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Protein

DNA replication licensing factor Mcm2

Gene

Mcm2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 DNA replication and cell proliferation.3 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri314 – 34027C4-typeSequence analysisAdd
BLAST
Nucleotide bindingi508 – 5158ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • cell proliferation Source: FlyBase
  • chromosome condensation Source: FlyBase
  • DNA duplex unwinding Source: GOC
  • DNA replication Source: FlyBase
  • DNA replication initiation Source: InterPro
  • lateral inhibition Source: FlyBase
  • neurogenesis Source: FlyBase
  • pre-replicative complex assembly involved in nuclear cell cycle DNA replication Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Cell cycle, Cell division, DNA replication

Keywords - Ligandi

ATP-binding, DNA-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiR-DME-176187. Activation of ATR in response to replication stress.
R-DME-68867. Assembly of the pre-replicative complex.
R-DME-68949. Orc1 removal from chromatin.
R-DME-68962. Activation of the pre-replicative complex.
R-DME-69052. Switching of origins to a post-replicative state.
R-DME-69300. Removal of licensing factors from origins.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA replication licensing factor Mcm2 (EC:3.6.4.12)
Alternative name(s):
Minichromosome maintenance 2 protein
Short name:
DmMCM2
Gene namesi
Name:Mcm2
ORF Names:CG7538
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0014861. Mcm2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi514 – 5141K → A: Reduces complex helicase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 887887DNA replication licensing factor Mcm2PRO_0000194090Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei26 – 261Phosphothreonine1 Publication
Modified residuei27 – 271Phosphoserine1 Publication
Modified residuei89 – 891Phosphoserine1 Publication
Modified residuei92 – 921Phosphoserine1 Publication
Modified residuei124 – 1241Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP49735.
PRIDEiP49735.

PTM databases

iPTMnetiP49735.

Expressioni

Gene expression databases

BgeeiP49735.
GenevisibleiP49735. DM.

Interactioni

Subunit structurei

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 Mcm10.Curated3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Mcm10Q9VIE62EBI-138228,EBI-91264
Mcm5Q9VGW63EBI-138228,EBI-83298
Mcm6Q9V4615EBI-138228,EBI-869161

Protein-protein interaction databases

BioGridi66154. 6 interactions.
DIPiDIP-22529N.
IntActiP49735. 6 interactions.
MINTiMINT-326578.
STRINGi7227.FBpp0081317.

Structurei

3D structure databases

ProteinModelPortaliP49735.
SMRiP49735. Positions 55-111, 180-798.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini458 – 665208MCMAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi640 – 6434Arginine finger

Sequence similaritiesi

Belongs to the MCM family.Curated
Contains 1 MCM domain.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri314 – 34027C4-typeSequence analysisAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0477. Eukaryota.
COG1241. LUCA.
GeneTreeiENSGT00790000123056.
InParanoidiP49735.
KOiK02540.
OMAiKYDRIAH.
OrthoDBiEOG71VSRZ.
PhylomeDBiP49735.

Family and domain databases

Gene3Di2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR031327. MCM.
IPR008045. MCM2.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11630:SF44. PTHR11630:SF44. 1 hit.
PfamiPF00493. MCM. 1 hit.
PF12619. MCM2_N. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01658. MCMPROTEIN2.
SMARTiSM00350. MCM. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P49735-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDNPSSPPPN TPSDAAERRD LRAAMTSPVG DFEPFENEDE ILGDQTVRDE
60 70 80 90 100
AEEEDGEELF GDNMENDYRP MPELDHYDPA LLDDEDDFSE MSQGDRFAAE
110 120 130 140 150
SEMRRRDRAA GIHRDDRDLG FGQSDDEDDV GPRAKRRAGE KAAVGEVEDT
160 170 180 190 200
EMVESIENLE DTKGHSTKEW VSMLGPRTEI ANRFQSFLRT FVDERGAYTY
210 220 230 240 250
RDRIRRMCEQ NMSSFVVSYT DLANKEHVLA YFLPEAPFQM LEIFDKVAKD
260 270 280 290 300
MVLSIFPTYE RVTTEIHVRI SELPLIEELR TFRKLHLNQL VRTLGVVTAT
310 320 330 340 350
TGVLPQLSVI KYDCVKCGYV LGPFVQSQNT EIKPGSCPEC QSTGPFSINM
360 370 380 390 400
EQTLYRNYQK ITLQESPGRI PAGRIPRSKD VILLADLCDQ CKPGDELEVT
410 420 430 440 450
GIYTNNYDGS LNTDQGFPVF ATVIIANHVV VKDSKQVVQS LTDEDIATIQ
460 470 480 490 500
KLSKDPRIVE RVVASMAPSI YGHDYIKRAL ALALFGGESK NPGEKHKVRG
510 520 530 540 550
DINLLICGDP GTAKSQFLKY TEKVAPRAVF TTGQGASAVG LTAYVRRNPV
560 570 580 590 600
SREWTLEAGA LVLADQGVCL IDEFDKMNDQ DRTSIHEAME QQSISISKAG
610 620 630 640 650
IVTSLQARCT VIAAANPIGG RYDPSMTFSE NVNLSEPILS RFDVLCVVKD
660 670 680 690 700
EFDPMQDQQL AKFVVHSHMK HHPSEEEQPE LEEPQLKTVD EIPQDLLRQY
710 720 730 740 750
IVYAKENIRP KLTNIDEDKI AKMYAQLRQE SFATGSLPIT VRHIESVIRM
760 770 780 790 800
SEAHARMHLR ENVMEADVSM AIRMMLESFI EAQKFSVMKK MRSTFQKYLS
810 820 830 840 850
FQKDHSELLF FILRQLTLDQ LAYIRCKDGP GATHVEIMER DLIERAKQLD
860 870 880
IVNLKPFYES DLFRTNGFSY DPKRRIILQI VVDGNTA
Length:887
Mass (Da):100,415
Last modified:October 1, 1996 - v1
Checksum:i26A7092109F09CBE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42762 mRNA. Translation: AAB36617.1.
AE014297 Genomic DNA. Translation: AAF54207.1.
AY069702 mRNA. Translation: AAL39847.1.
RefSeqiNP_477121.1. NM_057773.4.
UniGeneiDm.1996.

