DNA2/YHR164C Protein Information Help

Standard Name Dna2p 1
Systematic Name Yhr164cp
Alias Web2p
ORF Classification Verified
Description Tripartite DNA replication factor; has single-stranded DNA-dependent ATPase, ATP-dependent nuclease, and helicase activities; tracking protein for flap cleavage during Okazaki fragment maturation; involved in DNA repair and processing of meiotic DNA double strand breaks; required for normal life span; component of telomeric chromatin, with cell-cycle dependent localization; required for telomerase-dependent telomere synthesis; forms nuclear foci upon DNA replication stress (10, 11, 12, 13, 2, 3, 4, 5, 6, 7, 8, 9)
Name Description DNA synthesis defective 1
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 1,522
Molecular Weight (Da) 171,693
Isoelectric Point (pI) 6.43

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Dna2p (InterPro)
Physical Interactions There are 31 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI000005304D | P38859
MIPS: YHR164C
NCBI: 458906 | 6321958 | 731738 | NP_012034.1 | NM_001179295.1
GenBank/EMBL/DDBJ: DAA06857.1 | U00027
External Classifications EC: 3.1.-.- [Hydrolases acting on ester bonds ]
EC: 3.6.1.- [Hydrolases acting on acid anhydrides in phosphorous-containing anhydrides]
EC: 3.6.4.12 [DNA helicase]
Amino Acid Sequence (or in FASTA format)
       1  MPGTPQKNKR SASISVSPAK KTEEKEIIQN DSKAILSKQT KRKKKYAFAP
      51  INNLNGKNTK VSNASVLKSI AVSQVRNTSR TKDINKAVSK SVKQLPNSQV
     101  KPKREMSNLS RHHDFTQDED GPMEEVIWKY SPLQRDMSDK TTSAAEYSDD
     151  YEDVQNPSST PIVPNRLKTV LSFTNIQVPN ADVNQLIQEN GNEQVRPKPA
     201  EISTRESLRN IDDILDDIEG DLTIKPTITK FSDLPSSPIK APNVEKKAEV
     251  NAEEVDKMDS TGDSNDGDDS LIDILTQKYV EKRKSESQIT IQGNTNQKSG
     301  AQESCGKNDN TKSRGEIEDH ENVDNQAKTG NAFYENEEDS NCQRIKKNEK
     351  IEYNSSDEFS DDSLIELLNE TQTQVEPNTI EQDLDKVEKM VSDDLRIATD
     401  STLSAYALRA KSGAPRDGVV RLVIVSLRSV ELPKIGTQKI LECIDGKGEQ
     451  SSVVVRHPWV YLEFEVGDVI HIIEGKNIEN KRLLSDDKNP KTQLANDNLL
     501  VLNPDVLFSA TSVGSSVGCL RRSILQMQFQ DPRGEPSLVM TLGNIVHELL
     551  QDSIKYKLSH NKISMEIIIQ KLDSLLETYS FSIIICNEEI QYVKELVMKE
     601  HAENILYFVN KFVSKSNYGC YTSISGTRRT QPISISNVID IEENIWSPIY
     651  GLKGFLDATV EANVENNKKH IVPLEVKTGK SRSVSYEVQG LIYTLLLNDR
     701  YEIPIEFFLL YFTRDKNMTK FPSVLHSIKH ILMSRNRMSM NFKHQLQEVF
     751  GQAQSRFELP PLLRDSSCDS CFIKESCMVL NKLLEDGTPE ESGLVEGEFE
     801  ILTNHLSQNL ANYKEFFTKY NDLITKEESS ITCVNKELFL LDGSTRESRS
     851  GRCLSGLVVS EVVEHEKTEG AYIYCFSRRR NDNNSQSMLS SQIAANDFVI
     901  ISDEEGHFCL CQGRVQFINP AKIGISVKRK LLNNRLLDKE KGVTTIQSVV
     951  ESELEQSSLI ATQNLVTYRI DKNDIQQSLS LARFNLLSLF LPAVSPGVDI
    1001  VDERSKLCRK TKRSDGGNEI LRSLLVDNRA PKFRDANDDP VIPYKLSKDT
    1051  TLNLNQKEAI DKVMRAEDYA LILGMPGTGK TTVIAEIIKI LVSEGKRVLL
    1101  TSYTHSAVDN ILIKLRNTNI SIMRLGMKHK VHPDTQKYVP NYASVKSYND
    1151  YLSKINSTSV VATTCLGIND ILFTLNEKDF DYVILDEASQ ISMPVALGPL
    1201  RYGNRFIMVG DHYQLPPLVK NDAARLGGLE ESLFKTFCEK HPESVAELTL
    1251  QYRMCGDIVT LSNFLIYDNK LKCGNNEVFA QSLELPMPEA LSRYRNESAN
    1301  SKQWLEDILE PTRKVVFLNY DNCPDIIEQS EKDNITNHGE AELTLQCVEG
    1351  MLLSGVPCED IGVMTLYRAQ LRLLKKIFNK NVYDGLEILT ADQFQGRDKK
    1401  CIIISMVRRN SQLNGGALLK ELRRVNVAMT RAKSKLIIIG SKSTIGSVPE
    1451  IKSFVNLLEE RNWVYTMCKD ALYKYKFPDR SNAIDEARKG CGKRTGAKPI
    1501  TSKSKFVSDK PIIKEILQEY ES*                             

external links for Dna2p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily YPL+
Ashbya (AGD) BOND GPMdb (Mass Spec.) YeastGFP
Aspergillus (AspGD) BioPIXIE MIPS YeastRC Public Image Repository
Candida (CGD) CYC2008 (complexes) Pfam domains
Candida (CandidaDB) Complexome YeastRC Structure Prediction (Seattle)
YGOB DIP

YOGY GeneMANIA

References cited on this page View Complete Literature Guide for Dna2p
1) Dumas LB, et al.  (1982) New temperature-sensitive mutants of Saccharomyces cerevisiae affecting DNA replication. Mol Gen Genet 187(1):42-6
2) Budd ME and Campbell JL  (2000) The pattern of sensitivity of yeast dna2 mutants to DNA damaging agents suggests a role in DSB and postreplication repair pathways. Mutat Res 459(3):173-86
3) Budd ME and Campbell JL  (1997) A yeast replicative helicase, Dna2 helicase, interacts with yeast FEN-1 nuclease in carrying out its essential function. Mol Cell Biol 17(4):2136-42
4) Schlesinger MB and Formosa T  (2000) POB3 is required for both transcription and replication in the yeast Saccharomyces cerevisiae. Genetics 155(4):1593-606
5) 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(41):26880-90
6) Bae SH and Seo YS  (2000) Characterization of the enzymatic properties of the yeast dna2 Helicase/endonuclease suggests a new model for Okazaki fragment processing. J Biol Chem 275(48):38022-31
7) Hoopes LL, et al.  (2002) Mutations in DNA replication genes reduce yeast life span. Mol Cell Biol 22(12):4136-46
8) Choe W, et al.  (2002) Dynamic localization of an Okazaki fragment processing protein suggests a novel role in telomere replication. Mol Cell Biol 22(12):4202-17
9) 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(49):50840-9
10) 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(25):10171-6
11) Manfrini N, et al.  (2010) Processing of meiotic DNA double strand breaks requires cyclin-dependent kinase and multiple nucleases. J Biol Chem 285(15):11628-37
12) Balakrishnan L, et al.  (2010) Dna2 exhibits a unique strand end-dependent helicase function. J Biol Chem 285(50):38861-8
13) 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(9):966-76