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 | ||||||
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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-174, AND MASSSPECTROMETRY. |