RAD24_YEAST
ID RAD24_YEAST Reviewed; 659 AA.
AC P32641; D3DM81;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Checkpoint protein RAD24;
GN Name=RAD24; OrderedLocusNames=YER173W; ORFNames=SYGP-ORF60;
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 [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 [2]
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 [3]
RP INTERACTION WITH RFC2, AND IDENTIFICATION IN THE RAD24-RFC COMPLEX.
RX PubMed=10660302; DOI=10.1016/s0960-9822(99)00263-8;
RA Green C.M., Erdjument-Bromage H., Tempst P., Lowndes N.F.;
RT "A novel Rad24 checkpoint protein complex closely related to replication
RT factor C.";
RL Curr. Biol. 10:39-42(2000).
RN [4]
RP FUNCTION, INTERACTION WITH RCF5, AND MUTAGENESIS OF LYS-115.
RX PubMed=10913172; DOI=10.1128/mcb.20.16.5888-5896.2000;
RA Naiki T., Shimomura T., Kondo T., Matsumoto K., Sugimoto K.;
RT "Rfc5, in cooperation with rad24, controls DNA damage checkpoints
RT throughout the cell cycle in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 20:5888-5896(2000).
RN [5]
RP FUNCTION.
RX PubMed=11486023; DOI=10.1128/mcb.21.17.5838-5845.2001;
RA Naiki T., Kondo T., Nakada D., Matsumoto K., Sugimoto K.;
RT "Chl12 (Ctf18) forms a novel replication factor C-related complex and
RT functions redundantly with Rad24 in the DNA replication checkpoint
RT pathway.";
RL Mol. Cell. Biol. 21:5838-5845(2001).
RN [6]
RP INTERACTION WITH ECO1.
RX PubMed=12665596; DOI=10.1128/mcb.23.8.2999-3007.2003;
RA Kenna M.A., Skibbens R.V.;
RT "Mechanical link between cohesion establishment and DNA replication:
RT Ctf7p/Eco1p, a cohesion establishment factor, associates with three
RT different replication factor C complexes.";
RL Mol. Cell. Biol. 23:2999-3007(2003).
RN [7]
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 [8]
RP IDENTIFICATION IN THE RAD24-RFC COMPLEX, AND FUNCTION OF THE RAD24-RFC
RP COMPLEX.
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 [9]
RP IDENTIFICATION IN THE RAD24-RFC COMPLEX.
RX PubMed=15964801; DOI=10.1128/mcb.25.13.5445-5455.2005;
RA Bylund G.O., Burgers P.M.;
RT "Replication protein A-directed unloading of PCNA by the Ctf18 cohesion
RT establishment complex.";
RL Mol. Cell. Biol. 25:5445-5455(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-652 AND SER-654, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-652 AND SER-654, 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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Participates in checkpoint pathways arrest of the cell cycle,
CC a mechanism that allows the DNA repair pathways to act to restore the
CC integrity of the DNA prior to DNA synthesis or separation of the
CC replicated chromosomes. Regulates the DNA damage checkpoint pathway
CC throughout the cell cycle, when associated with RCF5. Component of the
CC RFC-like RAD24-RFC complex which loads the checkpoint clamp
CC DDC1:MEC3:RAD17 complex and is involved in DNA repair pathways. During
CC a clamp loading circle, the RFC:clamp complex binds to DNA and the
CC recognition of the double-stranded/single-stranded junction stimulates
CC ATP hydrolysis by RFC. The complex presumably provides bipartite ATP
CC sites in which one subunit supplies a catalytic site for hydrolysis of
CC ATP bound to the neighboring subunit. Dissociation of RFC from the
CC clamp leaves the clamp encircling DNA. {ECO:0000269|PubMed:10913172,
CC ECO:0000269|PubMed:11486023, ECO:0000269|PubMed:12604797}.
CC -!- SUBUNIT: Component of the RAD24-RFC complex which consists of RAD14,
CC RFC2, RFC3, RFC4 and RFC5 and associates with the checkpoint clamp
CC DDC1:MEC3:RAD17 complex. RAD24 interacts with ECO1.
CC {ECO:0000269|PubMed:10660302, ECO:0000269|PubMed:10913172,
CC ECO:0000269|PubMed:12604797, ECO:0000269|PubMed:12665596,
CC ECO:0000269|PubMed:15964801}.
CC -!- INTERACTION:
CC P32641; P39009: DUN1; NbExp=2; IntAct=EBI-14675, EBI-6194;
CC P32641; P40348: RFC2; NbExp=5; IntAct=EBI-14675, EBI-14992;
CC P32641; P38629: RFC3; NbExp=5; IntAct=EBI-14675, EBI-15000;
CC P32641; P40339: RFC4; NbExp=2; IntAct=EBI-14675, EBI-15009;
CC P32641; P38251: RFC5; NbExp=4; IntAct=EBI-14675, EBI-15016;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 752 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the rad17/RAD24 family. {ECO:0000305}.
