DNA repair protein RAD2 - RAD2 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P07276 (RAD2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 148. History...

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

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
DNA repair protein RAD2
EC=3.1.-.-

Gene names

Name:	RAD2
Ordered Locus Names:	YGR258C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1031 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Single-stranded DNA endonuclease involved in excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents. Essential for the incision step of excision-repair. Ref.7
Cofactor	Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding By similarity.
Subcellular location	Nucleus.
Miscellaneous	Present with 846 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the XPG/RAD2 endonuclease family. XPG subfamily.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Ligand	Magnesium Metal-binding
Molecular function	Endonuclease Hydrolase Nuclease
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA catabolic process, endonucleolytic Inferred from direct assay Ref.7. Source: GOC nucleotide-excision repair, DNA incision, 3'-to lesion Inferred from direct assay PubMed 7926735. Source: SGD transcription from RNA polymerase II promoter Inferred from genetic interaction PubMed 12110180. Source: SGD
Cellular_component	nucleotide-excision repair factor 3 complex Inferred from direct assay PubMed 8855246. Source: SGD
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction PubMed 15121901. Source: IntAct single-stranded DNA binding Inferred from electronic annotation. Source: InterPro single-stranded DNA endodeoxyribonuclease activity Inferred from direct assay Ref.7. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SEN1	Q00416	3	EBI-14757,EBI-16945

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1031

1031

DNA repair protein RAD2

PRO_0000154035

Regions

Region

1 – 95

N-domain

Region

756 – 884

129

I-domain

Sites

Metal binding

Magnesium 1 By similarity

Metal binding

Magnesium 1 By similarity

Metal binding

792

Magnesium 1 By similarity

Metal binding

794

Magnesium 1 By similarity

Metal binding

813

Magnesium 2 By similarity

Metal binding

815

Magnesium 2 By similarity

Metal binding

864

Magnesium 2 By similarity

Amino acid modifications

Modified residue

118

Phosphoserine Ref.10

Modified residue

367

Phosphoserine Ref.10

Modified residue

583

Phosphoserine Ref.9

Experimental info

Sequence conflict

782

F → L in AAT92876. Ref.5

Secondary structure

1031

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P07276 [UniParc].

Last modified November 1, 1991. Version 2.
Checksum: 682D4AECFBD7F0F3
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FASTA

1,031

117,838

        10         20         30         40         50         60 
MGVHSFWDIA GPTARPVRLE SLEDKRMAVD ASIWIYQFLK AVRDQEGNAV KNSHITGFFR 

        70         80         90        100        110        120 
RICKLLYFGI RPVFVFDGGV PVLKRETIRQ RKERRQGKRE SAKSTARKLL ALQLQNGSND 

       130        140        150        160        170        180 
NVKNSTPSSG SSVQIFKPQD EWDLPDIPGF KYDKEDARVN SNKTFEKLMN SINGDGLEDI 

       190        200        210        220        230        240 
DLDTINPASA EFEELPKATQ YLILSSLRLK SRLRMGYSKE QLETIFPNSM DFSRFQIDMV 

       250        260        270        280        290        300 
KRRNFFTQKL INTTGFQDGG ASKLNEEVIN RISGQKSKEY KLTKTNNGWI LGLGANDGSD 

       310        320        330        340        350        360 
AQKAIVIDDK DAGALVKQLD SNAEDGDVLR WDDLEDNSLK IVRHESSNAT TAPQKRSNRS 

       370        380        390        400        410        420 
EDEGCDSDEC EWEEVELKPK NVKFVEDFSL KAARLPYMGQ SLNNAGSKSF LDKRHDQASP 

       430        440        450        460        470        480 
SKTTPTMRIS RISVEDDDED YLKQIEEIEM MEAVQLSKME KKPEADDKSK IAKPVTSKGT 

       490        500        510        520        530        540 
EARPPIVQYG LLGAQPDSKQ PYHVTNLNSK SESVIKRTSK TVLSEFRPPS QQEDKGAILT 

       550        560        570        580        590        600 
EGEQNLNFIS HKIPQFDFNN ENSLLFQKNT ESNVSQEATK EKSPIPEMPS WFSSTASQQL 

       610        620        630        640        650        660 
YNPYNTTNFV EDKNVRNEQE SGAETTNKGS SYELLTGLNA TEILERESEK ESSNDENKDD 

       670        680        690        700        710        720 
DLEVLSEELF EDVPTKSQIS KEAEDNDSRK VESINKEHRK PLIFDYDFSE DEEDNIVENM 

       730        740        750        760        770        780 
IKEQEEFDTF KNTTLSTSAE RNVAENAFVE DELFEQQMKD KRDSDEVTMD MIKEVQELLS 

