| UniProt ID | NAT1_YEAST | |
|---|---|---|
| UniProt AC | P12945 | |
| Protein Name | N-terminal acetyltransferase A complex subunit NAT1 | |
| Gene Name | NAT1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 854 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | Non-catalytic component of the NatA N-terminal acetyltransferase, which catalyzes acetylation of proteins beginning with Met-Ser, Met-Gly and Met-Ala. N-acetylation plays a role in normal eukaryotic translation and processing, protect against proteolytic degradation and protein turnover. NAT1 anchors ARD1 and NAT5 to the ribosome and may present the N termini of nascent polypeptides for acetylation.. | |
| Protein Sequence | MSRKRSTKPKPAAKIALKKENDQFLEALKLYEGKQYKKSLKLLDAILKKDGSHVDSLALKGLDLYSVGEKDDAASYVANAIRKIEGASASPICCHVLGIYMRNTKEYKESIKWFTAALNNGSTNKQIYRDLATLQSQIGDFKNALVSRKKYWEAFLGYRANWTSLAVAQDVNGERQQAINTLSQFEKLAEGKISDSEKYEHSECLMYKNDIMYKAASDNQDKLQNVLKHLNDIEPCVFDKFGLLERKATIYMKLGQLKDASIVYRTLIKRNPDNFKYYKLLEVSLGIQGDNKLKKALYGKLEQFYPRCEPPKFIPLTFLQDKEELSKKLREYVLPQLERGVPATFSNVKPLYQRRKSKVSPLLEKIVLDYLSGLDPTQDPIPFIWTNYYLSQHFLFLKDFPKAQEYIDAALDHTPTLVEFYILKARILKHLGLMDTAAGILEEGRQLDLQDRFINCKTVKYFLRANNIDKAVEVASLFTKNDDSVNGIKDLHLVEASWFIVEQAEAYYRLYLDRKKKLDDLASLKKEVESDKSEQIANDIKENQWLVRKYKGLALKRFNAIPKFYKQFEDDQLDFHSYCMRKGTPRAYLEMLEWGKALYTKPMYVRAMKEASKLYFQMHDDRLKRKSDSLDENSDEIQNNGQNSSSQKKKAKKEAAAMNKRKETEAKSVAAYPSDQDNDVFGEKLIETSTPMEDFATEFYNNYSMQVREDERDYILDFEFNYRIGKLALCFASLNKFAKRFGTTSGLFGSMAIVLLHATRNDTPFDPILKKVVTKSLEKEYSENFPLNEISNNSFDWLNFYQEKFGKNDINGLLFLYRYRDDVPIGSSNLKEMIISSLSPLEPHSQNEILQYYL | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MSRKRSTKP ------CCCCCCCCC | 46.65 | - | |
| 14 | Acetylation | TKPKPAAKIALKKEN CCCCCHHHHHHHHHC | 30.53 | 25381059 | |
| 19 | Acetylation | AAKIALKKENDQFLE HHHHHHHHHCHHHHH | 63.70 | 24489116 | |
| 29 | Acetylation | DQFLEALKLYEGKQY HHHHHHHHHHCCHHH | 56.95 | 24489116 | |
| 41 | Acetylation | KQYKKSLKLLDAILK HHHHHHHHHHHHHHH | 54.84 | 24489116 | |
| 70 | Acetylation | DLYSVGEKDDAASYV CEEECCCHHHHHHHH | 55.79 | 24489116 | |
| 125 | Acetylation | LNNGSTNKQIYRDLA HHCCCCCHHHHHHHH | 37.85 | 24489116 | |
| 142 | Acetylation | QSQIGDFKNALVSRK HHHHHHHHHHHHHHH | 46.15 | 24489116 | |
| 187 | Acetylation | NTLSQFEKLAEGKIS HHHHHHHHHHCCCCC | 55.04 | 24489116 | |
| 192 | 2-Hydroxyisobutyrylation | FEKLAEGKISDSEKY HHHHHCCCCCCHHHC | 30.46 | - | |
| 194 | Phosphorylation | KLAEGKISDSEKYEH HHHCCCCCCHHHCCC | 38.27 | 28889911 | |
| 222 | Acetylation | AASDNQDKLQNVLKH HHCCCHHHHHHHHHH | 42.06 | 24489116 | |
| 276 | Acetylation | KRNPDNFKYYKLLEV HHCCCCCCEEEEEEE | 54.66 | 22865919 | |
| 322 | Acetylation | PLTFLQDKEELSKKL CCCCCCCHHHHHHHH | 39.88 | 24489116 | |
| 327 | Acetylation | QDKEELSKKLREYVL CCHHHHHHHHHHHHH | 69.33 | 24489116 | |
| 470 | Acetylation | LRANNIDKAVEVASL HHHCCHHHHHHHHHH | 51.00 | 24489116 | |
| 532 | Acetylation | KKEVESDKSEQIAND HHHHHCCCHHHHHHH | 66.23 | 24489116 | |
| 626 | Ubiquitination | HDDRLKRKSDSLDEN CHHHHHHCCCCCCCC | 57.96 | 23749301 | |
| 627 | Phosphorylation | DDRLKRKSDSLDENS HHHHHHCCCCCCCCH | 36.14 | 30377154 | |
| 629 | Phosphorylation | RLKRKSDSLDENSDE HHHHCCCCCCCCHHH | 44.82 | 28889911 | |
| 634 | Phosphorylation | SDSLDENSDEIQNNG CCCCCCCHHHHHHCC | 34.27 | 23749301 | |
| 644 | Phosphorylation | IQNNGQNSSSQKKKA HHHCCCCCHHHHHHH | 24.39 | 28889911 | |
| 646 | Phosphorylation | NNGQNSSSQKKKAKK HCCCCCHHHHHHHHH | 45.93 | 23749301 | |
| 668 | Phosphorylation | RKETEAKSVAAYPSD HHHHHHHHHHCCCCC | 24.84 | 21126336 | |
| 672 | Phosphorylation | EAKSVAAYPSDQDND HHHHHHCCCCCCCCC | 8.11 | 24961812 | |
| 674 | Phosphorylation | KSVAAYPSDQDNDVF HHHHCCCCCCCCCCC | 34.92 | 28152593 | |
| 726 | Acetylation | EFNYRIGKLALCFAS EEHHHHHHHHHHHHH | 28.37 | 24489116 | |
| 763 | Phosphorylation | LHATRNDTPFDPILK HHHHCCCCCCCHHHH | 29.42 | 27017623 | |
| 774 | Phosphorylation | PILKKVVTKSLEKEY HHHHHHHHHHHHHHH | 20.22 | 21177495 |
| 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 NAT1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NAT1_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 NAT1_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-674, AND MASSSPECTROMETRY. | |
