YEAST:DNA2

Species (Taxon ID)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s)	DNA2
Protein Name(s)	DNA replication ATP-dependent helicase/nuclease DNA2 DNA replication nuclease DNA2 DNA replication ATP-dependent helicase DNA2
External Links
UniProt	P38859
EMBL	U00027 BK006934
PIR	S48904
RefSeq	NP_012034.1
ProteinModelPortal	P38859
SMR	P38859
BioGrid	36598
DIP	DIP-2324N
IntAct	P38859
MINT	MINT-620090
STRING	4932.YHR164C
MaxQB	P38859
PaxDb	P38859
EnsemblFungi	[example_ID YHR164C]
GeneID	856569
KEGG	sce:YHR164C
CYGD	YHR164c
SGD	S000001207
eggNOG	COG1112
GeneTree	ENSGT00770000120532
HOGENOM	HOG000112234
InParanoid	P38859
KO	K10742
OMA	GNIVHEL
OrthoDB	EOG7FZ06K
BioCyc	YEAST:G3O-31198-MONOMER
Reactome	REACT_188901
NextBio	982411
PRO	PR:P38859
Proteomes	UP000002311
Genevestigator	P38859
GO	GO:0005737 GO:0005829 GO:0000784 GO:0005634 GO:0035861 GO:0051539 GO:0043139 GO:0017108 GO:0005524 GO:0004003 GO:0003677 GO:0046872 GO:0004518 GO:0000014 GO:0043142 GO:0006200 GO:0006974 GO:0000737 GO:0000729 GO:0032508 GO:0006281 GO:0033567 GO:0000733 GO:0006261 GO:0006273 GO:0000706 GO:0001302 GO:0000723
Gene3D	3.40.50.300
InterPro	IPR026851 IPR014808 IPR027417
PANTHER	PTHR10887:SF14
Pfam	PF08696
SUPFAM	SSF52540

