UniProt ID | NCL1_YEAST | |
---|---|---|
UniProt AC | P38205 | |
Protein Name | Multisite-specific tRNA:(cytosine-C(5))-methyltransferase | |
Gene Name | NCL1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 684 | |
Subcellular Localization | Nucleus, nucleolus . | |
Protein Description | Methylates cytosine to m5C at several positions in different tRNAs and pre-tRNAs containing intron. Able to modify tRNAs at all four positions (34, 40, 48 and 49) at which m5C has been found in tRNAs. May be involved in ribosome biogenesis as its disruption leads to increased sensitivity to the antibiotic paromomycin.. | |
Protein Sequence | MARRKNFKKGNKKTFGARDDSRAQKNWSELVKENEKWEKYYKTLALFPEDQWEEFKKTCQAPLPLTFRITGSRKHAGEVLNLFKERHLPNLTNVEFEGEKIKAPVELPWYPDHLAWQLDVPKTVIRKNEQFAKTQRFLVVENAVGNISRQEAVSMIPPIVLEVKPHHTVLDMCAAPGSKTAQLIEALHKDTDEPSGFVVANDADARRSHMLVHQLKRLNSANLMVVNHDAQFFPRIRLHGNSNNKNDVLKFDRILCDVPCSGDGTMRKNVNVWKDWNTQAGLGLHAVQLNILNRGLHLLKNNGRLVYSTCSLNPIENEAVVAEALRKWGDKIRLVNCDDKLPGLIRSKGVSKWPVYDRNLTEKTKGDEGTLDSFFSPSEEEASKFNLQNCMRVYPHQQNTGGFFITVFEKVEDSTEAATEKLSSETPALESEGPQTKKIKVEEVQKKERLPRDANEEPFVFVDPQHEALKVCWDFYGIDNIFDRNTCLVRNATGEPTRVVYTVCPALKDVIQANDDRLKIIYSGVKLFVSQRSDIECSWRIQSESLPIMKHHMKSNRIVEANLEMLKHLLIESFPNFDDIRSKNIDNDFVEKMTKLSSGCAFIDVSRNDPAKENLFLPVWKGNKCINLMVCKEDTHELLYRIFGIDANAKATPSAEEKEKEKETTESPAETTTGTSTEAPSAAN | |
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 |
---|---|---|---|---|---|
25 | Acetylation | RDDSRAQKNWSELVK CCCHHHHHHHHHHHH | 60.44 | 24489116 | |
28 | Phosphorylation | SRAQKNWSELVKENE HHHHHHHHHHHHHHH | 30.37 | 30377154 | |
36 | Acetylation | ELVKENEKWEKYYKT HHHHHHHHHHHHHHH | 72.70 | 24489116 | |
56 | Acetylation | EDQWEEFKKTCQAPL HHHHHHHHHHCCCCC | 50.91 | 25381059 | |
84 | Acetylation | GEVLNLFKERHLPNL HHHHHHHHHHCCCCC | 57.94 | 24489116 | |
100 | Acetylation | NVEFEGEKIKAPVEL EEEEECCEEECCEEC | 61.43 | 24489116 | |
154 | Phosphorylation | ISRQEAVSMIPPIVL CCHHHHHHCCCCEEE | 20.31 | 29688323 | |
168 | Phosphorylation | LEVKPHHTVLDMCAA EEECCCCCHHHCCCC | 21.52 | 29688323 | |
178 | Phosphorylation | DMCAAPGSKTAQLIE HCCCCCCCHHHHHHH | 26.27 | 29688323 | |
216 | Ubiquitination | HMLVHQLKRLNSANL HHHHHHHHHCCCCCE | 48.55 | 22817900 | |
220 | Phosphorylation | HQLKRLNSANLMVVN HHHHHCCCCCEEEEC | 24.11 | 30377154 | |
245 | Acetylation | LHGNSNNKNDVLKFD ECCCCCCCCCCEECC | 59.79 | 22865919 | |
250 | Acetylation | NNKNDVLKFDRILCD CCCCCCEECCEEEEE | 45.10 | 22865919 | |
268 | Ubiquitination | SGDGTMRKNVNVWKD CCCCCCCCCEEECCC | 55.19 | 23749301 | |
278 | Phosphorylation | NVWKDWNTQAGLGLH EECCCCCCCCCCCCC | 18.62 | 29136822 | |
352 | Acetylation | IRSKGVSKWPVYDRN HHCCCCCCCCCCCCC | 53.78 | 22865919 | |
414 | Phosphorylation | VFEKVEDSTEAATEK EEEECCCCHHHHHHH | 18.03 | 19779198 | |
415 | Phosphorylation | FEKVEDSTEAATEKL EEECCCCHHHHHHHH | 41.80 | 29136822 | |
419 | Phosphorylation | EDSTEAATEKLSSET CCCHHHHHHHHHCCC | 40.47 | 29136822 | |
421 | Acetylation | STEAATEKLSSETPA CHHHHHHHHHCCCCC | 49.68 | 24489116 | |
423 | Phosphorylation | EAATEKLSSETPALE HHHHHHHHCCCCCCC | 36.88 | 22369663 | |
424 | Phosphorylation | AATEKLSSETPALES HHHHHHHCCCCCCCC | 56.79 | 22369663 | |
426 | Phosphorylation | TEKLSSETPALESEG HHHHHCCCCCCCCCC | 18.79 | 22369663 | |
431 | Phosphorylation | SETPALESEGPQTKK CCCCCCCCCCCCCCE | 49.02 | 22369663 | |
436 | Phosphorylation | LESEGPQTKKIKVEE CCCCCCCCCEEEHHH | 37.12 | 22369663 | |
437 | Acetylation | ESEGPQTKKIKVEEV CCCCCCCCEEEHHHH | 47.45 | 24489116 | |
440 | Acetylation | GPQTKKIKVEEVQKK CCCCCEEEHHHHHHH | 53.09 | 22865919 | |
446 | Acetylation | IKVEEVQKKERLPRD EEHHHHHHHHCCCCC | 62.87 | 24489116 | |
508 | Ubiquitination | YTVCPALKDVIQAND EEECHHHHHHHHCCC | 52.64 | 23749301 | |
530 | Phosphorylation | SGVKLFVSQRSDIEC EEEEEEEECCCCCEE | 16.73 | 19779198 | |
592 | Acetylation | IDNDFVEKMTKLSSG CCHHHHHHHHHHCCC | 46.71 | 24489116 | |
606 | Phosphorylation | GCAFIDVSRNDPAKE CCEEEECCCCCHHHH | 22.94 | 26447709 | |
612 | Acetylation | VSRNDPAKENLFLPV CCCCCHHHHCCEEEE | 53.15 | 24489116 | |
654 | Phosphorylation | ANAKATPSAEEKEKE CCCCCCCCHHHHHHH | 43.91 | 19779198 | |
664 | Phosphorylation | EKEKEKETTESPAET HHHHHHCCCCCCCCC | 47.10 | 22369663 | |
665 | Phosphorylation | KEKEKETTESPAETT HHHHHCCCCCCCCCC | 35.24 | 22369663 | |
667 | Phosphorylation | KEKETTESPAETTTG HHHCCCCCCCCCCCC | 27.58 | 22369663 | |
671 | Phosphorylation | TTESPAETTTGTSTE CCCCCCCCCCCCCCC | 31.59 | 20377248 | |
672 | Phosphorylation | TESPAETTTGTSTEA CCCCCCCCCCCCCCC | 18.09 | 22369663 | |
673 | Phosphorylation | ESPAETTTGTSTEAP CCCCCCCCCCCCCCC | 45.97 | 19795423 | |
675 | Phosphorylation | PAETTTGTSTEAPSA CCCCCCCCCCCCCCC | 30.31 | 22369663 | |
676 | Phosphorylation | AETTTGTSTEAPSAA CCCCCCCCCCCCCCC | 26.12 | 25521595 | |
677 | Phosphorylation | ETTTGTSTEAPSAAN CCCCCCCCCCCCCCC | 35.68 | 19779198 | |
681 | Phosphorylation | GTSTEAPSAAN---- CCCCCCCCCCC---- | 47.24 | 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 NCL1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NCL1_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 NCL1_YEAST !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
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-423; SER-424; THR-426AND SER-431, 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 THR-665 AND SER-667, ANDMASS SPECTROMETRY. |