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Protein

Serine/threonine-protein kinase MEC1

Gene

MEC1

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

Functioni

Serine/threonine protein kinase which activates checkpoint signaling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Recruited in complex with protein LCD1 by the single-strand-binding protein complex RPA to DNA lesions in order to initiate the DNA repair by homologous recombination, after the MRX-complex and TEL1 are displaced. Phosphorylates LCD1 and RPA2, a subunit of RPA, involved in DNA replication, repair and recombination. Phosphorylates RAD9, CHK1 and RAD53, which leads to the activation of the CHK1 and RAD53 kinases involved in DNA damage repair cascade. Phosphorylates histone H2A to form H2AS128ph (gamma-H2A) at sites of DNA damage, also involved in the regulation of DNA damage response mechanism. Phosphorylates also SLX4 and RTT107 which are proteins involved in genome stability. Required for cell growth and meiotic recombination.12 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein kinase activity Source: SGD
  • protein serine/threonine kinase activity Source: UniProtKB-KW

GO - Biological processi

  • DNA damage induced protein phosphorylation Source: SGD
  • DNA recombination Source: SGD
  • DNA repair Source: UniProtKB-KW
  • DNA replication Source: SGD
  • histone phosphorylation Source: SGD
  • nucleobase-containing compound metabolic process Source: SGD
  • positive regulation of DNA-dependent DNA replication Source: SGD
  • reciprocal meiotic recombination Source: SGD
  • telomere maintenance Source: SGD
  • telomere maintenance via recombination Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

DNA damage, DNA repair, Meiosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29090-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase MEC1 (EC:2.7.11.1)
Alternative name(s):
ATR homolog
DNA-damage checkpoint kinase MEC1
Mitosis entry checkpoint protein 1
Gene namesi
Name:MEC1
Synonyms:ESR1, SAD3
Ordered Locus Names:YBR136W
ORF Names:YBR1012
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR136W.
SGDiS000000340. MEC1.

Subcellular locationi

  • Nucleus

  • Note: Localizes to nuclear DNA repair foci in response to DNA double strand breaks. The recruitment to DNA lesion sites requires its interaction with LCD1 and the presence of the RPA complex on DNA.

GO - Cellular componenti

  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi225 – 2251V → G in MEC1-101; impairs both the G1/S and intra-S damage checkpoints but not the G2/M damage checkpoint; when associated with P-552 and S-781. 1 Publication
Mutagenesisi552 – 5521S → P in MEC1-101; impairs both the G1/S and intra-S damage checkpoints but not the G2/M damage checkpoint; when associated with S-225 and S-781. 1 Publication
Mutagenesisi781 – 7811L → S in MEC1-101; impairs both the G1/S and intra-S damage checkpoints but not the G2/M damage checkpoint; when associated with S-225 and P-552. 1 Publication
Mutagenesisi1179 – 11791F → S in MEC1-100; impairs both the G1/S and intra-S damage checkpoints but not the G2/M damage checkpoint; when associated with S-1700. 1 Publication
Mutagenesisi1700 – 17001N → S in MEC1-100; impairs both the G1/S and intra-S damage checkpoints but not the G2/M damage checkpoint; when associated with S-1179. 1 Publication
Mutagenesisi2224 – 22241D → A: Impairs kinase activity; when associated with K-2229. 2 Publications
Mutagenesisi2229 – 22291N → K: Impairs kinase activity; when associated with A-2224. 1 Publication
Mutagenesisi2243 – 22431D → E: Impairs kinase activity. 1 Publication
Mutagenesisi2360 – 23623MYI → AAA in MEC1-85; disrupts interaction with RFA1 and severely impairs kinase activity. 1 Publication
Mutagenesisi2367 – 23682FW → AA in MEC1-87; decreases the level of MEC1 and impairs viability. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 23682368Serine/threonine-protein kinase MEC1PRO_0000088836Add
BLAST

Proteomic databases

MaxQBiP38111.
PeptideAtlasiP38111.

PTM databases

iPTMnetiP38111.

Expressioni

Developmental stagei

Induced during meiosis.

Interactioni

Subunit structurei

Interacts with LCD1, which is required for localization MEC1 to the RPA complex. Interacts directly with the RPA subunits RFA1 and RFA2.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DPB11P470272EBI-6668,EBI-25984
LCD1Q043777EBI-6668,EBI-35652

Protein-protein interaction databases

BioGridi32836. 210 interactions.
DIPiDIP-799N.
IntActiP38111. 17 interactions.
MINTiMINT-659495.

