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P46946 (COM1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
DNA endonuclease SAE2

EC=3.1.-.-
Alternative name(s):
Completion of meiotic recombination protein 1
Sporulation in the absence of SPO11 protein 2
Gene names
Name:SAE2
Synonyms:COM1
Ordered Locus Names:YGL175C
ORF Names:G1639
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length345 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Endonuclease that cooperates with the MRX complex in processing meiotic and mitotic double-strand breaks by allowing the endonucleolytic removal of SPO11 from the break sites and ensuring both resection and intrachromosomal association of the broken ends. Required for proper recovery from checkpoint-mediated cell cycle arrest after DNA damage. MRX complex and SAE2 remove a small oligonucleotide(s) from the DNA ends to form an early intermediate which is rapidly processed by EXO1 and/or SGS1 to generate extensive tracts of single-stranded DNA that serve as substrate for RAD51. Plays a transitional role in the dissociation of MRE11 from, and the recruitment of RAD52 to, repair foci. Ensures that both ends of a DSB participate in a recombination event and impairs the formation of palindromic structures in the genome. With TEL1, promotes microhomology-mediated end joining (MMEJ) but inhibits non-homologous end joining (NHEJ), likely by regulating MRE11-dependent ssDNA accumulation at DNA break. SAE2 and MRX are particularly important for removal of hairpins, bulky adducts and other irregular end structures. Facilitates telomere length reequilibration and subsequent checkpoint switch off. Involved in homing efficiency of VMA1 intein VDE and in repair of transposon excision sites. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.32 Ref.33

Subunit structure

Dimer or multimer. Interacts with MRE11. Ref.24

Subcellular location

Cytoplasm. Nucleus. Note: Accumulates in foci at the precise time when MRE11 foci disassemble and RAD52 foci assemble. Remains associated with DSBs along with MRE11 in nuclease-deficient cells. Ref.12 Ref.14 Ref.26

Post-translational modification

Phosphorylated forms accumulate periodically during the unperturbed cell cycle and in response to DNA damage in G2. Phosphorylated by MEC1 and TEL1. Mutagenesis experiments showed that several of the 5 residues located in canonical (S/T)Q motifs, which are favored for phosphorylation by ATM/ATR kinases (Ser-73, Thr-90, Ser-249, Thr-279 and Ser-289) may be phosphorylated. Phosphorylated at Ser-267 by CDC28 which is required to initiate meiotic DSB resection by allowing SPO11 removal from DSB ends. Ref.16 Ref.21 Ref.26 Ref.27 Ref.32 Ref.33

Miscellaneous

Present with 1030 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the COM1/SAE2/CtIP family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 345345DNA endonuclease SAE2
PRO_0000097565

Regions

Region21 – 172152DNA-binding

Amino acid modifications

Modified residue1431Phosphoserine Ref.31
Modified residue2671Phosphoserine; by CDC28 Ref.27 Ref.32

