RAD17_YEAST
ID RAD17_YEAST Reviewed; 401 AA.
AC P48581; D6W361;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=DNA damage checkpoint control protein RAD17;
DE AltName: Full=DNA repair exonuclease RAD17;
GN Name=RAD17; OrderedLocusNames=YOR368W;
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], FUNCTION, AND MUTAGENESIS OF GLU-128.
RX PubMed=8649984; DOI=10.1093/nar/24.9.1669;
RA Siede W., Nusspaumer G., Portillo V., Rodriguez R., Friedberg E.C.;
RT "Cloning and characterization of RAD17, a gene controlling cell cycle
RT responses to DNA damage in Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 24:1669-1675(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=7491494; DOI=10.1126/science.270.5241.1488;
RA Lydall D., Weinert T.A.;
RT "Yeast checkpoint genes in DNA damage processing: implications for repair
RT and arrest.";
RL Science 270:1488-1491(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
RP GENOME REANNOTATION.
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 [5]
RP FUNCTION OF THE CHECKPOINT CLAMP COMPLEX.
RX PubMed=12271137; DOI=10.1073/pnas.202463999;
RA Giannattasio M., Sommariva E., Vercillo R., Lippi-Boncambi F., Liberi G.,
RA Foiani M., Plevani P., Muzi-Falconi M.;
RT "A dominant-negative MEC3 mutant uncovers new functions for the Rad17
RT complex and Tel1.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12997-13002(2002).
RN [6]
RP INTERACTION OF THE CHECKPOINT CLAMP COMPLEX WITH THE RFC-RAD24 CHECKPOINT
RP CLAMP LOADER COMPLEX, FUNCTION OF THE CHECKPOINT CLAMP COMPLEX, AND LACK OF
RP EXONUCLEASE ACTIVITY.
RX PubMed=12604797; DOI=10.1073/pnas.0437148100;
RA Majka J., Burgers P.M.J.;
RT "Yeast Rad17/Mec3/Ddc1: a sliding clamp for the DNA damage checkpoint.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2249-2254(2003).
RN [7]
RP IDENTIFICATION IN THE CHECKPOINT CLAMP COMPLEX, AND FUNCTION OF THE
RP CHECKPOINT CLAMP COMPLEX.
RX PubMed=9891048; DOI=10.1128/mcb.19.2.1136;
RA Kondo T., Matsumoto K., Sugimoto K.;
RT "Role of a complex containing Rad17, Mec3, and Ddc1 in the yeast DNA damage
RT checkpoint pathway.";
RL Mol. Cell. Biol. 19:1136-1143(1999).
RN [8]
RP IDENTIFICATION IN THE CHECKPOINT CLAMP COMPLEX, AND FUNCTION OF THE
RP CHECKPOINT CLAMP COMPLEX.
RX PubMed=12672803; DOI=10.1074/jbc.m301260200;
RA Giannattasio M., Sabbioneda S., Minuzzo M., Plevani P., Muzi-Falconi M.;
RT "Correlation between checkpoint activation and in vivo assembly of the
RT yeast checkpoint complex Rad17-Mec3-Ddc1.";
RL J. Biol. Chem. 278:22303-22308(2003).
RN [9]
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 [10]
RP INTERACTION OF THE CHECKPOINT CLAMP COMPLEX WITH THE RFC-RAD24 CHECKPOINT
RP CLAMP LOADER COMPLEX.
RX PubMed=15014082; DOI=10.1074/jbc.m400898200;
RA Majka J., Chung B.Y., Burgers P.M.J.;
RT "Requirement for ATP by the DNA damage checkpoint clamp loader.";
RL J. Biol. Chem. 279:20921-20926(2004).
RN [11]
RP IDENTIFICATION IN THE CHECKPOINT CLAMP COMPLEX, AND FUNCTION OF THE
RP CHECKPOINT CLAMP COMPLEX.
RX PubMed=16137930; DOI=10.1016/j.dnarep.2005.07.008;
RA Majka J., Burgers P.M.J.;
RT "Function of Rad17/Mec3/Ddc1 and its partial complexes in the DNA damage
RT checkpoint.";
RL DNA Repair 4:1189-1194(2005).
RN [12]
RP INTERACTION WITH REV7, AND FUNCTION OF THE CHECKPOINT CLAMP COMPLEX.
RX PubMed=16169844; DOI=10.1074/jbc.m507638200;
RA Sabbioneda S., Minesinger B.K., Giannattasio M., Plevani P.,
RA Muzi-Falconi M., Jinks-Robertson S.;
RT "The 9-1-1 checkpoint clamp physically interacts with polzeta and is
RT partially required for spontaneous polzeta-dependent mutagenesis in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 280:38657-38665(2005).
RN [13]
RP INTERACTION WITH DDC1 AND MEC3.
RX PubMed=16202664; DOI=10.1016/j.dnarep.2005.08.018;
RA Cardone J.M., Revers L.F., Machado R.M., Bonatto D., Brendel M.,
RA Henriques J.A.P.;
RT "Psoralen-sensitive mutant pso9-1 of Saccharomyces cerevisiae contains a
RT mutant allele of the DNA damage checkpoint gene MEC3.";
RL DNA Repair 5:163-171(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [15]
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).