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DR EMBL; U18922; AAB64700.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07835.1; -; Genomic_DNA.
DR PIR; S30859; S30859.
DR RefSeq; NP_011100.1; NM_001179063.1.
DR PDB; 7SGZ; EM; 3.17 A; A=1-659.
DR PDB; 7SH2; EM; 3.23 A; A=1-659.
DR PDB; 7ST9; EM; 2.20 A; A=1-659.
DR PDB; 7STB; EM; 2.72 A; A=1-659.
DR PDB; 7STE; EM; 2.73 A; A=1-659.
DR PDBsum; 7SGZ; -.
DR PDBsum; 7SH2; -.
DR PDBsum; 7ST9; -.
DR PDBsum; 7STB; -.
DR PDBsum; 7STE; -.
DR AlphaFoldDB; P32641; -.
DR BioGRID; 36926; 208.
DR ComplexPortal; CPX-1807; Rad17 RFC-like complex.
DR DIP; DIP-5811N; -.
DR IntAct; P32641; 42.
DR STRING; 4932.YER173W; -.
DR iPTMnet; P32641; -.
DR MaxQB; P32641; -.
DR PaxDb; P32641; -.
DR PRIDE; P32641; -.
DR EnsemblFungi; YER173W_mRNA; YER173W; YER173W.
DR GeneID; 856920; -.
DR KEGG; sce:YER173W; -.
DR SGD; S000000975; RAD24.
DR VEuPathDB; FungiDB:YER173W; -.
DR eggNOG; KOG1970; Eukaryota.
DR GeneTree; ENSGT00440000039046; -.
DR HOGENOM; CLU_027373_0_0_1; -.
DR InParanoid; P32641; -.
DR OMA; ICLTECE; -.
DR BioCyc; YEAST:G3O-30333-MON; -.
DR Reactome; R-SCE-176187; Activation of ATR in response to replication stress.
DR PRO; PR:P32641; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P32641; protein.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0031389; C:Rad17 RFC-like complex; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003689; F:DNA clamp loader activity; IEA:InterPro.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IMP:SGD.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IBA:GO_Central.
DR GO; GO:0006289; P:nucleotide-excision repair; IMP:SGD.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:SGD.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004582; Checkpoint_prot_Rad17_Rad24.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR018324; Rad17/Rad24_fun/met.
DR PANTHER; PTHR12172; PTHR12172; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00602; rad24; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; DNA damage; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..659
FT /note="Checkpoint protein RAD24"
FT /id="PRO_0000209953"
FT REGION 24..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 109..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 654
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 115
FT /note="K->E: Reduces NTP-binding and hydrolysis. Shows DNA
FT damage sensitivity."
FT /evidence="ECO:0000269|PubMed:10913172"
FT MUTAGEN 115
FT /note="K->R: No effect on NTP-binding and hydrolysis.
FT Resistant to DNA damage."
FT /evidence="ECO:0000269|PubMed:10913172"
SQ SEQUENCE 659 AA; 75727 MW; 130FE54875CAA930 CRC64;
MDSTNLNKRP LLQYSLSSLG SQITKWSSSR PTSPVRKARS TENDFLSKQD TSSILPSIND
DGGEQWYEKF KPNCLEQVAI HKRKLKDVQE ALDAMFLPNA KHRILLLSGP SGCSKSTVIK
ELSKILVPKY RQNSNGTSFR STPNEHKVTE FRGDCIVNDL PQMESFSEFL KGARYLVMSN
LSLILIEDLP NVFHIDTRRR FQQLILQWLY SSEPLLPPLV ICITECEIPE NDNNYRKFGI
DYTFSAETIM NKEILMHPRL KRIKFNPINS TLLKKHLKFI CVQNMKMLKE KNKWNKRQEV
IDYIAQETGD IRSAITTLQF WATSSGSLPI STRESTISYF HAIGKVIHGS HSTNNDNEMI
NNLFENSNNL LSKEDFKLGI LENYNTFNKG EFSISDASSI VDCLSECDNM NGLPESNEYG
LREVRKTFRN ISKQGHNHGT VYFPREWKVR KLQNSFKVQA EDWLNVSLYK YNAVHSFRNI
TLEFGYYAPL IRKCQSYKKK YILYYLKNLP SGSSGPKQTM DKFSDIMKVE NGIDVVDRIG
GPIEALSVED GLAPLMDNDS NNCDHLEDQK KERDRRLRML IDQYERNVMM ANDDLEDEET
SFNDDPIVDS DSDNSNNIGN ETFGRSDEDE SLCEILSQRQ PRKAPVISES LSDSDLEIL