Structurei

3D structure databases

ProteinModelPortaliP38111.
SMRiP38111. Positions 2039-2326.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1399 – 1944546FATPROSITE-ProRule annotationAdd
BLAST
Domaini2082 – 2368287PI3K/PI4KPROSITE-ProRule annotationAdd
BLAST
Domaini2336 – 236833FATCPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2140 – 2368229Binding to the RPA complexAdd
BLAST

Sequence similaritiesi

Belongs to the PI3/PI4-kinase family. ATM subfamily.Curated
Contains 1 FAT domain.PROSITE-ProRule annotation
Contains 1 FATC domain.PROSITE-ProRule annotation
Contains 5 HEAT repeats.Curated
Contains 1 PI3K/PI4K domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00830000128321.
HOGENOMiHOG000034220.
InParanoidiP38111.
KOiK02543.
OMAiSYAVMAM.
OrthoDBiEOG7ZWD92.

Family and domain databases

Gene3Di1.10.1070.11. 2 hits.
1.25.10.10. 4 hits.
1.25.40.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR003152. FATC_dom.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
IPR011990. TPR-like_helical_dom.
IPR012993. UME.
[Graphical view]
PfamiPF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF08064. UME. 1 hit.
[Graphical view]
SMARTiSM01343. FATC. 1 hit.
SM00146. PI3Kc. 1 hit.
SM00802. UME. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS51189. FAT. 1 hit.
PS51190. FATC. 1 hit.
PS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38111-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESHVKYLDE LILAIKDLNS GVDSKVQIKK VPTDPSSSQE YAKSLKILNT
60 70 80 90 100
LIRNLKDQRR NNIMKNDTIF SKTVSALALL LEYNPFLLVM KDSNGNFEIQ
110 120 130 140 150
RLIDDFLNIS VLNYDNYHRI WFMRRKLGSW CKACVEFYGK PAKFQLTAHF
160 170 180 190 200
ENTMNLYEQA LTEVLLGKTE LLKFYDTLKG LYILLYWFTS EYSTFGNSIA
210 220 230 240 250
FLDSSLGFTK FDFNFQRLIR IVLYVFDSCE LAALEYAEIQ LKYISLVVDY
260 270 280 290 300
VCNRTISTAL DAPALVCCEQ LKFVLTTMHH FLDNKYGLLD NDPTMAKGIL
310 320 330 340 350
RLYSLCISND FSKCFVDHFP IDQWADFSQS EHFPFTQLTN KALSIVYFDL
360 370 380 390 400
KRRSLPVEAL KYDNKFNIWV YQSEPDSSLK NVTSPFDDRY KQLEKLRLLV
410 420 430 440 450
LKKFNKTERG TLLKYRVNQL SPGFFQRAGN DFKLILNEAS VSIQTCFKTN
460 470 480 490 500
NITRLTSWTV ILGRLACLES EKFSGTLPNS TKDMDNWYVC HLCDIEKTGN
510 520 530 540 550
PFVRINPNRP EAAGKSEIFR ILHSNFLSHP NIDEFSESLL SGILFSLHRI
560 570 580 590 600
FSHFQPPKLT DGNGQINKSF KLVQKCFMNS NRYLRLLSTR IIPLFNISDS
610 620 630 640 650
HNSEDEHTAT LIKFLQSQKL PVVKENLVIA WTQLTLTTSN DVFDTLLLKL
660 670 680 690 700
IDIFNSDDYS LRIMMTLQIK NMAKILKKTP YQLLSPILPV LLRQLGKNLV
710 720 730 740 750
ERKVGFQNLI ELLGYSSKTI LDIFQRYIIP YAIIQYKSDV LSEIAKIMCD
760 770 780 790 800
GDTSLINQMK VNLLKKNSRQ IFAVALVKHG LFSLDILETL FLNRAPTFDK
810 820 830 840 850
GYITAYLPDY KTLAEITKLY KNSVTKDASD SENANMILCS LRFLITNFEK
860 870 880 890 900
DKRHGSKYKN INNWTDDQEQ AFQKKLQDNI LGIFQVFSSD IHDVEGRTTY
910 920 930 940 950
YEKLRVINGI SFLIIYAPKK SIISALAQIS ICLQTGLGLK EVRYEAFRCW
960 970 980 990 1000
HLLVRHLNDE ELSTVIDSLI AFILQKWSEF NGKLRNIVYS ILDTLIKEKS
