UniProt ID | NOP12_YEAST | |
---|---|---|
UniProt AC | Q08208 | |
Protein Name | Nucleolar protein 12 | |
Gene Name | NOP12 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 459 | |
Subcellular Localization | Nucleus, nucleolus . | |
Protein Description | Involved in pre-25S rRNA processing.. | |
Protein Sequence | MSSAIDNLFGNIDEKKIESSVDKLFSSSCGPINKLEVKSKTRTVLPDSKKRERAAEADQEEKEASKPDVSDEQTEEVALPKVKKAKKSKRNDEDEDLEARYYAKLLNEEAEAEDDKPTVTKTDETSVPLTSAAKKVDFKEDELEKAERTVFIGNILSTVITSKKVYKEFKKLFGTNPIAETEESGNEKEEESSKKSDNNEFAIESIRFRSISFDEALPRKVAFVQQKFHKSRDTINAYIVYKNKSAVRKICSNLNAVVFQDHHLRVDSVAHPAPHDKKRSIFVGNLDFEEIEESLWKHFEPCGDIEYVRIIRDSKTNMGKGFAYVQFKDLQSVNKALLLNEKPMKSQKQEDENTKKPTKKARKLRVSRCKNMKKGTTIGTGLDRNGLTDSQRTRAGRAKKILGKADRATLGQEITIEGLRAKKGEGSTHLKKKKQRSATGRVTKRSIAFKKAQAEKSKK | |
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 | ------MSSAIDNLF ------CCHHHHHHH | 28.60 | 30377154 | |
3 | Phosphorylation | -----MSSAIDNLFG -----CCHHHHHHHC | 28.13 | 30377154 | |
16 | Acetylation | FGNIDEKKIESSVDK HCCCCHHHHHHHHHH | 50.05 | 24489116 | |
23 | Acetylation | KIESSVDKLFSSSCG HHHHHHHHHHHCCCC | 49.64 | 22865919 | |
26 | Phosphorylation | SSVDKLFSSSCGPIN HHHHHHHHCCCCCCC | 31.60 | 30377154 | |
27 | Phosphorylation | SVDKLFSSSCGPINK HHHHHHHCCCCCCCE | 23.47 | 30377154 | |
28 | Phosphorylation | VDKLFSSSCGPINKL HHHHHHCCCCCCCEE | 23.15 | 30377154 | |
34 | Acetylation | SSCGPINKLEVKSKT CCCCCCCEEEECCCC | 46.90 | 24489116 | |
62 | Acetylation | AEADQEEKEASKPDV HHHHHHHHHHHCCCC | 58.80 | 24489116 | |
65 | Phosphorylation | DQEEKEASKPDVSDE HHHHHHHHCCCCCHH | 45.90 | 22369663 | |
70 | Phosphorylation | EASKPDVSDEQTEEV HHHCCCCCHHHHHHH | 42.69 | 22369663 | |
74 | Phosphorylation | PDVSDEQTEEVALPK CCCCHHHHHHHHHHH | 31.87 | 25521595 | |
104 | Acetylation | LEARYYAKLLNEEAE HHHHHHHHHHCHHHH | 37.07 | 24489116 | |
116 | Acetylation | EAEAEDDKPTVTKTD HHHHCCCCCCCCCCC | 55.71 | 24489116 | |
121 | Acetylation | DDKPTVTKTDETSVP CCCCCCCCCCCCCCC | 50.03 | 24489116 | |
125 | Phosphorylation | TVTKTDETSVPLTSA CCCCCCCCCCCCCHH | 37.52 | 21440633 | |
126 | Phosphorylation | VTKTDETSVPLTSAA CCCCCCCCCCCCHHH | 21.49 | 27214570 | |
175 | Phosphorylation | EFKKLFGTNPIAETE HHHHHHCCCCCCCCC | 30.41 | 22890988 | |
181 | Phosphorylation | GTNPIAETEESGNEK CCCCCCCCCCCCCHH | 35.71 | 25521595 | |
184 | Phosphorylation | PIAETEESGNEKEEE CCCCCCCCCCHHHHH | 40.46 | 22369663 | |
192 | Phosphorylation | GNEKEEESSKKSDNN CCHHHHHHHCCCCCC | 51.22 | 22369663 | |
193 | Phosphorylation | NEKEEESSKKSDNNE CHHHHHHHCCCCCCC | 47.59 | 22369663 | |
212 | Phosphorylation | SIRFRSISFDEALPR HEEEEECCCCHHHHH | 28.08 | 25752575 | |
227 | Acetylation | KVAFVQQKFHKSRDT HHHHHHHHHHCCCCC | 32.14 | 24489116 | |
252 | Phosphorylation | SAVRKICSNLNAVVF HHHHHHHHCCCCEEE | 48.07 | 28889911 | |
342 | Acetylation | KALLLNEKPMKSQKQ HHHHHCCCCCCCCCC | 49.71 | 24489116 | |
367 | Phosphorylation | KARKLRVSRCKNMKK HHHHHHHHHHCCCCC | 26.06 | 19795423 | |
390 | Phosphorylation | DRNGLTDSQRTRAGR CCCCCCHHHHHHHHH | 19.14 | 23749301 | |
404 | Acetylation | RAKKILGKADRATLG HHHHHHCCCCHHCCC | 43.60 | 25381059 | |
427 | Phosphorylation | RAKKGEGSTHLKKKK HCCCCCCCCHHCHHH | 14.35 | 30377154 | |
443 | Phosphorylation | RSATGRVTKRSIAFK CCCCCCCCHHHHHHH | 21.27 | 28889911 |
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 NOP12_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NOP12_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 NOP12_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-70; THR-181; SER-184;SER-192; SER-212 AND SER-252, 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-70 AND SER-184, AND MASSSPECTROMETRY. | |
"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-184, 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-70 AND SER-184, AND MASSSPECTROMETRY. |