Experimental info

Mutagenesis721S → A: Reduces DNA damage-induced phosphorylation; when associated with A-73, A-75, A-76 and A-90. Ref.16
Mutagenesis731S → A: Reduces DNA damage-induced phosphorylation; when associated with A-73, A-75, A-76 and A-90. Abolishes DNA damage-induced phosphorylation and function in DNA repair; when associated with A-90, A-249, A-279 and A-289. Ref.16 Ref.21 Ref.26
Mutagenesis751T → A: Reduces DNA damage-induced phosphorylation; when associated with A-72, A-75, A-76 and A-90. Ref.16
Mutagenesis761S → A: Reduces DNA damage-induced phosphorylation; when associated with A-72, A-73, A-75 and A-90. Ref.16
Mutagenesis901T → A: Reduces DNA damage-induced phosphorylation; when associated with A-72, A-73, A-75 and A-76. Abolishes DNA damage-induced phosphorylation and function in DNA repair; when associated with A-73, A-249, A-279 and A-289. Ref.16 Ref.21 Ref.26
Mutagenesis2231R → A: Leads to camptothecin hypersensitivity and loss of function; when associated with A-225. Ref.27
Mutagenesis2251L → A: Leads to camptothecin hypersensitivity and loss of function; when associated with A-223. Ref.27
Mutagenesis2491S → A: Reduces DNA damage-induced phosphorylation; when associated with A-278, A-279, and A-289. Abolishes DNA damage-induced phosphorylation and function in DNA repair; when associated with A-73, A-90, A-279 and A-289. Ref.16 Ref.21 Ref.26
Mutagenesis2671S → A: Leads to camptothecin hypersensitivity and loss of function. Ref.27 Ref.32
Mutagenesis2671S → E: Leads to constitutive activation of the DNA repair function. Ref.27 Ref.32
Mutagenesis2701G → D: Abolishes DNA-binding and endonuclease activity. Ref.25
Mutagenesis2781S → A: Reduces DNA damage-induced phosphorylation; when associated with A-249, A-279, and A-289. Ref.16
Mutagenesis2791T → A: Reduces DNA damage-induced phosphorylation; when associated with A-249, A-278, and A-289. Abolishes DNA damage-induced phosphorylation and function in DNA repair; when associated with A-73, A-90, A-249 and A-289. Ref.16 Ref.21 Ref.26
Mutagenesis2891S → A: Reduces DNA damage-induced phosphorylation; when associated with A-249, A-278, and A-279. Abolishes DNA damage-induced phosphorylation and function in DNA repair; when associated with A-73, A-90, A-249 and A-279. Ref.16 Ref.21 Ref.26

Sequences

Sequence LengthMass (Da)Tools
P46946 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 284D57A3C11DD92B

FASTA34540,097
        10         20         30         40         50         60 
MVTGEENVYL KSSLSILKEL SLDELLNVQY DVTTLIAKRV QALQNRNKCV LEEPNSKLAE 

        70         80         90        100        110        120 
ILCHEKNAPQ QSSQTSAGPG EQDSEDFILT QFDEDIKKES AEVHYRNENK HTVQLPLVTM 

       130        140        150        160        170        180 
PPNRHKRKIS EFSSPLNGLN NLSDLEDCSD TVIHEKDNDK ENKTRKLLGI ELENPESTSP 

       190        200        210        220        230        240 
NLYKNVKDNF LFDFNTNPLT KRAWILEDFR PNEDIAPVKR GRRKLERFYA QVGKPEDSKH 

       250        260        270        280        290        300 
RSLSVVIESQ NSDYEFAFDN LRNRSKSPPG FGRLDFPSTQ EGNEDKKKSQ EIIRRKTKYR 

       310        320        330        340 
FLMASNNKIP PYEREYVFKR EQLNQIVDDG CFFWSDKLLQ IYARC 

« Hide

References

« Hide 'large scale' references
[1]"A general method for identifying recessive diploid-specific mutations in Saccharomyces cerevisiae, its application to the isolation of mutants blocked at intermediate stages of meiotic prophase and characterization of a new gene SAE2."
McKee A.H.Z., Kleckner N.
Genetics 146:797-816(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The sequence of an 11.1 kb fragment on the left arm of Saccharomyces cerevisiae chromosome VII reveals six open reading frames including NSP49, KEM1 and four putative new genes."
Bertani I., Coglievina M., Zaccaria P., Klima R., Bruschi C.V.
Yeast 11:1187-1194(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. expand/collapse author list , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
Nature 387:81-84(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]"Isolation of COM1, a new gene required to complete meiotic double-strand break-induced recombination in Saccharomyces cerevisiae."
Prinz S., Amon A., Klein F.
Genetics 146:781-795(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Direct coupling between meiotic DNA replication and recombination initiation."
Borde V., Goldman A.S., Lichten M.
Science 290:806-809(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Fidelity of mitotic double-strand-break repair in Saccharomyces cerevisiae: a role for SAE2/COM1."
Rattray A.J., McGill C.B., Shafer B.K., Strathern J.N.
Genetics 158:109-122(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Wild-type levels of Spo11-induced DSBs are required for normal single-strand resection during meiosis."
Neale M.J., Ramachandran M., Trelles-Sticken E., Scherthan H., Goldman A.S.
Mol. Cell 9:835-846(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"The Mre11 complex is required for repair of hairpin-capped double-strand breaks and prevention of chromosome rearrangements."
Lobachev K.S., Gordenin D.A., Resnick M.A.
Cell 108:183-193(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"VDE-initiated intein homing in Saccharomyces cerevisiae proceeds in a meiotic recombination-like manner."
Fukuda T., Nogami S., Ohya Y.
Genes Cells 8:587-602(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Sudden telomere lengthening triggers a Rad53-dependent checkpoint in Saccharomyces cerevisiae."
Viscardi V., Baroni E., Romano M., Lucchini G., Longhese M.P.
Mol. Biol. Cell 14:3126-3143(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[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]"Choreography of the DNA damage response: spatiotemporal relationships among checkpoint and repair proteins."
Lisby M., Barlow J.H., Burgess R.C., Rothstein R.
Cell 118:699-713(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[15]"Microhomology-dependent end joining and repair of transposon-induced DNA hairpins by host factors in Saccharomyces cerevisiae."
Yu J., Marshall K., Yamaguchi M., Haber J.E., Weil C.F.
Mol. Cell. Biol. 24:1351-1364(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"The functions of budding yeast Sae2 in the DNA damage response require Mec1- and Tel1-dependent phosphorylation."
Baroni E., Viscardi V., Cartagena-Lirola H., Lucchini G., Longhese M.P.
Mol. Cell. Biol. 24:4151-4165(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, MUTAGENESIS OF SER-72; SER-73; THR-75; SER-76; THR-90; SER-249; SER-278; THR-279 AND SER-289.
[17]"The control of Spo11's interaction with meiotic recombination hotspots."
Prieler S., Penkner A., Borde V., Klein F.
Genes Dev. 19:255-269(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"A mechanism of palindromic gene amplification in Saccharomyces cerevisiae."
Rattray A.J., Shafer B.K., Neelam B., Strathern J.N.
Genes Dev. 19:1390-1399(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[19]"Multiple endonucleases function to repair covalent topoisomerase I complexes in Saccharomyces cerevisiae."
Deng C., Brown J.A., You D., Brown J.M.
Genetics 170:591-600(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[20]"The Saccharomyces cerevisiae Sae2 protein promotes resection and bridging of double strand break ends."
Clerici M., Mantiero D., Lucchini G., Longhese M.P.
J. Biol. Chem. 280:38631-38638(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[21]"Budding yeast Sae2 is an in vivo target of the Mec1 and Tel1 checkpoint kinases during meiosis."
Cartagena-Lirola H., Guerini I., Viscardi V., Lucchini G., Longhese M.P.
Cell Cycle 5:1549-1559(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, MUTAGENESIS OF SER-73; THR-90; SER-249; THR-279 AND SER-289.
[22]"The Saccharomyces cerevisiae Sae2 protein negatively regulates DNA damage checkpoint signalling."
Clerici M., Mantiero D., Lucchini G., Longhese M.P.
EMBO Rep. 7:212-218(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[23]"Saccharomyces cerevisiae Sae2- and Tel1-dependent single-strand DNA formation at DNA break promotes microhomology-mediated end joining."
Lee K., Lee S.E.
Genetics 176:2003-2014(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[24]"Examining protein protein interactions using endogenously tagged yeast arrays: the cross-and-capture system."
Suter B., Fetchko M.J., Imhof R., Graham C.I., Stoffel-Studer I., Zbinden C., Raghavan M., Lopez L., Beneti L., Hort J., Fillingham J., Greenblatt J.F., Giaever G., Nislow C., Stagljar I.
Genome Res. 17:1774-1782(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, INTERACTION WITH MRE11.
[25]"Sae2 is an endonuclease that processes hairpin DNA cooperatively with the Mre11/Rad50/Xrs2 complex."
Lengsfeld B.M., Rattray A.J., Bhaskara V., Ghirlando R., Paull T.T.
Mol. Cell 28:638-651(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DNA-BINDING, DOMAIN, MUTAGENESIS OF GLY-270.
[26]"Sae2p phosphorylation is crucial for cooperation with Mre11p for resection of DNA double-strand break ends during meiotic recombination in Saccharomyces cerevisiae."
Terasawa M., Ogawa T., Tsukamoto Y., Ogawa H.
Genes Genet. Syst. 83:209-217(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF SER-73; THR-90; SER-249; THR-279 AND SER-289.
[27]"CDK targets Sae2 to control DNA-end resection and homologous recombination."
Huertas P., Cortes-Ledesma F., Sartori A.A., Aguilera A., Jackson S.P.
Nature 455:689-692(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ARG-223; LEU-225 AND SER-267, PHOSPHORYLATION AT SER-267.
[28]"Sae2, Exo1 and Sgs1 collaborate in DNA double-strand break processing."
Mimitou E.P., Symington L.S.
Nature 455:770-774(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[29]"Replicon dynamics, dormant origin firing, and terminal fork integrity after double-strand break formation."
Doksani Y., Bermejo R., Fiorani S., Haber J.E., Foiani M.
Cell 137:247-258(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[30]"Size-dependent palindrome-induced intrachromosomal recombination in yeast."
Lisnic B., Svetec I.K., Stafa A., Zgaga Z.
DNA Repair 8:383-389(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[31]"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-143, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[32]"Processing of meiotic DNA double strand breaks requires cyclin-dependent kinase and multiple nucleases."
Manfrini N., Guerini I., Citterio A., Lucchini G., Longhese M.P.
J. Biol. Chem. 285:11628-11637(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF SER-267, PHOSPHORYLATION AT SER-267.
[33]"A truncated DNA-damage-signaling response is activated after DSB formation in the G1 phase of Saccharomyces cerevisiae."
Janke R., Herzberg K., Rolfsmeier M., Mar J., Bashkirov V.I., Haghnazari E., Cantin G., Yates J.R. III, Heyer W.D.
Nucleic Acids Res. 38:2302-2313(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U49447 Genomic DNA. Translation: AAB96338.1.
X84705 Genomic DNA. Translation: CAA59178.1.
Z72697 Genomic DNA. Translation: CAA96887.1.
BK006941 Genomic DNA. Translation: DAA07938.1.
PIRS59236.
RefSeqNP_011340.1. NM_001181040.1.

3D structure databases

ProteinModelPortalP46946.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33078. 74 interactions.
DIPDIP-1603N.
IntActP46946. 5 interactions.
MINTMINT-391468.
STRING4932.YGL175C.

Proteomic databases

PaxDbP46946.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGL175C; YGL175C; YGL175C.
GeneID852700.
KEGGsce:YGL175C.

Organism-specific databases

CYGDYGL175c.
SGDS000003143. SAE2.

Phylogenomic databases

eggNOGNOG40707.
OrthoDBEOG7XPZGF.

Enzyme and pathway databases

BioCycYEAST:G3O-30663-MONOMER.
ReactomeREACT_189187. Meiosis.

Gene expression databases

GenevestigatorP46946.

Family and domain databases

ProtoNetSearch...

Other

NextBio972044.

Entry information

Entry nameCOM1_YEAST
AccessionPrimary (citable) accession number: P46946
Secondary accession number(s): D6VTX7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 97 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 VII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families