| UniProt ID | SP105_YEAST | |
|---|---|---|
| UniProt AC | P53148 | |
| Protein Name | Spindle pole body component SPC105 | |
| Gene Name | SPC105 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 917 | |
| Subcellular Localization |
Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Nucleus membrane Peripheral membrane protein Nucleoplasmic side. Chromosome, centromere, kinetochore. Localizes to the nuclear side of the spindle pole body. |
|
| Protein Description | Forms a kinetochore complex with SPC105 which is required for kinetochore binding by a discrete subset of kMAPs (BIM1, BIK1 and SLK19) and motors (CIN8, KAR3). Involved in kinetochore-microtubule binding and the spindle assembly checkpoint.. | |
| Protein Sequence | MNVDERSRIGGREKDAGPGKGILKQNQSSQMTSSFLENPGVRIPTRIITKKEVLDGSNTTSRINTSNLQSMVKRRVSFAPDVTLHSFTFVPEQNNEIKEPRRRKTSTNSPTKISSQEEPLVTSTQIDDARTEEKTAAEEDPDTSGMELTEPIVATPDSNKASQHDPTSMEMTEVFPRSIRQKNPDVEGESIESSQQIDDVEAVREETMELTAIHNVHDYDSISKDTVEGEPIDLTEYESKPYVPNSVSRSTGKSSDYSVERSNDKSDLSKSENKTNSSQPMEITDIFHADPQNPMSLHSDNNINNDGNEMELTQIQTNFDRDNHHIDESPSEKHAFSSNKRRKLDTVSDYAASVTTPVKEAKDTSGEDNDGDLEMMEKMSPITFSDVDNKIGTRSNDVFTIEPGTEDTGMQTATDDEEDGENVDDNGNKIVEKTRLPEIDKEGQSGIALPTQDYTLREFINEVGVGFLDTKLIDDLDKKVNFPLNSFNFVENQRIDNVFSAFYIDIPILEVEAFRCKELWRSINESKDKFKDFEAQIDKSHPPLLLQEYFSSDEKMKQLMRDQLQLVKGYSKLEAAMEWYEWRKKQLNGLELILAENLNTLKREYEKLNEEVEKVNSIRGKIRKLNEAIKEEIRSLKNLPSDSYKPTLMNRIKIEAFKQELMEHSISLSSSNDFTQEMRSLKLAIAKKSNDILTLRSEVASIDKKIEKRKLFTRFDLPKLRDTLKILESLTGVRFLKFSKATLSIAFLQLDDLRVDINLANFKNNPLSSMKVMNDSNNDDMSYHLFTMLLKNVEAEHQDSMLSNLFFAMKKWRPLLKYIKLLKLLFPVKITQTEEEEALLQFKDYDRRNKTAFFYVISLVSFAQGVFSENGQIPMKVHISTQQDYSPSREVLSDRITHKISGVLPSFTKSRIHLEFT | |
| 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 |
|---|---|---|---|---|---|
| 57 | Phosphorylation | KKEVLDGSNTTSRIN CCCCCCCCCCCCCCC | 30.58 | 21440633 | |
| 59 | Phosphorylation | EVLDGSNTTSRINTS CCCCCCCCCCCCCHH | 28.04 | 21440633 | |
| 60 | Phosphorylation | VLDGSNTTSRINTSN CCCCCCCCCCCCHHH | 21.91 | 21440633 | |
| 61 | Phosphorylation | LDGSNTTSRINTSNL CCCCCCCCCCCHHHH | 29.17 | 23749301 | |
| 65 | Phosphorylation | NTTSRINTSNLQSMV CCCCCCCHHHHHHHH | 19.34 | 24961812 | |
| 66 | Phosphorylation | TTSRINTSNLQSMVK CCCCCCHHHHHHHHH | 30.93 | 24961812 | |
| 70 | Phosphorylation | INTSNLQSMVKRRVS CCHHHHHHHHHHHCC | 28.80 | 27214570 | |
| 77 | Phosphorylation | SMVKRRVSFAPDVTL HHHHHHCCCCCCCEE | 17.55 | 21440633 | |
| 83 | Phosphorylation | VSFAPDVTLHSFTFV CCCCCCCEEEEEEEC | 26.57 | 24961812 | |
| 86 | Phosphorylation | APDVTLHSFTFVPEQ CCCCEEEEEEECCCC | 29.15 | 24961812 | |
| 105 | Phosphorylation | KEPRRRKTSTNSPTK CCCCCCCCCCCCCCC | 38.68 | 27017623 | |
| 109 | Phosphorylation | RRKTSTNSPTKISSQ CCCCCCCCCCCCCCC | 33.75 | 21440633 | |
