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DNA replication licensing factor MCM2 (EC 3.6.4.12) (Minichromosome maintenance protein 2 homolog) (Nuclear protein BM28)

 MCM2_HUMAN              Reviewed;         904 AA.
P49736; Q14577; Q15023; Q8N2V1; Q969W7; Q96AE1; Q9BRM7;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
16-JAN-2004, sequence version 4.
20-JUN-2018, entry version 201.
RecName: Full=DNA replication licensing factor MCM2;
EC=3.6.4.12;
AltName: Full=Minichromosome maintenance protein 2 homolog;
AltName: Full=Nuclear protein BM28;
Name=MCM2; Synonyms=BM28, CCNL1, CDCL1, KIAA0030;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
VARIANT GLN-166.
TISSUE=Colon carcinoma;
PubMed=8175912;
Todorov I.T., Pepperkok R., Philipova R.N., Kearsey S.E., Ansorge W.,
Werner D.;
"A human nuclear protein with sequence homology to a family of early S
phase proteins is required for entry into S phase and for cell
division.";
J. Cell Sci. 107:253-265(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Bone marrow;
PubMed=7584026; DOI=10.1093/dnares/1.1.27;
Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y.,
Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.;
"Prediction of the coding sequences of unidentified human genes. I.
The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by
analysis of randomly sampled cDNA clones from human immature myeloid
cell line KG-1.";
DNA Res. 1:27-35(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-68; PHE-135;
THR-396; MET-667 AND THR-727.
NIEHS SNPs program;
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-501 AND
THR-727.
TISSUE=Brain, Lung, Lymph, Muscle, Placenta, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 2-904.
TISSUE=Cervix carcinoma;
Mimura S., Nishimoto S., Kubota Y., Takisawa H., Nojima H.;
"Homo sapiens DNA replication licensing factor (huMCM2).";
Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-904.
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[7]
CHROMOSOMAL LOCATION.
PubMed=8258304;
Mincheva A., Todorov I.T., Werner D., Fink T.M., Lichter P.;
"The human gene for nuclear protein BM28 (CDCL1), a new member of the
early S-phase family of proteins, maps to chromosome band 3q21.";
Cytogenet. Cell Genet. 65:276-277(1994).
[8]
IDENTIFICATION IN THE MCM2-7 COMPLEX.
PubMed=9305914; DOI=10.1074/jbc.272.39.24508;
Ishimi Y.;
"A DNA helicase activity is associated with an MCM4, -6, and -7
protein complex.";
J. Biol. Chem. 272:24508-24513(1997).
[9]
INTERACTION WITH MCM10.
PubMed=11095689; DOI=10.1093/nar/28.23.4769;
Izumi M., Yanagi K., Mizuno T., Yokoi M., Kawasaki Y., Moon K.Y.,
Hurwitz J., Yatagai F., Hanaoka F.;
"The human homolog of Saccharomyces cerevisiae Mcm10 interacts with
replication factors and dissociates from nuclease-resistant nuclear
structures in G(2) phase.";
Nucleic Acids Res. 28:4769-4777(2000).
[10]
PHOSPHORYLATION AT SER-108, AND MUTAGENESIS OF SER-108.
PubMed=15210935; DOI=10.1073/pnas.0403410101;
Cortez D., Glick G., Elledge S.J.;
"Minichromosome maintenance proteins are direct targets of the ATM and
ATR checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 101:10078-10083(2004).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[12]
PHOSPHORYLATION AT SER-27; SER-41; SER-53; SER-108 AND SER-139,
MUTAGENESIS OF SER-27; SER-41 AND SER-139, IDENTIFICATION IN THE
MCM2-7 COMPLEX, AND ATPASE ACTIVITY OF THE MCM2-7 COMPLEX.
PubMed=16899510; DOI=10.1091/mbc.E06-03-0241;
Tsuji T., Ficarro S.B., Jiang W.;
"Essential role of phosphorylation of MCM2 by Cdc7/Dbf4 in the
initiation of DNA replication in mammalian cells.";
Mol. Biol. Cell 17:4459-4472(2006).
[13]
INTERACTION WITH KAT7.
PubMed=16387653; DOI=10.1016/j.molcel.2005.12.007;
Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W.,
Lane W.S., Tan S., Yang X.-J., Cote J.;
"ING tumor suppressor proteins are critical regulators of chromatin
acetylation required for genome expression and perpetuation.";
Mol. Cell 21:51-64(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-41, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Prostate cancer;
PubMed=17487921; DOI=10.1002/elps.200600782;
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
"Toward a global characterization of the phosphoproteome in prostate
cancer cells: identification of phosphoproteins in the LNCaP cell
line.";
Electrophoresis 28:2027-2034(2007).
[16]
PHOSPHORYLATION AT SER-40 AND SER-53.
PubMed=17062569; DOI=10.1074/jbc.M604457200;
Tenca P., Brotherton D., Montagnoli A., Rainoldi S., Albanese C.,
Santocanale C.;
"Cdc7 is an active kinase in human cancer cells undergoing replication
stress.";
J. Biol. Chem. 282:208-215(2007).
[17]
IDENTIFICATION IN THE MCM2-7 COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=17296731; DOI=10.1128/MCB.02384-06;
Sakwe A.M., Nguyen T., Athanasopoulos V., Shire K., Frappier L.;
"Identification and characterization of a novel component of the human
minichromosome maintenance complex.";
Mol. Cell. Biol. 27:3044-3055(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; THR-39; SER-40;
SER-41; SER-53 AND SER-139, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; THR-59; SER-108 AND
SER-139, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[25]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-216, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[26]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-13; SER-27; SER-41; SER-108 AND SER-139,
CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[28]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-13; SER-26; SER-27; SER-41; SER-139 AND
SER-381, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[29]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[30]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; THR-25; SER-26;
SER-27; SER-32; SER-40; SER-41; SER-139 AND SER-484, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-27; TYR-137 AND
SER-139, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[33]
FUNCTION, INVOLVEMENT IN DFNA70, VARIANT DFNA70 CYS-44, AND
CHARACTERIZATION OF VARIANT DFNA70 CYS-44.
PubMed=26196677; DOI=10.1371/journal.pone.0133522;
Gao J., Wang Q., Dong C., Chen S., Qi Y., Liu Y.;
"Whole exome sequencing identified MCM2 as a novel causative gene for
autosomal dominant nonsyndromic deafness in a chinese family.";
PLoS ONE 10:E0133522-E0133534(2015).
[34]
INTERACTION WITH DONSON.
PubMed=28191891; DOI=10.1038/ng.3790;
Reynolds J.J., Bicknell L.S., Carroll P., Higgs M.R., Shaheen R.,
Murray J.E., Papadopoulos D.K., Leitch A., Murina O., Tarnauskaite Z.,
Wessel S.R., Zlatanou A., Vernet A., von Kriegsheim A., Mottram R.M.,
Logan C.V., Bye H., Li Y., Brean A., Maddirevula S., Challis R.C.,
Skouloudaki K., Almoisheer A., Alsaif H.S., Amar A., Prescott N.J.,
Bober M.B., Duker A., Faqeih E., Seidahmed M.Z., Al Tala S.,
Alswaid A., Ahmed S., Al-Aama J.Y., Altmueller J., Al Balwi M.,
Brady A.F., Chessa L., Cox H., Fischetto R., Heller R.,
Henderson B.D., Hobson E., Nuernberg P., Percin E.F., Peron A.,
Spaccini L., Quigley A.J., Thakur S., Wise C.A., Yoon G., Alnemer M.,
Tomancak P., Yigit G., Taylor A.M., Reijns M.A., Simpson M.A.,
Cortez D., Alkuraya F.S., Mathew C.G., Jackson A.P., Stewart G.S.;
"Mutations in DONSON disrupt replication fork stability and cause
microcephalic dwarfism.";
Nat. Genet. 49:537-549(2017).
[35]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-178, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Acts as component of the MCM2-7 complex (MCM complex)
which is the putative replicative helicase essential for 'once per
cell cycle' DNA replication initiation and elongation in
eukaryotic cells. The active ATPase sites in the MCM2-7 ring are
formed through the interaction surfaces of two neighboring
subunits such that a critical structure of a conserved arginine
finger motif is provided in trans relative to the ATP-binding site
of the Walker A box of the adjacent subunit. The six ATPase active
sites, however, are likely to contribute differentially to the
complex helicase activity. Required for the entry in S phase and
for cell division. Plays a role in terminally differentiated hair
cells development of the cochlea and induces cells apoptosis.
{ECO:0000269|PubMed:26196677, ECO:0000269|PubMed:8175912}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: Component of the MCM2-7 complex. The complex forms a
toroidal hexameric ring with the proposed subunit order MCM2-MCM6-
MCM4-MCM7-MCM3-MCM5 (Probable). Interacts with DBF4 (By
similarity). Interacts with KAT7. May interact with MCM10.
Component of the replisome complex composed of at least DONSON,
MCM2, MCM7, PCNA and TICRR (PubMed:28191891). {ECO:0000250,
ECO:0000269|PubMed:11095689, ECO:0000269|PubMed:16387653,
ECO:0000269|PubMed:16899510, ECO:0000269|PubMed:17296731,
ECO:0000269|PubMed:28191891, ECO:0000269|PubMed:9305914,
ECO:0000305}.
-!- INTERACTION:
O43823:AKAP8; NbExp=7; IntAct=EBI-374819, EBI-1237481;
Q9Y294:ASF1A; NbExp=7; IntAct=EBI-374819, EBI-749553;
O75419:CDC45; NbExp=2; IntAct=EBI-374819, EBI-374969;
P49450:CENPA; NbExp=3; IntAct=EBI-374819, EBI-1751979;
P68431:HIST1H3D; NbExp=5; IntAct=EBI-374819, EBI-79722;
P62805:HIST2H4B; NbExp=8; IntAct=EBI-374819, EBI-302023;
Q9Y468:L3MBTL1; NbExp=2; IntAct=EBI-374819, EBI-1265089;
P25205:MCM3; NbExp=6; IntAct=EBI-374819, EBI-355153;
P33992:MCM5; NbExp=5; IntAct=EBI-374819, EBI-359410;
Q14566:MCM6; NbExp=14; IntAct=EBI-374819, EBI-374900;
P33993:MCM7; NbExp=21; IntAct=EBI-374819, EBI-355924;
Q9BTE3:MCMBP; NbExp=4; IntAct=EBI-374819, EBI-749378;
P53350:PLK1; NbExp=2; IntAct=EBI-374819, EBI-476768;
Q96H20:SNF8; NbExp=8; IntAct=EBI-374819, EBI-747719;
Q9NYB0:TERF2IP; NbExp=2; IntAct=EBI-374819, EBI-750109;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8175912}.
-!- PTM: Phosphorylated on Ser-108 by ATR in proliferating cells. Ser-
108 proliferation is increased by genotoxic agents. Ser-40 is
mediated by the CDC7-DBF4 and CDC7-DBF4B complexes, while Ser-53
phosphorylation is only mediated by the CDC7-DBF4 complex.
Phosphorylation by the CDC7-DBF4 complex during G1/S phase is
required for the initiation of DNA replication.
{ECO:0000269|PubMed:15210935, ECO:0000269|PubMed:16899510,
ECO:0000269|PubMed:17062569}.
-!- DISEASE: Deafness, autosomal dominant, 70 (DFNA70) [MIM:616968]: A
form of non-syndromic sensorineural hearing loss. Sensorineural
deafness results from damage to the neural receptors of the inner
ear, the nerve pathways to the brain, or the area of the brain
that receives sound information. DFNA70 is characterized by slowly
progressive, postlingual hearing impairment.
{ECO:0000269|PubMed:26196677}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Early fractionation of eukaryotic MCM proteins
yielded a variety of dimeric, trimeric and tetrameric complexes
with unclear biological significance. Specifically a MCM467
subcomplex is shown to have in vitro helicase activity which is
inhibited by the MCM2 subunit. The MCM2-7 hexamer is the proposed
physiological active complex.
-!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA04642.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAA12177.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA47749.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAA47749.1; Type=Frameshift; Positions=115, 124, 127, 129, 154, 158, 773, 811; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/mcm2/";
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EMBL; X67334; CAA47749.1; ALT_SEQ; mRNA.
EMBL; D21063; BAA04642.1; ALT_INIT; mRNA.
EMBL; AY675259; AAT70723.1; -; Genomic_DNA.
EMBL; BC006165; AAH06165.3; -; mRNA.
EMBL; BC007670; AAH07670.2; -; mRNA.
EMBL; BC007938; AAH07938.2; -; mRNA.
EMBL; BC014272; AAH14272.2; -; mRNA.
EMBL; BC017258; AAH17258.2; -; mRNA.
EMBL; BC017490; AAH17490.2; -; mRNA.
EMBL; BC030131; AAH30131.2; -; mRNA.
EMBL; D83987; BAA12177.1; ALT_INIT; mRNA.
EMBL; BT009734; AAP88736.1; -; mRNA.
CCDS; CCDS3043.1; -.
PIR; S42228; S42228.
RefSeq; NP_004517.2; NM_004526.3.
UniGene; Hs.477481; -.
PDB; 4UUZ; X-ray; 2.90 A; C=69-138.
PDB; 5BNV; X-ray; 2.79 A; C/F=61-130.
PDB; 5BNX; X-ray; 2.31 A; C=61-130.
PDB; 5BO0; X-ray; 2.91 A; C=61-130.
PDB; 5C3I; X-ray; 3.50 A; D/H/L/P/T/X=63-124.
PDB; 5JA4; X-ray; 2.42 A; C=61-130.
PDBsum; 4UUZ; -.
PDBsum; 5BNV; -.
PDBsum; 5BNX; -.
PDBsum; 5BO0; -.
PDBsum; 5C3I; -.
PDBsum; 5JA4; -.
ProteinModelPortal; P49736; -.
SMR; P49736; -.
BioGrid; 110339; 944.
ComplexPortal; CPX-2940; MCM complex.
CORUM; P49736; -.
DIP; DIP-31732N; -.
ELM; P49736; -.
IntAct; P49736; 67.
MINT; P49736; -.
STRING; 9606.ENSP00000265056; -.
iPTMnet; P49736; -.
PhosphoSitePlus; P49736; -.
SwissPalm; P49736; -.
DMDM; 41019490; -.
EPD; P49736; -.
MaxQB; P49736; -.
PaxDb; P49736; -.
PeptideAtlas; P49736; -.
PRIDE; P49736; -.
ProteomicsDB; 56058; -.
DNASU; 4171; -.
Ensembl; ENST00000265056; ENSP00000265056; ENSG00000073111.
GeneID; 4171; -.
KEGG; hsa:4171; -.
UCSC; uc003ejp.5; human.
CTD; 4171; -.
DisGeNET; 4171; -.
EuPathDB; HostDB:ENSG00000073111.13; -.
GeneCards; MCM2; -.
HGNC; HGNC:6944; MCM2.
HPA; CAB000303; -.
HPA; HPA031495; -.
HPA; HPA031496; -.
MalaCards; MCM2; -.
MIM; 116945; gene.
MIM; 616968; phenotype.
neXtProt; NX_P49736; -.
OpenTargets; ENSG00000073111; -.
PharmGKB; PA164742061; -.
eggNOG; KOG0477; Eukaryota.
eggNOG; COG1241; LUCA.
GeneTree; ENSGT00920000149148; -.
HOVERGEN; HBG106398; -.
InParanoid; P49736; -.
KO; K02540; -.
OMA; KYDCVKC; -.
OrthoDB; EOG091G026H; -.
PhylomeDB; P49736; -.
TreeFam; TF300772; -.
Reactome; R-HSA-176187; Activation of ATR in response to replication stress.
Reactome; R-HSA-176974; Unwinding of DNA.
Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
Reactome; R-HSA-68949; Orc1 removal from chromatin.
Reactome; R-HSA-68962; Activation of the pre-replicative complex.
Reactome; R-HSA-69052; Switching of origins to a post-replicative state.
SIGNOR; P49736; -.
ChiTaRS; MCM2; human.
GeneWiki; MCM2; -.
GenomeRNAi; 4171; -.
PMAP-CutDB; P49736; -.
PRO; PR:P49736; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000073111; -.
CleanEx; HS_CCNL1; -.
CleanEx; HS_MCM2; -.
ExpressionAtlas; P49736; baseline and differential.
Genevisible; P49736; HS.
GO; GO:0000785; C:chromatin; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0042555; C:MCM complex; IDA:UniProtKB.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
GO; GO:0000784; C:nuclear chromosome, telomeric region; HDA:BHF-UCL.
GO; GO:0005664; C:nuclear origin of replication recognition complex; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0003688; F:DNA replication origin binding; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0042393; F:histone binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
GO; GO:0090102; P:cochlea development; IMP:UniProtKB.
GO; GO:0006260; P:DNA replication; TAS:Reactome.
GO; GO:0006270; P:DNA replication initiation; IMP:UniProtKB.
GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:Ensembl.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
GO; GO:1905775; P:negative regulation of DNA helicase activity; IEA:InterPro.
GO; GO:0006334; P:nucleosome assembly; IEA:Ensembl.
InterPro; IPR031327; MCM.
InterPro; IPR008045; MCM2.
InterPro; IPR018525; MCM_CS.
InterPro; IPR001208; MCM_dom.
InterPro; IPR027925; MCM_N.
InterPro; IPR033762; MCM_OB.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR11630; PTHR11630; 1.
PANTHER; PTHR11630:SF44; PTHR11630:SF44; 1.
Pfam; PF00493; MCM; 1.
Pfam; PF12619; MCM2_N; 1.
Pfam; PF14551; MCM_N; 1.
Pfam; PF17207; MCM_OB; 1.
PRINTS; PR01657; MCMFAMILY.
PRINTS; PR01658; MCMPROTEIN2.
SMART; SM00350; MCM; 1.
SUPFAM; SSF50249; SSF50249; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00847; MCM_1; 1.
PROSITE; PS50051; MCM_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Cell cycle; Complete proteome;
Deafness; Disease mutation; DNA replication; DNA-binding; Helicase;
Hydrolase; Isopeptide bond; Metal-binding; Non-syndromic deafness;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
CHAIN 2 904 DNA replication licensing factor MCM2.
/FTId=PRO_0000194087.
DOMAIN 473 679 MCM.
ZN_FING 329 355 C4-type. {ECO:0000255}.
NP_BIND 523 530 ATP. {ECO:0000255}.
REGION 2 257 Interaction with KAT7. {ECO:0000250}.
MOTIF 655 658 Arginine finger.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 12 12 Phosphoserine.
{ECO:0000250|UniProtKB:P97310}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 25 25 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 26 26 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 27 27 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:16899510}.
MOD_RES 32 32 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 39 39 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 40 40 Phosphoserine; by CDC7.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:17062569}.
MOD_RES 41 41 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:16899510}.
MOD_RES 53 53 Phosphoserine; by CDC7.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:16899510,
ECO:0000269|PubMed:17062569}.
MOD_RES 59 59 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 108 108 Phosphoserine; by ATR.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:15210935,
ECO:0000269|PubMed:16899510}.
MOD_RES 137 137 Phosphotyrosine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 139 139 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:16899510}.
MOD_RES 216 216 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 381 381 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 484 484 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 178 178 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 44 44 R -> C (in DFNA70; increases the
apoptotic process; no effect on cell
proliferation and cell cycle phase;
dbSNP:rs375851208).
{ECO:0000269|PubMed:26196677}.
/FTId=VAR_077049.
VARIANT 68 68 D -> E (in dbSNP:rs3087452).
{ECO:0000269|Ref.3}.
/FTId=VAR_021111.
VARIANT 135 135 L -> F (in dbSNP:rs2307314).
{ECO:0000269|Ref.3}.
/FTId=VAR_021112.
VARIANT 166 166 E -> Q (in dbSNP:rs1048225).
{ECO:0000269|PubMed:8175912}.
/FTId=VAR_033298.
VARIANT 396 396 A -> T (in dbSNP:rs3087450).
{ECO:0000269|Ref.3}.
/FTId=VAR_016137.
VARIANT 501 501 G -> R (in dbSNP:rs13087457).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_033299.
VARIANT 667 667 V -> M (in dbSNP:rs2307311).
{ECO:0000269|Ref.3}.
/FTId=VAR_016138.
VARIANT 727 727 A -> T (in dbSNP:rs2307313).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.3}.
/FTId=VAR_016139.
