| UniProt ID | NBP2_YEAST | |
|---|---|---|
| UniProt AC | Q12163 | |
| Protein Name | NAP1-binding protein 2 | |
| Gene Name | NBP2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 236 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | Negatively regulates the high-osmolarity glycerol (HOG) pathway through its negative regulation of the HOG1 kinase activity. Mediates the binding between the PTC1 phosphatase and the PBS2 MAP/ERK kinase (MEK). With PTC1, regulates endoplasmic reticulum inheritance through the cell wall integrity (CWI) MAPK pathway by modulating the MAPK, SLT2.. | |
| Protein Sequence | MATMETTTQKDTNILKSGLKKTIGVLNEAVLQNGREVEAVQAGNSDTMEDTETTTIGYISIKDYAYADSNPLHYGYFDGDNEEDEMVSDSSNGEDTYNKRQSITLPDDYIVNQRAVALYDFEPENDNELRLAEGDIVFISYKHGQGWLVAENESGSKTGLVPEEFVSYIQPEDGENEVENKARPFYLTHLITQSVSPKNNIDNTNEDEYDDNDEWEDIDDVAEVEADMKTKLDISD | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MATMETTTQK -----CCCCCCCCHH | 17.78 | 30377154 | |
| 6 | Phosphorylation | --MATMETTTQKDTN --CCCCCCCCHHHHH | 25.07 | 30377154 | |
| 7 | Phosphorylation | -MATMETTTQKDTNI -CCCCCCCCHHHHHH | 17.58 | 30377154 | |
| 8 | Phosphorylation | MATMETTTQKDTNIL CCCCCCCCHHHHHHH | 40.83 | 30377154 | |
| 12 | Phosphorylation | ETTTQKDTNILKSGL CCCCHHHHHHHHHHH | 31.06 | 30377154 | |
| 45 | Phosphorylation | EAVQAGNSDTMEDTE EEEECCCCCCCCCCC | 33.27 | 28889911 | |
| 51 | Phosphorylation | NSDTMEDTETTTIGY CCCCCCCCCCEEEEE | 23.17 | 28889911 | |
| 64 | Phosphorylation | GYISIKDYAYADSNP EEEEECCEEECCCCC | 9.12 | 19795423 | |
| 66 | Phosphorylation | ISIKDYAYADSNPLH EEECCEEECCCCCCE | 12.52 | 19823750 | |
| 69 | Phosphorylation | KDYAYADSNPLHYGY CCEEECCCCCCEEEE | 31.98 | 19823750 | |
| 74 | Phosphorylation | ADSNPLHYGYFDGDN CCCCCCEEEECCCCC | 22.62 | 19823750 | |
| 76 | Phosphorylation | SNPLHYGYFDGDNEE CCCCEEEECCCCCCC | 7.42 | 19823750 | |
| 88 | Phosphorylation | NEEDEMVSDSSNGED CCCCCCCCCCCCCCC | 30.39 | 21440633 | |
| 90 | Phosphorylation | EDEMVSDSSNGEDTY CCCCCCCCCCCCCCC | 20.42 | 21440633 | |
| 91 | Phosphorylation | DEMVSDSSNGEDTYN CCCCCCCCCCCCCCC | 54.57 | 21440633 | |
| 96 | Phosphorylation | DSSNGEDTYNKRQSI CCCCCCCCCCCCCCE | 25.37 | 19795423 | |
| 97 | Phosphorylation | SSNGEDTYNKRQSIT CCCCCCCCCCCCCEE | 30.89 | 19795423 | |
| 102 | Phosphorylation | DTYNKRQSITLPDDY CCCCCCCCEECCCCE | 22.90 | 22369663 | |
| 104 | Phosphorylation | YNKRQSITLPDDYIV CCCCCCEECCCCEEE | 37.17 | 22369663 | |
| 109 | Phosphorylation | SITLPDDYIVNQRAV CEECCCCEEECCCEE | 17.72 | 27017623 | |
| 186 | Phosphorylation | ENKARPFYLTHLITQ CCCCCCCHHHHHHHC | 17.24 | 22369663 | |
| 188 | Phosphorylation | KARPFYLTHLITQSV CCCCCHHHHHHHCCC | 11.85 | 22369663 | |
| 192 | Phosphorylation | FYLTHLITQSVSPKN CHHHHHHHCCCCCCC | 22.58 | 25521595 | |
| 194 | Phosphorylation | LTHLITQSVSPKNNI HHHHHHCCCCCCCCC | 18.86 | 22369663 | |
| 196 | Phosphorylation | HLITQSVSPKNNIDN HHHHCCCCCCCCCCC | 35.09 | 22369663 | |
| 230 | Phosphorylation | EVEADMKTKLDISD- HHHHHHHCCCCCCC- | 30.15 | 21126336 | |
| 235 | Phosphorylation | MKTKLDISD------ HHCCCCCCC------ | 36.61 | 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 NBP2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NBP2_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 NBP2_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| 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-102; THR-104; SER-196AND SER-235, 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-102, 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-196, 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-196, AND MASSSPECTROMETRY. | |