| 111 | Phosphorylation | KTSTNSPTKISSQEE CCCCCCCCCCCCCCC | 40.61 | 30377154 | |
| 114 | Phosphorylation | TNSPTKISSQEEPLV CCCCCCCCCCCCCCC | 27.76 | 24961812 | |
| 115 | Phosphorylation | NSPTKISSQEEPLVT CCCCCCCCCCCCCCC | 45.12 | 21440633 | |
| 135 | Phosphorylation | DARTEEKTAAEEDPD CCHHHHHHHHHCCCC | 34.09 | 25704821 | |
| 143 | Phosphorylation | AAEEDPDTSGMELTE HHHCCCCCCCCEECC | 32.35 | 21440633 | |
| 144 | Phosphorylation | AEEDPDTSGMELTEP HHCCCCCCCCEECCC | 43.45 | 28152593 | |
| 149 | Phosphorylation | DTSGMELTEPIVATP CCCCCEECCCEEECC | 26.80 | 29734811 | |
| 155 | Phosphorylation | LTEPIVATPDSNKAS ECCCEEECCCCCCCC | 19.41 | 24961812 | |
| 158 | Phosphorylation | PIVATPDSNKASQHD CEEECCCCCCCCCCC | 41.24 | 24961812 | |
| 235 | Phosphorylation | EGEPIDLTEYESKPY CCCCCCCCEECCCCC | 32.54 | 24961812 | |
| 239 | Phosphorylation | IDLTEYESKPYVPNS CCCCEECCCCCCCCC | 37.72 | 24961812 | |
| 266 | Phosphorylation | VERSNDKSDLSKSEN CCCCCCHHHCCCCCC | 46.80 | 30377154 | |
| 329 | Phosphorylation | DNHHIDESPSEKHAF CCCCCCCCHHHHCCC | 29.94 | 29734811 | |
| 340 | Acetylation | KHAFSSNKRRKLDTV HCCCCCCCCCCCHHH | 56.37 | 25381059 | |
| 353 | Phosphorylation | TVSDYAASVTTPVKE HHHHHHHHCCCCCHH | 16.30 | 19823750 | |
| 355 | Phosphorylation | SDYAASVTTPVKEAK HHHHHHCCCCCHHCC | 23.92 | 19795423 | |
| 356 | Phosphorylation | DYAASVTTPVKEAKD HHHHHCCCCCHHCCC | 24.75 | 25521595 | |
| 364 | Phosphorylation | PVKEAKDTSGEDNDG CCHHCCCCCCCCCCC | 37.61 | 21551504 | |
| 365 | Phosphorylation | VKEAKDTSGEDNDGD CHHCCCCCCCCCCCC | 50.77 | 21551504 | |
| 380 | Phosphorylation | LEMMEKMSPITFSDV HHHHHHHCCCCHHHC | 24.99 | 22369663 | |
| 383 | Phosphorylation | MEKMSPITFSDVDNK HHHHCCCCHHHCCCC | 22.07 | 25521595 | |
| 385 | Phosphorylation | KMSPITFSDVDNKIG HHCCCCHHHCCCCCC | 28.24 | 20377248 | |
| 408 | Phosphorylation | IEPGTEDTGMQTATD ECCCCCCCCCCCCCC | 28.46 | 21440633 | |
| 412 | Phosphorylation | TEDTGMQTATDDEED CCCCCCCCCCCCCCC | 23.72 | 21440633 | |
| 414 | Phosphorylation | DTGMQTATDDEEDGE CCCCCCCCCCCCCCC | 47.58 | 20377248 | |
| 768 | Phosphorylation | NFKNNPLSSMKVMND CCCCCCCCCCEECCC | 29.64 | 27017623 | |
| 782 | Phosphorylation | DSNNDDMSYHLFTML CCCCCHHHHHHHHHH | 19.18 | 27017623 | |
| 783 | Phosphorylation | SNNDDMSYHLFTMLL CCCCHHHHHHHHHHH | 8.90 | 27017623 | |
| 787 | Phosphorylation | DMSYHLFTMLLKNVE HHHHHHHHHHHHHCC | 17.17 | 27017623 | |
| 906 | Phosphorylation | KISGVLPSFTKSRIH HHHCCCCCCCCCCEE | 41.19 | 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 SP105_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SP105_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 SP105_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-77; THR-356 AND SER-380,AND MASS 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 THR-356 AND SER-380, ANDMASS SPECTROMETRY. | |
