DNA repair protein RAD5 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P32849 (RAD5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 118. History...

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

Documents (3) |

Third-party data

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

Names and origin

Protein names

Recommended name:
DNA repair protein RAD5
EC=3.6.4.-

Alternative name(s):
Radiation sensitivity protein 5
Revertibility protein 2

Gene names

Name:	RAD5
Synonyms:	REV2, SNM2
Ordered Locus Names:	YLR032W

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	1169 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probable helicase, member of the UBC2/RAD6 epistasis group. Functions with the DNA repair protein RAD18 in error-free postreplication DNA repair. Involved in the maintenance of wild-type rates of instability of simple repetitive sequences such as poly(GT) repeats. Seems to be involved in maintaining a balance which acts in favor of error-prone non-homologous joining during DNA double-strand breaks repairs. Recruits the UBC13-MMS2 dimer to chromatin for DNA repair. Ref.1 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14
Cofactor	Magnesium, manganese or calcium.
Subunit structure	Homodimer. Interacts with POL30, RAD18, UBC9 and UBC13. Ref.7 Ref.10 Ref.11 Ref.14
Subcellular location	Cytoplasm. Nucleus Ref.7 Ref.12.
Miscellaneous	Present with 1520 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the SNF2/RAD54 helicase family. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain. Contains 1 RING-type zinc finger.
Biophysicochemical properties	Kinetic parameters: K_M=525 µM for ATP pH dependence: Optimum pH is 7.0. for ATPase activity.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Cytoplasm Nucleus
Domain	Zinc-finger
Ligand	ATP-binding DNA-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Helicase Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	double-strand break repair Inferred from mutant phenotype Ref.14. Source: SGD error-prone translesion synthesis Inferred from mutant phenotype PubMed 23142547. Source: SGD free ubiquitin chain polymerization Inferred from direct assay PubMed 19706603. Source: SGD protein polyubiquitination Inferred from direct assay PubMed 19706603. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay PubMed 22842922. Source: SGD nuclear chromatin Inferred from direct assay Ref.7. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA-dependent ATPase activity Inferred from direct assay PubMed 17936713. Source: SGD Y-form DNA binding Inferred from direct assay PubMed 17936713. Source: SGD four-way junction DNA binding Inferred from direct assay PubMed 17936713. Source: SGD four-way junction helicase activity Inferred from direct assay PubMed 17936713. Source: SGD zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1169

1169

DNA repair protein RAD5

PRO_0000056130

Regions

Domain

519 – 730

212

Helicase ATP-binding

Domain

995 – 1165

171

Helicase C-terminal

Nucleotide binding

532 – 539

ATP Potential

Zinc finger

914 – 961

RING-type

Motif

681 – 684

DEGH box

Compositional bias

42 – 60

Asp/Glu-rich (acidic)

Compositional bias

303 – 315

Arg/Lys-rich (basic)

Amino acid modifications

Modified residue

Phosphoserine Ref.15

Modified residue

129

Phosphoserine Ref.15

Modified residue

130

Phosphoserine Ref.15

Experimental info

Mutagenesis

538 – 539

KT → AA: Increased sensitivity toward ionizing radiation. Ref.14

Mutagenesis

914

C → S: Abolishes interaction with UBC13. Ref.7 Ref.11 Ref.14

Mutagenesis

916

I → A: Abolishes interaction with UBC13. Ref.11 Ref.14

Mutagenesis

944

Y → A: Abolishes interaction with UBC13. Ref.11 Ref.14

Mutagenesis

959

N → A: Abolishes interaction with UBC13. Ref.11 Ref.14

Sequence conflict

478

Q → R in AAB23590. Ref.4

Sequence conflict

635

T → N in AAB23590. Ref.4

Sequence conflict

846

G → S in AAB23590. Ref.4

Sequence conflict

898

R → S in AAB23590. Ref.4

Sequence conflict

973

V → A in AAB23590. Ref.4

Sequence conflict

1063

A → R in AAB23590. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

P32849 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 226B720097433EE2
Show »

FASTA

1,169

134,002

        10         20         30         40         50         60 
MSHIEQEERK RFFNDDLDTS ETSLNFKSEN KESFLFANSH NDDDDDVVVS VSDTTEGEGD 

