UniProt ID | NRD1_YEAST | |
---|---|---|
UniProt AC | P53617 | |
Protein Name | Protein NRD1 | |
Gene Name | NRD1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 575 | |
Subcellular Localization | Nucleus . | |
Protein Description | Plays a role in sequence-specific regulation of nuclear pre-mRNA abundance.. | |
Protein Sequence | MQQDDDFQNFVATLESFKDLKSGISGSRIKKLTTYALDHIDIESKIISLIIDYSRLCPDSHKLGSLYIIDSIGRAYLDETRSNSNSSSNKPGTCAHAINTLGEVIQELLSDAIAKSNQDHKEKIRMLLDIWDRSGLFQKSYLNAIRSKCFAMDISNNTANTASQQLSLDPKQRSKQILSNLKKSPPLNLNISLPTDLTSTDPAKQQAALFQVIAALQKHFKTLPSHTSVGTVAPPQAHTITEYGSRRERERERERYNSRRNRSRSPPAPFSQPSTGRKDRYPSVAQDQYSIGAPNTTFGTNNHHLYPDELNVSNNPHYRPKPVSYDSTLPPDHIKVYSRTLFIGGVPLNMKEWDLANVLKPFAEVQSVILNNSRKHAFVKVYSRHEAENVLQNFNKDGALPLRTRWGVGFGPRDCCDYQHGYSIIPMHRLTDADKKWSVSAQWGGTSGQPLVTGIVFEEPDIIVGEGVSSKAISQKMPTDSGRNGPRSGKPNKSGSISSISPVPYGNAPLASPPPQQYVQPMMQQPYGYAPNQPLPSQGPAAAAPPVPQQQFDPTAQLNSLMNMLNQQQQQQQQS | |
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 |
---|---|---|---|---|---|
263 | Phosphorylation | YNSRRNRSRSPPAPF HHHHCCCCCCCCCCC | 40.43 | 22369663 | |
265 | Phosphorylation | SRRNRSRSPPAPFSQ HHCCCCCCCCCCCCC | 36.16 | 22369663 | |
271 | Phosphorylation | RSPPAPFSQPSTGRK CCCCCCCCCCCCCCC | 39.87 | 22369663 | |
274 | Phosphorylation | PAPFSQPSTGRKDRY CCCCCCCCCCCCCCC | 35.54 | 22890988 | |
275 | Phosphorylation | APFSQPSTGRKDRYP CCCCCCCCCCCCCCC | 47.92 | 22890988 | |
396 | Acetylation | NVLQNFNKDGALPLR HHHHHCCCCCCCCCC | 54.09 | 24489116 | |
440 | Phosphorylation | ADKKWSVSAQWGGTS CCCCEEEEEECCCCC | 14.82 | 28747907 | |
446 | Phosphorylation | VSAQWGGTSGQPLVT EEEECCCCCCCCEEE | 26.25 | 28747907 | |
447 | Phosphorylation | SAQWGGTSGQPLVTG EEECCCCCCCCEEEE | 38.41 | 28747907 | |
453 | Phosphorylation | TSGQPLVTGIVFEEP CCCCCEEEEEEECCC | 28.95 | 28747907 | |
476 | Acetylation | SSKAISQKMPTDSGR CHHHHHHCCCCCCCC | 39.80 | 24489116 |
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 NRD1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NRD1_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 NRD1_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-263 AND SER-265, ANDMASS 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-263 AND SER-265, ANDMASS SPECTROMETRY. | |
"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-263 AND SER-265, ANDMASS SPECTROMETRY. | |
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 AND SER-265, ANDMASS SPECTROMETRY. |