1010 1020 1030 1040 1050
DLILKLKPYT TLALVGKPEL GILARDGQFA RMVNKIRSTT DLIPIFANNL
1060 1070 1080 1090 1100
KSSNKYVINQ NLDDIEVYLR RKQTERSIDF TPKKVGQTSD ITLVLGALLD
1110 1120 1130 1140 1150
TSHKFRNLDK DLCEKCAKCI SMIGVLDVTK HEFKRTTYSE NEVYDLNDSV
1160 1170 1180 1190 1200
QTIKFLIWVI NDILVPAFWQ SENPSKQLFV ALVIQESLKY CGLSSESWDM
1210 1220 1230 1240 1250
NHKELYPNEA KLWEKFNSVS KTTIYPLLSS LYLAQSWKEY VPLKYPSNNF
1260 1270 1280 1290 1300
KEGYKIWVKR FTLDLLKTGT TENHPLHVFS SLIREDDGSL SNFLLPYISL
1310 1320 1330 1340 1350
DIIIKAEKGT PYADILNGII IEFDSIFTCN LEGMNNLQVD SLRMCYESIF
1360 1370 1380 1390 1400
RVFEYCKKWA TEFKQNYSKL HGTFIIKDTK TTNMLLRIDE FLRTTPSDLL
1410 1420 1430 1440 1450
AQRSLETDSF ERSALYLEQC YRQNPHDKNQ NGQLLKNLQI TYEEIGDIDS
1460 1470 1480 1490 1500
LDGVLRTFAT GNLVSKIEEL QYSENWKLAQ DCFNVLGKFS DDPKTTTRML
1510 1520 1530 1540 1550
KSMYDHQLYS QIISNSSFHS SDGKISLSPD VKEWYSIGLE AANLEGNVQT
1560 1570 1580 1590 1600
LKNWVEQIES LRNIDDREVL LQYNIAKALI AISNEDPLRT QKYIHNSFRL
1610 1620 1630 1640 1650
IGTNFITSSK ETTLLKKQNL LMKLHSLYDL SFLSSAKDKF EYKSNTTILD
1660 1670 1680 1690 1700
YRMERIGADF VPNHYILSMR KSFDQLKMNE QADADLGKTF FTLAQLARNN
1710 1720 1730 1740 1750
ARLDIASESL MHCLERRLPQ AELEFAEILW KQGENDRALK IVQEIHEKYQ
1760 1770 1780 1790 1800
ENSSVNARDR AAVLLKFTEW LDLSNNSASE QIIKQYQDIF QIDSKWDKPY
1810 1820 1830 1840 1850
YSIGLYYSRL LERKKAEGYI TNGRFEYRAI SYFLLAFEKN TAKVRENLPK
1860 1870 1880 1890 1900
VITFWLDIAA ASISEAPGNR KEMLSKATED ICSHVEEALQ HCPTYIWYFV
1910 1920 1930 1940 1950
LTQLLSRLLH SHQSSAQIIM HILLSLAVEY PSHILWYITA LVNSNSSKRV
1960 1970 1980 1990 2000
LRGKHILEKY RQHSQNPHDL VSSALDLTKA LTRVCLQDVK SITSRSGKSL
2010 2020 2030 2040 2050
EKDFKFDMNV APSAMVVPVR KNLDIISPLE SNSMRGYQPF RPVVSIIRFG
2060 2070 2080 2090 2100
SSYKVFSSLK KPKQLNIIGS DGNIYGIMCK KEDVRQDNQY MQFATTMDFL
2110 2120 2130 2140 2150
LSKDIASRKR SLGINIYSVL SLREDCGILE MVPNVVTLRS ILSTKYESLK
2160 2170 2180 2190 2200
IKYSLKSLHD RWQHTAVDGK LEFYMEQVDK FPPILYQWFL ENFPDPINWF
2210 2220 2230 2240 2250
NARNTYARSY AVMAMVGHIL GLGDRHCENI LLDIQTGKVL HVDFDCLFEK
2260 2270 2280 2290 2300
GKRLPVPEIV PFRLTPNLLD ALGIIGTEGT FKKSSEVTLA LMRKNEVALM
2310 2320 2330 2340 2350
NVIETIMYDR NMDHSIQKAL KVLRNKIRGI DPQDGLVLSV AGQTETLIQE
2360
ATSEDNLSKM YIGWLPFW
Length:2,368
Mass (Da):273,342
Last modified:October 1, 1994 - v1
Checksum:iC06AEF9F0484A615
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti197 – 1971N → D in BAA01860 (PubMed:8065923).Curated
Sequence conflicti716 – 7161S → P in AAA74482 (PubMed:7926756).Curated
Sequence conflicti1255 – 12551K → Q in AAA74482 (PubMed:7926756).Curated
Sequence conflicti1276 – 12761L → G in AAA74482 (PubMed:7926756).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75891 Genomic DNA. Translation: CAA53494.1.
U31109 Genomic DNA. Translation: AAA74482.1.
D11088 Genomic DNA. Translation: BAA01860.1.
Z36005 Genomic DNA. Translation: CAA85094.1.
BK006936 Genomic DNA. Translation: DAA07252.1.
PIRiS46005.
RefSeqiNP_009694.3. NM_001178484.3.

Genome annotation databases

EnsemblFungiiYBR136W; YBR136W; YBR136W.
GeneIDi852433.
KEGGisce:YBR136W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75891 Genomic DNA. Translation: CAA53494.1.
U31109 Genomic DNA. Translation: AAA74482.1.
D11088 Genomic DNA. Translation: BAA01860.1.
Z36005 Genomic DNA. Translation: CAA85094.1.
BK006936 Genomic DNA. Translation: DAA07252.1.
PIRiS46005.
RefSeqiNP_009694.3. NM_001178484.3.

3D structure databases

ProteinModelPortaliP38111.
SMRiP38111. Positions 2039-2326.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32836. 210 interactions.
DIPiDIP-799N.
IntActiP38111. 17 interactions.
MINTiMINT-659495.

PTM databases

iPTMnetiP38111.

Proteomic databases

MaxQBiP38111.
PeptideAtlasiP38111.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR136W; YBR136W; YBR136W.
GeneIDi852433.
KEGGisce:YBR136W.

Organism-specific databases

EuPathDBiFungiDB:YBR136W.
SGDiS000000340. MEC1.

Phylogenomic databases

GeneTreeiENSGT00830000128321.
HOGENOMiHOG000034220.
InParanoidiP38111.
KOiK02543.
OMAiSYAVMAM.
OrthoDBiEOG7ZWD92.

Enzyme and pathway databases

BioCyciYEAST:G3O-29090-MONOMER.

Miscellaneous databases

NextBioi971318.
PROiP38111.