Genome annotation databases

EnsemblMetazoaiFBtr0081827; FBpp0081317; FBgn0014861.
GeneIDi40973.
KEGGidme:Dmel_CG7538.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42762 mRNA. Translation: AAB36617.1.
AE014297 Genomic DNA. Translation: AAF54207.1.
AY069702 mRNA. Translation: AAL39847.1.
RefSeqiNP_477121.1. NM_057773.4.
UniGeneiDm.1996.

3D structure databases

ProteinModelPortaliP49735.
SMRiP49735. Positions 55-111, 180-798.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi66154. 6 interactions.
DIPiDIP-22529N.
IntActiP49735. 6 interactions.
MINTiMINT-326578.
STRINGi7227.FBpp0081317.

PTM databases

iPTMnetiP49735.

Proteomic databases

PaxDbiP49735.
PRIDEiP49735.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0081827; FBpp0081317; FBgn0014861.
GeneIDi40973.
KEGGidme:Dmel_CG7538.

Organism-specific databases

CTDi4171.
FlyBaseiFBgn0014861. Mcm2.

Phylogenomic databases

eggNOGiKOG0477. Eukaryota.
COG1241. LUCA.
GeneTreeiENSGT00790000123056.
InParanoidiP49735.
KOiK02540.
OMAiKYDRIAH.
OrthoDBiEOG71VSRZ.
PhylomeDBiP49735.

Enzyme and pathway databases

ReactomeiR-DME-176187. Activation of ATR in response to replication stress.
R-DME-68867. Assembly of the pre-replicative complex.
R-DME-68949. Orc1 removal from chromatin.
R-DME-68962. Activation of the pre-replicative complex.
R-DME-69052. Switching of origins to a post-replicative state.
R-DME-69300. Removal of licensing factors from origins.

Miscellaneous databases

GenomeRNAii40973.
NextBioi821540.
PROiP49735.

Gene expression databases

BgeeiP49735.
GenevisibleiP49735. DM.

Family and domain databases

Gene3Di2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR031327. MCM.
IPR008045. MCM2.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11630:SF44. PTHR11630:SF44. 1 hit.
PfamiPF00493. MCM. 1 hit.
PF12619. MCM2_N. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01658. MCMPROTEIN2.
SMARTiSM00350. MCM. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cell proliferation and DNA replication defects in a Drosophila MCM2 mutant."
    Treisman J.E., Follette P.J., O'Farrell P.H., Rubin G.M.
    Genes Dev. 9:1709-1715(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Tissue: Eye-antennal disk.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  5. "Drosophila minichromosome maintenance 6 is required for chorion gene amplification and genomic replication."
    Schwed G., May N., Pechersky Y., Calvi B.R.
    Mol. Biol. Cell 13:607-620(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MCM6.
  6. "Drosophila MCM10 interacts with members of the prereplication complex and is required for proper chromosome condensation."
    Christensen T.W., Tye B.K.
    Mol. Biol. Cell 14:2206-2215(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MCM10.
  7. "Isolation of the Cdc45/Mcm2-7/GINS (CMG) complex, a candidate for the eukaryotic DNA replication fork helicase."
    Moyer S.E., Lewis P.W., Botchan M.R.
    Proc. Natl. Acad. Sci. U.S.A. 103:10236-10241(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MCM2-7 COMPLEX, FUNCTION OF THE MCM2-7 COMPLEX.
  8. "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
    Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
    Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-26; SER-27 AND SER-124, IDENTIFICATION BY MASS SPECTROMETRY.
  9. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89 AND SER-92, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  10. "Activation of the MCM2-7 helicase by association with Cdc45 and GINS proteins."
    Ilves I., Petojevic T., Pesavento J.J., Botchan M.R.
    Mol. Cell 37:247-258(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: RECONSTITUTION OF THE MCM2-7 COMPLEX, FUNCTION OF THE MCM2-7 COMPLEX, MUTAGENESIS OF LYS-514.

Entry informationi

Entry nameiMCM2_DROME
AccessioniPrimary (citable) accession number: P49735
Secondary accession number(s): Q9VHU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

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.