| UniProt ID | PNC1_YEAST | |
|---|---|---|
| UniProt AC | P53184 | |
| Protein Name | Nicotinamidase | |
| Gene Name | PNC1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 216 | |
| Subcellular Localization | Cytoplasm . Nucleus . Peroxisome . Concentrates in peroxisomes (PubMed:12736687). | |
| Protein Description | Catalyzes the deamidation of nicotinamide, an early step in the NAD(+) salvage pathway. Positively regulates SIR2-mediated silencing and longevity by preventing the accumulation of intracellular nicotinamide, an inhibitor of SIR2, during times of stress. Acts also on nicotinyl hydroxamate.. | |
| Protein Sequence | MKTLIVVDMQNDFISPLGSLTVPKGEELINPISDLMQDADRDWHRIVVTRDWHPSRHISFAKNHKDKEPYSTYTYHSPRPGDDSTQEGILWPVHCVKNTWGSQLVDQIMDQVVTKHIKIVDKGFLTDREYYSAFHDIWNFHKTDMNKYLEKHHTDEVYIVGVALEYCVKATAISAAELGYKTTVLLDYTRPISDDPEVINKVKEELKAHNINVVDK | |
| 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 | -----MKTLIVVDMQ -----CCEEEEEECC | 22.03 | 30377154 | |
| 15 | Phosphorylation | DMQNDFISPLGSLTV ECCCCCCCCCCCCEE | 17.67 | 30377154 | |
| 19 | Phosphorylation | DFISPLGSLTVPKGE CCCCCCCCCEECCCC | 28.66 | 30377154 | |
| 21 | Phosphorylation | ISPLGSLTVPKGEEL CCCCCCCEECCCCHH | 36.14 | 30377154 | |
| 59 | Phosphorylation | WHPSRHISFAKNHKD CCHHHHCCCCCCCCC | 17.02 | 28889911 | |
| 62 | Acetylation | SRHISFAKNHKDKEP HHHCCCCCCCCCCCC | 58.54 | 24489116 | |
| 71 | Phosphorylation | HKDKEPYSTYTYHSP CCCCCCCCCCEECCC | 26.17 | 21440633 | |
| 77 | Phosphorylation | YSTYTYHSPRPGDDS CCCCEECCCCCCCCC | 16.52 | 19779198 | |
| 84 | Phosphorylation | SPRPGDDSTQEGILW CCCCCCCCCCCCEEE | 36.41 | 28889911 | |
| 118 | 2-Hydroxyisobutyrylation | QVVTKHIKIVDKGFL HHHHHCEEEEECCCC | 36.07 | - | |
| 122 | Ubiquitination | KHIKIVDKGFLTDRE HCEEEEECCCCCCHH | 40.44 | 23749301 | |
| 122 | 2-Hydroxyisobutyrylation | KHIKIVDKGFLTDRE HCEEEEECCCCCCHH | 40.44 | - | |
| 122 | Acetylation | KHIKIVDKGFLTDRE HCEEEEECCCCCCHH | 40.44 | 24489116 | |
| 142 | Acetylation | HDIWNFHKTDMNKYL HHHHHCHHHHHHHHH | 41.92 | 24489116 | |
| 147 | Acetylation | FHKTDMNKYLEKHHT CHHHHHHHHHHHHCC | 44.57 | 24489116 | |
| 174 | Phosphorylation | CVKATAISAAELGYK HHHHHHHCHHHHCCC | 20.97 | 28889911 | |
| 201 | Acetylation | DDPEVINKVKEELKA CCHHHHHHHHHHHHH | 43.49 | 24489116 | |
| 207 | Acetylation | NKVKEELKAHNINVV HHHHHHHHHCCCCCC | 51.37 | 22865919 |
| 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 PNC1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PNC1_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 PNC1_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-174, AND MASSSPECTROMETRY. | |