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Protein

DNA replication licensing factor MCM2

Gene

Mcm2

Organism
Mus musculus (Mouse)
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 the entry in S phase and for cell division.

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri329 – 355C4-typeSequence analysisAdd BLAST27
Nucleotide bindingi523 – 530ATPSequence analysis8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • DNA helicase activity Source: InterPro
  • DNA replication origin binding Source: MGI
  • enzyme binding Source: BHF-UCL
  • histone binding Source: MGI
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cellular response to interleukin-4 Source: MGI
  • DNA replication initiation Source: MGI
  • DNA unwinding involved in DNA replication Source: MGI
  • nucleosome assembly Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Cell cycle, DNA replication

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiR-MMU-176187. Activation of ATR in response to replication stress.
R-MMU-68867. Assembly of the pre-replicative complex.
R-MMU-68949. Orc1 removal from chromatin.
R-MMU-68962. Activation of the pre-replicative complex.
R-MMU-69052. Switching of origins to a post-replicative state.
R-MMU-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 protein 2 homolog
Nuclear protein BM28
Gene namesi
Name:Mcm2
Synonyms:Bm28, Cdcl1, Kiaa0030, Mcmd2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:105380. Mcm2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi237L → P: Impairs interaction with KAT7. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001940882 – 904DNA replication licensing factor MCM2Add BLAST903

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei12PhosphoserineCombined sources1
Modified residuei21PhosphoserineCombined sources1
Modified residuei25PhosphothreonineBy similarity1
Modified residuei26PhosphoserineBy similarity1
Modified residuei27PhosphoserineCombined sources1
Modified residuei32PhosphoserineBy similarity1
Modified residuei39PhosphothreonineBy similarity1
Modified residuei40Phosphoserine; by CDC7By similarity1
Modified residuei41PhosphoserineCombined sources1
Modified residuei53Phosphoserine; by CDC7By similarity1
Modified residuei59PhosphothreonineBy similarity1
Modified residuei108PhosphoserineCombined sources1
Modified residuei137PhosphotyrosineBy similarity1
Modified residuei139PhosphoserineCombined sources1
Modified residuei140PhosphoserineCombined sources1
Modified residuei216N6-acetyllysineBy similarity1
Modified residuei381PhosphoserineBy similarity1
Modified residuei484PhosphoserineBy similarity1

Post-translational modificationi

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 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP97310.
MaxQBiP97310.
PaxDbiP97310.
PeptideAtlasiP97310.
PRIDEiP97310.

PTM databases

iPTMnetiP97310.
PhosphoSitePlusiP97310.
SwissPalmiP97310.

Miscellaneous databases

PMAP-CutDBP97310.

Expressioni

Gene expression databases

BgeeiENSMUSG00000002870.
ExpressionAtlasiP97310. baseline and differential.
GenevisibleiP97310. MM.

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. Interacts with KAT7 and DBF4. May interact with MCM10 (By similarity).By similarity

GO - Molecular functioni

  • enzyme binding Source: BHF-UCL
  • histone binding Source: MGI

Protein-protein interaction databases

BioGridi201346. 12 interactors.
DIPiDIP-33057N.
IntActiP97310. 15 interactors.
MINTiMINT-4101561.
STRINGi10090.ENSMUSP00000061923.

Structurei

3D structure databases

ProteinModelPortaliP97310.
SMRiP97310.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini473 – 680MCMAdd BLAST208

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 257Interaction with KAT71 PublicationAdd BLAST256

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi655 – 658Arginine finger4

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri329 – 355C4-typeSequence analysisAdd BLAST27

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0477. Eukaryota.
COG1241. LUCA.
GeneTreeiENSGT00850000132309.
HOVERGENiHBG106398.
InParanoidiP97310.
KOiK02540.
OMAiKYDRIAH.
OrthoDBiEOG091G026H.
PhylomeDBiP97310.
TreeFamiTF300772.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR031327. MCM.
IPR008045. MCM2.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR033762. MCM_OB.
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.
PF17207. MCM_OB. 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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P97310-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAESSESLSA SSPARQRRRI SDPLTSSPGR SSRRADALTS SPGRDLPPFE
60 70 80 90 100
DESEGLLGTE GPMEEEEDGE ELIGDGMERD YRPIPELDVY EAEGLALDDE
110 120 130 140 150
DVEELTASQR EAAERTMRQR DREAGRGLGR MRRGLLYDSS EEDEERPARK
160 170 180 190 200
RRHVERATED GEEDEEMIES IENLEDLKGH SVREWVSMAG PRLEIHHRFK
210 220 230 240 250
NFLRTHVDSH GHNVFKERIS DMCKENRESL VVNYEDLAAR EHVLAYFLPE
260 270 280 290 300
APAELLQIFD EAALEVVLAM YPKYDRITNH IHVRISHLPL VEELRSLRQL
310 320 330 340 350
HLNQLIRTSG VVTSCTGVLP QLSMVKYNCS KCNFVLGPFC QSQNQEVKPG
360 370 380 390 400
SCPECQSAGP FEINMEETIY QNYQRIRIQE SPGKVAAGRL PRSKDAILLA
410 420 430 440 450
DLVDSCKPGD EIELTGIYHN NYDGSLNTAN GFPVFATIIL ANHVAKKDNK
460 470 480 490 500
VAVGELTDED VKMITGLSKD QQIGEKIFAS IAPSIYGHED IKRGLALALF
510 520 530 540 550
GGEPKNPGGK HKVRGDINVL LCGDPGTAKS QFLKYIEKVS SRAIFTTGQG
560 570 580 590 600
ASAVGLTAYV QRHPVSREWT LEAGALVLAD RGVCLIDEFD KMNDQDRTSI
610 620 630 640 650
HEAMEQQSIS ISKAGIVTSL QARCTVIAAA NPIGGRYDPS LTFSENVDLT
660 670 680 690 700
EPIISRFDVL CVVRDTVDPV QDEMLARFVV GSHVRHHPSN KKDEGLTNGG
710 720 730 740 750
TLEPAMPNTY GVEPLPQEVL KKYIIYAKER VRPKLNQMDQ DKVARMYSDL
760 770 780 790 800
RKESMATGSI PITVRHIESM IRMAEAHARM HLRDYVMEDD VNMAIRVMME
810 820 830 840 850
SFIDTQKFSV MRSMRKTFAR YLSFRRDNND LLLFILKQLV AEQVTYQRNR
860 870 880 890 900
FGAQQDTIEI PEKDLMDKAR QINIHNLSAF YDSDLFKFNK FSRDLKRKLI