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0033567	DNA replication, Okazaki fragment processing	PMID:15448135^[1]	ECO:0000314			P	Lanes 1-7 are 5'-32P-radiolabeled while lanes 8-14 are 3'-32P-radiolabeled. Lanes 2–4 and 9–11 are under maximum-nuclease conditions, whereas lanes 5–7 and 12–14 are under maximum-helicase conditions. The resulting southern blot shows much smaller fragments in lanes 2-7, while in lanes 9-14 the DNA fragments are much larger and did not precipitate down the blot as far. Lanes 1 and 8 are substrate only controls.	complete
part_of	GO:0005634	nucleus	PMID:22842922^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0000729	DNA double-strand break processing	PMID:21841787^[3]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P39875	P	Seeded From UniProt	complete
enables	GO:0017108	5'-flap endonuclease activity	PMID:15448135^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	PMID:10101169^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006273	lagging strand elongation	PMID:10101169^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006273	lagging strand elongation	PMID:10330154^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006261	DNA-dependent DNA replication	PMID:7592912^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006261	DNA-dependent DNA replication	PMID:9710536^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:19520826^[8]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:19520826^[8]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0004003	ATP-dependent DNA helicase activity	PMID:7644470^[9]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0001302	replicative cell aging	PMID:12024027^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0000784	nuclear chromosome, telomeric region	PMID:12024033^[11]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0000733	DNA strand renaturation	PMID:17032657^[12]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0000723	telomere maintenance	PMID:12024033^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0000706	meiotic DNA double-strand break processing	PMID:20150422^[13]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000000981 SGD:S000004526	P	Seeded From UniProt	complete
enables	GO:0000014	single-stranded DNA endodeoxyribonuclease activity	PMID:23671118^[14]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000014	single-stranded DNA endodeoxyribonuclease activity	PMID:9756935^[15]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0051539	4 iron, 4 sulfur cluster binding	PMID:22684504^[16]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0043142	single-stranded DNA-dependent ATPase activity	PMID:22684504^[16]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0043139	5'-3' DNA helicase activity	PMID:20929864^[17]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0035861	site of double-strand break	PMID:21841787^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	PMID:21841787^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21841787^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0004518	nuclease activity	PMID:22684504^[16]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0000729	DNA double-strand break processing	PMID:21841787^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0071932	replication fork reversal	PMID:21873635^[18]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000094675 PomBase:SPBC16D10.04c	P	Seeded From UniProt	complete
enables	GO:0017108	5'-flap endonuclease activity	PMID:21873635^[18]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:2443732 PANTHER:PTN000094675 SGD:S000001207 UniProtKB:P51530	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[18]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000094675 PomBase:SPBC16D10.04c SGD:S000001207	C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21873635^[18]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000094675 SGD:S000001207 UniProtKB:A0A1P8ASY1 UniProtKB:P51530	C	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:21873635^[18]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000094509 UniProtKB:Q92900 UniProtKB:Q9HCE1	F	Seeded From UniProt	complete
part_of	GO:0000784	nuclear chromosome, telomeric region	PMID:21873635^[18]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:2443732 PANTHER:PTN000094675 PomBase:SPBC16D10.04c SGD:S000001207	C	Seeded From UniProt	complete
involved_in	GO:0032508	DNA duplex unwinding	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0043139	P	Seeded From UniProt	complete
involved_in	GO:0032508	DNA duplex unwinding	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004003	P	Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004518	P	Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004518	P	Seeded From UniProt	complete
enables	GO:0017108	5'-flap endonuclease activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR026851	F	Seeded From UniProt	complete
involved_in	GO:0033567	DNA replication, Okazaki fragment processing	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR026851	P	Seeded From UniProt	complete
enables	GO:0043142	single-stranded DNA-dependent ATPase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR026851	F	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-SCE-2564817	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0238	F	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F	Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0227	P	Seeded From UniProt	complete
part_of	GO:0005694	chromosome	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0158 UniProtKB-SubCell:SL-0468	C	Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0511	F	Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0234	P	Seeded From UniProt	complete
enables	GO:0004386	helicase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0347	F	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C	Seeded From UniProt	complete
enables	GO:0051536	iron-sulfur cluster binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0411	F	Seeded From UniProt	complete
enables	GO:0051539	4 iron, 4 sulfur cluster binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0004	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F	Seeded From UniProt	complete
involved_in	GO:0006260	DNA replication	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0235	P	Seeded From UniProt	complete
involved_in	GO:0008152	metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0511	P	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
enables	GO:0004518	nuclease activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0540	F	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Kao, HI et al. (2004) Dna2p helicase/nuclease is a tracking protein, like FEN1, for flap cleavage during Okazaki fragment maturation. J. Biol. Chem. 279 50840-9 PubMed GONUTS page
↑ Tkach, JM et al. (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat. Cell Biol. 14 966-76 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 Chen, X et al. (2011) Cell cycle regulation of DNA double-strand break end resection by Cdk1-dependent Dna2 phosphorylation. Nat. Struct. Mol. Biol. 18 1015-9 PubMed GONUTS page
↑ ^4.0 ^4.1 Formosa, T & Nittis, T (1999) Dna2 mutants reveal interactions with Dna polymerase alpha and Ctf4, a Pol alpha accessory factor, and show that full Dna2 helicase activity is not essential for growth. Genetics 151 1459-70 PubMed GONUTS page
↑ Parenteau, J & Wellinger, RJ (1999) Accumulation of single-stranded DNA and destabilization of telomeric repeats in yeast mutant strains carrying a deletion of RAD27. Mol. Cell. Biol. 19 4143-52 PubMed GONUTS page
↑ Budd, ME et al. (1995) DNA2 encodes a DNA helicase essential for replication of eukaryotic chromosomes. J. Biol. Chem. 270 26766-9 PubMed GONUTS page
↑ Braguglia, D et al. (1998) Semi-conservative replication in yeast nuclear extracts requires Dna2 helicase and supercoiled template. J. Mol. Biol. 281 631-49 PubMed GONUTS page
↑ ^8.0 ^8.1 Kosugi, S et al. (2009) Systematic identification of cell cycle-dependent yeast nucleocytoplasmic shuttling proteins by prediction of composite motifs. Proc. Natl. Acad. Sci. U.S.A. 106 10171-6 PubMed GONUTS page
↑ Budd, ME & Campbell, JL (1995) A yeast gene required for DNA replication encodes a protein with homology to DNA helicases. Proc. Natl. Acad. Sci. U.S.A. 92 7642-6 PubMed GONUTS page
↑ Hoopes, LL et al. (2002) Mutations in DNA replication genes reduce yeast life span. Mol. Cell. Biol. 22 4136-46 PubMed GONUTS page
↑ ^11.0 ^11.1 Choe, W et al. (2002) Dynamic localization of an Okazaki fragment processing protein suggests a novel role in telomere replication. Mol. Cell. Biol. 22 4202-17 PubMed GONUTS page
↑ Masuda-Sasa, T et al. (2006) Single strand annealing and ATP-independent strand exchange activities of yeast and human DNA2: possible role in Okazaki fragment maturation. J. Biol. Chem. 281 38555-64 PubMed GONUTS page
↑ Manfrini, N et al. (2010) Processing of meiotic DNA double strand breaks requires cyclin-dependent kinase and multiple nucleases. J. Biol. Chem. 285 11628-37 PubMed GONUTS page
↑ Levikova, M et al. (2013) Nuclease activity of Saccharomyces cerevisiae Dna2 inhibits its potent DNA helicase activity. Proc. Natl. Acad. Sci. U.S.A. 110 E1992-2001 PubMed GONUTS page
↑ Bae, SH et al. (1998) Dna2 of Saccharomyces cerevisiae possesses a single-stranded DNA-specific endonuclease activity that is able to act on double-stranded DNA in the presence of ATP. J. Biol. Chem. 273 26880-90 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 Pokharel, S & Campbell, JL (2012) Cross talk between the nuclease and helicase activities of Dna2: role of an essential iron-sulfur cluster domain. Nucleic Acids Res. 40 7821-30 PubMed GONUTS page
↑ Balakrishnan, L et al. (2010) Dna2 exhibits a unique strand end-dependent helicase function. J. Biol. Chem. 285 38861-8 PubMed GONUTS page
↑ ^18.0 ^18.1 ^18.2 ^18.3 ^18.4 ^18.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:15448135-1] 1.0 ^1.1 Kao, HI et al. (2004) Dna2p helicase/nuclease is a tracking protein, like FEN1, for flap cleavage during Okazaki fragment maturation. J. Biol. Chem. 279 50840-9 PubMed GONUTS page

