UniProt ID | SET1_YEAST | |
---|---|---|
UniProt AC | P38827 | |
Protein Name | Histone-lysine N-methyltransferase, H3 lysine-4 specific | |
Gene Name | SET1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 1080 | |
Subcellular Localization | Nucleus . Chromosome . | |
Protein Description | Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.. | |
Protein Sequence | MSNYYRRAHASSGSYRQPQEQPQYSRSGHYQYSNGHSHQQYSSQYNQRRRYNHNDGTRRRYNDDRPHSSNNASTRQYYATNNSQSGPYVNKKSDISSRRGMSQSRYSNSNVHNTLASSSGSLPTESALLLQQRPPSVLRYNTDNLKSKFHYFDPIKGEFFNKDKMLSWKATDKEFSETGYYVVKELQDGQFKFKIKHRHPEIKASDPRNENGIMTSGKVATHRKCRNSLILLPRISYDRYSLGPPPSCEIVVYPAQDSTTTNIQDISIKNYFKKYGEISHFEAFNDPNSALPLHVYLIKYASSDGKINDAAKAAFSAVRKHESSGCFIMGFKFEVILNKHSILNNIISKFVEINVKKLQKLQENLKKAKEKEAENEKAKELQGKDITLPKEPKVDTLSHSSGSEKRIPYDLLGVVNNRPVLHVSKIFVAKHRFCVEDFKYKLRGYRCAKFIDHPTGIYIIFNDIAHAQTCSNAESGNLTIMSRSRRIPILIKFHLILPRFQNRTRFNKSSSSSNSTNVPIKYESKEEFIEATAKQILKDLEKTLHVDIKKRLIGPTVFDALDHANFPELLAKRELKEKEKRQQIASKIAEDELKRKEEAKRDFDLFGLYGGYAKSNKRNLKRHNSLALDHTSLKRKKLSNGIKPMAHLLNEETDSKETTPLNDEGITRVSKEHDEEDENMTSSSSEEEEEEAPDKKFKSESEPTTPESDHLHGIKPLVPDQNGSSDVLDASSMYKPTATEIPEPVYPPEEYDLKYSQTLSSMDLQNAIKDEEDMLILKQLLSTYTPTVTPETSAALEYKIWQSRRKVLEEEKASDWQIELNGTLFDSELQPGSSFKAEGFRKIADKLKINYLPHRRRVHQPLNTVNIHNERNEYTPELCQREESSNKEPSDSVPQEVSSSRDNRASNRRFQQDIEAQKAAIGTESELLSLNQLNKRKKPVMFARSAIHNWGLYALDSIAAKEMIIEYVGERIRQPVAEMREKRYLKNGIGSSYLFRVDENTVIDATKKGGIARFINHCCDPNCTAKIIKVGGRRRIVIYALRDIAASEELTYDYKFEREKDDEERLPCLCGAPNCKGFLN | |
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 |
---|---|---|---|---|---|
32 | Phosphorylation | SRSGHYQYSNGHSHQ CCCCCCCCCCCCCCH | 9.27 | 27017623 | |
33 | Phosphorylation | RSGHYQYSNGHSHQQ CCCCCCCCCCCCCHH | 22.32 | 27017623 | |
42 | Phosphorylation | GHSHQQYSSQYNQRR CCCCHHHHHHHHHHH | 13.46 | 27017623 | |
80 | Phosphorylation | STRQYYATNNSQSGP CCCEEEECCCCCCCC | 20.86 | 30377154 | |
96 | Phosphorylation | VNKKSDISSRRGMSQ CCCCCCCCCCCCCCC | 23.84 | 30377154 | |
192 | Acetylation | ELQDGQFKFKIKHRH ECCCCCEEEEEEECC | 37.55 | 24489116 | |
509 | Phosphorylation | NRTRFNKSSSSSNST CCCCCCCCCCCCCCC | 36.23 | 30377154 | |
625 | Phosphorylation | RNLKRHNSLALDHTS HHHHHHCCCCCCCHH | 14.64 | 17330950 | |
634 | Acetylation | ALDHTSLKRKKLSNG CCCCHHHHHHHHHCC | 63.04 | 25381059 | |
653 | Phosphorylation | AHLLNEETDSKETTP HHHHCCCCCCCCCCC | 39.12 | 24961812 | |
655 | Phosphorylation | LLNEETDSKETTPLN HHCCCCCCCCCCCCC | 39.55 | 20377248 | |
658 | Phosphorylation | EETDSKETTPLNDEG CCCCCCCCCCCCHHC | 37.13 | 22369663 | |
659 | Phosphorylation | ETDSKETTPLNDEGI CCCCCCCCCCCHHCC | 27.20 | 22369663 | |
667 | Phosphorylation | PLNDEGITRVSKEHD CCCHHCCCEECCCCC | 35.56 | 24961812 | |
699 | Phosphorylation | APDKKFKSESEPTTP CCCCCCCCCCCCCCC | 49.87 | 21440633 | |
701 | Phosphorylation | DKKFKSESEPTTPES CCCCCCCCCCCCCCC | 56.84 | 21440633 | |
704 | Phosphorylation | FKSESEPTTPESDHL CCCCCCCCCCCCCCC | 51.43 | 21551504 | |
705 | Phosphorylation | KSESEPTTPESDHLH CCCCCCCCCCCCCCC | 35.46 | 21440633 | |
708 | Phosphorylation | SEPTTPESDHLHGIK CCCCCCCCCCCCCCC | 31.37 | 21440633 | |
783 | Phosphorylation | ILKQLLSTYTPTVTP HHHHHHHCCCCCCCH | 31.24 | 24961812 | |
785 | Phosphorylation | KQLLSTYTPTVTPET HHHHHCCCCCCCHHC | 16.75 | 28889911 | |
787 | Phosphorylation | LLSTYTPTVTPETSA HHHCCCCCCCHHCHH | 29.25 | 27017623 | |
798 | Phosphorylation | ETSAALEYKIWQSRR HCHHHHHHHHHHHHH | 14.50 | 27017623 | |
874 | Phosphorylation | IHNERNEYTPELCQR CCCCCCCCCHHHHHH | 31.01 | 29136822 | |
875 | Phosphorylation | HNERNEYTPELCQRE CCCCCCCCHHHHHHH | 12.24 | 19547744 | |
890 | Phosphorylation | ESSNKEPSDSVPQEV HHCCCCCCCCCCHHH | 43.54 | 29688323 | |
892 | Phosphorylation | SNKEPSDSVPQEVSS CCCCCCCCCCHHHHC | 39.78 | 29688323 | |
898 | Phosphorylation | DSVPQEVSSSRDNRA CCCCHHHHCCCCCHH | 23.11 | 29688323 | |
899 | Phosphorylation | SVPQEVSSSRDNRAS CCCHHHHCCCCCHHH | 34.27 | 29688323 | |
900 | Phosphorylation | VPQEVSSSRDNRASN CCHHHHCCCCCHHHH | 35.83 | 29688323 | |
982 | Acetylation | PVAEMREKRYLKNGI HHHHHHHHHHHHCCC | 35.66 | 22865919 |
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 SET1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SET1_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 SET1_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-655; THR-785 ANDTHR-875, 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-625, 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-625, AND MASSSPECTROMETRY. |