P12753 (RAD50_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

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

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	1312 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	DNA damage DNA repair Meiosis
Domain	Coiled coil
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP 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_component	Mre11 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_function	ATP 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 protein binding Inferred from physical interaction PubMed 9845372. Source: IntAct 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
MRE11	P32829	4	EBI-14700,EBI-11255

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1312	1312	DNA repair protein RAD50		PRO_0000138648
Regions
	Domain	640 – 741	102	Zinc-hook
	Nucleotide binding	34 – 41	8	ATP Potential
	Coiled coil	185 – 347	163	Potential
	Coiled coil	403 – 558	156	Potential
	Coiled coil	640 – 678	39	Potential
	Coiled coil	712 – 741	30	Potential
	Coiled coil	787 – 1108	322	Potential
	Compositional bias	1204 – 1241	38	Ala/Asp-rich (DA-box)
Sites
	Metal binding	687	1	Zinc By similarity
	Metal binding	690	1	Zinc By similarity
Amino acid modifications
	Modified residue	469	1	Phosphoserine Ref.6
	Modified residue	568	1	Phosphothreonine Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P12753 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: 58A0AA173AC5677E	FASTA	1,312	152,569
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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]	"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.
PIR	BWBYDL. S05808.
RefSeq	NP_014149.1. NM_001183088.1.
3D structure databases
ProteinModelPortal	P12753.
SMR	P12753. Positions 1204-1294.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	35589. 282 interactions.
DIP	DIP-2419N.
IntAct	P12753. 17 interactions.
MINT	MINT-435300.
STRING	4932.YNL250W.
Proteomic databases
MaxQB	P12753.
PaxDb	P12753.
PeptideAtlas	P12753.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YNL250W; YNL250W; YNL250W.
GeneID	855471.
KEGG	sce:YNL250W.
Organism-specific databases
CYGD	YNL250w.
SGD	S000005194. RAD50.
Phylogenomic databases
eggNOG	COG0419.
GeneTree	ENSGT00390000018781.
HOGENOM	HOG000192269.
KO	K10866.
OMA	PEYIYCL.
OrthoDB	EOG74BK1D.
Enzyme and pathway databases
BioCyc	YEAST:G3O-33247-MONOMER.
Reactome	REACT_190740. Cell Cycle.
Gene expression databases
Genevestigator	P12753.
Family and domain databases
Gene3D	3.40.50.300. 3 hits.
InterPro	IPR027417. P-loop_NTPase. IPR004584. Rad50_eukaryotes. IPR007517. Rad50_Zn_hook. IPR013134. Zn_hook_Rad50. [Graphical view]
PANTHER	PTHR18867. PTHR18867. 1 hit.
Pfam	PF04423. Rad50_zn_hook. 1 hit. [Graphical view]
SUPFAM	SSF52540. SSF52540. 3 hits.
TIGRFAMs	TIGR00606. rad50. 1 hit.
PROSITE	PS51131. ZN_HOOK. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	979418.
PRO	P12753.

Entry information

Entry name

RAD50_YEAST

Accession

Primary (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:	June 11, 2014
This is version 144 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program