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DNA endonuclease SAE2 (EC 3.1.-.-) (Completion of meiotic recombination protein 1) (Sporulation in the absence of SPO11 protein 2)

 COM1_YEAST              Reviewed;         345 AA.
P46946; D6VTX7;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
25-OCT-2017, entry version 130.
RecName: Full=DNA endonuclease SAE2;
EC=3.1.-.-;
AltName: Full=Completion of meiotic recombination protein 1;
AltName: Full=Sporulation in the absence of SPO11 protein 2;
Name=SAE2; Synonyms=COM1; OrderedLocusNames=YGL175C; ORFNames=G1639;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9215888;
McKee A.H.Z., Kleckner N.;
"A general method for identifying recessive diploid-specific mutations
in Saccharomyces cerevisiae, its application to the isolation of
mutants blocked at intermediate stages of meiotic prophase and
characterization of a new gene SAE2.";
Genetics 146:797-816(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8619317; DOI=10.1002/yea.320111209;
Bertani I., Coglievina M., Zaccaria P., Klima R., Bruschi C.V.;
"The sequence of an 11.1 kb fragment on the left arm of Saccharomyces
cerevisiae chromosome VII reveals six open reading frames including
NSP49, KEM1 and four putative new genes.";
Yeast 11:1187-1194(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869;
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
FUNCTION.
PubMed=9215887;
Prinz S., Amon A., Klein F.;
"Isolation of COM1, a new gene required to complete meiotic double-
strand break-induced recombination in Saccharomyces cerevisiae.";
Genetics 146:781-795(1997).
[6]
FUNCTION.
PubMed=11052944; DOI=10.1126/science.290.5492.806;
Borde V., Goldman A.S., Lichten M.;
"Direct coupling between meiotic DNA replication and recombination
initiation.";
Science 290:806-809(2000).
[7]
FUNCTION.
PubMed=11333222;
Rattray A.J., McGill C.B., Shafer B.K., Strathern J.N.;
"Fidelity of mitotic double-strand-break repair in Saccharomyces
cerevisiae: a role for SAE2/COM1.";
Genetics 158:109-122(2001).
[8]
FUNCTION.
PubMed=11983174; DOI=10.1016/S1097-2765(02)00498-7;
Neale M.J., Ramachandran M., Trelles-Sticken E., Scherthan H.,
Goldman A.S.;
"Wild-type levels of Spo11-induced DSBs are required for normal
single-strand resection during meiosis.";
Mol. Cell 9:835-846(2002).
[9]
FUNCTION.
PubMed=11832209; DOI=10.1016/S0092-8674(02)00614-1;
Lobachev K.S., Gordenin D.A., Resnick M.A.;
"The Mre11 complex is required for repair of hairpin-capped double-
strand breaks and prevention of chromosome rearrangements.";
Cell 108:183-193(2002).
[10]
FUNCTION.
PubMed=12839620; DOI=10.1046/j.1365-2443.2003.00659.x;
Fukuda T., Nogami S., Ohya Y.;
"VDE-initiated intein homing in Saccharomyces cerevisiae proceeds in a
meiotic recombination-like manner.";
Genes Cells 8:587-602(2003).
[11]
FUNCTION.
PubMed=12925751; DOI=10.1091/mbc.E02-11-0719;
Viscardi V., Baroni E., Romano M., Lucchini G., Longhese M.P.;
"Sudden telomere lengthening triggers a Rad53-dependent checkpoint in
Saccharomyces cerevisiae.";
Mol. Biol. Cell 14:3126-3143(2003).
[12]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[13]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15369670; DOI=10.1016/j.cell.2004.08.015;
Lisby M., Barlow J.H., Burgess R.C., Rothstein R.;
"Choreography of the DNA damage response: spatiotemporal relationships
among checkpoint and repair proteins.";
Cell 118:699-713(2004).
[15]
FUNCTION.
PubMed=14729978; DOI=10.1128/MCB.24.3.1351-1364.2004;
Yu J., Marshall K., Yamaguchi M., Haber J.E., Weil C.F.;
"Microhomology-dependent end joining and repair of transposon-induced
DNA hairpins by host factors in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 24:1351-1364(2004).
[16]
FUNCTION, PHOSPHORYLATION, AND MUTAGENESIS OF SER-72; SER-73; THR-75;
SER-76; THR-90; SER-249; SER-278; THR-279 AND SER-289.
PubMed=15121837; DOI=10.1128/MCB.24.10.4151-4165.2004;
Baroni E., Viscardi V., Cartagena-Lirola H., Lucchini G.,
Longhese M.P.;
"The functions of budding yeast Sae2 in the DNA damage response
require Mec1- and Tel1-dependent phosphorylation.";
Mol. Cell. Biol. 24:4151-4165(2004).
[17]
FUNCTION.
PubMed=15655113; DOI=10.1101/gad.321105;
Prieler S., Penkner A., Borde V., Klein F.;
"The control of Spo11's interaction with meiotic recombination
hotspots.";
Genes Dev. 19:255-269(2005).
[18]
FUNCTION.
PubMed=15937224; DOI=10.1101/gad.1315805;
Rattray A.J., Shafer B.K., Neelam B., Strathern J.N.;
"A mechanism of palindromic gene amplification in Saccharomyces
cerevisiae.";
Genes Dev. 19:1390-1399(2005).
[19]
FUNCTION.
PubMed=15834151; DOI=10.1534/genetics.104.028795;
Deng C., Brown J.A., You D., Brown J.M.;
"Multiple endonucleases function to repair covalent topoisomerase I
complexes in Saccharomyces cerevisiae.";
Genetics 170:591-600(2005).
[20]
FUNCTION.
PubMed=16162495; DOI=10.1074/jbc.M508339200;
Clerici M., Mantiero D., Lucchini G., Longhese M.P.;
"The Saccharomyces cerevisiae Sae2 protein promotes resection and
bridging of double strand break ends.";
J. Biol. Chem. 280:38631-38638(2005).
[21]
FUNCTION, PHOSPHORYLATION, AND MUTAGENESIS OF SER-73; THR-90; SER-249;
THR-279 AND SER-289.
PubMed=16861895; DOI=10.4161/cc.5.14.2916;
Cartagena-Lirola H., Guerini I., Viscardi V., Lucchini G.,
Longhese M.P.;
"Budding yeast Sae2 is an in vivo target of the Mec1 and Tel1
checkpoint kinases during meiosis.";
Cell Cycle 5:1549-1559(2006).
[22]
FUNCTION.
PubMed=16374511; DOI=10.1038/sj.embor.7400593;
Clerici M., Mantiero D., Lucchini G., Longhese M.P.;
"The Saccharomyces cerevisiae Sae2 protein negatively regulates DNA
damage checkpoint signalling.";
EMBO Rep. 7:212-218(2006).
[23]
FUNCTION.
PubMed=17565964; DOI=10.1534/genetics.107.076539;
Lee K., Lee S.E.;
"Saccharomyces cerevisiae Sae2- and Tel1-dependent single-strand DNA
formation at DNA break promotes microhomology-mediated end joining.";
Genetics 176:2003-2014(2007).
[24]
SUBUNIT, AND INTERACTION WITH MRE11.
PubMed=17989249; DOI=10.1101/gr.6667007;
Suter B., Fetchko M.J., Imhof R., Graham C.I., Stoffel-Studer I.,
Zbinden C., Raghavan M., Lopez L., Beneti L., Hort J., Fillingham J.,
Greenblatt J.F., Giaever G., Nislow C., Stagljar I.;
"Examining protein protein interactions using endogenously tagged
yeast arrays: the cross-and-capture system.";
Genome Res. 17:1774-1782(2007).
[25]
FUNCTION, DNA-BINDING, DOMAIN, AND MUTAGENESIS OF GLY-270.
PubMed=18042458; DOI=10.1016/j.molcel.2007.11.001;
Lengsfeld B.M., Rattray A.J., Bhaskara V., Ghirlando R., Paull T.T.;
"Sae2 is an endonuclease that processes hairpin DNA cooperatively with
the Mre11/Rad50/Xrs2 complex.";
Mol. Cell 28:638-651(2007).
[26]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND MUTAGENESIS OF
SER-73; THR-90; SER-249; THR-279 AND SER-289.
PubMed=18670132; DOI=10.1266/ggs.83.209;
Terasawa M., Ogawa T., Tsukamoto Y., Ogawa H.;
"Sae2p phosphorylation is crucial for cooperation with Mre11p for
resection of DNA double-strand break ends during meiotic recombination
in Saccharomyces cerevisiae.";
Genes Genet. Syst. 83:209-217(2008).
[27]
FUNCTION, MUTAGENESIS OF ARG-223; LEU-225 AND SER-267, AND
PHOSPHORYLATION AT SER-267.
PubMed=18716619; DOI=10.1038/nature07215;
Huertas P., Cortes-Ledesma F., Sartori A.A., Aguilera A.,
Jackson S.P.;
"CDK targets Sae2 to control DNA-end resection and homologous
recombination.";
Nature 455:689-692(2008).
[28]
FUNCTION.
PubMed=18806779; DOI=10.1038/nature07312;
Mimitou E.P., Symington L.S.;
"Sae2, Exo1 and Sgs1 collaborate in DNA double-strand break
processing.";
Nature 455:770-774(2008).
[29]
FUNCTION.
PubMed=19361851; DOI=10.1016/j.cell.2009.02.016;
Doksani Y., Bermejo R., Fiorani S., Haber J.E., Foiani M.;
"Replicon dynamics, dormant origin firing, and terminal fork integrity
after double-strand break formation.";
Cell 137:247-258(2009).
[30]
FUNCTION.
PubMed=19124276; DOI=10.1016/j.dnarep.2008.11.017;
Lisnic B., Svetec I.K., Stafa A., Zgaga Z.;
"Size-dependent palindrome-induced intrachromosomal recombination in
yeast.";
DNA Repair 8:383-389(2009).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[32]
FUNCTION, MUTAGENESIS OF SER-267, AND PHOSPHORYLATION AT SER-267.
PubMed=20150422; DOI=10.1074/jbc.M110.104083;
Manfrini N., Guerini I., Citterio A., Lucchini G., Longhese M.P.;
"Processing of meiotic DNA double strand breaks requires cyclin-
dependent kinase and multiple nucleases.";
J. Biol. Chem. 285:11628-11637(2010).
[33]
FUNCTION, AND PHOSPHORYLATION.
PubMed=20061370; DOI=10.1093/nar/gkp1222;
Janke R., Herzberg K., Rolfsmeier M., Mar J., Bashkirov V.I.,
Haghnazari E., Cantin G., Yates J.R. III, Heyer W.D.;
"A truncated DNA-damage-signaling response is activated after DSB
formation in the G1 phase of Saccharomyces cerevisiae.";
Nucleic Acids Res. 38:2302-2313(2010).
-!- FUNCTION: Endonuclease that cooperates with the MRX complex in
processing meiotic and mitotic double-strand breaks by allowing
the endonucleolytic removal of SPO11 from the break sites and
ensuring both resection and intrachromosomal association of the
broken ends. Required for proper recovery from checkpoint-mediated
cell cycle arrest after DNA damage. MRX complex and SAE2 remove a
small oligonucleotide(s) from the DNA ends to form an early
intermediate which is rapidly processed by EXO1 and/or SGS1 to
generate extensive tracts of single-stranded DNA that serve as
substrate for RAD51. Plays a transitional role in the dissociation
of MRE11 from, and the recruitment of RAD52 to, repair foci.
Ensures that both ends of a DSB participate in a recombination
event and impairs the formation of palindromic structures in the
genome. With TEL1, promotes microhomology-mediated end joining
(MMEJ) but inhibits non-homologous end joining (NHEJ), likely by
regulating MRE11-dependent ssDNA accumulation at DNA break. SAE2
and MRX are particularly important for removal of hairpins, bulky
adducts and other irregular end structures. Facilitates telomere
length reequilibration and subsequent checkpoint switch off.
Involved in homing efficiency of VMA1 intein VDE and in repair of
transposon excision sites. {ECO:0000269|PubMed:11052944,
ECO:0000269|PubMed:11333222, ECO:0000269|PubMed:11832209,
ECO:0000269|PubMed:11983174, ECO:0000269|PubMed:12839620,
ECO:0000269|PubMed:12925751, ECO:0000269|PubMed:14729978,
ECO:0000269|PubMed:15121837, ECO:0000269|PubMed:15369670,
ECO:0000269|PubMed:15655113, ECO:0000269|PubMed:15834151,
ECO:0000269|PubMed:15937224, ECO:0000269|PubMed:16162495,
ECO:0000269|PubMed:16374511, ECO:0000269|PubMed:16861895,
ECO:0000269|PubMed:17565964, ECO:0000269|PubMed:18042458,
ECO:0000269|PubMed:18670132, ECO:0000269|PubMed:18716619,
ECO:0000269|PubMed:18806779, ECO:0000269|PubMed:19124276,
ECO:0000269|PubMed:19361851, ECO:0000269|PubMed:20061370,
ECO:0000269|PubMed:20150422, ECO:0000269|PubMed:9215887}.
-!- SUBUNIT: Dimer or multimer. Interacts with MRE11.
{ECO:0000269|PubMed:17989249}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-16440, EBI-16440;
P32829:MRE11; NbExp=2; IntAct=EBI-16440, EBI-11255;
P33301:XRS2; NbExp=3; IntAct=EBI-16440, EBI-20599;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
Nucleus {ECO:0000269|PubMed:15369670,
ECO:0000269|PubMed:18670132}. Note=Accumulates in foci at the
precise time when MRE11 foci disassemble and RAD52 foci assemble
(PubMed:18670132). Remains associated with DSBs along with MRE11
in nuclease-deficient cells (PubMed:18670132).
-!- PTM: Phosphorylated forms accumulate periodically during the
unperturbed cell cycle and in response to DNA damage in G2.
Phosphorylated by MEC1 and TEL1. Mutagenesis experiments showed
that several of the 5 residues located in canonical (S/T)Q motifs,
which are favored for phosphorylation by ATM/ATR kinases (Ser-73,
Thr-90, Ser-249, Thr-279 and Ser-289) may be phosphorylated.
Phosphorylated at Ser-267 by CDC28 which is required to initiate
meiotic DSB resection by allowing SPO11 removal from DSB ends.
{ECO:0000269|PubMed:15121837, ECO:0000269|PubMed:16861895,
ECO:0000269|PubMed:18670132, ECO:0000269|PubMed:18716619,
ECO:0000269|PubMed:20061370, ECO:0000269|PubMed:20150422}.
-!- MISCELLANEOUS: Present with 1030 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the COM1/SAE2/CtIP family. {ECO:0000305}.
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EMBL; U49447; AAB96338.1; -; Genomic_DNA.
EMBL; X84705; CAA59178.1; -; Genomic_DNA.
EMBL; Z72697; CAA96887.1; -; Genomic_DNA.
EMBL; BK006941; DAA07938.1; -; Genomic_DNA.
PIR; S59236; S59236.
RefSeq; NP_011340.1; NM_001181040.1.
ProteinModelPortal; P46946; -.
BioGrid; 33078; 137.
DIP; DIP-1603N; -.
IntAct; P46946; 8.
MINT; MINT-391468; -.
STRING; 4932.YGL175C; -.
iPTMnet; P46946; -.
MaxQB; P46946; -.
PRIDE; P46946; -.
EnsemblFungi; YGL175C; YGL175C; YGL175C.
GeneID; 852700; -.
KEGG; sce:YGL175C; -.
EuPathDB; FungiDB:YGL175C; -.
SGD; S000003143; SAE2.
InParanoid; P46946; -.
OMA; WTHENED; -.
OrthoDB; EOG092C34HO; -.
BioCyc; YEAST:G3O-30663-MONOMER; -.
Reactome; R-SCE-912446; Meiotic recombination.
PRO; PR:P46946; -.
Proteomes; UP000002311; Chromosome VII.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0030870; C:Mre11 complex; IDA:SGD.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
GO; GO:0004520; F:endodeoxyribonuclease activity; EXP:Reactome.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IDA:SGD.
GO; GO:0000737; P:DNA catabolic process, endonucleolytic; IDA:SGD.
GO; GO:0000729; P:DNA double-strand break processing; IMP:SGD.
GO; GO:0010791; P:DNA double-strand break processing involved in repair via synthesis-dependent strand annealing; IMP:SGD.
GO; GO:0031292; P:gene conversion at mating-type locus, DNA double-strand break processing; IMP:SGD.
GO; GO:0042138; P:meiotic DNA double-strand break formation; IGI:SGD.
GO; GO:0000706; P:meiotic DNA double-strand break processing; IMP:SGD.
GO; GO:0035306; P:positive regulation of dephosphorylation; IMP:SGD.
GO; GO:1905779; P:positive regulation of exonuclease activity; IDA:SGD.
GO; GO:0000723; P:telomere maintenance; IMP:SGD.
GO; GO:0031860; P:telomeric 3' overhang formation; IMP:SGD.
1: Evidence at protein level;
Complete proteome; Cytoplasm; DNA damage; DNA repair; DNA-binding;
Endonuclease; Hydrolase; Meiosis; Nuclease; Nucleus; Phosphoprotein;
Reference proteome.
CHAIN 1 345 DNA endonuclease SAE2.
/FTId=PRO_0000097565.
REGION 21 172 DNA-binding.
MOD_RES 143 143 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 267 267 Phosphoserine; by CDC28.
{ECO:0000269|PubMed:18716619,
ECO:0000269|PubMed:20150422}.
MUTAGEN 72 72 S->A: Reduces DNA damage-induced
phosphorylation; when associated with A-
73, A-75, A-76 and A-90.
