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Entry version 170 (13 Feb 2019)
Sequence version 1 (01 Feb 1995)
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Protein

DNA replication ATP-dependent helicase/nuclease DNA2

Gene

DNA2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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.6 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

[4Fe-4S] cluster1 PublicationNote: Binds 1 [4Fe-4S] cluster.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi519Iron-sulfur (4Fe-4S)1
Metal bindingi768Iron-sulfur (4Fe-4S)1
Metal bindingi771Iron-sulfur (4Fe-4S)1
Metal bindingi777Iron-sulfur (4Fe-4S)1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi1074 – 1081ATPBy similarity8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding, Helicase, Hydrolase, Multifunctional enzyme, Nuclease
Biological processDNA damage, DNA repair, DNA replication
Ligand4Fe-4S, ATP-binding, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-31198-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-2564818 Cytosolic iron-sulfur cluster assembly (yeast)
R-SCE-69166 Removal of the Flap Intermediate

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
DNA replication ATP-dependent helicase/nuclease DNA2
Including the following 2 domains:
DNA replication nuclease DNA2 (EC:3.1.-.-)
DNA replication ATP-dependent helicase DNA2 (EC:3.6.4.12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:DNA2
Ordered Locus Names:YHR164C
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome VIII

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YHR164C

Saccharomyces Genome Database

More...
SGDi
S000001207 DNA2

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi4T → A: Abolishes phosphorylation by CDK1, leading to a poor recruitment at double-strand. break (DSB) sites following DNA damage; when associated with A-17 and A-237. 1 Publication1
Mutagenesisi17S → A: Abolishes phosphorylation by CDK1, leading to a poor recruitment at double-strand. break (DSB) sites following DNA damage; when associated with A-4 and A-237. 1 Publication1
Mutagenesisi17S → D: Mimics phosphorylation; restores nuclear localization and recruitment at double-strand. break (DSB) sites following DNA damage; when associated with D-237. 1 Publication1
Mutagenesisi237S → A: Abolishes phosphorylation by CDK1, leading to a poor recruitment at double-strand. break (DSB) sites following DNA damage; when associated with A-4 and A-17. 1 Publication1
Mutagenesisi237S → D: Mimics phosphorylation; restores nuclear localization and recruitment at double-strand. break (DSB) sites following DNA damage; when associated with D-17. 1 Publication1
Mutagenesisi504P → S in dna2-1; temperature-sensitive mutant unable to grow at 37 degrees Celsius, probably due to abolition of iron-sulfur-binding. 1 Publication1
Mutagenesisi519C → A: Abolishes iron-sulfur-binding; when associated with A-768; A-771 and A-777. Impaired nuclease and ATPase activities; when associated with A-768. 1 Publication1
Mutagenesisi675E → A: Nuclease dead mutant. No helicase activity when the 5'-end of the substrate is blocked. 1 Publication1
Mutagenesisi677K → R: Nuclease dead mutant. No helicase activity when the 5'-end of the substrate is blocked. 1 Publication1
Mutagenesisi768C → A: Abolishes iron-sulfur-binding; when associated with A-519; A-771 and A-777. Impaired nuclease and ATPase activities; when associated with A-519. 1 Publication1
Mutagenesisi771C → A: Abolishes iron-sulfur-binding; when associated with A-519; A-768 and A-777. Impaired nuclease and ATPase activities; when associated with A-777. 1 Publication1
Mutagenesisi777C → A: Abolishes iron-sulfur-binding; when associated with A-519; A-768 and A-771. Impaired nuclease and ATPase activities; when associated with A-771. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000807111 – 1522DNA replication ATP-dependent helicase/nuclease DNA2Add BLAST1522

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei4Phosphothreonine1 Publication1
Modified residuei17Phosphoserine; by CDK11 Publication1
Modified residuei237Phosphoserine; by CDK11 Publication1
Modified residuei962PhosphothreonineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated at Ser-17 and Ser-237 by CDK1 in response to DNA damage, leading to promote recruitment to double-strand break (DSB) sites and DNA resection.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P38859

