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P53840 (TOF1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Topoisomerase 1-associated factor 1
Gene names
Name:TOF1
Ordered Locus Names:YNL273W
ORF Names:N0636
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1238 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Forms a fork protection complex (FPC) with CSM3 and which is required for chromosome segregation during meiosis and DNA damage repair. FPC coordinates leading and lagging strand synthesis and moves with the replication fork. FPC stabilizes replication forks in a configuration that is recognized by replication checkpoint sensors and protects stalled replication forks against the fork-releasing activity of RRM3 helicase. Ref.4 Ref.5 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15

Subunit structure

Component of the fork protection complex (FPC) consisting of TOF1 and CSM3. Interacts with WSS1 and ESC4. Ref.8 Ref.9 Ref.10 Ref.13

Subcellular location

Nucleus. Note: Associated with chromatin during S phase. Ref.5 Ref.6

Miscellaneous

Present with 952 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the timeless family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CDC45Q080323EBI-28257,EBI-4292
CSM3Q046598EBI-28257,EBI-28093

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12381238Topoisomerase 1-associated factor 1
PRO_0000072620

Amino acid modifications

Modified residue6261Phosphoserine Ref.17
Modified residue6541Phosphoserine Ref.17
Modified residue10561Phosphoserine Ref.18
Modified residue10581Phosphoserine Ref.18
Modified residue12131Phosphoserine Ref.16 Ref.17 Ref.18

Sequences

Sequence LengthMass (Da)Tools
P53840 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: CF8FEC33EE0088E9

FASTA1,238141,120
        10         20         30         40         50         60 
MSADLQQGTT NAADFSLTVL RARIALLATA IGGPDYTSQI DPPPYKLGDD CLACLKDLKR 

        70         80         90        100        110        120 
WFKLVDDQQK RWDVAMAVAE YRILTDDLLP ILIDWENKCS LAAKLAKNNP DHEEFRNKAY 

       130        140        150        160        170        180 
YDKIALNCLQ LLVLMTWPLI VTEQSSSNQI TLYGELKKHQ LVYKKTILSM ESGKVLRAAI 

       190        200        210        220        230        240 
RLALDVIKID RLSRTPRDNM VLKLVLNFFR NVIAIEPGEF TINTKKSMPK KGITSIDTLP 

       250        260        270        280        290        300 
PNVSMDDISL NTVISSFHKN KVFGFLLTLT SSLSKEFDQD FINIPLLEIM FYFTKDVNQE 

       310        320        330        340        350        360 
LLFPRQFETG THSKVVNKNE SSSANNIVTS AGFELSKLLQ KEHQMRKNVI KHTSARHSRF 

       370        380        390        400        410        420 
GGLLSIQTPD KTRLTVSGSQ ALVDEKIALQ KLDDSKKWNK RIIKKHQSVA AEGLPNSLLN 

       430        440        450        460        470        480 
SQTGKAIFFT ESNGKHFKEF INNFIDSGFN ILLHSVTNYF TTEQDRMVTL EQVEYLLFFA 

       490        500        510        520        530        540 
WFVKYQLLRS KIDNSADIKQ VSEALKEVTF ILVSSLLRSA YDLKNWTVTH AGMIAFNELL 

       550        560        570        580        590        600 
NLVSRTKAAQ EEDSTDIEFI VSRLFSDERI QLLSNLPKIG SKYSLQFMKS CIELTHSVLK 

       610        620        630        640        650        660 
VLEQYSDDKT LVIEGKSRRQ KKFNISEGDI TKLIEEENVD RDEALDILTS SLRSIEVNFQ 

       670        680        690        700        710        720 
KVQANYMTEP VIETYINFLE RFRELEDDSI KKVFSFFHRV FVQAKEQALL FRFDLIILLR 

       730        740        750        760        770        780 
EMLSPDGLDR MSRSRKYVSQ FSDYFLARLK KRLKKSPAWF VGLLFPPLHN SEVGFYQRYG 

       790        800        810        820        830        840 
EYNVLNNESM YAAPASQFKP IPDEEALPPS ILLDMKYGVL VSTLLDDGKT ELLDQLLKHI 

       850        860        870        880        890        900 
THTLDIFKSW LTVNVNAGKE TVNPPNEYFT LTGVLNNDPI FKDKDYRALL LLIGYSIPRK 

       910        920        930        940        950        960 
INEPCFLPGT VEVSDLTVSC ELVKKYLSTP FETPNGLPSS SYLLRVRSEK DSFSHNEQDG 

       970        980        990       1000       1010       1020 
WEGDDDYDYN DPYIVPDDQI LSKSDAAYFK DLDNNASDKL KGTKFSKGIA RSKKKDKRKR 

      1030       1040       1050       1060       1070       1080 
RKGEAKTNLP MFGDQDDERP QTVRERHGVF SKEFISDSED DEDLMNPIFF ENETYMRWLL 

      1090       1100       1110       1120       1130       1140 
DKNNGQLTED RYIQFAKFAA ERMNNGGVVT GDYTSLFGGS IPSIESIRAT ESSSFAPDKS 

      1150       1160       1170       1180       1190       1200 
LISLASHVAS EMSIFDVNNN NNNQLSDDDV NSESRNSLGS SQPSNSQNMF QSEVYSRKES 

      1210       1220       1230 
TKRSLEASAA DESDEDEEAI RLFGKKSRVV LSQGDSDD 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. expand/collapse author list , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Identification and characterization of the genes for two topoisomerase I-interacting proteins from Saccharomyces cerevisiae."
Park H., Sternglanz R.
Yeast 15:35-41(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[4]"Tof1p regulates DNA damage responses during S phase in Saccharomyces cerevisiae."
Foss E.J.
Genetics 157:567-577(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"S-phase checkpoint proteins Tof1 and Mrc1 form a stable replication-pausing complex."
Katou Y., Kanoh Y., Bando M., Noguchi H., Tanaka H., Ashikari T., Sugimoto K., Shirahige K.
Nature 424:1078-1083(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]"Identification of protein complexes required for efficient sister chromatid cohesion."
Mayer M.L., Pot I., Chang M., Xu H., Aneliunas V., Kwok T., Newitt R., Aebersold R., Boone C., Brown G.W., Hieter P.
Mol. Biol. Cell 15:1736-1745(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CSM3.
[9]"Coordinated functions of WSS1, PSY2 and TOF1 in the DNA damage response."
O'Neill B.M., Hanway D., Winzeler E.A., Romesberg F.E.
Nucleic Acids Res. 32:6519-6530(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH WSS1.
[10]"Uncoupling of unwinding from DNA synthesis implies regulation of MCM helicase by Tof1/Mrc1/Csm3 checkpoint complex."
Nedelcheva M.N., Roguev A., Dolapchiev L.B., Shevchenko A., Taskov H.B., Shevchenko A., Stewart A.F., Stoynov S.S.
J. Mol. Biol. 347:509-521(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE FPC COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[11]"Mrc1 and Tof1 promote replication fork progression and recovery independently of Rad53."
Tourriere H., Versini G., Cordon-Preciado V., Alabert C., Pasero P.
Mol. Cell 19:699-706(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Disruption of mechanisms that prevent rereplication triggers a DNA damage response."
Archambault V., Ikui A.E., Drapkin B.J., Cross F.R.
Mol. Cell. Biol. 25:6707-6721(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Esc4/Rtt107 and the control of recombination during replication."
Chin J.K., Bashkirov V.I., Heyer W.-D., Romesberg F.E.
DNA Repair 5:618-628(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ESC4.
[14]"Genetic analysis of Saccharomyces cerevisiae H2A serine 129 mutant suggests a functional relationship between H2A and the sister-chromatid cohesion partners Csm3-Tof1 for the repair of topoisomerase I-induced DNA damage."
Redon C., Pilch D.R., Bonner W.M.
Genetics 172:67-76(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE FPC COMPLEX.
[15]"The Tof1p-Csm3p protein complex counteracts the Rrm3p helicase to control replication termination of Saccharomyces cerevisiae."
Mohanty B.K., Bairwa N.K., Bastia D.
Proc. Natl. Acad. Sci. U.S.A. 103:897-902(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE FPC COMPLEX.
[16]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1213, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[17]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626; SER-654 AND SER-1213, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1056; SER-1058 AND SER-1213, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z71549 Genomic DNA. Translation: CAA96181.1.
BK006947 Genomic DNA. Translation: DAA10287.1.
PIRS63247.
RefSeqNP_014126.1. NM_001183111.1.

3D structure databases

ProteinModelPortalP53840.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35567. 206 interactions.
DIPDIP-4272N.
IntActP53840. 8 interactions.
MINTMINT-529011.
STRING4932.YNL273W.

Proteomic databases

PaxDbP53840.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL273W; YNL273W; YNL273W.
GeneID855448.
KEGGsce:YNL273W.

Organism-specific databases

CYGDYNL273w.
SGDS000005217. TOF1.

Phylogenomic databases

eggNOGNOG310534.
HOGENOMHOG000057108.
KOK10997.
OMAGDDCLAC.
OrthoDBEOG7PGF01.

Enzyme and pathway databases

BioCycYEAST:G3O-33267-MONOMER.

Gene expression databases

GenevestigatorP53840.

Family and domain databases

InterProIPR006906. Timeless.
[Graphical view]
PfamPF04821. TIMELESS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio979352.

Entry information

Entry nameTOF1_YEAST
AccessionPrimary (citable) accession number: P53840
Secondary accession number(s): D6W0S1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIV

Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families