| UniProt ID | SMY1_YEAST | |
|---|---|---|
| UniProt AC | P32364 | |
| Protein Name | Kinesin-related protein SMY1 | |
| Gene Name | SMY1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 656 | |
| Subcellular Localization | Cytoplasm, cytoskeleton . | |
| Protein Description | Possible microtubule-based motor that can interact or substitute with myosin 2 (MYO2).. | |
| Protein Sequence | MHWNIISKEQSSSSVSLPTLDSSEPCHIEVILRAIPEKGLQNNESTFKIDPYENTVLFRTNNPLHETTKETHSTFQFDKVFDANATQEDVQKFLVHPIINDVLNGYNGTVITYGPSFSGKSYSLIGSKESEGILPNICKTLFDTLEKNEETKGDSFSVSVLAFEIYMEKTYDLLVPLPERKPLKLHRSSSKMDLEIKDICPAHVGSYEDLRSYIQAVQNVGNRMACGDKTERSRSHLVFQLHVEQRNRKDDILKNSSLYLVDLHGAEKFDKRTESTLSQDALKKLNQSIEALKNTVRSLSMKERDSAYSAKGSHSSAYRESQLTEVLKDSLGGNRKTKVILTCFLSNVPTTLSTLEFGDSIRQINNKVTDNTTGLNLKKKMDLFIQDMKIKDDNYVAQINILKAEIDSLKSLHNKSLPEDDEKKMLENTKKENIKLKLQLDSITQLLSSSTNEDPNNRIDEEVSEILTKRCEQIAQLELSFDRQMNSNSKLQQELEYKKSKEEALESMNVRLLEQIQLQEREIQELLTTNAILKGELETHTKLTETRSERIKSLESSVKELSLNKSAIPSPRRGSMSSSSGNTMLHIEEGSEISNSPWSANTSSKPLVWGARKVSSSSIATTGSQESFVARPFKKGLNLHSIKVTSSTPKSPSSGS | |
| 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 |
|---|---|---|---|---|---|
| 13 | Phosphorylation | ISKEQSSSSVSLPTL CCCCCCCCCCCCCCC | 39.75 | 21440633 | |
| 16 | Phosphorylation | EQSSSSVSLPTLDSS CCCCCCCCCCCCCCC | 30.49 | 21440633 | |
| 188 | Phosphorylation | KPLKLHRSSSKMDLE CCCCCCCCCCCCCCC | 28.37 | 21440633 | |
| 189 | Phosphorylation | PLKLHRSSSKMDLEI CCCCCCCCCCCCCCH | 33.65 | 28889911 | |
| 190 | Phosphorylation | LKLHRSSSKMDLEIK CCCCCCCCCCCCCHH | 32.99 | 17330950 | |
| 206 | Phosphorylation | ICPAHVGSYEDLRSY HCCCCCCCHHHHHHH | 25.02 | 27214570 | |
| 207 | Phosphorylation | CPAHVGSYEDLRSYI CCCCCCCHHHHHHHH | 13.92 | 27214570 | |
| 353 | Phosphorylation | SNVPTTLSTLEFGDS CCCCCCHHHHHCCHH | 28.93 | 27214570 | |
| 553 | Phosphorylation | TRSERIKSLESSVKE HHHHHHHHHHHHHHH | 34.69 | 23749301 | |
| 562 | Phosphorylation | ESSVKELSLNKSAIP HHHHHHHHCCCCCCC | 30.87 | 19684113 | |
| 565 | Ubiquitination | VKELSLNKSAIPSPR HHHHHCCCCCCCCCC | 46.70 | 19722269 | |
| 566 | Phosphorylation | KELSLNKSAIPSPRR HHHHCCCCCCCCCCC | 30.29 | 25005228 | |
| 570 | Phosphorylation | LNKSAIPSPRRGSMS CCCCCCCCCCCCCCC | 25.56 | 21551504 | |
| 575 | Phosphorylation | IPSPRRGSMSSSSGN CCCCCCCCCCCCCCC | 17.43 | 21440633 | |
| 577 | Phosphorylation | SPRRGSMSSSSGNTM CCCCCCCCCCCCCEE | 28.85 | 19779198 | |
| 578 | Phosphorylation | PRRGSMSSSSGNTML CCCCCCCCCCCCEEE | 21.63 | 20377248 | |
| 579 | Phosphorylation | RRGSMSSSSGNTMLH CCCCCCCCCCCEEEE | 34.65 | 19779198 | |
| 583 | Phosphorylation | MSSSSGNTMLHIEEG CCCCCCCEEEEEECC | 25.33 | 21440633 | |
| 591 | Phosphorylation | MLHIEEGSEISNSPW EEEEECCCCCCCCCC | 34.73 | 21551504 | |
| 615 | Phosphorylation | VWGARKVSSSSIATT EEEEEEECCCCCCCC | 27.77 | 19823750 | |
| 616 | Phosphorylation | WGARKVSSSSIATTG EEEEEECCCCCCCCC | 30.96 | 19823750 | |
| 617 | Phosphorylation | GARKVSSSSIATTGS EEEEECCCCCCCCCC | 20.46 | 24961812 | |
| 618 | Phosphorylation | ARKVSSSSIATTGSQ EEEECCCCCCCCCCC | 20.42 | 21440633 | |
| 621 | Phosphorylation | VSSSSIATTGSQESF ECCCCCCCCCCCHHH | 29.98 | 20377248 | |
| 622 | Phosphorylation | SSSSIATTGSQESFV CCCCCCCCCCCHHHC | 26.30 | 21440633 | |
| 624 | Phosphorylation | SSIATTGSQESFVAR CCCCCCCCCHHHCCC | 28.78 | 20377248 | |
| 627 | Phosphorylation | ATTGSQESFVARPFK CCCCCCHHHCCCCCC | 19.86 | 20377248 | |
| 646 | Phosphorylation | LHSIKVTSSTPKSPS CEEEEEEECCCCCCC | 34.89 | 19823750 | |
| 647 | Phosphorylation | HSIKVTSSTPKSPSS EEEEEEECCCCCCCC | 39.09 | 19823750 | |
| 648 | Phosphorylation | SIKVTSSTPKSPSSG EEEEEECCCCCCCCC | 34.21 | 19823750 | |
| 651 | Phosphorylation | VTSSTPKSPSSGS-- EEECCCCCCCCCC-- | 31.08 | 25752575 | |
| 653 | Phosphorylation | SSTPKSPSSGS---- ECCCCCCCCCC---- | 55.19 | 21440633 | |
| 654 | Phosphorylation | STPKSPSSGS----- CCCCCCCCCC----- | 46.57 | 19823750 | |
| 656 | Phosphorylation | PKSPSSGS------- CCCCCCCC------- | 38.71 | 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 SMY1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SMY1_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 SMY1_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-190; SER-553 ANDSER-575, AND MASS SPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, AND MASSSPECTROMETRY. | |
