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P46946

- COM1_YEAST

UniProt

P46946 - COM1_YEAST

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Protein

DNA endonuclease SAE2

Gene
SAE2, COM1, YGL175C, G1639
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.25 Publications

GO - Molecular functioni

  1. double-stranded DNA binding Source: SGD
  2. endodeoxyribonuclease activity Source: Reactome
  3. single-stranded DNA endodeoxyribonuclease activity Source: SGD

GO - Biological processi

  1. DNA catabolic process, endonucleolytic Source: SGD
  2. DNA double-strand break processing Source: SGD
  3. gene conversion at mating-type locus, DNA double-strand break processing Source: SGD
  4. meiotic DNA double-strand break formation Source: SGD
  5. meiotic DNA double-strand break processing Source: SGD
  6. telomere maintenance Source: SGD
  7. telomeric 3' overhang formation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

DNA damage, DNA repair, Meiosis

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30663-MONOMER.
ReactomeiREACT_189186. Meiotic recombination.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:SAE2
Synonyms:COM1
Ordered Locus Names:YGL175C
ORF Names:G1639
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGL175c.
SGDiS000003143. SAE2.

Subcellular locationi

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.3 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi72 – 721S → A: Reduces DNA damage-induced phosphorylation; when associated with A-73, A-75, A-76 and A-90. 1 Publication
Mutagenesisi73 – 731S → 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. 3 Publications
Mutagenesisi75 – 751T → A: Reduces DNA damage-induced phosphorylation; when associated with A-72, A-75, A-76 and A-90. 1 Publication
Mutagenesisi76 – 761S → A: Reduces DNA damage-induced phosphorylation; when associated with A-72, A-73, A-75 and A-90. 1 Publication
Mutagenesisi90 – 901T → 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. 3 Publications
Mutagenesisi223 – 2231R → A: Leads to camptothecin hypersensitivity and loss of function; when associated with A-225. 1 Publication
Mutagenesisi225 – 2251L → A: Leads to camptothecin hypersensitivity and loss of function; when associated with A-223. 1 Publication
Mutagenesisi249 – 2491S → 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. 3 Publications
Mutagenesisi267 – 2671S → A: Leads to camptothecin hypersensitivity and loss of function. 2 Publications
Mutagenesisi267 – 2671S → E: Leads to constitutive activation of the DNA repair function. 2 Publications
Mutagenesisi270 – 2701G → D: Abolishes DNA-binding and endonuclease activity. 1 Publication
Mutagenesisi278 – 2781S → A: Reduces DNA damage-induced phosphorylation; when associated with A-249, A-279, and A-289. 1 Publication
Mutagenesisi279 – 2791T → 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. 3 Publications
Mutagenesisi289 – 2891S → 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. 3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 345345DNA endonuclease SAE2PRO_0000097565Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei143 – 1431Phosphoserine1 Publication
Modified residuei267 – 2671Phosphoserine; by CDC282 Publications

Post-translational modificationi

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.6 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP46946.
PaxDbiP46946.

Expressioni

Gene expression databases

GenevestigatoriP46946.

Interactioni

Subunit structurei

Dimer or multimer. Interacts with MRE11.1 Publication

Protein-protein interaction databases

BioGridi33078. 79 interactions.
DIPiDIP-1603N.
IntActiP46946. 5 interactions.
MINTiMINT-391468.
STRINGi4932.YGL175C.

Structurei

3D structure databases

ProteinModelPortaliP46946.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 172152DNA-bindingAdd
BLAST

Sequence similaritiesi

Belongs to the COM1/SAE2/CtIP family.

Phylogenomic databases

eggNOGiNOG40707.
OMAiGINIERY.
OrthoDBiEOG7XPZGF.

Sequencei

Sequence statusi: Complete.

P46946-1 [UniParc]FASTAAdd to Basket

« Hide

MVTGEENVYL KSSLSILKEL SLDELLNVQY DVTTLIAKRV QALQNRNKCV    50
LEEPNSKLAE ILCHEKNAPQ QSSQTSAGPG EQDSEDFILT QFDEDIKKES 100
AEVHYRNENK HTVQLPLVTM PPNRHKRKIS EFSSPLNGLN NLSDLEDCSD 150
TVIHEKDNDK ENKTRKLLGI ELENPESTSP NLYKNVKDNF LFDFNTNPLT 200
KRAWILEDFR PNEDIAPVKR GRRKLERFYA QVGKPEDSKH RSLSVVIESQ 250
NSDYEFAFDN LRNRSKSPPG FGRLDFPSTQ EGNEDKKKSQ EIIRRKTKYR 300
FLMASNNKIP PYEREYVFKR EQLNQIVDDG CFFWSDKLLQ IYARC 345
Length:345
Mass (Da):40,097
Last modified:November 1, 1995 - v1
Checksum:i284D57A3C11DD92B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U49447 Genomic DNA. Translation: AAB96338.1.
X84705 Genomic DNA. Translation: CAA59178.1.
Z72697 Genomic DNA. Translation: CAA96887.1.
BK006941 Genomic DNA. Translation: DAA07938.1.
PIRiS59236.
RefSeqiNP_011340.1. NM_001181040.1.

Genome annotation databases

EnsemblFungiiYGL175C; YGL175C; YGL175C.
GeneIDi852700.
KEGGisce:YGL175C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U49447 Genomic DNA. Translation: AAB96338.1 .
X84705 Genomic DNA. Translation: CAA59178.1 .
Z72697 Genomic DNA. Translation: CAA96887.1 .
BK006941 Genomic DNA. Translation: DAA07938.1 .
PIRi S59236.
RefSeqi NP_011340.1. NM_001181040.1.

3D structure databases

ProteinModelPortali P46946.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33078. 79 interactions.
DIPi DIP-1603N.
IntActi P46946. 5 interactions.
MINTi MINT-391468.
STRINGi 4932.YGL175C.

Proteomic databases

MaxQBi P46946.
PaxDbi P46946.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGL175C ; YGL175C ; YGL175C .
GeneIDi 852700.
KEGGi sce:YGL175C.

Organism-specific databases

CYGDi YGL175c.
SGDi S000003143. SAE2.

Phylogenomic databases

eggNOGi NOG40707.
OMAi GINIERY.
OrthoDBi EOG7XPZGF.

Enzyme and pathway databases

BioCyci YEAST:G3O-30663-MONOMER.
Reactomei REACT_189186. Meiotic recombination.

Miscellaneous databases

NextBioi 972044.

Gene expression databases

Genevestigatori P46946.

Family and domain databases

ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  13. 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.

Entry informationi

Entry nameiCOM1_YEAST
AccessioniPrimary (citable) accession number: P46946
Secondary accession number(s): D6VTX7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 3, 2014
This is version 100 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 1030 molecules/cell in log phase SD medium.

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

External Data

Dasty 3

Similar proteinsi