MUTAGEN 27 27 S->A: Impairs ATPase activity of the MCM-
2-7 complex and reduces phosphorylation
by the CDC7-DBF4 complex; when associated
with A-41 and A-139.
{ECO:0000269|PubMed:16899510}.
MUTAGEN 41 41 S->A: Impairs ATPase activity of the MCM-
2-7 complex and reduces phosphorylation
by the CDC7-DBF4 complex; when associated
with A-27 and A-139.
{ECO:0000269|PubMed:16899510}.
MUTAGEN 108 108 S->A: Reduces phosphorylation by ATR.
{ECO:0000269|PubMed:15210935}.
MUTAGEN 139 139 S->A: Impairs ATPase activity of the MCM-
2-7 complex and reduces phosphorylation
by the CDC7-DBF4 complex; when associated
with A-27 and A-41.
{ECO:0000269|PubMed:16899510}.
CONFLICT 1 1 M -> S (in Ref. 1; CAA47749).
{ECO:0000305}.
CONFLICT 109 109 Q -> R (in Ref. 1; CAA47749).
{ECO:0000305}.
CONFLICT 388 388 G -> R (in Ref. 1; CAA47749).
{ECO:0000305}.
CONFLICT 407 408 KP -> NA (in Ref. 1; CAA47749 and 5;
BAA12177). {ECO:0000305}.
CONFLICT 495 495 L -> P (in Ref. 1; CAA47749).
{ECO:0000305}.
CONFLICT 555 556 GL -> AV (in Ref. 1; CAA47749).
{ECO:0000305}.
STRAND 70 74 {ECO:0000244|PDB:5JA4}.
HELIX 77 81 {ECO:0000244|PDB:5BNX}.
HELIX 85 88 {ECO:0000244|PDB:5BNX}.
STRAND 98 100 {ECO:0000244|PDB:5BO0}.
HELIX 108 123 {ECO:0000244|PDB:5BNX}.
SEQUENCE 904 AA; 101896 MW; 52C6DC61F128B404 CRC64;
MAESSESFTM ASSPAQRRRG NDPLTSSPGR SSRRTDALTS SPGRDLPPFE DESEGLLGTE
GPLEEEEDGE ELIGDGMERD YRAIPELDAY EAEGLALDDE DVEELTASQR EAAERAMRQR
DREAGRGLGR MRRGLLYDSD EEDEERPARK RRQVERATED GEEDEEMIES IENLEDLKGH
SVREWVSMAG PRLEIHHRFK NFLRTHVDSH GHNVFKERIS DMCKENRESL VVNYEDLAAR
EHVLAYFLPE APAELLQIFD EAALEVVLAM YPKYDRITNH IHVRISHLPL VEELRSLRQL
HLNQLIRTSG VVTSCTGVLP QLSMVKYNCN KCNFVLGPFC QSQNQEVKPG SCPECQSAGP
FEVNMEETIY QNYQRIRIQE SPGKVAAGRL PRSKDAILLA DLVDSCKPGD EIELTGIYHN
NYDGSLNTAN GFPVFATVIL ANHVAKKDNK VAVGELTDED VKMITSLSKD QQIGEKIFAS
IAPSIYGHED IKRGLALALF GGEPKNPGGK HKVRGDINVL LCGDPGTAKS QFLKYIEKVS
SRAIFTTGQG ASAVGLTAYV QRHPVSREWT LEAGALVLAD RGVCLIDEFD KMNDQDRTSI
HEAMEQQSIS ISKAGIVTSL QARCTVIAAA NPIGGRYDPS LTFSENVDLT EPIISRFDIL
CVVRDTVDPV QDEMLARFVV GSHVRHHPSN KEEEGLANGS AAEPAMPNTY GVEPLPQEVL
KKYIIYAKER VHPKLNQMDQ DKVAKMYSDL RKESMATGSI PITVRHIESM IRMAEAHARI
HLRDYVIEDD VNMAIRVMLE SFIDTQKFSV MRSMRKTFAR YLSFRRDNNE LLLFILKQLV
AEQVTYQRNR FGAQQDTIEV PEKDLVDKAR QINIHNLSAF YDSELFRMNK FSHDLKRKMI
LQQF


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