        70         80         90        100        110        120 
RSIVPVRREI EEEGQNQFIT ELLRIIPEMP KDLVMELNEK FGSQEEGLSL ALSHYFDHNS 

       130        140        150        160        170        180 
GTSISKIPSS PNQLNTLSDT SNSTLSPSSF HPKRRRIYGF RNQTRLEDKV TWKRFIGALQ 

       190        200        210        220        230        240 
VTGMATRPTV RPLKYGSQMK LKRSSEEISA TKVYDSRGRK KASMASLVRI FDIQYDREIG 

       250        260        270        280        290        300 
RVSEDIAQIL YPLLSSHEIS FEVTLIFCDN KRLSIGDSFI LQLDCFLTSL IFEERNDGES 

       310        320        330        340        350        360 
LMKRRRTEGG NKREKDNGNF GRTLTETDEE LESRSKRLAL LKLFDKLRLK PILDEQKALE 

       370        380        390        400        410        420 
KHKIELNSDP EIIDLDNDEI CSNQVTEVHN NLRDTQHEEE TMNLNQLKTF YKAAQSSESL 

       430        440        450        460        470        480 
KSLPETEPSR DVFKLELRNY QKQGLTWMLR REQEFAKAAS DGEASETGAN MINPLWKQFK 

       490        500        510        520        530        540 
WPNDMSWAAQ NLQQDHVNVE DGIFFYANLH SGEFSLAKPI LKTMIKGGIL SDEMGLGKTV 

       550        560        570        580        590        600 
AAYSLVLSCP HDSDVVDKKL FDIENTAVSD NLPSTWQDNK KPYASKTTLI VVPMSLLTQW 

       610        620        630        640        650        660 
SNEFTKANNS PDMYHEVYYG GNVSSLKTLL TKTKTPPTVV LTTYGIVQNE WTKHSKGRMT 

       670        680        690        700        710        720 
DEDVNISSGL FSVNFYRIII DEGHNIRNRT TVTSKAVMAL QGKCKWVLTG TPIINRLDDL 

       730        740        750        760        770        780 
YSLVKFLELD PWRQINYWKT FVSTPFESKN YKQAFDVVNA ILEPVLLRRT KQMKDKDGKP 

       790        800        810        820        830        840 
LVELPPKEVV IKRLPFSKSQ DLLYKFLLDK AEVSVKSGIA RGDLLKKYST ILVHILRLRQ 

       850        860        870        880        890        900 
VCCHPGLIGS QDENDEDLSK NNKLVTEQTV ELDSLMRVVS ERFDNSFSKE ELDAMIQRLK 

       910        920        930        940        950        960 
VKYPDNKSFQ SLECSICTTE PMDLDKALFT ECGHSFCEKC LFEYIEFQNS KNLGLKCPNC 

       970        980        990       1000       1010       1020 
RNQIDACRLL ALVQTNSNSK NLEFKPYSPA SKSSKITALL KELQLLQDSS AGEQVVIFSQ 

      1030       1040       1050       1060       1070       1080 
FSTYLDILEK ELTHTFSKDV AKIYKFDGRL SLKERTSVLA DFAVKDYSRQ KILLLSLKAG 

      1090       1100       1110       1120       1130       1140 
GVGLNLTCAS HAYMMDPWWS PSMEDQAIDR LHRIGQTNSV KVMRFIIQDS IEEKMLRIQE 

