YEN1_YEAST
ID YEN1_YEAST Reviewed; 759 AA.
AC P40028; D3DLU1; Q02463;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Holliday junction resolvase YEN1;
DE EC=3.1.-.-;
GN Name=YEN1; OrderedLocusNames=YER041W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sigma 1278B;
RA El-Berry H.M., Cooper T.G.;
RT "Sequence of an open reading frame 3' to the GLN3 gene.";
RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 59.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [6]
RP FUNCTION.
RX PubMed=19020614; DOI=10.1038/nature07470;
RA Ip S.C., Rass U., Blanco M.G., Flynn H.R., Skehel J.M., West S.C.;
RT "Identification of Holliday junction resolvases from humans and yeast.";
RL Nature 456:357-361(2008).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=19520826; DOI=10.1073/pnas.0900604106;
RA Kosugi S., Hasebe M., Tomita M., Yanagawa H.;
RT "Systematic identification of cell cycle-dependent yeast nucleocytoplasmic
RT shuttling proteins by prediction of composite motifs.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:10171-10176(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-730 AND SER-731, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [9]
RP FUNCTION.
RX PubMed=20106725; DOI=10.1016/j.dnarep.2009.12.017;
RA Blanco M.G., Matos J., Rass U., Ip S.C., West S.C.;
RT "Functional overlap between the structure-specific nucleases Yen1 and
RT Mus81-Mms4 for DNA-damage repair in S. cerevisiae.";
RL DNA Repair 9:394-402(2010).
RN [10]
RP FUNCTION.
RX PubMed=21172663; DOI=10.1016/j.molcel.2010.11.016;
RA Ho C.K., Mazon G., Lam A.F., Symington L.S.;
RT "Mus81 and Yen1 promote reciprocal exchange during mitotic recombination to
RT maintain genome integrity in budding yeast.";
RL Mol. Cell 40:988-1000(2010).
RN [11]
RP MUTAGENESIS OF ASP-41; ILE-97; LYS-298; LYS-469; PHE-478; LYS-484; ARG-486;
RP TYR-487; ASN-526; LEU-528; TRP-529 AND LEU-530.
RX PubMed=26682650; DOI=10.7554/elife.12256;
RA Lee S.H., Princz L.N., Klugel M.F., Habermann B., Pfander B.,
RA Biertumpfel C.;
RT "Human Holliday junction resolvase GEN1 uses a chromodomain for efficient
RT DNA recognition and cleavage.";
RL Elife 4:0-0(2015).
CC -!- FUNCTION: Endonuclease which resolves Holliday junctions by the
CC introduction of symmetrically related cuts across the junction point,
CC to produce nicked duplex products in which the nicks can be readily
CC ligated. Four-way DNA intermediates, also known as Holliday junctions,
CC are formed during homologous recombination and DNA repair, and their
CC resolution is necessary for proper chromosome segregation. Involved in
CC DNA-damage repair in vegetative cells. {ECO:0000269|PubMed:19020614,
CC ECO:0000269|PubMed:20106725, ECO:0000269|PubMed:21172663}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19520826}. Nucleus
CC {ECO:0000269|PubMed:19520826}. Note=Predominantly nuclear in G1-
CC arrested cells, but cytoplasmically localized after release from G1
CC arrest.
CC -!- MISCELLANEOUS: Present with 131 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. GEN subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA60376.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U13615; AAA60376.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U18796; AAB64576.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07695.2; -; Genomic_DNA.
DR PIR; S50544; S50544.
DR RefSeq; NP_010959.2; NM_001178932.2.
DR AlphaFoldDB; P40028; -.
DR BioGRID; 36777; 66.
DR DIP; DIP-6450N; -.
DR IntAct; P40028; 9.
DR MINT; P40028; -.
DR STRING; 4932.YER041W; -.
DR iPTMnet; P40028; -.
DR MaxQB; P40028; -.
DR PaxDb; P40028; -.
DR PRIDE; P40028; -.
DR EnsemblFungi; YER041W_mRNA; YER041W; YER041W.
DR GeneID; 856764; -.
DR KEGG; sce:YER041W; -.
DR SGD; S000000843; YEN1.
DR VEuPathDB; FungiDB:YER041W; -.
DR eggNOG; KOG2520; Eukaryota.
DR HOGENOM; CLU_016401_0_0_1; -.
DR InParanoid; P40028; -.
DR OMA; FDGPMKP; -.
DR BioCyc; YEAST:G3O-30222-MON; -.
DR BRENDA; 3.1.21.10; 984.
DR PRO; PR:P40028; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40028; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0008409; F:5'-3' exonuclease activity; IBA:GO_Central.
DR GO; GO:0017108; F:5'-flap endonuclease activity; ISS:UniProtKB.
DR GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IDA:SGD.
DR GO; GO:0000400; F:four-way junction DNA binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IGI:SGD.
DR GO; GO:0006281; P:DNA repair; IGI:SGD.
DR GO; GO:0031297; P:replication fork processing; ISS:UniProtKB.
DR CDD; cd09906; H3TH_YEN1; 1.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR006086; XPG-I_dom.
DR InterPro; IPR006084; XPG/Rad2.
DR InterPro; IPR006085; XPG_DNA_repair_N.
