| UniProt ID | DNA2_YEAST | |
|---|---|---|
| UniProt AC | P38859 | |
| Protein Name | DNA replication ATP-dependent helicase/nuclease DNA2 | |
| Gene Name | DNA2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1522 | |
| Subcellular Localization | Nucleus. Chromosome. Recruited to double-strand. break (DSB) sites following phosphorylation at Ser-17 and Ser-237. | |
| Protein Description | Key enzyme involved in DNA replication and DNA repair. Involved in Okazaki fragments processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. Also involved in 5'-end resection of DNA during double-strand break (DSB) repair by mediating the cleavage of 5'-ssDNA. Possesses different enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5'-3' helicase and endonuclease activities. While the ATPase and endonuclease activities are well-defined and play a key role in Okazaki fragments processing and DSB repair, the 5'-3' DNA helicase activity is atypical: it cannot load onto its tracking strand internally and has an absolute free 5'-end requirement. Helicase activity may promote the motion of DNA2 on the flap, helping the nuclease function.. | |
| Protein Sequence | MPGTPQKNKRSASISVSPAKKTEEKEIIQNDSKAILSKQTKRKKKYAFAPINNLNGKNTKVSNASVLKSIAVSQVRNTSRTKDINKAVSKSVKQLPNSQVKPKREMSNLSRHHDFTQDEDGPMEEVIWKYSPLQRDMSDKTTSAAEYSDDYEDVQNPSSTPIVPNRLKTVLSFTNIQVPNADVNQLIQENGNEQVRPKPAEISTRESLRNIDDILDDIEGDLTIKPTITKFSDLPSSPIKAPNVEKKAEVNAEEVDKMDSTGDSNDGDDSLIDILTQKYVEKRKSESQITIQGNTNQKSGAQESCGKNDNTKSRGEIEDHENVDNQAKTGNAFYENEEDSNCQRIKKNEKIEYNSSDEFSDDSLIELLNETQTQVEPNTIEQDLDKVEKMVSDDLRIATDSTLSAYALRAKSGAPRDGVVRLVIVSLRSVELPKIGTQKILECIDGKGEQSSVVVRHPWVYLEFEVGDVIHIIEGKNIENKRLLSDDKNPKTQLANDNLLVLNPDVLFSATSVGSSVGCLRRSILQMQFQDPRGEPSLVMTLGNIVHELLQDSIKYKLSHNKISMEIIIQKLDSLLETYSFSIIICNEEIQYVKELVMKEHAENILYFVNKFVSKSNYGCYTSISGTRRTQPISISNVIDIEENIWSPIYGLKGFLDATVEANVENNKKHIVPLEVKTGKSRSVSYEVQGLIYTLLLNDRYEIPIEFFLLYFTRDKNMTKFPSVLHSIKHILMSRNRMSMNFKHQLQEVFGQAQSRFELPPLLRDSSCDSCFIKESCMVLNKLLEDGTPEESGLVEGEFEILTNHLSQNLANYKEFFTKYNDLITKEESSITCVNKELFLLDGSTRESRSGRCLSGLVVSEVVEHEKTEGAYIYCFSRRRNDNNSQSMLSSQIAANDFVIISDEEGHFCLCQGRVQFINPAKIGISVKRKLLNNRLLDKEKGVTTIQSVVESELEQSSLIATQNLVTYRIDKNDIQQSLSLARFNLLSLFLPAVSPGVDIVDERSKLCRKTKRSDGGNEILRSLLVDNRAPKFRDANDDPVIPYKLSKDTTLNLNQKEAIDKVMRAEDYALILGMPGTGKTTVIAEIIKILVSEGKRVLLTSYTHSAVDNILIKLRNTNISIMRLGMKHKVHPDTQKYVPNYASVKSYNDYLSKINSTSVVATTCLGINDILFTLNEKDFDYVILDEASQISMPVALGPLRYGNRFIMVGDHYQLPPLVKNDAARLGGLEESLFKTFCEKHPESVAELTLQYRMCGDIVTLSNFLIYDNKLKCGNNEVFAQSLELPMPEALSRYRNESANSKQWLEDILEPTRKVVFLNYDNCPDIIEQSEKDNITNHGEAELTLQCVEGMLLSGVPCEDIGVMTLYRAQLRLLKKIFNKNVYDGLEILTADQFQGRDKKCIIISMVRRNSQLNGGALLKELRRVNVAMTRAKSKLIIIGSKSTIGSVPEIKSFVNLLEERNWVYTMCKDALYKYKFPDRSNAIDEARKGCGKRTGAKPITSKSKFVSDKPIIKEILQEYES | |
| 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 |
|---|---|---|---|---|---|