      1150       1160 
KKRTIGEAMD TDEDERRKRR IEEIQMLFE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Saccharomyces cerevisiae RAD5-encoded DNA repair protein contains DNA helicase and zinc-binding sequence motifs and affects the stability of simple repetitive sequences in the genome." Johnson R.E., Henderson S.T., Petes T.D., Prakash S., Bankmann M., Prakash L. Mol. Cell. Biol. 12:3807-3818(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. Hoheisel J.D. Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"The REV2 gene of Saccharomyces cerevisiae: cloning and DNA sequence." Ahne F., Baur M., Eckardt-Schupp F. Curr. Genet. 22:277-282(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 402-1063.
[5]	"Yeast DNA repair protein RAD5 that promotes instability of simple repetitive sequences is a DNA-dependent ATPase." Johnson R.E., Prakash S., Prakash L. J. Biol. Chem. 269:28259-28262(1994) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[6]	"The RAD5 gene product is involved in the avoidance of non-homologous end-joining of DNA double strand breaks in the yeast Saccharomyces cerevisiae." Ahne F., Ja B., Eckardt-Schupp F. Nucleic Acids Res. 25:743-749(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair." Ulrich H.D., Jentsch S. EMBO J. 19:3388-3397(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-914, SUBUNIT, INTERACTION WITH RAD18 AND UBC13.
[8]	"The Saccharomyces cerevisiae RAD6 group is composed of an error-prone and two error-free postreplication repair pathways." Xiao W., Chow B.L., Broomfield S., Hanna M. Genetics 155:1633-1641(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"Requirement of RAD5 and MMS2 for postreplication repair of UV-damaged DNA in Saccharomyces cerevisiae." Torres-Ramos C.A., Prakash S., Prakash L. Mol. Cell. Biol. 22:2419-2426(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO." Hoege C., Pfander B., Moldovan G.-L., Pyrowolakis G., Jentsch S. Nature 419:135-141(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH POL30 AND UBC9.
[11]	"Protein-protein interactions within an E2-RING finger complex. Implications for ubiquitin-dependent DNA damage repair." Ulrich H.D. J. Biol. Chem. 278:7051-7058(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, INTERACTION WITH UBC13, MUTAGENESIS OF CYS-914; ILE-916; TYR-944 AND ASN-959.
[12]	"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].
[13]	"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].
[14]	"The RING finger ATPase Rad5p of Saccharomyces cerevisiae contributes to DNA double-strand break repair in a ubiquitin-independent manner." Chen S., Davies A.A., Sagan D., Ulrich H.D. Nucleic Acids Res. 33:5878-5886(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH POL30; RAD18 AND UBC13, MUTAGENESIS OF 538-LYS-THR-539.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-129 AND SER-130, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M96644 Genomic DNA. Translation: AAA34951.1. Z73204 Genomic DNA. Translation: CAA97556.1. S46103 Genomic DNA. Translation: AAB23590.1. BK006945 Genomic DNA. Translation: DAA09350.1.
PIR	S64859.
RefSeq	NP_013132.1. NM_001181919.1.
3D structure databases
ProteinModelPortal	P32849.
SMR	P32849. Positions 527-900, 909-969, 993-1142.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5830N.
IntAct	P32849. 3 interactions.
MINT	MINT-2784640.
STRING	4932.YLR032W.
Proteomic databases
PaxDb	P32849.
PeptideAtlas	P32849.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR032W; YLR032W; YLR032W.
GeneID	850719.
KEGG	sce:YLR032W.
Organism-specific databases
CYGD	YLR032w.
SGD	S000004022. RAD5.
Phylogenomic databases
eggNOG	COG0553.
GeneTree	ENSGT00700000104586.
HOGENOM	HOG000040492.
KO	K15505.
OMA	MDPWWSP.
OrthoDB	EOG4J40R2.
Gene expression databases
Genevestigator	P32849.
GermOnline	YLR032W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	IPR014001. Helicase_ATP-bd. IPR001650. Helicase_C. IPR014905. HIP116_Rad5p_N. IPR000330. SNF2_N. IPR018957. Znf_C3HC4_RING-type. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. IPR017907. Znf_RING_CS. [Graphical view]
Pfam	PF00271. Helicase_C. 1 hit. PF08797. HIRAN. 1 hit. PF00176. SNF2_N. 1 hit. PF00097. zf-C3HC4. 1 hit. [Graphical view]
SMART	SM00487. DEXDc. 1 hit. SM00490. HELICc. 1 hit. SM00910. HIRAN. 1 hit. SM00184. RING. 1 hit. [Graphical view]
PROSITE	PS51192. HELICASE_ATP_BIND_1. 1 hit. PS51194. HELICASE_CTER. 1 hit. PS00518. ZF_RING_1. 1 hit. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	966793.

Entry information

Entry name

RAD5_YEAST

Accession

Primary (citable) accession number: P32849
Secondary accession number(s): D6VY34

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	May 1, 2013
This is version 118 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XII

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

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

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

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents