UniProt ID | NGR1_YEAST | |
---|---|---|
UniProt AC | P32831 | |
Protein Name | Negative growth regulatory protein NGR1 | |
Gene Name | NGR1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 672 | |
Subcellular Localization | ||
Protein Description | May be an RNA-binding protein involved in control of an RNA processing pathway that influences the regulation of cell growth in early log phase. Can bind to RNA and single-stranded DNA but not double-stranded DNA.. | |
Protein Sequence | MMSNVANASQRQENPYIIPLPPSSTVETSTEPPRTLWMGDLDPSFDEATIEEIWSKLDKKVIVKLIRAKKNLLIPCSSTSSSNNNTSEENAENQQSASNSTDQLDNSQMININGISFIDPSTTQLHHAGYCFVEFETQKDAKFALSLNATPLPNFYSPTTNSQTNPTFKRTFRLNWASGATLQSSIPSTPEFSLFVGDLSPTATEADLLSLFQTRFKSVKTVRVMTDPLTGSSRCFGFVRFGDEDERRRALIEMSGKWFQGRALRVAYATPRNNMMLQLQEQQQQQQQLQQQHQQLDQEDNNGPLLIKTANNLIQNNSNMLPLNALHNAPPMHLNEGGISNMRVNDSLPSNTYNTDPTNTTVFVGGLVPKTTEFQLRSLFKPFGPILNVRIPNGKNCGFVKFEKRIDAEASIQGLQGFIVGGSPIRLSWGRPSSSNAKTNSTIMGASQYMSSNGLRAPSAASSVDNSKQILEQYAEDKRRLFLHQQQQQQQQQQQDGNFSMEQMAHNNYYNYNNYDYHRNKNGSHSDLVNLQRSNVPYMQEDGALYPHQYSSPSYSLHPTGNQFSNATNNLPQFGNAMSISMQLPNGNSNKTASSMNTNPNTNMIMNSNMNMNMNVNPVPYGMGNGANMYDVSRMMTPPLNIAPNSNNSKSSIMNKHPNRNNVPPIHPSLLH | |
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 |
---|---|---|---|---|---|
1 | Acetylation | -------MMSNVANA -------CCCCCCCH | 6.32 | 22814378 | |
2 (in isoform 2) | Acetylation | - | 3.92 | 22814378 | |
255 | Phosphorylation | RRALIEMSGKWFQGR HHHHHHHCCCCHHHC | 25.16 | 27017623 | |
381 | Acetylation | FQLRSLFKPFGPILN HHHHHHCCCCCCEEE | 44.74 | 24489116 | |
401 | Acetylation | GKNCGFVKFEKRIDA CCCCEEEEEEECCCH | 45.61 | 25381059 | |
459 | Phosphorylation | SNGLRAPSAASSVDN CCCCCCCCHHHCCCC | 35.17 | 25752575 | |
463 | Phosphorylation | RAPSAASSVDNSKQI CCCCHHHCCCCHHHH | 28.85 | 23749301 | |
478 | Acetylation | LEQYAEDKRRLFLHQ HHHHHHHHHHHHHHH | 30.81 | 24489116 | |
524 | Phosphorylation | YHRNKNGSHSDLVNL CCCCCCCCHHHHHHC | 29.25 | 22369663 | |
526 | Phosphorylation | RNKNGSHSDLVNLQR CCCCCCHHHHHHCHH | 34.04 | 22369663 | |
637 | Phosphorylation | YDVSRMMTPPLNIAP CCHHHCCCCCCCCCC | 16.65 | 22369663 |
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 NGR1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NGR1_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 NGR1_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-459; SER-524 ANDSER-526, AND MASS SPECTROMETRY. | |
"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-524, AND MASSSPECTROMETRY. | |
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524, AND MASSSPECTROMETRY. |