[PMID:22842922-2] Tkach, JM et al. (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat. Cell Biol. 14 966-76 PubMed GONUTS page

[PMID:21841787-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 Chen, X et al. (2011) Cell cycle regulation of DNA double-strand break end resection by Cdk1-dependent Dna2 phosphorylation. Nat. Struct. Mol. Biol. 18 1015-9 PubMed GONUTS page

[PMID:10101169-4] 4.0 ^4.1 Formosa, T & Nittis, T (1999) Dna2 mutants reveal interactions with Dna polymerase alpha and Ctf4, a Pol alpha accessory factor, and show that full Dna2 helicase activity is not essential for growth. Genetics 151 1459-70 PubMed GONUTS page

[PMID:10330154-5] Parenteau, J & Wellinger, RJ (1999) Accumulation of single-stranded DNA and destabilization of telomeric repeats in yeast mutant strains carrying a deletion of RAD27. Mol. Cell. Biol. 19 4143-52 PubMed GONUTS page

[PMID:7592912-6] Budd, ME et al. (1995) DNA2 encodes a DNA helicase essential for replication of eukaryotic chromosomes. J. Biol. Chem. 270 26766-9 PubMed GONUTS page

[PMID:9710536-7] Braguglia, D et al. (1998) Semi-conservative replication in yeast nuclear extracts requires Dna2 helicase and supercoiled template. J. Mol. Biol. 281 631-49 PubMed GONUTS page

[PMID:19520826-8] 8.0 ^8.1 Kosugi, S et al. (2009) Systematic identification of cell cycle-dependent yeast nucleocytoplasmic shuttling proteins by prediction of composite motifs. Proc. Natl. Acad. Sci. U.S.A. 106 10171-6 PubMed GONUTS page

[PMID:7644470-9] Budd, ME & Campbell, JL (1995) A yeast gene required for DNA replication encodes a protein with homology to DNA helicases. Proc. Natl. Acad. Sci. U.S.A. 92 7642-6 PubMed GONUTS page

[PMID:12024027-10] Hoopes, LL et al. (2002) Mutations in DNA replication genes reduce yeast life span. Mol. Cell. Biol. 22 4136-46 PubMed GONUTS page

[PMID:12024033-11] 11.0 ^11.1 Choe, W et al. (2002) Dynamic localization of an Okazaki fragment processing protein suggests a novel role in telomere replication. Mol. Cell. Biol. 22 4202-17 PubMed GONUTS page

[PMID:17032657-12] Masuda-Sasa, T et al. (2006) Single strand annealing and ATP-independent strand exchange activities of yeast and human DNA2: possible role in Okazaki fragment maturation. J. Biol. Chem. 281 38555-64 PubMed GONUTS page

[PMID:20150422-13] Manfrini, N et al. (2010) Processing of meiotic DNA double strand breaks requires cyclin-dependent kinase and multiple nucleases. J. Biol. Chem. 285 11628-37 PubMed GONUTS page

[PMID:23671118-14] Levikova, M et al. (2013) Nuclease activity of Saccharomyces cerevisiae Dna2 inhibits its potent DNA helicase activity. Proc. Natl. Acad. Sci. U.S.A. 110 E1992-2001 PubMed GONUTS page

[PMID:9756935-15] Bae, SH et al. (1998) Dna2 of Saccharomyces cerevisiae possesses a single-stranded DNA-specific endonuclease activity that is able to act on double-stranded DNA in the presence of ATP. J. Biol. Chem. 273 26880-90 PubMed GONUTS page

[PMID:22684504-16] 16.0 ^16.1 ^16.2 Pokharel, S & Campbell, JL (2012) Cross talk between the nuclease and helicase activities of Dna2: role of an essential iron-sulfur cluster domain. Nucleic Acids Res. 40 7821-30 PubMed GONUTS page

[PMID:20929864-17] Balakrishnan, L et al. (2010) Dna2 exhibits a unique strand end-dependent helicase function. J. Biol. Chem. 285 38861-8 PubMed GONUTS page

[PMID:21873635-18] 18.0 ^18.1 ^18.2 ^18.3 ^18.4 ^18.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

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YEAST:DNA2

Contents

Annotations

Notes

References

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