DR InterPro; IPR037316; Yen1_H3TH.
DR PANTHER; PTHR11081; PTHR11081; 3.
DR Pfam; PF00867; XPG_I; 1.
DR PRINTS; PR00853; XPGRADSUPER.
DR SMART; SM00484; XPGI; 1.
DR SMART; SM00485; XPGN; 1.
DR SUPFAM; SSF47807; SSF47807; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA damage; DNA repair; Endonuclease; Hydrolase; Nuclease;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..759
FT /note="Holliday junction resolvase YEN1"
FT /id="PRO_0000202629"
FT REGION 62..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 730
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 731
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 41
FT /note="D->N: Mutants do not survive after treatment with
FT DNA-damaging agent MMS."
FT /evidence="ECO:0000269|PubMed:26682650"
FT MUTAGEN 97
FT /note="I->E: Mutants show a slight growth defect after
FT treatment with DNA-damaging agent MMS."
FT /evidence="ECO:0000269|PubMed:26682650"
FT MUTAGEN 298
FT /note="K->E: Mutants show a very strong growth defect after
FT treatment with DNA-damaging agent MMS."
FT /evidence="ECO:0000269|PubMed:26682650"
FT MUTAGEN 469
FT /note="K->E: Mutants show a growth defect after treatment
FT with DNA-damaging agent MMS."
FT /evidence="ECO:0000269|PubMed:26682650"
FT MUTAGEN 478
FT /note="F->A: Mutants show a growth defect after treatment
FT with DNA-damaging agent MMS."
FT /evidence="ECO:0000269|PubMed:26682650"
FT MUTAGEN 484
FT /note="K->E: Mutants show a growth defect after treatment
FT with DNA-damaging agent MMS."
FT /evidence="ECO:0000269|PubMed:26682650"
FT MUTAGEN 486
FT /note="R->E: Mutants show a strong growth defect after
FT treatment with DNA-damaging agent MMS."
FT /evidence="ECO:0000269|PubMed:26682650"
FT MUTAGEN 487
FT /note="Y->A: Mutants show a strong growth defect after
FT treatment with DNA-damaging agent MMS."
FT /evidence="ECO:0000269|PubMed:26682650"
FT MUTAGEN 526
FT /note="N->A: Mutants show a growth defect after treatment
FT with DNA-damaging agent MMS."
FT /evidence="ECO:0000269|PubMed:26682650"
FT MUTAGEN 528
FT /note="L->D: Mutants show a growth defect after treatment
FT with DNA-damaging agent MMS."
FT /evidence="ECO:0000269|PubMed:26682650"
FT MUTAGEN 529
FT /note="W->A: Mutants show a growth defect after treatment
FT with DNA-damaging agent MMS."
FT /evidence="ECO:0000269|PubMed:26682650"
FT MUTAGEN 530
FT /note="L->A: Mutants show no effect after treatment with
FT DNA-damaging agent MMS."
FT /evidence="ECO:0000269|PubMed:26682650"
FT CONFLICT 59
FT /note="A -> P (in Ref. 2; AAB64576)"
FT /evidence="ECO:0000305"
FT CONFLICT 164..165
FT /note="LL -> FV (in Ref. 1; AAA60376)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="Y -> C (in Ref. 1; AAA60376)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 759 AA; 87364 MW; CE1305A9F78CA300 CRC64;
MGVSQIWEFL KPYLQDSRIP LRKFVIDFNK SQKRAPRIAI DAYGWLFECG FIQNIDISAR
SRSRSRSPTR SPRDSDIDSS QEYYGSRSYT TTGKAVINFI SRLKELLSLN VEFLLVFDGV
MKPSFKRKFN HEQNATTCDD EKEYYSSWEQ HVKNHEVYGN CKGLLAPSDP EFISLVRKLL
DLMNISYVIA CGEGEAQCVW LQVSGAVDFI LSNDSDTLVF GGEKILKNYS KFYDDFGPSS
ITSHSPSRHH DSKESFVTVI DLPKINKVAG KKFDRLSLLF FSVLLGADYN RGVKGLGKNK
SLQLAQCEDP NFSMEFYDIF KDFNLEDLTS ESLRKSRYRL FQKRLYLYCK DHSVELFGRN
YPVLLNQGSF EGWPSTVAIM HYFHPIVQPY FDEEVLSDKY INMAGNGHYR NLNFNELKYF
LQSLNLPQIS SFDKWFHDSM HEMFLLREFL SIDESDNIGK GNMRITEEKI MNIDGGKFQI
PCFKIRYTTF LPNIPISSQS PLKRSNSPSR SKSPTRRQMD IMEHPNSLWL PKYLIPQSHP
LVIQYYETQQ LIQKEKEKKG KKSNKSRLPQ KNNLDEFLRK HTSPIKSIGK VGESRKEILE
PVRKRLFVDT DEDTSLEEIP APTRLTTVDE HSDNDDDSLI FVDEITNSQS VLDSSPGKRI
RDLTQDEQVD VWKDVIEISP IKKSRTTNAE KNPPESGLKS RSSITINARL QGTKMLPPNL
TAPRLEREHS SVLDQLVTDA QDTVDRFVAC DSDSSSTIE
