P32829 (MRE11_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Double-strand break repair protein MRE11

Gene names

Name:	MRE11
Ordered Locus Names:	YMR224C
ORF Names:	YM9959.06C

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

General annotation (Comments)

Function	Involved in DNA double-strand break repair (DSBR). Possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity. Also involved in meiotic DSB processing. Ref.5 Ref.6
Cofactor	Manganese By similarity.
Subunit structure	Forms a complex with RAD50 and XRS2.
Subcellular location	Nucleus.
Miscellaneous	Present with 432 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the MRE11/RAD32 family.

Ontologies

Keywords
Biological process	DNA damage DNA repair Meiosis
Cellular component	Nucleus
Ligand	Manganese
Molecular function	Endonuclease Exonuclease Hydrolase Nuclease
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ascospore formation Inferred from mutant phenotype PubMed 17396017. Source: SGD base-excision repair Inferred from mutant phenotype PubMed 20040573. Source: SGD double-strand break repair via break-induced replication Inferred from mutant phenotype PubMed 17321803. 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 regulation of transcription during meiosis Inferred from mutant phenotype PubMed 17396017. Source: SGD
Cellular_component	Mre11 complex Inferred from physical interaction PubMed 9845372. Source: SGD mitochondrion Inferred from direct assay PubMed 14576278PubMed 16823961. Source: SGD nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	3'-5'-exodeoxyribonuclease activity Inferred from experiment. Source: Reactome G-quadruplex DNA binding Inferred from direct assay PubMed 17698079. Source: SGD double-stranded telomeric DNA binding Inferred from direct assay PubMed 17698079. Source: SGD endodeoxyribonuclease activity Inferred from direct assay PubMed 16116037. Source: SGD manganese ion binding Inferred from electronic annotation. Source: InterPro protein complex scaffold Inferred from mutant phenotype PubMed 9845372. Source: SGD single-stranded telomeric DNA binding Inferred from direct assay PubMed 17698079. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RAD50	P12753	5	EBI-11255,EBI-14700
XRS2	P33301	7	EBI-11255,EBI-20599

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 692	692	Double-strand break repair protein MRE11		PRO_0000138680
Sites
	Active site	125	1	Proton donor By similarity
Amino acid modifications
	Modified residue	558	1	Phosphothreonine Ref.8
	Modified residue	560	1	Phosphoserine Ref.8 Ref.9
Natural variations
	Natural variant	380	1	P → S in strain: SK1.
	Natural variant	659	1	P → S in strain: SK1.

Sequences

	Sequence		Length	Mass (Da)
	P32829 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: D58433E32E852B73	FASTA	692	77,650
	10 20 30 40 50 60 MDYPDPDTIR ILITTDNHVG YNENDPITGD DSWKTFHEVM MLAKNNNVDM VVQSGDLFHV 70 80 90 100 110 120 NKPSKKSLYQ VLKTLRLCCM GDKPCELELL SDPSQVFHYD EFTNVNYEDP NFNISIPVFG 130 140 150 160 170 180 ISGNHDDASG DSLLCPMDIL HATGLINHFG KVIESDKIKV VPLLFQKGST KLALYGLAAV 190 200 210 220 230 240 RDERLFRTFK DGGVTFEVPT MREGEWFNLM CVHQNHTGHT NTAFLPEQFL PDFLDMVIWG 250 260 270 280 290 300 HEHECIPNLV HNPIKNFDVL QPGSSVATSL CEAEAQPKYV FILDIKYGEA PKMTPIPLET 310 320 330 340 350 360 IRTFKMKSIS LQDVPHLRPH DKDATSKYLI EQVEEMIRDA NEETKQKLAD DGEGDMVAEL 370 380 390 400 410 420 PKPLIRLRVD YSAPSNTQSP IDYQVENPRR FSNRFVGRVA NGNNVVQFYK KRSPVTRSKK 430 440 450 460 470 480 SGINGTSISD RDVEKLFSES GGELEVQTLV NDLLNKMQLS LLPEVGLNEA VKKFVDKDEK 490 500 510 520 530 540 TALKEFISHE ISNEVGILST NEEFLRTDDA EEMKALIKQV KRANSVRPTP PKENDETNFA 550 560 570 580 590 600 FNGNGLDSFR SSNREVRTGS PDITQSHVDN ESRITHISQA ESSKPTSKPK RVRTATKKKI 610 620 630 640 650 660 PAFSDSTVIS DAENELGDNN DAQDDVDIDE NDIIMVSTDE EDASYGLLNG RKTKTKTRPA 670 680 690 ASTKTASRRG KGRASRTPKT DILGSLLAKK RK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Interaction of Mre11 and Rad50: two proteins required for DNA repair and meiosis-specific double-strand break formation in Saccharomyces cerevisiae." Johzuka K., Ogawa H. Genetics 139:1521-1532(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-643.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. , Skelton J., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:90-93(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]	"Recombination-dependent lethals in Yeast." Nairz K., Klein F. Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: SK1.
[5]	"Functions of the yeast meiotic recombination genes, MRE11 and MRE2." Ogawa H., Johzuka K., Nakagawa T., Leem S.H., Hagihara A.H. Adv. Biophys. 31:67-76(1995) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"The 3' to 5' exonuclease activity of Mre 11 facilitates repair of DNA double-strand breaks." Paull T.T., Gellert M. Mol. Cell 1:969-979(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"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].
[8]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-558 AND SER-560, MASS SPECTROMETRY.
[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-560, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D11463 Genomic DNA. Translation: BAA02017.1. Z49939 Genomic DNA. Translation: CAA90195.1. U60829 Genomic DNA. Translation: AAB61454.1. BK006946 Genomic DNA. Translation: DAA10123.1.
PIR	S57592.
RefSeq	NP_013951.1. NM_001182731.1.
3D structure databases
ProteinModelPortal	P32829.
SMR	P32829. Positions 7-412.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1313N.
IntAct	P32829. 5 interactions.
MINT	MINT-388080.
Proteomic databases
PaxDb	P32829.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YMR224C; YMR224C; YMR224C.
GeneID	855264.
KEGG	sce:YMR224C.
Organism-specific databases
CYGD	YMR224c.
SGD	S000004837. MRE11.
Phylogenomic databases
eggNOG	COG0420.
GeneTree	ENSGT00390000017288.
HOGENOM	HOG000216581.
KO	K10865.
OMA	FVNKQVT.
OrthoDB	EOG4P2T9Q.
Enzyme and pathway databases
Reactome	REACT_128851. Meiosis.
Gene expression databases
Genevestigator	P32829.
GermOnline	YMR224C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR003701. DNA_repair_Mre11. IPR004843. Metallo_PEstase_dom. IPR007281. Mre11_DNA-bd. [Graphical view]
PANTHER	PTHR10139. PTHR10139. 1 hit.
Pfam	PF00149. Metallophos. 1 hit. PF04152. Mre11_DNA_bind. 1 hit. [Graphical view]
PIRSF	PIRSF000882. DSB_repair_MRE11. 1 hit.
TIGRFAMs	TIGR00583. mre11. 1 hit.
ProtoNet	Search...
Other
NextBio	978864.

Entry information

Entry name

MRE11_YEAST

Accession

Primary (citable) accession number: P32829
Secondary accession number(s): D6W049, P87289, Q07173

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 131 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program