UniProt ID | SET2_YEAST | |
---|---|---|
UniProt AC | P46995 | |
Protein Name | Histone-lysine N-methyltransferase, H3 lysine-36 specific | |
Gene Name | SET2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 733 | |
Subcellular Localization | Nucleus. Chromosome . | |
Protein Description | Histone methyltransferase that methylates histone H3 to form H3K36me. Involved in transcription elongation as well as in transcription repression. The methyltransferase activity requires the recruitment to the RNA polymerase II, which is CTK1 dependent.. | |
Protein Sequence | MSKNQSVSASEDEKEILNNNAEGHKPQRLFDQEPDLTEEALTKFENLDDCIYANKRIGTFKNNDFMECDCYEEFSDGVNHACDEDSDCINRLTLIECVNDLCSSCGNDCQNQRFQKKQYAPIAIFKTKHKGYGVRAEQDIEANQFIYEYKGEVIEEMEFRDRLIDYDQRHFKHFYFMMLQNGEFIDATIKGSLARFCNHSCSPNAYVNKWVVKDKLRMGIFAQRKILKGEEITFDYNVDRYGAQAQKCYCEEPNCIGFLGGKTQTDAASLLPQNIADALGVTVSMEKKWLKLKKLSGEPIIKNENENINIEFLQSLEVQPIDSPVDVTKIMSVLLQQDNKIIASKLLKRLFTIDDDSLRHQAIKLHGYTCFSKMLKLFITEQPQVDGKGNETEEDDIKFIKGILDFLLELPKTTRNGIESSQIDNVVKTLPAKFPFLKPNCDELLEKWSKFETYKRITKKDINVAASKMIDLRRVRLPPGWEIIHENGRPLYYNAEQKTKLHYPPSGSSKVFSSRSNTQVNSPSSSGIPKTPGALDSKKHKLSDEEYERKKQKRLEYERIALERAKQEELESLKQKLKLENERKSVLEDIIAEANKQKELQKEEAKKLVEAKEAKRLKRKTVSQSQRLEHNWNKFFASFVPNLIKKNPQSKQFDHENIKQCAKDIVKILTTKELKKDSSRAPPDDLTKGKRHKVKEFINSYMDKIILKKKQKKALALSSASTRMSSPPPSTSS | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSKNQSVSA ------CCCCCCCCC | 40.07 | 21126336 | |
6 | Phosphorylation | --MSKNQSVSASEDE --CCCCCCCCCCHHH | 27.68 | 22890988 | |
8 | Phosphorylation | MSKNQSVSASEDEKE CCCCCCCCCCHHHHH | 31.18 | 22890988 | |
10 | Phosphorylation | KNQSVSASEDEKEIL CCCCCCCCHHHHHHH | 37.77 | 25521595 | |
127 | Phosphorylation | APIAIFKTKHKGYGV CCEEEEECCCCCCCC | 27.86 | 28889911 | |
263 | Phosphorylation | IGFLGGKTQTDAASL EEECCCCCHHCHHHH | 39.72 | 27017623 | |
265 | Phosphorylation | FLGGKTQTDAASLLP ECCCCCHHCHHHHCC | 32.60 | 27017623 | |
284 | Phosphorylation | DALGVTVSMEKKWLK HHHCCCEEHHHHHHH | 16.32 | 27017623 | |
499 | Phosphorylation | YYNAEQKTKLHYPPS EEECCCCCCCCCCCC | 38.23 | 21440633 | |
509 | Phosphorylation | HYPPSGSSKVFSSRS CCCCCCCCCCEECCC | 36.04 | 21440633 | |
513 | Phosphorylation | SGSSKVFSSRSNTQV CCCCCCEECCCCCCC | 28.03 | 21440633 | |
514 | Phosphorylation | GSSKVFSSRSNTQVN CCCCCEECCCCCCCC | 28.41 | 21440633 | |
516 | Phosphorylation | SKVFSSRSNTQVNSP CCCEECCCCCCCCCC | 46.29 | 22369663 | |
518 | Phosphorylation | VFSSRSNTQVNSPSS CEECCCCCCCCCCCC | 34.83 | 22369663 | |
522 | Phosphorylation | RSNTQVNSPSSSGIP CCCCCCCCCCCCCCC | 27.57 | 22369663 | |
524 | Phosphorylation | NTQVNSPSSSGIPKT CCCCCCCCCCCCCCC | 36.64 | 20377248 | |
525 | Phosphorylation | TQVNSPSSSGIPKTP CCCCCCCCCCCCCCC | 35.65 | 22369663 | |
526 | Phosphorylation | QVNSPSSSGIPKTPG CCCCCCCCCCCCCCC | 45.11 | 21440633 | |
543 | Phosphorylation | DSKKHKLSDEEYERK CCCCCCCCHHHHHHH | 48.02 | 30377154 | |
585 | Phosphorylation | KLENERKSVLEDIIA HHHHHHHHHHHHHHH | 37.85 | 30377154 | |
695 | Acetylation | KGKRHKVKEFINSYM CCCHHHHHHHHHHHH | 52.27 | 24489116 | |
718 | Phosphorylation | QKKALALSSASTRMS HHHHHHHHCCCHHCC | 20.46 | 28889911 | |
719 | Phosphorylation | KKALALSSASTRMSS HHHHHHHCCCHHCCC | 27.39 | 30377154 | |
721 | Phosphorylation | ALALSSASTRMSSPP HHHHHCCCHHCCCCC | 20.63 | 28889911 | |
722 | Phosphorylation | LALSSASTRMSSPPP HHHHCCCHHCCCCCC | 30.06 | 28889911 | |
725 | Phosphorylation | SSASTRMSSPPPSTS HCCCHHCCCCCCCCC | 36.08 | 21551504 | |
726 | Phosphorylation | SASTRMSSPPPSTSS CCCHHCCCCCCCCCC | 31.89 | 23749301 | |
730 | Phosphorylation | RMSSPPPSTSS---- HCCCCCCCCCC---- | 46.85 | 21551504 | |
731 | Phosphorylation | MSSPPPSTSS----- CCCCCCCCCC----- | 38.47 | 21551504 | |
732 | Phosphorylation | SSPPPSTSS------ CCCCCCCCC------ | 38.09 | 21551504 | |
733 | Phosphorylation | SPPPSTSS------- CCCCCCCC------- | 44.31 | 21551504 |
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 SET2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SET2_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 SET2_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-522, AND MASSSPECTROMETRY. |