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Serine/threonine-protein kinase MEC1 (EC 2.7.11.1) (ATR homolog) (DNA-damage checkpoint kinase MEC1) (Mitosis entry checkpoint protein 1)

 ATR_YEAST               Reviewed;        2368 AA.
P38111; D6VQD2; Q02580;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
01-OCT-1994, sequence version 1.
23-MAY-2018, entry version 171.
RecName: Full=Serine/threonine-protein kinase MEC1;
EC=2.7.11.1;
AltName: Full=ATR homolog;
AltName: Full=DNA-damage checkpoint kinase MEC1;
AltName: Full=Mitosis entry checkpoint protein 1;
Name=MEC1; Synonyms=ESR1, SAD3; OrderedLocusNames=YBR136W;
ORFNames=YBR1012;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
PubMed=8065923; DOI=10.1093/nar/22.15.3104;
Kato R., Ogawa H.;
"An essential gene, ESR1, is required for mitotic cell growth, DNA
repair and meiotic recombination in Saccharomyces cerevisiae.";
Nucleic Acids Res. 22:3104-3112(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7926756; DOI=10.1101/gad.8.6.652;
Weinert T.A., Kiser G.L., Hartwell L.H.;
"Mitotic checkpoint genes in budding yeast and the dependence of
mitosis on DNA replication and repair.";
Genes Dev. 8:652-665(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8091856; DOI=10.1002/yea.320100002;
Becam A.-M., Cullin C., Grzybowska E., Lacroute F., Nasr F.,
Ozier-Kalogeropoulos O., Palucha A., Slonimski P.P., Zagulski M.,
Herbert C.J.;
"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.";
Yeast 10:S1-S11(1994).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7813418;
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.;
"Complete DNA sequence of yeast chromosome II.";
EMBO J. 13:5795-5809(1994).
[5]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
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.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[6]
FUNCTION.
PubMed=8553072; DOI=10.1126/science.271.5247.357;
Sanchez Y., Desany B.A., Jones W.J., Liu Q., Wang B., Elledge S.J.;
"Regulation of RAD53 by the ATM-like kinases MEC1 and TEL1 in yeast
cell cycle checkpoint pathways.";
Science 271:357-360(1996).
[7]
PHOSPHORYLATION OF RPA2.
PubMed=8986766; DOI=10.1073/pnas.93.26.15075;
Brush G.S., Morrow D.M., Hieter P., Kelly T.J.;
"The ATM homologue MEC1 is required for phosphorylation of replication
protein A in yeast.";
Proc. Natl. Acad. Sci. U.S.A. 93:15075-15080(1996).
[8]
INTERACTION WITH LCD1.
PubMed=11060031; DOI=10.1093/emboj/19.21.5801;
Rouse J., Jackson S.P.;
"LCD1: an essential gene involved in checkpoint control and regulation
of the MEC1 signalling pathway in Saccharomyces cerevisiae.";
EMBO J. 19:5801-5812(2000).
[9]
PHOSPHORYLATION OF LCD1, AND INTERACTION WITH LCD1.
PubMed=10950868;
Paciotti V., Clerici M., Lucchini G., Longhese M.P.;
"The checkpoint protein Ddc2, functionally related to S. pombe Rad26,
interacts with Mec1 and is regulated by Mec1-dependent phosphorylation
in budding yeast.";
Genes Dev. 14:2046-2059(2000).
[10]
FUNCTION.
PubMed=11140636; DOI=10.1038/35050000;
Downs J.A., Lowndes N.F., Jackson S.P.;
"A role for Saccharomyces cerevisiae histone H2A in DNA repair.";
Nature 408:1001-1004(2000).
[11]
IDENTIFICATION AS A KINASE, FUNCTION, AND MUTAGENESIS OF ASP-2224 AND
ASN-2229.
PubMed=11095737; DOI=10.1073/pnas.250475697;
Mallory J.C., Petes T.D.;
"Protein kinase activity of Tel1p and Mec1p, two Saccharomyces
cerevisiae proteins related to the human ATM protein kinase.";
Proc. Natl. Acad. Sci. U.S.A. 97:13749-13754(2000).
