | 22369663 | |
| 90 | Phosphorylation | SQTSRRTTMEPLSIP CCCCCCCCCCCCCCC | 20.09 | 22369663 | |
| 95 | Phosphorylation | RTTMEPLSIPKNRSI CCCCCCCCCCCCCHH | 47.78 | 19823750 | |
| 101 | Phosphorylation | LSIPKNRSIVRLTNQ CCCCCCCHHEEECCC | 34.52 | 20377248 | |
| 106 | Phosphorylation | NRSIVRLTNQFSPMD CCHHEEECCCCCCCC | 19.19 | 19823750 | |
| 110 | Phosphorylation | VRLTNQFSPMDDPKS EEECCCCCCCCCCCC | 15.00 | 17330950 | |
| 117 | Phosphorylation | SPMDDPKSPTPMRSF CCCCCCCCCCCCCCE | 39.12 | 22369663 | |
| 119 | Phosphorylation | MDDPKSPTPMRSFRI CCCCCCCCCCCCEEE | 36.49 | 22369663 | |
| 131 | Phosphorylation | FRITSRHSGNQQSMD EEEEECCCCCCCCCC | 38.03 | 28889911 | |
| 136 | Phosphorylation | RHSGNQQSMDQEASD CCCCCCCCCCCCHHH | 17.98 | 30377154 | |
| 163 | Phosphorylation | EDRMEVDSILSSDRK HHHHHHHHHHCCCCC | 30.52 | 22369663 | |
| 166 | Phosphorylation | MEVDSILSSDRKANH HHHHHHHCCCCCCCC | 28.64 | 22369663 | |
| 167 | Phosphorylation | EVDSILSSDRKANHN HHHHHHCCCCCCCCC | 37.68 | 22369663 | |
| 207 | Acetylation | EAQLTIEKLQRKQLH HHHHHHHHHHHCHHH | 46.17 | 24489116 | |
| 363 | Phosphorylation | FLTKPQDSSSEEVAS HCCCCCCCCHHHHHH | 30.43 | 22369663 | |
| 364 | Phosphorylation | LTKPQDSSSEEVASL CCCCCCCCHHHHHHH | 50.48 | 22369663 | |
| 365 | Phosphorylation | TKPQDSSSEEVASLT CCCCCCCHHHHHHHH | 41.55 | 22369663 | |
| 370 | Phosphorylation | SSSEEVASLTKKLEE CCHHHHHHHHHHHHH | 41.57 | 22369663 | |
| 372 | Phosphorylation | SEEVASLTKKLEEAN HHHHHHHHHHHHHHH | 24.52 | 23749301 |
| 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 BIK1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BIK1_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 BIK1_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-83; THR-89; THR-90;SER-95; SER-110; SER-117; SER-167; SER-365 AND SER-370, 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-110, AND MASSSPECTROMETRY. | |