CC -!- FUNCTION: Component of the checkpoint clamp complex involved in the
CC surveillance mechanism that allows the DNA repair pathways to act to
CC restore the integrity of the DNA prior to DNA synthesis or separation
CC of the replicated chromosomes. Associates with sites of DNA damage and
CC modulates the MEC1 signaling pathway and the activation of RAD53 in
CC response to DNA damage at phase G1. The complex also physically
CC regulates DNA polymerase zeta-dependent mutagenesis by controlling the
CC access of polymerase zeta to damaged DNA. Contrary to its human
CC counterpart, the 9-1-1 complex, the checkpoint clamp complex shows no
CC detectable exonuclease activity. {ECO:0000269|PubMed:12271137,
CC ECO:0000269|PubMed:12604797, ECO:0000269|PubMed:12672803,
CC ECO:0000269|PubMed:16137930, ECO:0000269|PubMed:16169844,
CC ECO:0000269|PubMed:7491494, ECO:0000269|PubMed:8649984,
CC ECO:0000269|PubMed:9891048}.
CC -!- SUBUNIT: Component of the checkpoint clamp complex composed of DDC1,
CC MEC3 and RAD17. The interaction with MEC3 is performed in a RAD17-
CC dependent manner. The checkpoint clamp complex loads onto DNA.
CC Interacts with the DNA polymerase zeta subunit REV7. 2 RAD17 subunits
CC form also a hetero trimer with one MEC3 subunit.
CC {ECO:0000269|PubMed:12604797, ECO:0000269|PubMed:12672803,
CC ECO:0000269|PubMed:15014082, ECO:0000269|PubMed:16137930,
CC ECO:0000269|PubMed:16169844, ECO:0000269|PubMed:16202664,
CC ECO:0000269|PubMed:9891048}.
CC -!- INTERACTION:
CC P48581; Q08949: DDC1; NbExp=4; IntAct=EBI-14652, EBI-30769;
CC P48581; Q02574: MEC3; NbExp=11; IntAct=EBI-14652, EBI-10658;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 189 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the rad1 family. {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; U37460; AAA80545.1; -; Genomic_DNA.
DR EMBL; U30796; AAA93250.1; -; Genomic_DNA.
DR EMBL; Z75276; CAA99699.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11127.1; -; Genomic_DNA.
DR PIR; S59670; S59670.
DR RefSeq; NP_015013.1; NM_001183788.1.
DR PDB; 7SGZ; EM; 3.17 A; G=1-401.
DR PDB; 7SH2; EM; 3.23 A; G=1-401.
DR PDB; 7ST9; EM; 2.20 A; F=1-401.
DR PDB; 7STB; EM; 2.72 A; F=1-401.
DR PDBsum; 7SGZ; -.
DR PDBsum; 7SH2; -.
DR PDBsum; 7ST9; -.
DR PDBsum; 7STB; -.
DR AlphaFoldDB; P48581; -.
DR SMR; P48581; -.
DR BioGRID; 34751; 225.
DR ComplexPortal; CPX-1806; Rad17-Mec3-Ddc1 checkpoint clamp complex.
DR DIP; DIP-1546N; -.
DR IntAct; P48581; 7.
DR MINT; P48581; -.
DR STRING; 4932.YOR368W; -.
DR CarbonylDB; P48581; -.
DR iPTMnet; P48581; -.
DR MaxQB; P48581; -.
DR PaxDb; P48581; -.
DR PRIDE; P48581; -.
DR EnsemblFungi; YOR368W_mRNA; YOR368W; YOR368W.
DR GeneID; 854550; -.
DR KEGG; sce:YOR368W; -.
DR SGD; S000005895; RAD17.
DR VEuPathDB; FungiDB:YOR368W; -.
DR eggNOG; KOG3194; Eukaryota.
DR GeneTree; ENSGT00500000044913; -.
DR HOGENOM; CLU_057555_0_0_1; -.
DR InParanoid; P48581; -.
DR OMA; VHLEHIT; -.
DR BioCyc; YEAST:G3O-33836-MON; -.
DR Reactome; R-SCE-176187; Activation of ATR in response to replication stress.
DR ChiTaRS; RAD17; yeast.
DR PRO; PR:P48581; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P48581; protein.
DR GO; GO:0030896; C:checkpoint clamp complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IPI:SGD.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IDA:ComplexPortal.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006302; P:double-strand break repair; IMP:SGD.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:SGD.
DR InterPro; IPR016587; Rad17.
DR InterPro; IPR003021; Rad1_Rec1_Rad17.
DR PANTHER; PTHR10870; PTHR10870; 1.
DR Pfam; PF02144; Rad1; 1.
DR PIRSF; PIRSF011769; Cell_cycle_RAD17; 1.
DR PRINTS; PR01245; RAD1REC1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; DNA-binding; Hydrolase; Nuclease;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..401
FT /note="DNA damage checkpoint control protein RAD17"
FT /id="PRO_0000097150"
FT REGION 367..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MUTAGEN 128
FT /note="E->K: In RAD17-1; UV-sensitive."
FT /evidence="ECO:0000269|PubMed:8649984"
SQ SEQUENCE 401 AA; 45580 MW; BFF7074676C483C9 CRC64;
MRINSELANK FSASTVHLEH ITTALSCLTP FGSKDDVLIF IDADGLSFVR ENNHVIKIQL
LLSRELFMSY SYRNETEDHM KLCVKINHIL DSVSVMNRNS DDIVECTLSY DGHGSPFVLI
FEDSFISERV EYSTYLIKDF DTNGLELDRE RISFEAIIKG EALHSALKDL KEIGCKECYV
YAKTEANDEN VFALISKSQL GFSKIKLPSN RSILEKLQVF DGDSTTVIDG FAVIGFFDFT
SFDKIRKSTK IASKVLFRMD VHGVLSVNIL SQTDDVIITD TTRPSNNRPG SIRQLQLPKD
YPGIVIEVCM LEKESIDEAA QTEIELLMET NELGNRNSFK KSTIRKRYGT DKGNETSNDN
LLQLNGKKIK LPSEEENNKN RESEDEENHC KYPTKDIPIF F