Family and domain databases

Gene3Di1.10.1070.11. 2 hits.
1.25.10.10. 4 hits.
1.25.40.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR003152. FATC_dom.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
IPR011990. TPR-like_helical_dom.
IPR012993. UME.
[Graphical view]
PfamiPF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF08064. UME. 1 hit.
[Graphical view]
SMARTiSM01343. FATC. 1 hit.
SM00146. PI3Kc. 1 hit.
SM00802. UME. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS51189. FAT. 1 hit.
PS51190. FATC. 1 hit.
PS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "An essential gene, ESR1, is required for mitotic cell growth, DNA repair and meiotic recombination in Saccharomyces cerevisiae."
    Kato R., Ogawa H.
    Nucleic Acids Res. 22:3104-3112(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION.
  2. "Mitotic checkpoint genes in budding yeast and the dependence of mitosis on DNA replication and repair."
    Weinert T.A., Kiser G.L., Hartwell L.H.
    Genes Dev. 8:652-665(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The sequence of 29.7 kb from the right arm of chromosome II reveals 13 complete open reading frames, of which ten correspond to new genes."
    Becam A.-M., Cullin C., Grzybowska E., Lacroute F., Nasr F., Ozier-Kalogeropoulos O., Palucha A., Slonimski P.P., Zagulski M., Herbert C.J.
    Yeast 10:S1-S11(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "Regulation of RAD53 by the ATM-like kinases MEC1 and TEL1 in yeast cell cycle checkpoint pathways."
    Sanchez Y., Desany B.A., Jones W.J., Liu Q., Wang B., Elledge S.J.
    Science 271:357-360(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "The ATM homologue MEC1 is required for phosphorylation of replication protein A in yeast."
    Brush G.S., Morrow D.M., Hieter P., Kelly T.J.
    Proc. Natl. Acad. Sci. U.S.A. 93:15075-15080(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION OF RPA2.
  8. "LCD1: an essential gene involved in checkpoint control and regulation of the MEC1 signalling pathway in Saccharomyces cerevisiae."
    Rouse J., Jackson S.P.
    EMBO J. 19:5801-5812(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LCD1.
  9. "The checkpoint protein Ddc2, functionally related to S. pombe Rad26, interacts with Mec1 and is regulated by Mec1-dependent phosphorylation in budding yeast."
    Paciotti V., Clerici M., Lucchini G., Longhese M.P.
    Genes Dev. 14:2046-2059(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION OF LCD1, INTERACTION WITH LCD1.
  10. "A role for Saccharomyces cerevisiae histone H2A in DNA repair."
    Downs J.A., Lowndes N.F., Jackson S.P.
    Nature 408:1001-1004(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Protein kinase activity of Tel1p and Mec1p, two Saccharomyces cerevisiae proteins related to the human ATM protein kinase."
    Mallory J.C., Petes T.D.
    Proc. Natl. Acad. Sci. U.S.A. 97:13749-13754(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS A KINASE, FUNCTION, MUTAGENESIS OF ASP-2224 AND ASN-2229.
  12. "Characterization of mec1 kinase-deficient mutants and of new hypomorphic mec1 alleles impairing subsets of the DNA damage response pathway."
    Paciotti V., Clerici M., Scotti M., Lucchini G., Longhese M.P.
    Mol. Cell. Biol. 21:3913-3925(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH LCD1, PHOSPHORYLATION OF LCD1, MUTAGENESIS OF VAL-225; SER-552; LEU-781; PHE-1179; ASN-1700; ASP-2224 AND ASP-2243.
  13. "MEC3, MEC1, and DDC2 are essential components of a telomere checkpoint pathway required for cell cycle arrest during senescence in Saccharomyces cerevisiae."
    Enomoto S., Glowczewski L., Berman J.
    Mol. Biol. Cell 13:2626-2638(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Yeast histone 2A serine 129 is essential for the efficient repair of checkpoint-blind DNA damage."
    Redon C., Pilch D.R., Rogakou E.P., Orr A.H., Lowndes N.F., Bonner W.M.
    EMBO Rep. 4:678-684(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "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.
  16. "Distribution and dynamics of chromatin modification induced by a defined DNA double-strand break."
    Shroff R., Arbel-Eden A., Pilch D.R., Ira G., Bonner W.M., Petrini J.H.J., Haber J.E., Lichten M.
    Curr. Biol. 14:1703-1711(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "Esc4p, a new target of Mec1p (ATR), promotes resumption of DNA synthesis after DNA damage."
    Rouse J.
    EMBO J. 23:1188-1197(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION OF RTT107.
  18. "Slx4 becomes phosphorylated after DNA damage in a Mec1/Tel1-dependent manner and is required for repair of DNA alkylation damage."
    Flott S., Rouse J.
    Biochem. J. 391:325-333(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION OF SLX4.
  19. "Activation of the checkpoint kinase Rad53 by the phosphatidyl inositol kinase-like kinase Mec1."
    Ma J.-L., Lee S.-J., Duong J.K., Stern D.F.
    J. Biol. Chem. 281:3954-3963(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE MEC1-LCD1 COMPLEX, PHOSPHORYLATION OF LCD1 AND RAD53.
  20. "Role of the C-terminus of Mec1 checkpoint kinase in its localization to sites of DNA damage."
    Nakada D., Hirano Y., Tanaka Y., Sugimoto K.
    Mol. Biol. Cell 16:5227-5235(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH LCD1; RFA1 AND RFA2, MUTAGENESIS OF 2360-MET--ILE-2362 AND 2367-PHE-TRP-2368.
  21. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiATR_YEAST
AccessioniPrimary (citable) accession number: P38111
Secondary accession number(s): D6VQD2, Q02580
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: May 11, 2016
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.