[12]
FUNCTION, INTERACTION WITH LCD1, PHOSPHORYLATION OF LCD1, AND
MUTAGENESIS OF VAL-225; SER-552; LEU-781; PHE-1179; ASN-1700; ASP-2224
AND ASP-2243.
PubMed=11359899; DOI=10.1128/MCB.21.12.3913-3925.2001;
Paciotti V., Clerici M., Scotti M., Lucchini G., Longhese M.P.;
"Characterization of mec1 kinase-deficient mutants and of new
hypomorphic mec1 alleles impairing subsets of the DNA damage response
pathway.";
Mol. Cell. Biol. 21:3913-3925(2001).
[13]
FUNCTION.
PubMed=12181334; DOI=10.1091/mbc.02-02-0012;
Enomoto S., Glowczewski L., Berman J.;
"MEC3, MEC1, and DDC2 are essential components of a telomere
checkpoint pathway required for cell cycle arrest during senescence in
Saccharomyces cerevisiae.";
Mol. Biol. Cell 13:2626-2638(2002).
[14]
FUNCTION.
PubMed=12792653; DOI=10.1038/sj.embor.embor871;
Redon C., Pilch D.R., Rogakou E.P., Orr A.H., Lowndes N.F.,
Bonner W.M.;
"Yeast histone 2A serine 129 is essential for the efficient repair of
checkpoint-blind DNA damage.";
EMBO Rep. 4:678-684(2003).
[15]
FUNCTION.
PubMed=15369670; DOI=10.1016/j.cell.2004.08.015;
Lisby M., Barlow J.H., Burgess R.C., Rothstein R.;
"Choreography of the DNA damage response: spatiotemporal relationships
among checkpoint and repair proteins.";
Cell 118:699-713(2004).
[16]
FUNCTION.
PubMed=15458641; DOI=10.1016/j.cub.2004.09.047;
Shroff R., Arbel-Eden A., Pilch D.R., Ira G., Bonner W.M.,
Petrini J.H.J., Haber J.E., Lichten M.;
"Distribution and dynamics of chromatin modification induced by a
defined DNA double-strand break.";
Curr. Biol. 14:1703-1711(2004).
[17]
PHOSPHORYLATION OF RTT107.
PubMed=14988729; DOI=10.1038/sj.emboj.7600129;
Rouse J.;
"Esc4p, a new target of Mec1p (ATR), promotes resumption of DNA
synthesis after DNA damage.";
EMBO J. 23:1188-1197(2004).
[18]
FUNCTION, AND PHOSPHORYLATION OF SLX4.
PubMed=15975089; DOI=10.1042/BJ20050768;
Flott S., Rouse J.;
"Slx4 becomes phosphorylated after DNA damage in a Mec1/Tel1-dependent
manner and is required for repair of DNA alkylation damage.";
Biochem. J. 391:325-333(2005).
[19]
FUNCTION OF THE MEC1-LCD1 COMPLEX, AND PHOSPHORYLATION OF LCD1 AND
RAD53.
PubMed=16365046; DOI=10.1074/jbc.M507508200;
Ma J.-L., Lee S.-J., Duong J.K., Stern D.F.;
"Activation of the checkpoint kinase Rad53 by the phosphatidyl
inositol kinase-like kinase Mec1.";
J. Biol. Chem. 281:3954-3963(2006).
[20]
FUNCTION, INTERACTION WITH LCD1; RFA1 AND RFA2, AND MUTAGENESIS OF
2360-MET--ILE-2362 AND 2367-PHE-TRP-2368.
PubMed=16148046; DOI=10.1091/mbc.E05-05-0405;
Nakada D., Hirano Y., Tanaka Y., Sugimoto K.;
"Role of the C-terminus of Mec1 checkpoint kinase in its localization
to sites of DNA damage.";
Mol. Biol. Cell 16:5227-5235(2005).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
-!- FUNCTION: 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. {ECO:0000269|PubMed:11095737,
ECO:0000269|PubMed:11140636, ECO:0000269|PubMed:11359899,
ECO:0000269|PubMed:12181334, ECO:0000269|PubMed:12792653,
ECO:0000269|PubMed:15369670, ECO:0000269|PubMed:15458641,
ECO:0000269|PubMed:15975089, ECO:0000269|PubMed:16148046,
ECO:0000269|PubMed:16365046, ECO:0000269|PubMed:8065923,
ECO:0000269|PubMed:8553072}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Interacts with LCD1, which is required for localization
MEC1 to the RPA complex. Interacts directly with the RPA subunits
RFA1 and RFA2. {ECO:0000269|PubMed:10950868,
ECO:0000269|PubMed:11060031, ECO:0000269|PubMed:11359899,
ECO:0000269|PubMed:16148046}.
-!- INTERACTION:
P47027:DPB11; NbExp=3; IntAct=EBI-6668, EBI-25984;
Q04377:LCD1; NbExp=8; IntAct=EBI-6668, EBI-35652;
-!- SUBCELLULAR LOCATION: 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.
-!- DEVELOPMENTAL STAGE: Induced during meiosis.
-!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
{ECO:0000305}.
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EMBL; X75891; CAA53494.1; -; Genomic_DNA.
EMBL; U31109; AAA74482.1; -; Genomic_DNA.
EMBL; D11088; BAA01860.1; -; Genomic_DNA.
EMBL; Z36005; CAA85094.1; -; Genomic_DNA.
EMBL; BK006936; DAA07252.1; -; Genomic_DNA.
PIR; S46005; S46005.
RefSeq; NP_009694.3; NM_001178484.3.
PDB; 5X6O; EM; 3.90 A; C=1-2368.
PDBsum; 5X6O; -.
ProteinModelPortal; P38111; -.
SMR; P38111; -.
BioGrid; 32836; 356.
DIP; DIP-799N; -.
IntAct; P38111; 23.
MINT; P38111; -.
STRING; 4932.YBR136W; -.
iPTMnet; P38111; -.
MaxQB; P38111; -.
PaxDb; P38111; -.
PRIDE; P38111; -.
EnsemblFungi; YBR136W; YBR136W; YBR136W.
GeneID; 852433; -.
KEGG; sce:YBR136W; -.
EuPathDB; FungiDB:YBR136W; -.
SGD; S000000340; MEC1.
GeneTree; ENSGT00830000128321; -.
HOGENOM; HOG000034220; -.
InParanoid; P38111; -.
KO; K02543; -.
OMA; WRRFPEH; -.
OrthoDB; EOG092C00SN; -.
BioCyc; YEAST:G3O-29090-MONOMER; -.
Reactome; R-SCE-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
PRO; PR:P38111; -.
Proteomes; UP000002311; Chromosome II.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; IDA:SGD.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0006975; P:DNA damage induced protein phosphorylation; IMP:SGD.
GO; GO:0006310; P:DNA recombination; IMP:SGD.
GO; GO:0006281; P:DNA repair; IBA:GO_Central.
GO; GO:0006260; P:DNA replication; IMP:SGD.
GO; GO:0016572; P:histone phosphorylation; IMP:SGD.
GO; GO:0006139; P:nucleobase-containing compound metabolic process; IGI:SGD.
GO; GO:2000105; P:positive regulation of DNA-dependent DNA replication; IMP:SGD.
GO; GO:0007131; P:reciprocal meiotic recombination; IMP:SGD.
GO; GO:0000723; P:telomere maintenance; IDA:SGD.
GO; GO:0000722; P:telomere maintenance via recombination; IGI:SGD.
Gene3D; 1.10.1070.11; -; 1.
Gene3D; 1.25.40.10; -; 1.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR003152; FATC_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000403; PI3/4_kinase_cat_dom.
InterPro; IPR036940; PI3/4_kinase_cat_sf.
InterPro; IPR018936; PI3/4_kinase_CS.
InterPro; IPR003151; PIK-rel_kinase_FAT.
InterPro; IPR014009; PIK_FAT.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR012993; UME.
Pfam; PF02259; FAT; 1.
Pfam; PF02260; FATC; 1.
Pfam; PF00454; PI3_PI4_kinase; 1.
Pfam; PF08064; UME; 1.
SMART; SM01343; FATC; 1.
SMART; SM00146; PI3Kc; 1.
SMART; SM00802; UME; 1.
SUPFAM; SSF48371; SSF48371; 3.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS51189; FAT; 1.
PROSITE; PS51190; FATC; 1.
PROSITE; PS00915; PI3_4_KINASE_1; 1.
PROSITE; PS00916; PI3_4_KINASE_2; 1.
PROSITE; PS50290; PI3_4_KINASE_3; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Chromatin regulator; Complete proteome;
DNA damage; DNA repair; Kinase; Meiosis; Nucleotide-binding; Nucleus;
Reference proteome; Serine/threonine-protein kinase; Transferase.
CHAIN 1 2368 Serine/threonine-protein kinase MEC1.
/FTId=PRO_0000088836.
DOMAIN 1399 1944 FAT. {ECO:0000255|PROSITE-
ProRule:PRU00534}.
DOMAIN 2082 2368 PI3K/PI4K. {ECO:0000255|PROSITE-
ProRule:PRU00269}.
DOMAIN 2336 2368 FATC. {ECO:0000255|PROSITE-
ProRule:PRU00534, ECO:0000255|PROSITE-
ProRule:PRU00535}.
REGION 2140 2368 Binding to the RPA complex.
MUTAGEN 225 225 V->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.
{ECO:0000269|PubMed:11359899}.
MUTAGEN 552 552 S->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.
{ECO:0000269|PubMed:11359899}.
MUTAGEN 781 781 L->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.
{ECO:0000269|PubMed:11359899}.
MUTAGEN 1179 1179 F->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.
{ECO:0000269|PubMed:11359899}.
MUTAGEN 1700 1700 N->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.
{ECO:0000269|PubMed:11359899}.
MUTAGEN 2224 2224 D->A: Impairs kinase activity; when
associated with K-2229.
{ECO:0000269|PubMed:11095737,
ECO:0000269|PubMed:11359899}.
MUTAGEN 2229 2229 N->K: Impairs kinase activity; when
associated with A-2224.
{ECO:0000269|PubMed:11095737}.
MUTAGEN 2243 2243 D->E: Impairs kinase activity.
{ECO:0000269|PubMed:11359899}.
MUTAGEN 2360 2362 MYI->AAA: In MEC1-85; disrupts
interaction with RFA1 and severely
impairs kinase activity.
{ECO:0000269|PubMed:16148046}.
MUTAGEN 2367 2368 FW->AA: In MEC1-87; decreases the level
of MEC1 and impairs viability.
{ECO:0000269|PubMed:16148046}.
CONFLICT 197 197 N -> D (in Ref. 1; BAA01860).
{ECO:0000305}.
CONFLICT 716 716 S -> P (in Ref. 2; AAA74482).
{ECO:0000305}.
CONFLICT 1255 1255 K -> Q (in Ref. 2; AAA74482).
{ECO:0000305}.
CONFLICT 1276 1276 L -> G (in Ref. 2; AAA74482).
{ECO:0000305}.
SEQUENCE 2368 AA; 273342 MW; C06AEF9F0484A615 CRC64;
MESHVKYLDE LILAIKDLNS GVDSKVQIKK VPTDPSSSQE YAKSLKILNT LIRNLKDQRR
NNIMKNDTIF SKTVSALALL LEYNPFLLVM KDSNGNFEIQ RLIDDFLNIS VLNYDNYHRI
WFMRRKLGSW CKACVEFYGK PAKFQLTAHF ENTMNLYEQA LTEVLLGKTE LLKFYDTLKG
LYILLYWFTS EYSTFGNSIA FLDSSLGFTK FDFNFQRLIR IVLYVFDSCE LAALEYAEIQ
LKYISLVVDY VCNRTISTAL DAPALVCCEQ LKFVLTTMHH FLDNKYGLLD NDPTMAKGIL
RLYSLCISND FSKCFVDHFP IDQWADFSQS EHFPFTQLTN KALSIVYFDL KRRSLPVEAL
KYDNKFNIWV YQSEPDSSLK NVTSPFDDRY KQLEKLRLLV LKKFNKTERG TLLKYRVNQL
SPGFFQRAGN DFKLILNEAS VSIQTCFKTN NITRLTSWTV ILGRLACLES EKFSGTLPNS
