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P12753 (RAD50_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 repair protein RAD50

EC=3.6.-.-
Alternative name(s):
153 kDa protein
Gene names
Name:RAD50
Ordered Locus Names:YNL250W
ORF Names:N0872
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1312 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in DNA double-strand break repair (DSBR). The rad50/mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific exonuclease activity. Rad50 provides ATP-dependent control of mre11 by unwinding and/or repositioning DNA ends into the mre11 active site.

Cofactor

Binds 1 zinc ion per homodimer By similarity.

Subunit structure

Homodimer By similarity. Forms a complex with MRE11.

Domain

The zinc-hook, which separates the large intramolecular coiled coil regions, contains 2 Cys residues that coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another RAD50 molecule, thereby forming a V-shaped homodimer By similarity.

Miscellaneous

Present with 830 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the SMC family. RAD50 subfamily.

Contains 1 zinc-hook domain.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Meiosis
   DomainCoiled coil
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay PubMed 15546877. Source: GOC

base-excision repair

Inferred from mutant phenotype PubMed 20040573. Source: SGD

double-strand break repair via break-induced replication

Traceable author statement PubMed 11459961. Source: SGD

double-strand break repair via nonhomologous end joining

Inferred from mutant phenotype PubMed 12399380. Source: SGD

meiotic DNA double-strand break formation

Traceable author statement PubMed 9334324. Source: SGD

meiotic DNA double-strand break processing

Traceable author statement PubMed 9334324. Source: SGD

meiotic nuclear division

Inferred from mutant phenotype PubMed 17349953. Source: SGD

mitochondrial double-strand break repair via homologous recombination

Inferred from mutant phenotype PubMed 22214610. Source: SGD

negative regulation of endodeoxyribonuclease activity

Inferred from direct assay PubMed 17698079. Source: SGD

nucleotide phosphorylation

Inferred from direct assay PubMed 17349953. Source: GOC

telomere maintenance

Inferred from mutant phenotype PubMed 17349953. Source: SGD

telomere maintenance via recombination

Inferred from mutant phenotype PubMed 11238918. Source: SGD

   Cellular_componentMre11 complex

Inferred from physical interaction PubMed 9845372. Source: SGD

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 9845372. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity

Inferred from direct assay PubMed 15546877. Source: SGD

G-quadruplex DNA binding

Inferred from direct assay PubMed 17698079. Source: SGD

adenylate kinase activity

Inferred from direct assay PubMed 17349953. Source: SGD

double-stranded DNA binding

Inferred from direct assay PubMed 8367302. Source: SGD

double-stranded telomeric DNA binding

Inferred from direct assay PubMed 17698079. Source: SGD

nuclease activity

Inferred from electronic annotation. Source: InterPro

single-stranded telomeric DNA binding

Inferred from direct assay PubMed 17698079. Source: SGD

telomeric DNA binding

Inferred from direct assay PubMed 15721260. Source: SGD

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MRE11P328294EBI-14700,EBI-11255

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13121312DNA repair protein RAD50
PRO_0000138648

Regions

Domain640 – 741102Zinc-hook
Nucleotide binding34 – 418ATP Potential
Coiled coil185 – 347163 Potential
Coiled coil403 – 558156 Potential
Coiled coil640 – 67839 Potential
Coiled coil712 – 74130 Potential
Coiled coil787 – 1108322 Potential
Compositional bias1204 – 124138Ala/Asp-rich (DA-box)

Sites

Metal binding6871Zinc By similarity
Metal binding6901Zinc By similarity

Amino acid modifications

Modified residue4691Phosphoserine Ref.6
Modified residue5681Phosphothreonine Ref.6

Sequences

Sequence LengthMass (Da)Tools
P12753 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 58A0AA173AC5677E

FASTA1,312152,569
        10         20         30         40         50         60 
MSAIYKLSIQ GIRSFDSNDR ETIEFGKPLT LIVGMNGSGK TTIIECLKYA TTGDLPPNSK 

        70         80         90        100        110        120 
GGVFIHDPKI TGEKDIRAQV KLAFTSANGL NMIVTRNIQL LMKKTTTTFK TLEGQLVAIN 

       130        140        150        160        170        180 
NSGDRSTLST RSLELDAQVP LYLGVPKAIL EYVIFCHQED SLWPLSEPSN LKKKFDEIFQ 

       190        200        210        220        230        240 
AMKFTKALDN LKSIKKDMSV DIKLLKQSVE HLKLDKDRSK AMKLNIHQLQ TKIDQYNEEV 

       250        260        270        280        290        300 
SEIESQLNEI TEKSDKLFKS NQDFQKILSK VENLKNTKLS ISDQVKRLSN SIDILDLSKP 

       310        320        330        340        350        360 
DLQNLLANFS KVLMDKNNQL RDLETDISSL KDRQSSLQSL SNSLIRRQGE LEAGKETYEK 

       370        380        390        400        410        420 
NRNHLSSLKE AFQHKFQGLS NIENSDMAQV NHEMSQFKAF ISQDLTDTID QFAKDIQLKE 

       430        440        450        460        470        480 
TNLSDLIKSI TVDSQNLEYN KKDRSKLIHD SEELAEKLKS FKSLSTQDSL NHELENLKTY 

       490        500        510        520        530        540 
KEKLQSWESE NIIPKLNQKI EEKNNEMIIL ENQIEKFQDR IMKTNQQADL YAKLGLIKKS 

       550        560        570        580        590        600 
INTKLDELQK ITEKLQNDSR IRQVFPLTQE FQRADLEMDF QKLFINMQKN IAINNKKMHE 

       610        620        630        640        650        660 
LDRRYTNALY NLNTIEKDLQ DNQKSKEKVI QLLSENLPED CTIDEYNDVL EETELSYKTA 

       670        680        690        700        710        720 
LENLKMHQTT LEFNRKALEI AERDSCCYLC SRKFENESFK SKLLQELKTK TDANFEKTLK 

       730        740        750        760        770        780 
DTVQNEKEYL HSLRLLEKHI ITLNSINEKI DNSQKCLEKA KEETKTSKSK LDELEVDSTK 

       790        800        810        820        830        840 
LKDEKELAES EIRPLIEKFT YLEKELKDLE NSSKTISEEL SIYNTSEDGI QTVDELRDQQ 

       850        860        870        880        890        900 
RKMNDSLREL RKTISDLQME KDEKVRENSR MINLIKEKEL TVSEIESSLT QKQNIDDSIR 

       910        920        930        940        950        960 
SKRENINDID SRVKELEARI ISLKNKKDEA QSVLDKVKNE RDIQVRNKQK TVADINRLID 

       970        980        990       1000       1010       1020 
RFQTIYNEVV DFEAKGFDEL QTTIKELELN KAQMLELKEQ LDLKSNEVNE EKRKLADSNN 

      1030       1040       1050       1060       1070       1080 
EEKNLKQNLE LIELKSQLQH IESEISRLDV QNAEAERDKY QEESLRLRTR FEKLSSENAG 

      1090       1100       1110       1120       1130       1140 
KLGEMKQLQN QIDSLTHQLR TDYKDIEKNY HKEWVELQTR SFVTDDIDVY SKALDSAIMK 

      1150       1160       1170       1180       1190       1200 
YHGLKMQDIN RIIDELWKRT YSGTDIDTIK IRSDEVSSTV KGKSYNYRVV MYKQDVELDM 

      1210       1220       1230       1240       1250       1260 
RGRCSAGQKV LASIIIRLAL SETFGANCGV IALDEPTTNL DEENIESLAK SLHNIINMRR 

      1270       1280       1290       1300       1310 
HQKNFQLIVI THDEKFLGHM NAAAFTDHFF KVKRDDRQKS QIEWVDINRV TY 

« Hide

References

« Hide 'large scale' references
[1]"The yeast RAD50 gene encodes a predicted 153-kD protein containing a purine nucleotide-binding domain and two large heptad-repeat regions."
Alani E., Subbiah S., Kleckner N.
Genetics 122:47-57(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: RE821.
[2]"Sequence analysis of the 33 kb long region between ORC5 and SUI1 from the left arm of chromosome XIV from Saccharomyces cerevisiae."
Sen-Gupta M., Gueldener U., Beinhauer J.D., Fiedler T.A., Hegemann J.H.
Yeast 13:849-860(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. expand/collapse author list , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"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].
[6]"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-469 AND THR-568, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14814 Genomic DNA. Translation: CAA32919.1.
X96722 Genomic DNA. Translation: CAA65494.1.
Z71526 Genomic DNA. Translation: CAA96157.1.
BK006947 Genomic DNA. Translation: DAA10309.1.
PIRBWBYDL. S05808.
RefSeqNP_014149.1. NM_001183088.1.

3D structure databases

ProteinModelPortalP12753.
SMRP12753. Positions 3-100, 1145-1305.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35589. 282 interactions.
DIPDIP-2419N.
IntActP12753. 17 interactions.
MINTMINT-435300.
STRING4932.YNL250W.

Proteomic databases

PaxDbP12753.
PeptideAtlasP12753.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL250W; YNL250W; YNL250W.
GeneID855471.
KEGGsce:YNL250W.

Organism-specific databases

CYGDYNL250w.
SGDS000005194. RAD50.

Phylogenomic databases

eggNOGCOG0419.
GeneTreeENSGT00390000018781.
HOGENOMHOG000192269.
KOK10866.
OMALNELGTH.
OrthoDBEOG74BK1D.

Enzyme and pathway databases

BioCycYEAST:G3O-33247-MONOMER.
ReactomeREACT_189187. Meiosis.

Gene expression databases

GenevestigatorP12753.

Family and domain databases

Gene3D3.40.50.300. 3 hits.
InterProIPR027417. P-loop_NTPase.
IPR004584. Rad50_eukaryotes.
IPR007517. Rad50_Zn_hook.
IPR013134. Zn_hook_Rad50.
[Graphical view]
PANTHERPTHR18867. PTHR18867. 1 hit.
PfamPF04423. Rad50_zn_hook. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 3 hits.
TIGRFAMsTIGR00606. rad50. 1 hit.
PROSITEPS51131. ZN_HOOK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio979418.
PROP12753.

Entry information

Entry nameRAD50_YEAST
AccessionPrimary (citable) accession number: P12753
Secondary accession number(s): D6W0U3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: April 16, 2014
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIV

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

Yeast

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

SIMILARITY comments

Index of protein domains and families