       790        800        810        820        830        840 
RFGIPYITAP MEAEAQCAEL LQLNLVDGII TDDSDVFLFG GTKIYKNMFH EKNYVEFYDA 

       850        860        870        880        890        900 
ESILKLLGLD RKNMIELAQL LGSDYTNGLK GMGPVSSIEV IAEFGNLKNF KDWYNNGQFD 

       910        920        930        940        950        960 
KRKQETENKF EKDLRKKLVN NEIILDDDFP SVMVYDAYMR PEVDHDTTPF VWGVPDLDML 

       970        980        990       1000       1010       1020 
RSFMKTQLGW PHEKSDEILI PLIRDVNKRK KKGKQKRINE FFPREYISGD KKLNTSKRIS 

      1030 
TATGKLKKRK M

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The RAD2 gene of Saccharomyces cerevisiae: nucleotide sequence and transcript mapping." Nicolet C.M., Chenevert J.M., Friedberg E.C. Gene 36:225-234(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Nucleotide sequence, transcript mapping, and regulation of the RAD2 gene of Saccharomyces cerevisiae." Madura K., Prakash S. J. Bacteriol. 166:914-923(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. Kleine K. Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"The reference genome sequence of Saccharomyces cerevisiae: Then and now." Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M. G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	"Analysis of an 11.6 kb region from the right arm of chromosome VII of Saccharomyces cerevisiae between the RAD2 and the MES1 genes reveals the presence of three new genes." Clemente M.L., Sartori G., Cardazzo B., Carignani G. Yeast 13:287-290(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-51. Strain: ATCC 96604 / S288c / FY1679.
[7]	"Yeast excision repair gene RAD2 encodes a single-stranded DNA endonuclease." Habraken Y., Sung P., Prakash L., Prakash S. Nature 366:365-368(1993) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[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] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"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-583, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"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-118 AND SER-367, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M10275 Genomic DNA. Translation: AAA66928.1.
Y07777 Genomic DNA. Translation: CAA69080.1.
Z73043 Genomic DNA. Translation: CAA97287.1.
BK006941 Genomic DNA. Translation: DAA08349.1.
AY692857 Genomic DNA. Translation: AAT92876.1.

PIR

A29839.

RefSeq

NP_011774.1. NM_001181387.1.

3D structure databases

PDBe
RCSB-PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2LOX	NMR	-	B	642-690	[»]

ProteinModelPortal

P07276.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

33510. 45 interactions.

DIP

DIP-5869N.

IntAct

P07276. 1 interaction.

MINT

MINT-683829.

STRING

4932.YGR258C.

Proteomic databases

MaxQB

P07276.

PaxDb

P07276.

PeptideAtlas

P07276.

PRIDE

P07276.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YGR258C; YGR258C; YGR258C.

GeneID

853174.

KEGG

sce:YGR258C.

Organism-specific databases

CYGD

YGR258c.

SGD

S000003490. RAD2.

Phylogenomic databases

eggNOG

COG0258.

GeneTree

ENSGT00640000091542.

HOGENOM

HOG000214817.

K10846.

OMA

FQATMRD.

OrthoDB

EOG7QK0MK.

Enzyme and pathway databases

BioCyc

YEAST:G3O-30928-MONOMER.

Gene expression databases

Genevestigator

P07276.

Family and domain databases

Gene3D

3.40.50.1010. 2 hits.

InterPro

IPR020045. 5-3_exonuclease_C.
IPR008918. HhH2.
IPR029060. PIN_domain-like.
IPR006086. XPG-I_dom.
IPR001044. XPG/Rad2_eukaryotes.
IPR019974. XPG_CS.
IPR006085. XPG_DNA_repair_N.
[Graphical view]

PANTHER

PTHR11081:SF1. PTHR11081:SF1. 1 hit.

Pfam

PF00867. XPG_I. 1 hit.
PF00752. XPG_N. 1 hit.
[Graphical view]

PRINTS

PR00066. XRODRMPGMNTG.

SMART

SM00279. HhH2. 1 hit.
SM00484. XPGI. 1 hit.
SM00485. XPGN. 1 hit.
[Graphical view]

SUPFAM

SSF47807. SSF47807. 2 hits.
SSF88723. SSF88723. 2 hits.

TIGRFAMs

TIGR00600. rad2. 1 hit.

PROSITE

PS00841. XPG_1. 1 hit.
PS00842. XPG_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

973302.

PRO

P07276.

Entry information

Entry name

RAD2_YEAST

Accession

Primary (citable) accession number: P07276
Secondary accession number(s): D6VV38, E9P8X9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	November 1, 1991
Last modified:	June 11, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents