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Protein

DNA replication licensing factor MCM2

Gene

MCM2

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

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; specifically the MCM2-MCM5 association is proposed to be reversible and to mediate a open ring conformation which may facilitate DNA loading. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity. Necessary for cell growth.2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri341 – 367C4-typeSequence analysisAdd BLAST27
Nucleotide bindingi543 – 550ATPSequence analysis8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • chromatin binding Source: SGD
  • DNA helicase activity Source: InterPro
  • DNA replication origin binding Source: SGD
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • cellular response to DNA damage stimulus Source: SGD
  • DNA replication initiation Source: InterPro
  • DNA strand elongation involved in DNA replication Source: SGD
  • double-strand break repair via break-induced replication Source: SGD
  • negative regulation of ATP-dependent DNA helicase activity Source: SGD
  • nuclear DNA replication Source: SGD
  • pre-replicative complex assembly involved in nuclear cell cycle DNA replication Source: SGD
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

BioCyciYEAST:G3O-28926-MONOMER.
ReactomeiR-SCE-176974. Unwinding of DNA.
R-SCE-68949. Orc1 removal from chromatin.
R-SCE-68962. Activation of the pre-replicative complex.
R-SCE-69052. Switching of origins to a post-replicative state.
R-SCE-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
Gene namesi
Name:MCM2
Ordered Locus Names:YBL023C
ORF Names:YBL0438
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBL023C.
SGDiS000000119. MCM2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • DNA replication preinitiation complex Source: SGD
  • MCM complex Source: SGD
  • nuclear pre-replicative complex Source: SGD
  • nucleoplasm Source: Reactome
  • nucleus Source: SGD
  • replication fork protection complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi364C → Y, F, S or H: Loss of activity. 1 Publication1
Mutagenesisi367C → Y, F, S or H: Loss of activity. 1 Publication1
Mutagenesisi549K → A: Reduces MCM2-7 complex helicase activity. Abolishes MCM2-7 complex helicase activity; when associated with MCM5 A-422. Reduces MCM2-7 complex helicase activity; when associated with MCM3 A-415. 1 Publication1
Mutagenesisi676R → A: Loss of MCM2-7 complex helicase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001940911 – 868DNA replication licensing factor MCM2Add BLAST868

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei14PhosphoserineCombined sources1
Modified residuei16PhosphoserineCombined sources1
Modified residuei23PhosphoserineCombined sources1
Modified residuei164PhosphoserineCombined sources1
Modified residuei170PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP29469.
PRIDEiP29469.

PTM databases

iPTMnetiP29469.

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; loaded onto DNA, forms a head-head double hexamer.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DIA2Q084963EBI-10533,EBI-31943
MCM4P306657EBI-10533,EBI-4326

Protein-protein interaction databases

BioGridi32675. 116 interactors.
DIPiDIP-2291N.
IntActiP29469. 47 interactors.
MINTiMINT-469073.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JA8electron microscopy3.8021-868[»]
3JC5electron microscopy4.7021-868[»]
3JC6electron microscopy3.7021-868[»]
3JC7electron microscopy4.8021-868[»]
ProteinModelPortaliP29469.
SMRiP29469.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini493 – 700MCMAdd BLAST208

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi675 – 678Arginine finger4

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri341 – 367C4-typeSequence analysisAdd BLAST27

Keywords - Domaini

Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00850000132309.
HOGENOMiHOG000224124.
InParanoidiP29469.
KOiK02540.
OMAiKYDRIAH.
OrthoDBiEOG092C0VUM.

