UniProt ID | DNLI1_YEAST | |
---|---|---|
UniProt AC | P04819 | |
Protein Name | DNA ligase 1 | |
Gene Name | CDC9 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 755 | |
Subcellular Localization |
Isoform Mitochondrial: Mitochondrion. Isoform Nuclear: Nucleus. |
|
Protein Description | DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. The mitochondrial form is required for mitochondrial DNA maintenance but is non-essential while the nuclear form is essential for cell viability.. | |
Protein Sequence | MRRLLTGCLLSSARPLKSRLPLLMSSSLPSSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNVSGEEEYATKKLKQTAVTHTVAAPSSMGSNFSSIPSSAPSSGVADSPQQSQRLVGEVEDALSSNNNDHYSSNIPYSEVCEVFNKIEAISSRLEIIRICSDFFIKIMKQSSKNLIPTTYLFINRLGPDYEAGLELGLGENLLMKTISETCGKSMSQIKLKYKDIGDLGEIAMGARNVQPTMFKPKPLTVGEVFKNLRAIAKTQGKDSQLKKMKLIKRMLTACKGIEAKFLIRSLESKLRIGLAEKTVLISLSKALLLHDENREDSPDKDVPMDVLESAQQKIRDAFCQVPNYEIVINSCLEHGIMNLDKYCTLRPGIPLKPMLAKPTKAINEVLDRFQGETFTSEYKYDGERAQVHLLNDGTMRIYSRNGENMTERYPEINITDFIQDLDTTKNLILDCEAVAWDKDQGKILPFQVLSTRKRKDVELNDVKVKVCLFAFDILCYNDERLINKSLKERREYLTKVTKVVPGEFQYATQITTNNLDELQKFLDESVNHSCEGLMVKMLEGPESHYEPSKRSRNWLKLKKDYLEGVGDSLDLCVLGAYYGRGKRTGTYGGFLLGCYNQDTGEFETCCKIGTGFSDEMLQLLHDRLTPTIIDGPKATFVFDSSAEPDVWFEPTTLFEVLTADLSLSPIYKAGSATFDKGVSLRFPRFLRIREDKGVEDATSSDQIVELYENQSHMQN | |
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 |
---|---|---|---|---|---|
2 (in isoform 2) | Acetylation | - | 37.64 | 22814378 | |
18 | Phosphorylation | SSARPLKSRLPLLMS HCCCCHHHHHHHHHC | 46.89 | 19823750 | |
25 | Phosphorylation | SRLPLLMSSSLPSSA HHHHHHHCCCCCCCC | 19.42 | 26447709 | |
26 | Phosphorylation | RLPLLMSSSLPSSAG HHHHHHCCCCCCCCC | 23.17 | 19823750 | |
27 | Phosphorylation | LPLLMSSSLPSSAGK HHHHHCCCCCCCCCC | 36.67 | 19823750 | |
30 | Phosphorylation | LMSSSLPSSAGKKPK HHCCCCCCCCCCCCC | 37.81 | 19823750 | |
31 | Phosphorylation | MSSSLPSSAGKKPKQ HCCCCCCCCCCCCCH | 38.82 | 19823750 | |
49 | Acetylation | ARFFTSMKNKPTEGT HHHHHHHCCCCCCCC | 62.68 | 24489116 | |
51 | Acetylation | FFTSMKNKPTEGTPS HHHHHCCCCCCCCCC | 48.04 | 25381059 | |
53 | Phosphorylation | TSMKNKPTEGTPSPK HHHCCCCCCCCCCCC | 48.97 | 22890988 | |
56 | Phosphorylation | KNKPTEGTPSPKKSS CCCCCCCCCCCCCCC | 17.86 | 22890988 | |
58 | Phosphorylation | KPTEGTPSPKKSSKH CCCCCCCCCCCCCCH | 49.54 | 25521595 | |
61 | Acetylation | EGTPSPKKSSKHMLE CCCCCCCCCCCHHHH | 64.44 | 25381059 | |
64 | Acetylation | PSPKKSSKHMLEDRM CCCCCCCCHHHHHHH | 39.87 | 25381059 | |
75 | Phosphorylation | EDRMDNVSGEEEYAT HHHHHCCCCHHHHHH | 46.90 | 22369663 | |
80 | Phosphorylation | NVSGEEEYATKKLKQ CCCCHHHHHHHHHHH | 23.89 | 22890988 | |
82 | Phosphorylation | SGEEEYATKKLKQTA CCHHHHHHHHHHHHE | 28.01 | 22890988 | |
83 | Acetylation | GEEEYATKKLKQTAV CHHHHHHHHHHHHEE | 48.19 | 25381059 | |
119 | Phosphorylation | PSSGVADSPQQSQRL CCCCCCCCHHHHHHH | 18.18 | 28152593 | |
123 | Phosphorylation | VADSPQQSQRLVGEV CCCCHHHHHHHHHHH | 16.42 | 28889911 | |
189 | Phosphorylation | SSKNLIPTTYLFINR HCCCCCCCCHHHHHH | 22.53 | 21440633 | |
201 | Phosphorylation | INRLGPDYEAGLELG HHHHCCCHHHHHHCC | 15.71 | 21440633 | |
234 | Acetylation | SQIKLKYKDIGDLGE HHHEEEECCCCCHHH | 41.08 | 24489116 | |
255 | Acetylation | NVQPTMFKPKPLTVG CCCCCCCCCCCCCHH | 41.11 | 24489116 | |
266 | Acetylation | LTVGEVFKNLRAIAK CCHHHHHHHHHHHHH | 61.32 | 24489116 | |
337 | Phosphorylation | HDENREDSPDKDVPM CCCCCCCCCCCCCCH | 30.19 | 21440633 | |
419 | Acetylation | ETFTSEYKYDGERAQ CCCCCEEEECCCEEE | 32.58 | 24489116 | |
420 | Phosphorylation | TFTSEYKYDGERAQV CCCCEEEECCCEEEE | 28.42 | 28132839 | |
434 | Phosphorylation | VHLLNDGTMRIYSRN EEEECCCCEEEEECC | 13.21 | 28132839 | |
524 | Acetylation | NDERLINKSLKERRE CCHHHHCHHHHHHHH | 50.61 | 25381059 | |
535 | Ubiquitination | ERREYLTKVTKVVPG HHHHHHHHHEEECCC | 45.36 | 23749301 | |
537 | Phosphorylation | REYLTKVTKVVPGEF HHHHHHHEEECCCCC | 21.48 | 19779198 | |
548 | Phosphorylation | PGEFQYATQITTNNL CCCCHHEEEEECCCH | 18.64 | 19779198 |
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 DNLI1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DNLI1_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 DNLI1_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-58 AND SER-75, AND MASSSPECTROMETRY. | |
"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-58, 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-58 AND SER-75, AND MASSSPECTROMETRY. |