TKDMDNWYVC HLCDIEKTGN PFVRINPNRP EAAGKSEIFR ILHSNFLSHP NIDEFSESLL
SGILFSLHRI FSHFQPPKLT DGNGQINKSF KLVQKCFMNS NRYLRLLSTR IIPLFNISDS
HNSEDEHTAT LIKFLQSQKL PVVKENLVIA WTQLTLTTSN DVFDTLLLKL IDIFNSDDYS
LRIMMTLQIK NMAKILKKTP YQLLSPILPV LLRQLGKNLV ERKVGFQNLI ELLGYSSKTI
LDIFQRYIIP YAIIQYKSDV LSEIAKIMCD GDTSLINQMK VNLLKKNSRQ IFAVALVKHG
LFSLDILETL FLNRAPTFDK GYITAYLPDY KTLAEITKLY KNSVTKDASD SENANMILCS
LRFLITNFEK DKRHGSKYKN INNWTDDQEQ AFQKKLQDNI LGIFQVFSSD IHDVEGRTTY
YEKLRVINGI SFLIIYAPKK SIISALAQIS ICLQTGLGLK EVRYEAFRCW HLLVRHLNDE
ELSTVIDSLI AFILQKWSEF NGKLRNIVYS ILDTLIKEKS DLILKLKPYT TLALVGKPEL
GILARDGQFA RMVNKIRSTT DLIPIFANNL KSSNKYVINQ NLDDIEVYLR RKQTERSIDF
TPKKVGQTSD ITLVLGALLD TSHKFRNLDK DLCEKCAKCI SMIGVLDVTK HEFKRTTYSE
NEVYDLNDSV QTIKFLIWVI NDILVPAFWQ SENPSKQLFV ALVIQESLKY CGLSSESWDM
NHKELYPNEA KLWEKFNSVS KTTIYPLLSS LYLAQSWKEY VPLKYPSNNF KEGYKIWVKR
FTLDLLKTGT TENHPLHVFS SLIREDDGSL SNFLLPYISL DIIIKAEKGT PYADILNGII
IEFDSIFTCN LEGMNNLQVD SLRMCYESIF RVFEYCKKWA TEFKQNYSKL HGTFIIKDTK
TTNMLLRIDE FLRTTPSDLL AQRSLETDSF ERSALYLEQC YRQNPHDKNQ NGQLLKNLQI
TYEEIGDIDS LDGVLRTFAT GNLVSKIEEL QYSENWKLAQ DCFNVLGKFS DDPKTTTRML
KSMYDHQLYS QIISNSSFHS SDGKISLSPD VKEWYSIGLE AANLEGNVQT LKNWVEQIES
LRNIDDREVL LQYNIAKALI AISNEDPLRT QKYIHNSFRL IGTNFITSSK ETTLLKKQNL
LMKLHSLYDL SFLSSAKDKF EYKSNTTILD YRMERIGADF VPNHYILSMR KSFDQLKMNE
QADADLGKTF FTLAQLARNN ARLDIASESL MHCLERRLPQ AELEFAEILW KQGENDRALK
IVQEIHEKYQ ENSSVNARDR AAVLLKFTEW LDLSNNSASE QIIKQYQDIF QIDSKWDKPY
YSIGLYYSRL LERKKAEGYI TNGRFEYRAI SYFLLAFEKN TAKVRENLPK VITFWLDIAA
ASISEAPGNR KEMLSKATED ICSHVEEALQ HCPTYIWYFV LTQLLSRLLH SHQSSAQIIM
HILLSLAVEY PSHILWYITA LVNSNSSKRV LRGKHILEKY RQHSQNPHDL VSSALDLTKA
LTRVCLQDVK SITSRSGKSL EKDFKFDMNV APSAMVVPVR KNLDIISPLE SNSMRGYQPF
RPVVSIIRFG SSYKVFSSLK KPKQLNIIGS DGNIYGIMCK KEDVRQDNQY MQFATTMDFL
LSKDIASRKR SLGINIYSVL SLREDCGILE MVPNVVTLRS ILSTKYESLK IKYSLKSLHD
RWQHTAVDGK LEFYMEQVDK FPPILYQWFL ENFPDPINWF NARNTYARSY AVMAMVGHIL
GLGDRHCENI LLDIQTGKVL HVDFDCLFEK GKRLPVPEIV PFRLTPNLLD ALGIIGTEGT
FKKSSEVTLA LMRKNEVALM NVIETIMYDR NMDHSIQKAL KVLRNKIRGI DPQDGLVLSV
AGQTETLIQE ATSEDNLSKM YIGWLPFW


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E1119d Mouse ELISA Kit FOR Mitotic checkpoint serine per threonine-protein kinase BUB1 beta 96T
BUB1B_HUMAN Human ELISA Kit FOR Mitotic checkpoint serine per threonine-protein kinase BUB1 beta 96T
CSB-EL002883MO Mouse Mitotic checkpoint serine per threonine-protein kinase BUB1 beta(BUB1B) ELISA kit 96T
BUB1B_MOUSE ELISA Kit FOR Mitotic checkpoint serine per threonine-protein kinase BUB1 beta; organism: Mouse; gene name: Bub1b 96T