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. 2 hits.
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. 2 hits.
PROSITEiPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P29469-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDNRRRRRE EDDSDSENEL PPSSPQQHFR GGMNPVSSPI GSPDMINPEG
60 70 80 90 100
DDNEVDDVPD IDEVEEQMNE VDLMDDNMYE DYAADHNRDR YDPDQVDDRE
110 120 130 140 150
QQELSLSERR RIDAQLNERD RLLRNVAYID DEDEEQEGAA QLDEMGLPVQ
160 170 180 190 200
RRRRRRQYED LENSDDDLLS DMDIDPLREE LTLESLSNVK ANSYSEWITQ
210 220 230 240 250
PNVSRTIARE LKSFLLEYTD ETGRSVYGAR IRTLGEMNSE SLEVNYRHLA
260 270 280 290 300
ESKAILALFL AKCPEEMLKI FDLVAMEATE LHYPDYARIH SEIHVRISDF
310 320 330 340 350
PTIYSLRELR ESNLSSLVRV TGVVTRRTGV FPQLKYVKFN CLKCGSILGP
360 370 380 390 400
FFQDSNEEIR ISFCTNCKSK GPFRVNGEKT VYRNYQRVTL QEAPGTVPPG
410 420 430 440 450
RLPRHREVIL LADLVDVSKP GEEVEVTGIY KNNYDGNLNA KNGFPVFATI
460 470 480 490 500
IEANSIKRRE GNTANEGEEG LDVFSWTEEE EREFRKISRD RGIIDKIISS
510 520 530 540 550
MAPSIYGHRD IKTAVACSLF GGVPKNVNGK HSIRGDINVL LLGDPGTAKS
560 570 580 590 600
QILKYVEKTA HRAVFATGQG ASAVGLTASV RKDPITKEWT LEGGALVLAD
610 620 630 640 650
KGVCLIDEFD KMNDQDRTSI HEAMEQQSIS ISKAGIVTTL QARCSIIAAA
660 670 680 690 700
NPNGGRYNST LPLAQNVSLT EPILSRFDIL CVVRDLVDEE ADERLATFVV
710 720 730 740 750
DSHVRSHPEN DEDREGEELK NNGESAIEQG EDEINEQLNA RQRRLQRQRK
760 770 780 790 800
KEEEISPIPQ ELLMKYIHYA RTKIYPKLHQ MDMDKVSRVY ADLRRESIST
810 820 830 840 850
GSFPITVRHL ESILRIAESF AKMRLSEFVS SYDLDRAIKV VVDSFVDAQK
860
VSVRRQLRRS FAIYTLGH
Length:868
Mass (Da):98,780
Last modified:October 1, 1994 - v2
Checksum:iF38FF682581B0EC0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti164S → T in CAA37615 (PubMed:2044961).Curated1
Sequence conflicti172 – 173MD → IH in CAA37615 (PubMed:2044961).Curated2
Sequence conflicti529G → P in CAA37615 (PubMed:2044961).Curated1
Sequence conflicti578A → R in CAA37615 (PubMed:2044961).Curated1
Sequence conflicti583D → H in CAA37615 (PubMed:2044961).Curated1
Sequence conflicti712E → Q in CAA37615 (PubMed:2044961).Curated1
Sequence conflicti733 – 747Missing in CAA37615 (PubMed:2044961).CuratedAdd BLAST15
Sequence conflicti859 – 868RSFAIYTLGH → SLSQFIPWVTKTLLFLRISG YEDKKFSVSIHVLAILFSIY KFPLFFV in CAA37615 (PubMed:2044961).Curated10

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti392E → K in allele MCM2-1. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77291 Genomic DNA. Translation: CAA54503.1.
X53539 Genomic DNA. Translation: CAA37615.1.
Z35784 Genomic DNA. Translation: CAA84842.1.
X74544 Genomic DNA. Translation: CAA52635.1.
BK006936 Genomic DNA. Translation: DAA07097.1.
PIRiS45757.
RefSeqiNP_009530.1. NM_001178263.1.

Genome annotation databases

EnsemblFungiiYBL023C; YBL023C; YBL023C.
GeneIDi852258.
KEGGisce:YBL023C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77291 Genomic DNA. Translation: CAA54503.1.
X53539 Genomic DNA. Translation: CAA37615.1.
Z35784 Genomic DNA. Translation: CAA84842.1.
X74544 Genomic DNA. Translation: CAA52635.1.
BK006936 Genomic DNA. Translation: DAA07097.1.
PIRiS45757.
RefSeqiNP_009530.1. NM_001178263.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JA8electron microscopy3.8021-868[»]
3JC5electron microscopy4.7021-868[»]
3JC6electron microscopy3.7021-868[»]
3JC7electron microscopy4.8021-868[»]
ProteinModelPortaliP29469.
SMRiP29469.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32675. 116 interactors.
DIPiDIP-2291N.
IntActiP29469. 47 interactors.
MINTiMINT-469073.

PTM databases

iPTMnetiP29469.

Proteomic databases

MaxQBiP29469.
PRIDEiP29469.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBL023C; YBL023C; YBL023C.
GeneIDi852258.
KEGGisce:YBL023C.

Organism-specific databases

EuPathDBiFungiDB:YBL023C.
SGDiS000000119. MCM2.

Phylogenomic databases

GeneTreeiENSGT00850000132309.
HOGENOMiHOG000224124.
InParanoidiP29469.
KOiK02540.
OMAiKYDRIAH.
OrthoDBiEOG092C0VUM.

Enzyme and pathway databases

BioCyciYEAST:G3O-28926-MONOMER.
ReactomeiR-SCE-176974. Unwinding of DNA.
R-SCE-68949. Orc1 removal from chromatin.
R-SCE-68962. Activation of the pre-replicative complex.
R-SCE-69052. Switching of origins to a post-replicative state.
R-SCE-69300. Removal of licensing factors from origins.

Miscellaneous databases

PROiP29469.

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. 2 hits.
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. 2 hits.
PROSITEiPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMCM2_YEAST
AccessioniPrimary (citable) accession number: P29469
Secondary accession number(s): D6VPX7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 1, 1994
Last modified: November 30, 2016
This is version 164 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1690 molecules/cell in log phase SD medium.1 Publication
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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. 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.