UniProt ID | BRE2_YEAST | |
---|---|---|
UniProt AC | P43132 | |
Protein Name | COMPASS component BRE2 | |
Gene Name | BRE2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 505 | |
Subcellular Localization | Nucleus . Chromosome, telomere . | |
Protein Description | The COMPASS (Set1C) complex 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 | MKLGIIPYQEGTDIVYKNALQGQQEGKRPNLPQMEATHQIKSSVQGTSYEFVRTEDIPLNRRHFVYRPCSANPFFTILGYGCTEYPFDHSGMSVMDRSEGLSISRDGNDLVSVPDQYGWRTARSDVCIKEGMTYWEVEVIRGGNKKFADGVNNKENADDSVDEVQSGIYEKMHKQVNDTPHLRFGVCRREASLEAPVGFDVYGYGIRDISLESIHEGKLNCVLENGSPLKEGDKIGFLLSLPSIHTQIKQAKEFTKRRIFALNSHMDTMNEPWREDAENGPSRKKLKQETTNKEFQRALLEDIEYNDVVRDQIAIRYKNQLFFEATDYVKTTKPEYYSSDKRERQDYYQLEDSYLAIFQNGKYLGKAFENLKPLLPPFSELQYNEKFYLGYWQHGEARDESNDKNTTSAKKKKQQQKKKKGLILRNKYVNNNKLGYYPTISCFNGGTARIISEEDKLEYLDQIRSAYCVDGNSKVNTLDTLYKEQIAEDIVWDIIDELEQIALQQ | |
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 |
---|---|---|---|---|---|
8 | Phosphorylation | MKLGIIPYQEGTDIV CCCCCCCCCCCCCEE | 14.59 | 28132839 | |
12 | Phosphorylation | IIPYQEGTDIVYKNA CCCCCCCCCEEHHHH | 23.07 | 19823750 | |
16 | Phosphorylation | QEGTDIVYKNALQGQ CCCCCEEHHHHHCCC | 10.00 | 19795423 | |
160 | Phosphorylation | NKENADDSVDEVQSG CCCCCCCCHHHHHHH | 31.83 | 22369663 | |
166 | Phosphorylation | DSVDEVQSGIYEKMH CCHHHHHHHHHHHHH | 32.13 | 22369663 | |
169 | Phosphorylation | DEVQSGIYEKMHKQV HHHHHHHHHHHHHHH | 17.02 | 22369663 | |
227 | Phosphorylation | NCVLENGSPLKEGDK CEEEECCCCCCCCCE | 38.34 | 20377248 | |
428 | Phosphorylation | GLILRNKYVNNNKLG CEEEECCCCCCCCCC | 16.38 | 30377154 | |
436 | Phosphorylation | VNNNKLGYYPTISCF CCCCCCCCCCEEEEE | 19.39 | 30377154 | |
437 | Phosphorylation | NNNKLGYYPTISCFN CCCCCCCCCEEEEEC | 7.66 | 30377154 | |
439 | Phosphorylation | NKLGYYPTISCFNGG CCCCCCCEEEEECCC | 14.92 | 30377154 | |
441 | Phosphorylation | LGYYPTISCFNGGTA CCCCCEEEEECCCEE | 18.35 | 30377154 |
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 BRE2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BRE2_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 BRE2_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-227, AND MASSSPECTROMETRY. | |
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, AND MASSSPECTROMETRY. |