LQQF
Length:904
Mass (Da):102,078
Last modified:April 13, 2004 - v3
Checksum:i7B61C13DAD1CAC58
GO

Sequence cautioni

The sequence BAC97849 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti70E → G in AAC16250 (PubMed:9371513).Curated1
Sequence conflicti135L → P in AAC16250 (PubMed:9371513).Curated1
Sequence conflicti185W → R in BAA22148 (PubMed:9077461).Curated1
Sequence conflicti271Y → H in AAC16250 (PubMed:9371513).Curated1
Sequence conflicti506N → D in AAC36510 (PubMed:9798653).Curated1
Sequence conflicti521L → S in AAC36510 (PubMed:9798653).Curated1
Sequence conflicti648D → N in AAC36510 (PubMed:9798653).Curated1
Sequence conflicti822L → I in AAC16250 (PubMed:9371513).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86725 mRNA. Translation: BAA22148.1.
AF004105 mRNA. Translation: AAC16250.1.
AK129039 mRNA. Translation: BAC97849.1. Different initiation.
AK088156 mRNA. Translation: BAC40178.1.
BC055318 mRNA. Translation: AAH55318.1.
U89403 mRNA. Translation: AAC36510.1.
CCDSiCCDS39554.1.
PIRiT10067.
RefSeqiNP_032590.2. NM_008564.2.
UniGeneiMm.16711.

Genome annotation databases

EnsembliENSMUST00000058011; ENSMUSP00000061923; ENSMUSG00000002870.
GeneIDi17216.
KEGGimmu:17216.
UCSCiuc009cvx.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86725 mRNA. Translation: BAA22148.1.
AF004105 mRNA. Translation: AAC16250.1.
AK129039 mRNA. Translation: BAC97849.1. Different initiation.
AK088156 mRNA. Translation: BAC40178.1.
BC055318 mRNA. Translation: AAH55318.1.
U89403 mRNA. Translation: AAC36510.1.
CCDSiCCDS39554.1.
PIRiT10067.
RefSeqiNP_032590.2. NM_008564.2.
UniGeneiMm.16711.

3D structure databases

ProteinModelPortaliP97310.
SMRiP97310.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201346. 12 interactors.
DIPiDIP-33057N.
IntActiP97310. 15 interactors.
MINTiMINT-4101561.
STRINGi10090.ENSMUSP00000061923.

PTM databases

iPTMnetiP97310.
PhosphoSitePlusiP97310.
SwissPalmiP97310.

Proteomic databases

EPDiP97310.
MaxQBiP97310.
PaxDbiP97310.
PeptideAtlasiP97310.
PRIDEiP97310.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000058011; ENSMUSP00000061923; ENSMUSG00000002870.
GeneIDi17216.
KEGGimmu:17216.
UCSCiuc009cvx.2. mouse.

Organism-specific databases

CTDi4171.
MGIiMGI:105380. Mcm2.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG0477. Eukaryota.
COG1241. LUCA.
GeneTreeiENSGT00850000132309.
HOVERGENiHBG106398.
InParanoidiP97310.
KOiK02540.
OMAiKYDRIAH.
OrthoDBiEOG091G026H.
PhylomeDBiP97310.
TreeFamiTF300772.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiMcm2. mouse.
PMAP-CutDBP97310.
PROiP97310.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000002870.
ExpressionAtlasiP97310. baseline and differential.
GenevisibleiP97310. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR031327. MCM.
IPR008045. MCM2.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR033762. MCM_OB.
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.
PF17207. MCM_OB. 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...

Entry informationi

Entry nameiMCM2_MOUSE
AccessioniPrimary (citable) accession number: P97310
Secondary accession number(s): O08971, O89057, Q8C2R0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 13, 2004
Last modified: November 30, 2016
This is version 163 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.