TOF1_YEAST
ID TOF1_YEAST Reviewed; 1238 AA.
AC P53840; D6W0S1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Topoisomerase 1-associated factor 1;
GN Name=TOF1; OrderedLocusNames=YNL273W; ORFNames=N0636;
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=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(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 IDENTIFICATION.
RX PubMed=10028183;
RX DOI=10.1002/(sici)1097-0061(19990115)15:1<35::aid-yea340>3.0.co;2-r;
RA Park H., Sternglanz R.;
RT "Identification and characterization of the genes for two topoisomerase I-
RT interacting proteins from Saccharomyces cerevisiae.";
RL Yeast 15:35-41(1999).
RN [4]
RP FUNCTION.
RX PubMed=11156979; DOI=10.1093/genetics/157.2.567;
RA Foss E.J.;
RT "Tof1p regulates DNA damage responses during S phase in Saccharomyces
RT cerevisiae.";
RL Genetics 157:567-577(2001).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12944972; DOI=10.1038/nature01900;
RA Katou Y., Kanoh Y., Bando M., Noguchi H., Tanaka H., Ashikari T.,
RA Sugimoto K., Shirahige K.;
RT "S-phase checkpoint proteins Tof1 and Mrc1 form a stable replication-
RT pausing complex.";
RL Nature 424:1078-1083(2003).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(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 FUNCTION, AND INTERACTION WITH CSM3.
RX PubMed=14742714; DOI=10.1091/mbc.e03-08-0619;
RA Mayer M.L., Pot I., Chang M., Xu H., Aneliunas V., Kwok T., Newitt R.,
RA Aebersold R., Boone C., Brown G.W., Hieter P.;
RT "Identification of protein complexes required for efficient sister
RT chromatid cohesion.";
RL Mol. Biol. Cell 15:1736-1745(2004).
RN [9]
RP FUNCTION, AND INTERACTION WITH WSS1.
RX PubMed=15598824; DOI=10.1093/nar/gkh994;
RA O'Neill B.M., Hanway D., Winzeler E.A., Romesberg F.E.;
RT "Coordinated functions of WSS1, PSY2 and TOF1 in the DNA damage response.";
RL Nucleic Acids Res. 32:6519-6530(2004).
RN [10]
RP FUNCTION, IDENTIFICATION IN THE FPC COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15755447; DOI=10.1016/j.jmb.2005.01.041;
RA Nedelcheva M.N., Roguev A., Dolapchiev L.B., Shevchenko A., Taskov H.B.,
RA Shevchenko A., Stewart A.F., Stoynov S.S.;
RT "Uncoupling of unwinding from DNA synthesis implies regulation of MCM
RT helicase by Tof1/Mrc1/Csm3 checkpoint complex.";
RL J. Mol. Biol. 347:509-521(2005).
RN [11]
RP FUNCTION.
RX PubMed=16137625; DOI=10.1016/j.molcel.2005.07.028;
RA Tourriere H., Versini G., Cordon-Preciado V., Alabert C., Pasero P.;
RT "Mrc1 and Tof1 promote replication fork progression and recovery
RT independently of Rad53.";
RL Mol. Cell 19:699-706(2005).
RN [12]
RP FUNCTION.
RX PubMed=16024805; DOI=10.1128/mcb.25.15.6707-6721.2005;
RA Archambault V., Ikui A.E., Drapkin B.J., Cross F.R.;
RT "Disruption of mechanisms that prevent rereplication triggers a DNA damage
RT response.";
RL Mol. Cell. Biol. 25:6707-6721(2005).
RN [13]
RP INTERACTION WITH ESC4.
RX PubMed=16569515; DOI=10.1016/j.dnarep.2006.02.005;
RA Chin J.K., Bashkirov V.I., Heyer W.-D., Romesberg F.E.;
RT "Esc4/Rtt107 and the control of recombination during replication.";
RL DNA Repair 5:618-628(2006).
RN [14]
RP FUNCTION OF THE FPC COMPLEX.
RX PubMed=16219777; DOI=10.1534/genetics.105.046128;
RA Redon C., Pilch D.R., Bonner W.M.;
RT "Genetic analysis of Saccharomyces cerevisiae H2A serine 129 mutant
RT suggests a functional relationship between H2A and the sister-chromatid
RT cohesion partners Csm3-Tof1 for the repair of topoisomerase I-induced DNA
RT damage.";
RL Genetics 172:67-76(2006).
RN [15]
RP FUNCTION OF THE FPC COMPLEX.
RX PubMed=16418273; DOI=10.1073/pnas.0506540103;
RA Mohanty B.K., Bairwa N.K., Bastia D.;
RT "The Tof1p-Csm3p protein complex counteracts the Rrm3p helicase to control
RT replication termination of Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:897-902(2006).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1213, AND IDENTIFICATION BY
RP 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626; SER-654 AND SER-1213,
RP AND 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1056; SER-1058 AND SER-1213,
RP AND 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).
CC -!- FUNCTION: Forms a fork protection complex (FPC) with CSM3 and which is
CC required for chromosome segregation during meiosis and DNA damage
CC repair. FPC coordinates leading and lagging strand synthesis and moves
CC with the replication fork. FPC stabilizes replication forks in a
CC configuration that is recognized by replication checkpoint sensors and
CC protects stalled replication forks against the fork-releasing activity
CC of RRM3 helicase. {ECO:0000269|PubMed:11156979,
CC ECO:0000269|PubMed:12944972, ECO:0000269|PubMed:14742714,
CC ECO:0000269|PubMed:15598824, ECO:0000269|PubMed:15755447,
CC ECO:0000269|PubMed:16024805, ECO:0000269|PubMed:16137625,
CC ECO:0000269|PubMed:16219777, ECO:0000269|PubMed:16418273}.
CC -!- SUBUNIT: Component of the fork protection complex (FPC) consisting of
CC TOF1 and CSM3. Interacts with WSS1 and ESC4.
CC {ECO:0000269|PubMed:14742714, ECO:0000269|PubMed:15598824,
CC ECO:0000269|PubMed:15755447, ECO:0000269|PubMed:16569515}.
CC -!- INTERACTION:
CC P53840; Q08032: CDC45; NbExp=3; IntAct=EBI-28257, EBI-4292;
CC P53840; Q04659: CSM3; NbExp=7; IntAct=EBI-28257, EBI-28093;
CC P53840; P25588: MRC1; NbExp=4; IntAct=EBI-28257, EBI-412442;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12944972,
CC ECO:0000269|PubMed:14562095}. Note=Associated with chromatin during S
CC phase.
CC -!- MISCELLANEOUS: Present with 952 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the timeless family. {ECO:0000305}.
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DR EMBL; Z71549; CAA96181.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10287.1; -; Genomic_DNA.
DR PIR; S63247; S63247.
DR RefSeq; NP_014126.1; NM_001183111.1.
DR PDB; 6SKL; EM; 3.70 A; X=1-1238.
DR PDB; 7PMK; EM; 3.20 A; X=1-1238.
DR PDB; 7PMN; EM; 3.20 A; X=1-1238.
DR PDBsum; 6SKL; -.
DR PDBsum; 7PMK; -.
DR PDBsum; 7PMN; -.
DR AlphaFoldDB; P53840; -.
DR SMR; P53840; -.
DR BioGRID; 35567; 320.
DR ComplexPortal; CPX-1673; Replication fork protection complex.
DR DIP; DIP-4272N; -.
DR IntAct; P53840; 8.
DR MINT; P53840; -.
DR STRING; 4932.YNL273W; -.
DR iPTMnet; P53840; -.
DR MaxQB; P53840; -.
DR PaxDb; P53840; -.
DR PRIDE; P53840; -.
DR EnsemblFungi; YNL273W_mRNA; YNL273W; YNL273W.
DR GeneID; 855448; -.
DR KEGG; sce:YNL273W; -.
DR SGD; S000005217; TOF1.
DR VEuPathDB; FungiDB:YNL273W; -.
DR eggNOG; KOG1974; Eukaryota.
DR GeneTree; ENSGT00390000015124; -.
DR HOGENOM; CLU_008440_0_0_1; -.
DR InParanoid; P53840; -.
DR OMA; WLKLYDE; -.
DR BioCyc; YEAST:G3O-33267-MON; -.
DR PRO; PR:P53840; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53840; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0043596; C:nuclear replication fork; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0031298; C:replication fork protection complex; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IDA:ComplexPortal.
DR GO; GO:0006260; P:DNA replication; IMP:SGD.
DR GO; GO:0000076; P:DNA replication checkpoint signaling; IMP:SGD.
DR GO; GO:0043570; P:maintenance of DNA repeat elements; IMP:SGD.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:SGD.
DR GO; GO:0043111; P:replication fork arrest; IMP:SGD.
DR GO; GO:0048478; P:replication fork protection; IDA:ComplexPortal.
DR InterPro; IPR044998; Timeless.
DR InterPro; IPR006906; Timeless_N.
DR PANTHER; PTHR22940; PTHR22940; 1.
DR Pfam; PF04821; TIMELESS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; DNA damage; DNA repair;
KW DNA replication inhibitor; Meiosis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1238
FT /note="Topoisomerase 1-associated factor 1"
FT /id="PRO_0000072620"
FT REGION 1008..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1022
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1051
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 654
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 1056
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1058
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT HELIX 14..31
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 51..64
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 65..70
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 88..103
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 118..135
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 147..169
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 174..187
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 196..214
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 250..259
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 262..271
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 283..294
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 330..351
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 385..394
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 418..420
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 431..447
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 449..460
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 464..466
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 469..492
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 498..505
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 507..522
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 526..549
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 557..564
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 568..579
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 580..582
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 585..605
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 659..666
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 669..679
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 680..684
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 687..702
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 707..710
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 713..723
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 733..755
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 759..762
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 771..779
FT /evidence="ECO:0007829|PDB:7PMK"
SQ SEQUENCE 1238 AA; 141120 MW; CF8FEC33EE0088E9 CRC64;
MSADLQQGTT NAADFSLTVL RARIALLATA IGGPDYTSQI DPPPYKLGDD CLACLKDLKR
WFKLVDDQQK RWDVAMAVAE YRILTDDLLP ILIDWENKCS LAAKLAKNNP DHEEFRNKAY
YDKIALNCLQ LLVLMTWPLI VTEQSSSNQI TLYGELKKHQ LVYKKTILSM ESGKVLRAAI
RLALDVIKID RLSRTPRDNM VLKLVLNFFR NVIAIEPGEF TINTKKSMPK KGITSIDTLP
PNVSMDDISL NTVISSFHKN KVFGFLLTLT SSLSKEFDQD FINIPLLEIM FYFTKDVNQE
LLFPRQFETG THSKVVNKNE SSSANNIVTS AGFELSKLLQ KEHQMRKNVI KHTSARHSRF
GGLLSIQTPD KTRLTVSGSQ ALVDEKIALQ KLDDSKKWNK RIIKKHQSVA AEGLPNSLLN
SQTGKAIFFT ESNGKHFKEF INNFIDSGFN ILLHSVTNYF TTEQDRMVTL EQVEYLLFFA
WFVKYQLLRS KIDNSADIKQ VSEALKEVTF ILVSSLLRSA YDLKNWTVTH AGMIAFNELL
NLVSRTKAAQ EEDSTDIEFI VSRLFSDERI QLLSNLPKIG SKYSLQFMKS CIELTHSVLK
VLEQYSDDKT LVIEGKSRRQ KKFNISEGDI TKLIEEENVD RDEALDILTS SLRSIEVNFQ
KVQANYMTEP VIETYINFLE RFRELEDDSI KKVFSFFHRV FVQAKEQALL FRFDLIILLR
EMLSPDGLDR MSRSRKYVSQ FSDYFLARLK KRLKKSPAWF VGLLFPPLHN SEVGFYQRYG
EYNVLNNESM YAAPASQFKP IPDEEALPPS ILLDMKYGVL VSTLLDDGKT ELLDQLLKHI
THTLDIFKSW LTVNVNAGKE TVNPPNEYFT LTGVLNNDPI FKDKDYRALL LLIGYSIPRK
INEPCFLPGT VEVSDLTVSC ELVKKYLSTP FETPNGLPSS SYLLRVRSEK DSFSHNEQDG
WEGDDDYDYN DPYIVPDDQI LSKSDAAYFK DLDNNASDKL KGTKFSKGIA RSKKKDKRKR
RKGEAKTNLP MFGDQDDERP QTVRERHGVF SKEFISDSED DEDLMNPIFF ENETYMRWLL
DKNNGQLTED RYIQFAKFAA ERMNNGGVVT GDYTSLFGGS IPSIESIRAT ESSSFAPDKS
LISLASHVAS EMSIFDVNNN NNNQLSDDDV NSESRNSLGS SQPSNSQNMF QSEVYSRKES
TKRSLEASAA DESDEDEEAI RLFGKKSRVV LSQGDSDD
