DNA damage checkpoint control protein RAD17 - Saccharomyces cerevisiae (Baker's yeast)

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P48581 (RAD17_YEAST)

Last modified January 19, 2010. Version 77. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
    DNA damage checkpoint control protein RAD17
    EC=3.1.11.2
Alternative name(s):
    DNA repair exonuclease RAD17

Gene names

Name:	RAD17
Ordered Locus Names:	YOR368W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Hide | Top

Protein attributes

Sequence length	401 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Function	Exonuclease 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. Ref.1 Ref.2 Ref.4 Ref.5 Ref.6 Ref.7 Ref.10 Ref.11
Catalytic activity	Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
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.5 Ref.11 Ref.9 Ref.12
Subcellular location	Nucleus Potential.
Miscellaneous	Present with 189 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Belongs to the rad1 family.

Hide | Top

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Ligand	DNA-binding
Molecular function	Exonuclease Hydrolase Nuclease
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	DNA damage checkpoint Inferred from mutant phenotype. Source: SGD double-strand break repair Inferred from mutant phenotype. Source: SGD reciprocal meiotic recombination Inferred from mutant phenotype. Source: SGD
Cellular component	checkpoint clamp complex Ref.5 Ref.6 Inferred from direct assay. Source: SGD
Molecular function	damaged DNA binding Inferred from electronic annotation. Source: InterPro double-stranded DNA binding Ref.5 Inferred from direct assay. Source: SGD exodeoxyribonuclease III activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Hide | Top

Binary interactions

With	Entry	#Exp.	IntAct
DBP5	P20449	1	EBI-14652,EBI-5617
DDC1	Q08949	2	EBI-14652,EBI-30769
MEC3	Q02574	4	EBI-14652,EBI-10658
UBI1	P61864	1	EBI-14652,EBI-19797

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 401

401

DNA damage checkpoint control protein RAD17

PRO_0000097150

Amino acid modifications

Modified residue

Phosphoserine Ref.15

Modified residue

357

Phosphoserine Ref.15 Ref.14

Modified residue

383

Phosphoserine Ref.13

Experimental info

Mutagenesis

128

E → K in RAD17-1; UV-sensitive. Ref.1

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P48581-1 [UniParc].

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

FASTA

401

45,580

        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

Hide | Top

References

	« Hide 'large scale' referencesShow '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. Kleine K. Nature 387:98-102(1997) [PubMed: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	"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.
[5]	"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.
[6]	"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.
[7]	"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.
[8]	"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].
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.

Hide | Top

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.
PIR	S59670.
RefSeq	NP_015013.1.
3D structure databases
SMR	P48581. Positions 11-267.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1546N.
IntAct	P48581. 10 interactions.
STRING	P48581.
Genome annotation databases
Ensembl	YOR368W; YOR368W; YOR368W; Saccharomyces cerevisiae. [Genome view]
GeneID	854550.
KEGG	sce:YOR368W.
NMPDR	fig\|4932.3.peg.6132.
Organism-specific databases
CYGD	YOR368w.
SGD	S000005895. RAD17.
Phylogenomic databases
eggNOG	fuNOG04822.
HOGENOM	HBG202934.
OMA	HLEHITT.
OrthoDB	EOG9B5QNJ.
PhylomeDB	P48581.
Enzyme and pathway databases
BRENDA	3.1.11.2. 250.
Gene expression databases
ArrayExpress	P48581.
Genevestigator	P48581.
GermOnline	YOR368W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR016587. Cell_cycle_RAD17. IPR003021. Rad1_Rec1. [Graphical view]
PANTHER	PTHR10870. Rad1_Rec1. 1 hit.
Pfam	PF02144. Rad1. 1 hit. [Graphical view]
PIRSF	PIRSF011769. Cell_cycle_RAD17. 1 hit.
PRINTS	PR01245. RAD1REC1.
ProtoNet	Search...
Other Resources
NextBio	976967.

Hide | Top

Entry information

Entry name

RAD17_YEAST

Accession

Primary (citable) accession number: P48581

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	January 19, 2010
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

Hide | Top

Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents