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Protein

DNA repair protein RAD5

Gene

RAD5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.8 Publications

Cofactori

Kineticsi

  1. KM=525 µM for ATP

pH dependencei

Optimum pH is 7.0. for ATPase activity.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi532 – 5398ATPPROSITE-ProRule annotation
Zinc fingeri914 – 96148RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA-dependent ATPase activity Source: SGD
  3. four-way junction DNA binding Source: SGD
  4. four-way junction helicase activity Source: SGD
  5. Y-form DNA binding Source: SGD
  6. zinc ion binding Source: InterPro

GO - Biological processi

  1. DNA duplex unwinding Source: GOC
  2. double-strand break repair Source: SGD
  3. error-prone translesion synthesis Source: SGD
  4. free ubiquitin chain polymerization Source: SGD
  5. postreplication repair Source: SGD
  6. protein polyubiquitination Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

ATP-binding, DNA-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-32191-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA repair protein RAD5 (EC:3.6.4.-)
Alternative name(s):
Radiation sensitivity protein 5
Revertibility protein 2
Gene namesi
Name:RAD5
Synonyms:REV2, SNM2
Ordered Locus Names:YLR032W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XII

Organism-specific databases

CYGDiYLR032w.
EuPathDBiFungiDB:YLR032W.
SGDiS000004022. RAD5.

Subcellular locationi

GO - Cellular componenti

  1. chromosome, telomeric region Source: SGD
  2. cytoplasm Source: UniProtKB-SubCell
  3. nuclear chromatin Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi538 – 5392KT → AA: Increased sensitivity toward ionizing radiation. 1 Publication
Mutagenesisi914 – 9141C → S: Abolishes interaction with UBC13. 2 Publications
Mutagenesisi916 – 9161I → A: Abolishes interaction with UBC13. 1 Publication
Mutagenesisi944 – 9441Y → A: Abolishes interaction with UBC13. 1 Publication
Mutagenesisi959 – 9591N → A: Abolishes interaction with UBC13. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 11691168DNA repair protein RAD5PRO_0000056130Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei20 – 201Phosphoserine1 Publication
Modified residuei23 – 231Phosphoserine1 Publication
Modified residuei129 – 1291Phosphoserine1 Publication
Modified residuei130 – 1301Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP32849.
PaxDbiP32849.
PeptideAtlasiP32849.

Expressioni

Gene expression databases

GenevestigatoriP32849.

Interactioni

Subunit structurei

Homodimer. Interacts with POL30, RAD18, UBC9 and UBC13.4 Publications

Protein-protein interaction databases

BioGridi31306. 161 interactions.
DIPiDIP-5830N.
IntActiP32849. 3 interactions.
MINTiMINT-2784640.
STRINGi4932.YLR032W.

Structurei

3D structure databases

ProteinModelPortaliP32849.
SMRiP32849. Positions 527-900, 909-969, 993-1142.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini519 – 730212Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini995 – 1165171Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi681 – 6844DEGH box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi42 – 6019Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi303 – 31513Arg/Lys-rich (basic)Add
BLAST

Sequence similaritiesi

Belongs to the SNF2/RAD54 helicase family.Curated
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri914 – 96148RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0553.
GeneTreeiENSGT00780000122054.
HOGENOMiHOG000040492.
InParanoidiP32849.
KOiK15505.
OMAiKHGLSWM.
OrthoDBiEOG7PCJR9.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.40.50.300. 4 hits.
InterProiIPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR014905. HIRAN.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00271. Helicase_C. 1 hit.
PF08797. HIRAN. 1 hit.
PF00176. SNF2_N. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00910. HIRAN. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 4 hits.
PROSITEiPS51192. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P32849-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHIEQEERK RFFNDDLDTS ETSLNFKSEN KESFLFANSH NDDDDDVVVS
60 70 80 90 100
VSDTTEGEGD RSIVPVRREI EEEGQNQFIT ELLRIIPEMP KDLVMELNEK
110 120 130 140 150
FGSQEEGLSL ALSHYFDHNS GTSISKIPSS PNQLNTLSDT SNSTLSPSSF
160 170 180 190 200
HPKRRRIYGF RNQTRLEDKV TWKRFIGALQ VTGMATRPTV RPLKYGSQMK
210 220 230 240 250
LKRSSEEISA TKVYDSRGRK KASMASLVRI FDIQYDREIG RVSEDIAQIL
260 270 280 290 300
YPLLSSHEIS FEVTLIFCDN KRLSIGDSFI LQLDCFLTSL IFEERNDGES
310 320 330 340 350
LMKRRRTEGG NKREKDNGNF GRTLTETDEE LESRSKRLAL LKLFDKLRLK
360 370 380 390 400
PILDEQKALE KHKIELNSDP EIIDLDNDEI CSNQVTEVHN NLRDTQHEEE
410 420 430 440 450
TMNLNQLKTF YKAAQSSESL KSLPETEPSR DVFKLELRNY QKQGLTWMLR
460 470 480 490 500
REQEFAKAAS DGEASETGAN MINPLWKQFK WPNDMSWAAQ NLQQDHVNVE
510 520 530 540 550
DGIFFYANLH SGEFSLAKPI LKTMIKGGIL SDEMGLGKTV AAYSLVLSCP
560 570 580 590 600
HDSDVVDKKL FDIENTAVSD NLPSTWQDNK KPYASKTTLI VVPMSLLTQW
610 620 630 640 650
SNEFTKANNS PDMYHEVYYG GNVSSLKTLL TKTKTPPTVV LTTYGIVQNE
660 670 680 690 700
WTKHSKGRMT DEDVNISSGL FSVNFYRIII DEGHNIRNRT TVTSKAVMAL
710 720 730 740 750
QGKCKWVLTG TPIINRLDDL YSLVKFLELD PWRQINYWKT FVSTPFESKN
760 770 780 790 800
YKQAFDVVNA ILEPVLLRRT KQMKDKDGKP LVELPPKEVV IKRLPFSKSQ
810 820 830 840 850
DLLYKFLLDK AEVSVKSGIA RGDLLKKYST ILVHILRLRQ VCCHPGLIGS
860 870 880 890 900
QDENDEDLSK NNKLVTEQTV ELDSLMRVVS ERFDNSFSKE ELDAMIQRLK
910 920 930 940 950
VKYPDNKSFQ SLECSICTTE PMDLDKALFT ECGHSFCEKC LFEYIEFQNS
960 970 980 990 1000
KNLGLKCPNC RNQIDACRLL ALVQTNSNSK NLEFKPYSPA SKSSKITALL
1010 1020 1030 1040 1050
KELQLLQDSS AGEQVVIFSQ FSTYLDILEK ELTHTFSKDV AKIYKFDGRL
1060 1070 1080 1090 1100
SLKERTSVLA DFAVKDYSRQ KILLLSLKAG GVGLNLTCAS HAYMMDPWWS
1110 1120 1130 1140 1150
PSMEDQAIDR LHRIGQTNSV KVMRFIIQDS IEEKMLRIQE KKRTIGEAMD
1160
TDEDERRKRR IEEIQMLFE
Length:1,169
Mass (Da):134,002
Last modified:October 1, 1993 - v1
Checksum:i226B720097433EE2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti478 – 4781Q → R in AAB23590 (PubMed:1394508).Curated
Sequence conflicti635 – 6351T → N in AAB23590 (PubMed:1394508).Curated
Sequence conflicti846 – 8461G → S in AAB23590 (PubMed:1394508).Curated
Sequence conflicti898 – 8981R → S in AAB23590 (PubMed:1394508).Curated
Sequence conflicti973 – 9731V → A in AAB23590 (PubMed:1394508).Curated
Sequence conflicti1063 – 10631A → R in AAB23590 (PubMed:1394508).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96644 Genomic DNA. Translation: AAA34951.1.
Z73204 Genomic DNA. Translation: CAA97556.1.
S46103 Genomic DNA. Translation: AAB23590.1.
BK006945 Genomic DNA. Translation: DAA09350.1.
PIRiS64859.
RefSeqiNP_013132.1. NM_001181919.1.

Genome annotation databases

EnsemblFungiiYLR032W; YLR032W; YLR032W.
GeneIDi850719.
KEGGisce:YLR032W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96644 Genomic DNA. Translation: AAA34951.1.
Z73204 Genomic DNA. Translation: CAA97556.1.
S46103 Genomic DNA. Translation: AAB23590.1.
BK006945 Genomic DNA. Translation: DAA09350.1.
PIRiS64859.
RefSeqiNP_013132.1. NM_001181919.1.

3D structure databases

ProteinModelPortaliP32849.
SMRiP32849. Positions 527-900, 909-969, 993-1142.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31306. 161 interactions.
DIPiDIP-5830N.
IntActiP32849. 3 interactions.
MINTiMINT-2784640.
STRINGi4932.YLR032W.

Proteomic databases

MaxQBiP32849.
PaxDbiP32849.
PeptideAtlasiP32849.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR032W; YLR032W; YLR032W.
GeneIDi850719.
KEGGisce:YLR032W.

Organism-specific databases

CYGDiYLR032w.
EuPathDBiFungiDB:YLR032W.
SGDiS000004022. RAD5.

Phylogenomic databases

eggNOGiCOG0553.
GeneTreeiENSGT00780000122054.
HOGENOMiHOG000040492.
InParanoidiP32849.
KOiK15505.
OMAiKHGLSWM.
OrthoDBiEOG7PCJR9.

Enzyme and pathway databases

BioCyciYEAST:G3O-32191-MONOMER.

Miscellaneous databases

NextBioi966793.
PROiP32849.

Gene expression databases

GenevestigatoriP32849.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.40.50.300. 4 hits.
InterProiIPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR014905. HIRAN.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00271. Helicase_C. 1 hit.
PF08797. HIRAN. 1 hit.
PF00176. SNF2_N. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00910. HIRAN. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 4 hits.
PROSITEiPS51192. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  13. 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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-20; SER-23; SER-129 AND SER-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRAD5_YEAST
AccessioniPrimary (citable) accession number: P32849
Secondary accession number(s): D6VY34
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: April 29, 2015
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1520 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.