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P48581 (RAD17_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
DNA damage checkpoint control protein RAD17
Alternative name(s):
DNA repair exonuclease RAD17
Gene names
Name:RAD17
Ordered Locus Names:YOR368W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length401 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the checkpoint clamp complex involved in the surveillance mechanism that allows the DNA repair pathways to act to restore the integrity of the DNA prior to DNA synthesis or separation of the replicated chromosomes. Associates with sites of DNA damage and modulates the MEC1 signaling pathway and the activation of RAD53 in response to DNA damage at phase G1. The complex also physically regulates DNA polymerase zeta-dependent mutagenesis by controlling the access of polymerase zeta to damaged DNA. Contrary to its human counterpart, the 9-1-1 complex, the checkpoint clamp complex shows no detectable exonuclease activity. Ref.1 Ref.2 Ref.5 Ref.6 Ref.7 Ref.8 Ref.11 Ref.12

Subunit structure

Component of the checkpoint clamp complex composed of DDC1, MEC3 and RAD17. The interaction with MEC3 is performed in a RAD17-dependent manner. The checkpoint clamp complex loads onto DNA. Interacts with the DNA polymerase zeta subunit REV7. 2 RAD17 subunits form also an hetero trimer with one MEC3 subunit. Ref.6 Ref.10 Ref.12 Ref.13

Subcellular location

Nucleus Potential.

Miscellaneous

Present with 189 molecules/cell in log phase SD medium. Ref.9

Sequence similarities

Belongs to the rad1 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DDC1Q089494EBI-14652,EBI-30769
MEC3Q025749EBI-14652,EBI-10658

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 401401DNA damage checkpoint control protein RAD17
PRO_0000097150

Amino acid modifications

Modified residue51Phosphoserine Ref.16
Modified residue3571Phosphoserine Ref.15 Ref.16
Modified residue3831Phosphoserine Ref.14

Experimental info

Mutagenesis1281E → K in RAD17-1; UV-sensitive. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P48581 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: BFF7074676C483C9

FASTA40145,580
        10         20         30         40         50         60 
MRINSELANK FSASTVHLEH ITTALSCLTP FGSKDDVLIF IDADGLSFVR ENNHVIKIQL 

        70         80         90        100        110        120 
LLSRELFMSY SYRNETEDHM KLCVKINHIL DSVSVMNRNS DDIVECTLSY DGHGSPFVLI 

       130        140        150        160        170        180 
FEDSFISERV EYSTYLIKDF DTNGLELDRE RISFEAIIKG EALHSALKDL KEIGCKECYV 

       190        200        210        220        230        240 
YAKTEANDEN VFALISKSQL GFSKIKLPSN RSILEKLQVF DGDSTTVIDG FAVIGFFDFT 

       250        260        270        280        290        300 
SFDKIRKSTK IASKVLFRMD VHGVLSVNIL SQTDDVIITD TTRPSNNRPG SIRQLQLPKD 

       310        320        330        340        350        360 
YPGIVIEVCM LEKESIDEAA QTEIELLMET NELGNRNSFK KSTIRKRYGT DKGNETSNDN 

       370        380        390        400 
LLQLNGKKIK LPSEEENNKN RESEDEENHC KYPTKDIPIF F 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of RAD17, a gene controlling cell cycle responses to DNA damage in Saccharomyces cerevisiae."
Siede W., Nusspaumer G., Portillo V., Rodriguez R., Friedberg E.C.
Nucleic Acids Res. 24:1669-1675(1996) [PubMed: 8649984] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF GLU-128.
[2]"Yeast checkpoint genes in DNA damage processing: implications for repair and arrest."
Lydall D., Weinert T.A.
Science 270:1488-1491(1995) [PubMed: 7491494] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
Nature 387:98-102(1997) [PubMed: 9169874] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"A dominant-negative MEC3 mutant uncovers new functions for the Rad17 complex and Tel1."
Giannattasio M., Sommariva E., Vercillo R., Lippi-Boncambi F., Liberi G., Foiani M., Plevani P., Muzi-Falconi M.
Proc. Natl. Acad. Sci. U.S.A. 99:12997-13002(2002) [PubMed: 12271137] [Abstract]
Cited for: FUNCTION OF THE CHECKPOINT CLAMP COMPLEX.
[6]"Yeast Rad17/Mec3/Ddc1: a sliding clamp for the DNA damage checkpoint."
Majka J., Burgers P.M.J.
Proc. Natl. Acad. Sci. U.S.A. 100:2249-2254(2003) [PubMed: 12604797] [Abstract]
Cited for: INTERACTION OF THE CHECKPOINT CLAMP COMPLEX WITH THE RFC-RAD24 CHECKPOINT CLAMP LOADER COMPLEX, FUNCTION OF THE CHECKPOINT CLAMP COMPLEX, LACK OF EXONUCLEASE ACTIVITY.
[7]"Role of a complex containing Rad17, Mec3, and Ddc1 in the yeast DNA damage checkpoint pathway."
Kondo T., Matsumoto K., Sugimoto K.
Mol. Cell. Biol. 19:1136-1143(1999) [PubMed: 9891048] [Abstract]
Cited for: IDENTIFICATION IN THE CHECKPOINT CLAMP COMPLEX, FUNCTION OF THE CHECKPOINT CLAMP COMPLEX.
[8]"Correlation between checkpoint activation and in vivo assembly of the yeast checkpoint complex Rad17-Mec3-Ddc1."
Giannattasio M., Sabbioneda S., Minuzzo M., Plevani P., Muzi-Falconi M.
J. Biol. Chem. 278:22303-22308(2003) [PubMed: 12672803] [Abstract]
Cited for: IDENTIFICATION IN THE CHECKPOINT CLAMP COMPLEX, FUNCTION OF THE CHECKPOINT CLAMP COMPLEX.
[9]"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: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]"Requirement for ATP by the DNA damage checkpoint clamp loader."
Majka J., Chung B.Y., Burgers P.M.J.
J. Biol. Chem. 279:20921-20926(2004) [PubMed: 15014082] [Abstract]
Cited for: INTERACTION OF THE CHECKPOINT CLAMP COMPLEX WITH THE RFC-RAD24 CHECKPOINT CLAMP LOADER COMPLEX.
[11]"Function of Rad17/Mec3/Ddc1 and its partial complexes in the DNA damage checkpoint."
Majka J., Burgers P.M.J.
DNA Repair 4:1189-1194(2005) [PubMed: 16137930] [Abstract]
Cited for: IDENTIFICATION IN THE CHECKPOINT CLAMP COMPLEX, FUNCTION OF THE CHECKPOINT CLAMP COMPLEX.
[12]"The 9-1-1 checkpoint clamp physically interacts with polzeta and is partially required for spontaneous polzeta-dependent mutagenesis in Saccharomyces cerevisiae."
Sabbioneda S., Minesinger B.K., Giannattasio M., Plevani P., Muzi-Falconi M., Jinks-Robertson S.
J. Biol. Chem. 280:38657-38665(2005) [PubMed: 16169844] [Abstract]
Cited for: INTERACTION WITH REV7, FUNCTION OF THE CHECKPOINT CLAMP COMPLEX.
[13]"Psoralen-sensitive mutant pso9-1 of Saccharomyces cerevisiae contains a mutant allele of the DNA damage checkpoint gene MEC3."
Cardone J.M., Revers L.F., Machado R.M., Bonatto D., Brendel M., Henriques J.A.P.
DNA Repair 5:163-171(2006) [PubMed: 16202664] [Abstract]
Cited for: INTERACTION WITH DDC1 AND MEC3.
[14]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, MASS SPECTROMETRY.
[15]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, MASS SPECTROMETRY.
[16]"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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5 AND SER-357, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U37460 Genomic DNA. Translation: AAA80545.1.
U30796 Genomic DNA. Translation: AAA93250.1.
Z75276 Genomic DNA. Translation: CAA99699.1.
BK006948 Genomic DNA. Translation: DAA11127.1.
PIRS59670.
RefSeqNP_015013.1. NM_001183788.1.

3D structure databases

ProteinModelPortalP48581.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-1546N.
IntActP48581. 9 interactions.
MINTMINT-408918.
STRINGP48581.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOR368W; YOR368W; YOR368W.
GeneID854550.
KEGGsce:YOR368W.
NMPDRfig|4932.3.peg.6132.

Organism-specific databases

CYGDYOR368w.
SGDS000005895. RAD17.

Phylogenomic databases

eggNOGfuNOG04822.
HOGENOMHBG202934.
OMAEIGCKEC.
OrthoDBEOG4NW2VQ.

Gene expression databases

ArrayExpressP48581.
GenevestigatorP48581.
GermOnlineYOR368W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR016587. Cell_cycle_RAD17.
IPR003021. Rad1_Rec1.
[Graphical view]
KOK02830.
PANTHERPTHR10870. Rad1_Rec1. 1 hit.
PfamPF02144. Rad1. 1 hit.
[Graphical view]
PIRSFPIRSF011769. Cell_cycle_RAD17. 1 hit.
PRINTSPR01245. RAD1REC1.
ProtoNetSearch...

Other

NextBio976967.

Entry information

Entry nameRAD17_YEAST
AccessionPrimary (citable) accession number: P48581
Secondary accession number(s): D6W361
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: December 14, 2011
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

SIMILARITY comments

Index of protein domains and families