BUB1_MOUSE ELISA Kit FOR Mitotic checkpoint serine per threonine-protein kinase BUB1; organism: Mouse; gene name: Bub1 96T
EIAAB33643 Cell cycle checkpoint protein RAD1,DNA repair exonuclease rad1 homolog,Homo sapiens,hRAD1,Human,RAD1,Rad1-like DNA damage checkpoint protein,REC1
EIAAB33644 Cell cycle checkpoint protein RAD1,DNA repair exonuclease rad1 homolog,Mouse,mRAD1,Mus musculus,Rad1,Rad1-like DNA damage checkpoint protein,Rec1
EIAAB31334 Bos taurus,Bovine,PKN,PKN1,PRK1,PRKCL1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein kinase PKN-alpha,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine
EIAAB31332 Mouse,Mus musculus,Pkn,Pkn1,Prk1,Prkcl1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine protein kinase N
LF-MA0267 anti-Chk2 (Checkpoint kinase 2) (31A2), Mouse monoclonal to Chk2 (Checkpoint kinase 2), Isotype IgG1, Host Mouse 100 ul
LF-MA0266 anti-Chk2 (Checkpoint kinase 2) (20A8), Mouse monoclonal to Chk2 (Checkpoint kinase 2), Isotype IgG1, Host Mouse 100 ul
LF-PA0059 anti-Chk1(Checkpoint kinase 1) , Rabbit polyclonal to Chk1(Checkpoint kinase 1) , Isotype IgG, Host Rabbit 100 ul
GWB-5BE1E2 Serine threonine-protein kinase SNF1-like kinase 2 (SNF1LK2) Salt-inducible protein kinase 2 (SIK2) Mouse anti-Human Monoclonal
GWB-CEE83D Serine threonine-protein kinase SNF1-like kinase 2 (SNF1LK2) Salt-inducible protein kinase 2 (SIK2) Rabbit anti-Human Polyclonal
LF-PA41523 anti-Mitotic Checkpoint Kinase BUB1, Rabbit polyclonal to Mitotic Checkpoint Kinase BUB1, Isotype IgG, Host Rabbit 50 ug
27-724 Checkpoint suppressor 1 is a member of the forkhead_winged helix transcription factor family. Checkpoints are eukaryotic DNA damage-inducible cell cycle arrests at G1 and G2. Checkpoint suppressor 1 s 0.1 mg
20-373-85037 Checkpoint serine_threonine-protein kinase BUB1 - EC 2.7.11.1 Monoclonal 0.05 ml
20-373-85007 Checkpoint serine_threonine-protein kinase BUB1 - EC 2.7.11.1 Monoclonal 0.1 ml
CCD23_BOVIN Mouse ELISA Kit FOR Serine per threonine-protein kinase PRP4 homolog 96T
TM141_MOUSE Mouse ELISA Kit FOR Serine per threonine-protein kinase PRP4 homolog 96T
H0317 Serine threonine-protein kinase PRP4 homolog (PRPF4B), Rat, ELISA Kit 96T
E0071m Mouse ELISA Kit FOR Serine per threonine-protein kinase PRP4 homolog 96T
PRP4B_HUMAN Human ELISA Kit FOR Serine per threonine-protein kinase PRP4 homolog 96T
H0315 Serine threonine-protein kinase PRP4 homolog (PRPF4B), Human, ELISA Kit 96T
H0316 Serine threonine-protein kinase PRP4 homolog (PRPF4B), Mouse, ELISA Kit 96T


 

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