| 4 | Phosphorylation | ----MPGTPQKNKRS ----CCCCCCCCCCC | 33.02 | 21841787 | |
| 11 | Phosphorylation | TPQKNKRSASISVSP CCCCCCCCCCEECCC | 28.16 | 22369663 | |
| 13 | Phosphorylation | QKNKRSASISVSPAK CCCCCCCCEECCCCC | 19.35 | 22369663 | |
| 15 | Phosphorylation | NKRSASISVSPAKKT CCCCCCEECCCCCCC | 17.66 | 22369663 | |
| 17 | Phosphorylation | RSASISVSPAKKTEE CCCCEECCCCCCCCC | 16.61 | 22369663 | |
| 89 | Phosphorylation | KDINKAVSKSVKQLP HHHHHHHHHHHHHCC | 24.87 | 19795423 | |
| 91 | Phosphorylation | INKAVSKSVKQLPNS HHHHHHHHHHHCCCC | 27.34 | 19795423 | |
| 138 | Phosphorylation | SPLQRDMSDKTTSAA CCCCCCCCCCCCCHH | 40.00 | 21551504 | |
| 143 | Phosphorylation | DMSDKTTSAAEYSDD CCCCCCCCHHHCCCC | 30.61 | 21551504 | |
| 147 | Phosphorylation | KTTSAAEYSDDYEDV CCCCHHHCCCCHHCC | 16.81 | 21551504 | |
| 148 | Phosphorylation | TTSAAEYSDDYEDVQ CCCHHHCCCCHHCCC | 18.60 | 21440633 | |
| 151 | Phosphorylation | AAEYSDDYEDVQNPS HHHCCCCHHCCCCCC | 21.01 | 23749301 | |
| 172 | Phosphorylation | NRLKTVLSFTNIQVP CCHHHHHHCCCCCCC | 26.20 | 21440633 | |
| 236 | Phosphorylation | TKFSDLPSSPIKAPN EECCCCCCCCCCCCC | 56.92 | 22369663 | |
| 237 | Phosphorylation | KFSDLPSSPIKAPNV ECCCCCCCCCCCCCC | 28.80 | 22369663 | |
| 261 | Phosphorylation | EVDKMDSTGDSNDGD HHHCCCCCCCCCCCC | 40.52 | 21551504 | |
| 270 | Phosphorylation | DSNDGDDSLIDILTQ CCCCCCCHHHHHHHH | 31.78 | 21551504 | |
| 285 | Phosphorylation | KYVEKRKSESQITIQ HHHHHCCCCCCEEEE | 46.65 | 21440633 | |
| 287 | Phosphorylation | VEKRKSESQITIQGN HHHCCCCCCEEEECC | 33.69 | 23749301 | |
| 290 | Phosphorylation | RKSESQITIQGNTNQ CCCCCCEEEECCCCC | 10.30 | 23749301 | |
| 313 | Phosphorylation | GKNDNTKSRGEIEDH CCCCCCCCCCCCCCC | 43.40 | 25704821 | |
| 340 | Phosphorylation | FYENEEDSNCQRIKK CCCCCCCCCCCCCCC | 42.67 | 21440633 | |
| 392 | Phosphorylation | DKVEKMVSDDLRIAT HHHHHHHCCCCHHCC | 23.16 | 23749301 | |
| 755 | Phosphorylation | EVFGQAQSRFELPPL HHHHHCHHHCCCCHH | 41.79 | 24603354 | |
| 848 | Phosphorylation | LDGSTRESRSGRCLS EECCCCCCCCCCCCC | 28.58 | 28889911 | |
| 962 | Phosphorylation | EQSSLIATQNLVTYR HHCCEEEEECEEEEE | 15.82 | 21841787 | |
| 1138 | Phosphorylation | VHPDTQKYVPNYASV CCCCCCCCCCCCCCC | 16.01 | 28132839 | |
| 1142 | Phosphorylation | TQKYVPNYASVKSYN CCCCCCCCCCCCCHH | 8.32 | 28132839 | |
| 1148 | Phosphorylation | NYASVKSYNDYLSKI CCCCCCCHHHHHHHC | 13.31 | 28132839 | |
| 1375 | Acetylation | RAQLRLLKKIFNKNV HHHHHHHHHHHCCCC | 48.71 | 25381059 | |
| 1376 | Acetylation | AQLRLLKKIFNKNVY HHHHHHHHHHCCCCC | 53.12 | 25381059 | |
| 1474 | Acetylation | MCKDALYKYKFPDRS HHHHHHHHCCCCCCC | 42.70 | 24489116 |
* 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 DNA2_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-236; SER-237 ANDTHR-962, 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 SER-236 AND SER-237, ANDMASS SPECTROMETRY. | |