{ECO:0000269|PubMed:15121837}.
MUTAGEN 73 73 S->A: Reduces DNA damage-induced
phosphorylation; when associated with A-
73, A-75, A-76 and A-90. Abolishes DNA
damage-induced phosphorylation and
function in DNA repair; when associated
with A-90, A-249, A-279 and A-289.
{ECO:0000269|PubMed:15121837,
ECO:0000269|PubMed:16861895,
ECO:0000269|PubMed:18670132}.
MUTAGEN 75 75 T->A: Reduces DNA damage-induced
phosphorylation; when associated with A-
72, A-75, A-76 and A-90.
{ECO:0000269|PubMed:15121837}.
MUTAGEN 76 76 S->A: Reduces DNA damage-induced
phosphorylation; when associated with A-
72, A-73, A-75 and A-90.
{ECO:0000269|PubMed:15121837}.
MUTAGEN 90 90 T->A: Reduces DNA damage-induced
phosphorylation; when associated with A-
72, A-73, A-75 and A-76. Abolishes DNA
damage-induced phosphorylation and
function in DNA repair; when associated
with A-73, A-249, A-279 and A-289.
{ECO:0000269|PubMed:15121837,
ECO:0000269|PubMed:16861895,
ECO:0000269|PubMed:18670132}.
MUTAGEN 223 223 R->A: Leads to camptothecin
hypersensitivity and loss of function;
when associated with A-225.
{ECO:0000269|PubMed:18716619}.
MUTAGEN 225 225 L->A: Leads to camptothecin
hypersensitivity and loss of function;
when associated with A-223.
{ECO:0000269|PubMed:18716619}.
MUTAGEN 249 249 S->A: Reduces DNA damage-induced
phosphorylation; when associated with A-
278, A-279, and A-289. Abolishes DNA
damage-induced phosphorylation and
function in DNA repair; when associated
with A-73, A-90, A-279 and A-289.
{ECO:0000269|PubMed:15121837,
ECO:0000269|PubMed:16861895,
ECO:0000269|PubMed:18670132}.
MUTAGEN 267 267 S->A: Leads to camptothecin
hypersensitivity and loss of function.
{ECO:0000269|PubMed:18716619,
ECO:0000269|PubMed:20150422}.
MUTAGEN 267 267 S->E: Leads to constitutive activation of
the DNA repair function.
{ECO:0000269|PubMed:18716619,
ECO:0000269|PubMed:20150422}.
MUTAGEN 270 270 G->D: Abolishes DNA-binding and
endonuclease activity.
{ECO:0000269|PubMed:18042458}.
MUTAGEN 278 278 S->A: Reduces DNA damage-induced
phosphorylation; when associated with A-
249, A-279, and A-289.
{ECO:0000269|PubMed:15121837}.
MUTAGEN 279 279 T->A: Reduces DNA damage-induced
phosphorylation; when associated with A-
249, A-278, and A-289. Abolishes DNA
damage-induced phosphorylation and
function in DNA repair; when associated
with A-73, A-90, A-249 and A-289.
{ECO:0000269|PubMed:15121837,
ECO:0000269|PubMed:16861895,
ECO:0000269|PubMed:18670132}.
MUTAGEN 289 289 S->A: Reduces DNA damage-induced
phosphorylation; when associated with A-
249, A-278, and A-279. Abolishes DNA
damage-induced phosphorylation and
function in DNA repair; when associated
with A-73, A-90, A-249 and A-279.
{ECO:0000269|PubMed:15121837,
ECO:0000269|PubMed:16861895,
ECO:0000269|PubMed:18670132}.
SEQUENCE 345 AA; 40097 MW; 284D57A3C11DD92B CRC64;
MVTGEENVYL KSSLSILKEL SLDELLNVQY DVTTLIAKRV QALQNRNKCV LEEPNSKLAE
ILCHEKNAPQ QSSQTSAGPG EQDSEDFILT QFDEDIKKES AEVHYRNENK HTVQLPLVTM
PPNRHKRKIS EFSSPLNGLN NLSDLEDCSD TVIHEKDNDK ENKTRKLLGI ELENPESTSP
NLYKNVKDNF LFDFNTNPLT KRAWILEDFR PNEDIAPVKR GRRKLERFYA QVGKPEDSKH
RSLSVVIESQ NSDYEFAFDN LRNRSKSPPG FGRLDFPSTQ EGNEDKKKSQ EIIRRKTKYR
FLMASNNKIP PYEREYVFKR EQLNQIVDDG CFFWSDKLLQ IYARC


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