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P38859

PRoteomics IDEntifications database

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PRIDEi
P38859

Consortium for Top Down Proteomics

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TopDownProteomicsi
P38859

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P38859

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
36598, 567 interactors

Database of interacting proteins

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DIPi
DIP-2324N

Protein interaction database and analysis system

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IntActi
P38859, 11 interactors

Molecular INTeraction database

More...
MINTi
P38859

STRING: functional protein association networks

More...
STRINGi
4932.YHR164C

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11522
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5HOGX-ray3.09D/E207-223[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P38859

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P38859

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni450 – 900Nuclease activityAdd BLAST451
Regioni901 – 1522Helicase activityAdd BLAST622

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the DNA2/NAM7 helicase family.Curated

Phylogenomic databases

Ensembl GeneTree

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GeneTreei
ENSGT00940000165719

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000112234

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P38859

KEGG Orthology (KO)

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KOi
K10742

Identification of Orthologs from Complete Genome Data

More...
OMAi
IKAGCKP

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR026851 Dna2
IPR014808 DNA_replication_fac_Dna2_N
IPR027417 P-loop_NTPase

The PANTHER Classification System

More...
PANTHERi
PTHR10887:SF14 PTHR10887:SF14, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF08696 Dna2, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540 SSF52540, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P38859-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPGTPQKNKR SASISVSPAK KTEEKEIIQN DSKAILSKQT KRKKKYAFAP
60 70 80 90 100
INNLNGKNTK VSNASVLKSI AVSQVRNTSR TKDINKAVSK SVKQLPNSQV
110 120 130 140 150
KPKREMSNLS RHHDFTQDED GPMEEVIWKY SPLQRDMSDK TTSAAEYSDD
160 170 180 190 200
YEDVQNPSST PIVPNRLKTV LSFTNIQVPN ADVNQLIQEN GNEQVRPKPA
210 220 230 240 250
EISTRESLRN IDDILDDIEG DLTIKPTITK FSDLPSSPIK APNVEKKAEV
260 270 280 290 300
NAEEVDKMDS TGDSNDGDDS LIDILTQKYV EKRKSESQIT IQGNTNQKSG
310 320 330 340 350
AQESCGKNDN TKSRGEIEDH ENVDNQAKTG NAFYENEEDS NCQRIKKNEK
360 370 380 390 400
IEYNSSDEFS DDSLIELLNE TQTQVEPNTI EQDLDKVEKM VSDDLRIATD
410 420 430 440 450
STLSAYALRA KSGAPRDGVV RLVIVSLRSV ELPKIGTQKI LECIDGKGEQ
460 470 480 490 500
SSVVVRHPWV YLEFEVGDVI HIIEGKNIEN KRLLSDDKNP KTQLANDNLL
510 520 530 540 550
VLNPDVLFSA TSVGSSVGCL RRSILQMQFQ DPRGEPSLVM TLGNIVHELL
560 570 580 590 600
QDSIKYKLSH NKISMEIIIQ KLDSLLETYS FSIIICNEEI QYVKELVMKE
610 620 630 640 650
HAENILYFVN KFVSKSNYGC YTSISGTRRT QPISISNVID IEENIWSPIY
660 670 680 690 700
GLKGFLDATV EANVENNKKH IVPLEVKTGK SRSVSYEVQG LIYTLLLNDR
710 720 730 740 750
YEIPIEFFLL YFTRDKNMTK FPSVLHSIKH ILMSRNRMSM NFKHQLQEVF
760 770 780 790 800
GQAQSRFELP PLLRDSSCDS CFIKESCMVL NKLLEDGTPE ESGLVEGEFE
810 820 830 840 850
ILTNHLSQNL ANYKEFFTKY NDLITKEESS ITCVNKELFL LDGSTRESRS
860 870 880 890 900
GRCLSGLVVS EVVEHEKTEG AYIYCFSRRR NDNNSQSMLS SQIAANDFVI
910 920 930 940 950
ISDEEGHFCL CQGRVQFINP AKIGISVKRK LLNNRLLDKE KGVTTIQSVV
960 970 980 990 1000
ESELEQSSLI ATQNLVTYRI DKNDIQQSLS LARFNLLSLF LPAVSPGVDI
1010 1020 1030 1040 1050
VDERSKLCRK TKRSDGGNEI LRSLLVDNRA PKFRDANDDP VIPYKLSKDT
1060 1070 1080 1090 1100
TLNLNQKEAI DKVMRAEDYA LILGMPGTGK TTVIAEIIKI LVSEGKRVLL
1110 1120 1130 1140 1150
TSYTHSAVDN ILIKLRNTNI SIMRLGMKHK VHPDTQKYVP NYASVKSYND
1160 1170 1180 1190 1200
YLSKINSTSV VATTCLGIND ILFTLNEKDF DYVILDEASQ ISMPVALGPL
1210 1220 1230 1240 1250
RYGNRFIMVG DHYQLPPLVK NDAARLGGLE ESLFKTFCEK HPESVAELTL
1260 1270 1280 1290 1300
QYRMCGDIVT LSNFLIYDNK LKCGNNEVFA QSLELPMPEA LSRYRNESAN
1310 1320 1330 1340 1350
SKQWLEDILE PTRKVVFLNY DNCPDIIEQS EKDNITNHGE AELTLQCVEG
1360 1370 1380 1390 1400
MLLSGVPCED IGVMTLYRAQ LRLLKKIFNK NVYDGLEILT ADQFQGRDKK
1410 1420 1430 1440 1450
CIIISMVRRN SQLNGGALLK ELRRVNVAMT RAKSKLIIIG SKSTIGSVPE
1460 1470 1480 1490 1500
IKSFVNLLEE RNWVYTMCKD ALYKYKFPDR SNAIDEARKG CGKRTGAKPI
1510 1520
TSKSKFVSDK PIIKEILQEY ES
Length:1,522
Mass (Da):171,694
Last modified:February 1, 1995 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i213A0458A6C69D78
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U00027 Genomic DNA Translation: AAB68010.1
BK006934 Genomic DNA Translation: DAA06857.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S48904

NCBI Reference Sequences

More...
RefSeqi
NP_012034.1, NM_001179295.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YHR164C_mRNA; YHR164C_mRNA; YHR164C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
856569

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YHR164C

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00027 Genomic DNA Translation: AAB68010.1
BK006934 Genomic DNA Translation: DAA06857.1
PIRiS48904
RefSeqiNP_012034.1, NM_001179295.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5HOGX-ray3.09D/E207-223[»]
ProteinModelPortaliP38859
SMRiP38859
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36598, 567 interactors
DIPiDIP-2324N
IntActiP38859, 11 interactors
MINTiP38859
STRINGi4932.YHR164C

PTM databases

iPTMnetiP38859

Proteomic databases

MaxQBiP38859
PaxDbiP38859
PRIDEiP38859
TopDownProteomicsiP38859

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYHR164C_mRNA; YHR164C_mRNA; YHR164C
GeneIDi856569
KEGGisce:YHR164C

Organism-specific databases

EuPathDBiFungiDB:YHR164C
SGDiS000001207 DNA2

Phylogenomic databases

GeneTreeiENSGT00940000165719
HOGENOMiHOG000112234
InParanoidiP38859
KOiK10742
OMAiIKAGCKP

Enzyme and pathway databases

BioCyciYEAST:G3O-31198-MONOMER
ReactomeiR-SCE-2564818 Cytosolic iron-sulfur cluster assembly (yeast)
R-SCE-69166 Removal of the Flap Intermediate

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P38859

Family and domain databases

InterProiView protein in InterPro
IPR026851 Dna2
IPR014808 DNA_replication_fac_Dna2_N
IPR027417 P-loop_NTPase
PANTHERiPTHR10887:SF14 PTHR10887:SF14, 1 hit
PfamiView protein in Pfam
PF08696 Dna2, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDNA2_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P38859
Secondary accession number(s): D3DLB3
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: February 13, 2019
This is version 170 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names
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