DNA2_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DNA2_SCHPO
• UniProt AC: Q9URU2
• Protein Name: DNA replication ATP-dependent helicase/nuclease dna2
• Gene Name: dna2
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 1397
• Subcellular Localization: Cytoplasm. Nucleus. Chromosome, telomere. Recruited to double-strand. break (DSB) sites.
• 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. Is a target of the intra-S phase checkpoint, associating with stalled replication forks when phosphorylated at Ser-219 and preventing the stalled replication forks from reversing. Also involved in 5'-end resection of DNA during double-strand break (DSB) repair by mediating the cleavage of 5'-ssDNA. Also required for the production of G-rich single-strand overhangs at telomere ends and thus in telomere length maintenance. 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: MFNDQSKTTSSVKGICATTDNNHGNLKKTNSTPFRKNYLLNGRTKLKLENFAYNASTEISSPKISEKKHSSLPIKRKNTFNESSTSFSPFTKAHKEITDDLKPDKSFTRKSDLNSQDMPVCFQETSKDLCRSSSTQHLLDHQTTDSTIIDMKPVSTNSKSDVFTLYTDETVLLRRCASDNKPLINNNLSSSNVSENQSRSFGSYDEVKNQGNNLHKVPSLVSIIRNARSSEQSRIAANSSCLLKGSDTEIDEDDFALEAEDLAALDSLERQYSQLPNSTVTASAKDIEKTAKVNHVGGDLQSYCSATKASDATINEEPVNLALDKACNSLPDINSDFIDDWDDSCDGCTPGELCEFSSEYTVLEVHEDFIFHEGNHFRQLKLILEANDILHQLFLRGDWTETSIFVGDSIRVEATFDKDNTAIVDNDKGLIIIHPKILMSATAVASSFPCLRKAVISDRVGIYGPPTKAMVTGNILHDFFQHALYRGIDALENVDINLETSIKTYISDIYFADLSLDEIREELDARLPLLKSIVERYLISKKNDNNNESIHISRLLDIEESIWSPRFGLKGNIDATVEVVLTEKPESSSTLTLPLELKTGRYVDNISHFAQSLLYTLLISDRYGINTNQALLCYLENSTIKNLVASNSQLRGLIMTRNSLAQHNFRRSLPEMISNRKICDHCSLVSECLFFQKMSDKGVANSNGLTESWNEWMREVKDEDLEFYKKWEKLLNQEERLLLLKRGDVLTFDTEELEAYGKTLYPLYITKEDIVCLEIDDRVFHYKFAFLNDNGYPRNFLHSGFSVGERVFISDEHGHWSLAKGHIVHIQDSCIEVRTRHRLHIPWLKMPNFDFKKNQVFFGNYEDSKLSFIGSNHTRYRIDKDEFSSGIASIRGTLMSSVLPDAPLIIRDMIIRLKPPKFCNSALIDPEFLKCLNEDQITALKKCHAAEHYSLILGMPGTGKTTTISSLIRSLLAKKKKILLTSFTHLAVDNILIKLKGCDSTIVRLGSPHKIHPLVKEFCLTEGTTFDDLASLKHFYEDPQIVACSSLGVYHSIFNKRKFDYCIIDEASQIPLPICLGPLQLAEKFVLVGDHYQLPPLVKNSRTSKDGLSLSLFKLLSEKHPEAVTTLRLQYRMNEDINSLSSELIYGGNLVCGSKTISQKKLILPKAHLSDGLPDSSSSLHWVNKLINPSHSVIFFNTDDILGVESKTNNILENHTEAFLIEQAVSSFLERGVKQSSIGIISIYKSQVELLSKNLKSFTEIEINTVDRYQGRDKDIILISFVRSNSKNLVGELLRDWHRLNVALSRAKVKCIMFGSLSTLSSSNIVSHLLKLLEKNKWIFTLNENDIATKFDENSSPIKDCSQVATTNNAKVIIRKNQRFFNSDNLCEKAILPQLEF

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
79	Phosphorylation	LPIKRKNTFNESSTS CCCCCCCCCCCCCCC	30.76	25720772
86	Phosphorylation	TFNESSTSFSPFTKA CCCCCCCCCCCCHHH	26.19	25720772
134	Phosphorylation	KDLCRSSSTQHLLDH HHHHHCCCCHHHHCC	20.32	28889911
200	Phosphorylation	VSENQSRSFGSYDEV CCCCCCCCCCCHHHH	26.66	28889911
219	Phosphorylation	NNLHKVPSLVSIIRN CCCCCCCHHHHHHHC	27.09	22682245
222	Phosphorylation	HKVPSLVSIIRNARS CCCCHHHHHHHCCCC	4.54	25720772
273	Phosphorylation	DSLERQYSQLPNSTV HHHHHHHHCCCCCCE	12.47	25720772
1355	Phosphorylation	ATKFDENSSPIKDCS CCCCCCCCCCCCCHH	50.02	24763107
1356	Phosphorylation	TKFDENSSPIKDCSQ CCCCCCCCCCCCHHH	35.13	24763107

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
219	S	Phosphorylation	Kinase	CHEK2	-	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DNA2_SCHPO !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of DNA2_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TAZ1_SCHPO	taz1	genetic	15485922
DPOD3_SCHPO	cdc27	genetic	10880469
DNLI1_SCHPO	cdc17	genetic	10880469
DPOD2_SCHPO	cdc1	genetic	10880469
FEN1_SCHPO	rad2	genetic	10880469
CDC24_SCHPO	cdc24	genetic	10880469
PIF1_SCHPO	pfh1	genetic	15302919
DPOD3_SCHPO	cdc27	physical	10880469
DNLI1_SCHPO	cdc17	physical	10880469
CDC24_SCHPO	cdc24	physical	10880469
DPOD2_SCHPO	cdc1	physical	10880469
FEN1_SCHPO	rad2	physical	10880469
CDC24_SCHPO	cdc24	physical	15576681
DPOD_SCHPO	cdc6	genetic	15576681
DPOD3_SCHPO	cdc27	genetic	15576681

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.