UniProtKB - P29469 (MCM2_YEAST)
DNA replication licensing factor MCM2
MCM2
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 PublicationsMiscellaneous
Catalytic activityi
- EC:3.6.4.12
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 341 – 367 | C4-typeSequence analysisAdd BLAST | 27 | |
Nucleotide bindingi | 543 – 550 | ATPSequence analysis | 8 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- ATP hydrolysis activity Source: RHEA
- chromatin binding Source: SGD
- DNA helicase activity Source: UniProtKB-EC
- DNA replication origin binding Source: SGD
- metal ion binding Source: UniProtKB-KW
GO - Biological processi
- cellular response to DNA damage stimulus Source: SGD
- DNA strand elongation involved in DNA replication Source: SGD
- DNA unwinding involved in DNA replication Source: ComplexPortal
- double-strand break repair via break-induced replication Source: SGD
- mitotic DNA replication initiation Source: SGD
- negative regulation of DNA helicase activity Source: SGD
- pre-replicative complex assembly involved in nuclear cell cycle DNA replication Source: SGD
- regulation of DNA-dependent DNA replication initiation Source: ComplexPortal
Keywordsi
Molecular function | DNA-binding, Helicase, Hydrolase |
Biological process | Cell cycle, DNA replication |
Ligand | ATP-binding, Metal-binding, Nucleotide-binding, Zinc |
Enzyme and pathway databases
Reactomei | 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 |
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 |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
SGDi | S000000119, MCM2 |
VEuPathDBi | FungiDB:YBL023C |
Subcellular locationi
Nucleus
Nucleus
- CMG complex Source: SGD
- DNA replication preinitiation complex Source: SGD
- nuclear pre-replicative complex Source: SGD
- nuclear replication fork Source: ComplexPortal
- nucleoplasm Source: Reactome
- nucleus Source: SGD
- replication fork protection complex Source: SGD
Other locations
- cytoplasm Source: SGD
- MCM complex Source: SGD
Keywords - Cellular componenti
NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 364 | C → Y, F, S or H: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 367 | C → Y, F, S or H: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 549 | K → 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 Publication | 1 | |
Mutagenesisi | 676 | R → A: Loss of MCM2-7 complex helicase activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000194091 | 1 – 868 | DNA replication licensing factor MCM2Add BLAST | 868 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 14 | PhosphoserineCombined sources | 1 | |
Modified residuei | 16 | PhosphoserineCombined sources | 1 | |
Modified residuei | 23 | PhosphoserineCombined sources | 1 | |
Modified residuei | 164 | PhosphoserineCombined sources | 1 | |
Modified residuei | 170 | PhosphoserineCombined sources | 1 |
Keywords - PTMi
PhosphoproteinProteomic databases
MaxQBi | P29469 |
PaxDbi | P29469 |
PRIDEi | P29469 |
PTM databases
iPTMneti | P29469 |
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 PublicationsBinary interactionsi
P29469
With | #Exp. | IntAct |
---|---|---|
CDC6 [P09119] | 4 | EBI-10533,EBI-4447 |
DIA2 [Q08496] | 4 | EBI-10533,EBI-31943 |
MCM4 [P30665] | 15 | EBI-10533,EBI-4326 |
SMT3 [Q12306] | 2 | EBI-10533,EBI-17490 |
Protein-protein interaction databases
BioGRIDi | 32675, 202 interactors |
ComplexPortali | CPX-2944, MCM complex |
DIPi | DIP-2291N |
IntActi | P29469, 53 interactors |
MINTi | P29469 |
STRINGi | 4932.YBL023C |
Miscellaneous databases
RNActi | P29469, protein |
Structurei
Secondary structure
3D structure databases
SMRi | P29469 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 493 – 700 | MCMAdd BLAST | 208 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 65 | DisorderedSequence analysisAdd BLAST | 65 | |
Regioni | 87 – 106 | DisorderedSequence analysisAdd BLAST | 20 | |
Regioni | 704 – 728 | DisorderedSequence analysisAdd BLAST | 25 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 675 – 678 | Arginine finger | 4 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 1 – 15 | Basic and acidic residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 19 – 33 | Polar residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 49 – 65 | Acidic residuesSequence analysisAdd BLAST | 17 | |
Compositional biasi | 704 – 727 | Basic and acidic residuesSequence analysisAdd BLAST | 24 |
Sequence similaritiesi
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 341 – 367 | C4-typeSequence analysisAdd BLAST | 27 |
Keywords - Domaini
Zinc-fingerPhylogenomic databases
eggNOGi | KOG0477, Eukaryota |
GeneTreei | ENSGT01040000240460 |
HOGENOMi | CLU_000995_0_0_1 |
InParanoidi | P29469 |
OMAi | DCVKCGY |
Family and domain databases
Gene3Di | 3.40.50.300, 1 hit |
InterProi | View protein in InterPro IPR031327, MCM IPR008045, MCM2 IPR018525, MCM_CS IPR001208, MCM_dom IPR041562, MCM_lid IPR027925, MCM_N IPR033762, MCM_OB IPR012340, NA-bd_OB-fold IPR027417, P-loop_NTPase |
PANTHERi | PTHR11630, PTHR11630, 1 hit PTHR11630:SF44, PTHR11630:SF44, 1 hit |
Pfami | View protein in Pfam PF00493, MCM, 1 hit PF12619, MCM2_N, 1 hit PF17855, MCM_lid, 1 hit PF14551, MCM_N, 1 hit PF17207, MCM_OB, 1 hit |
PRINTSi | PR01657, MCMFAMILY PR01658, MCMPROTEIN2 |
SMARTi | View protein in SMART SM00350, MCM, 1 hit |
SUPFAMi | SSF50249, SSF50249, 1 hit SSF52540, SSF52540, 1 hit |
PROSITEi | View protein in PROSITE PS00847, MCM_1, 1 hit PS50051, MCM_2, 1 hit |
i Sequence
Sequence statusi: Complete.
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 164 | S → T in CAA37615 (PubMed:2044961).Curated | 1 | |
Sequence conflicti | 172 – 173 | MD → IH in CAA37615 (PubMed:2044961).Curated | 2 | |
Sequence conflicti | 529 | G → P in CAA37615 (PubMed:2044961).Curated | 1 | |
Sequence conflicti | 578 | A → R in CAA37615 (PubMed:2044961).Curated | 1 | |
Sequence conflicti | 583 | D → H in CAA37615 (PubMed:2044961).Curated | 1 | |
Sequence conflicti | 712 | E → Q in CAA37615 (PubMed:2044961).Curated | 1 | |
Sequence conflicti | 733 – 747 | Missing in CAA37615 (PubMed:2044961).CuratedAdd BLAST | 15 | |
Sequence conflicti | 859 – 868 | RSFAIYTLGH → SLSQFIPWVTKTLLFLRISG YEDKKFSVSIHVLAILFSIY KFPLFFV in CAA37615 (PubMed:2044961).Curated | 10 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 392 | E → 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 |
PIRi | S45757 |
RefSeqi | NP_009530.1, NM_001178263.1 |
Genome annotation databases
EnsemblFungii | YBL023C_mRNA; YBL023C; YBL023C |
GeneIDi | 852258 |
KEGGi | sce:YBL023C |
Similar proteinsi
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 |
PIRi | S45757 |
RefSeqi | NP_009530.1, NM_001178263.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3JA8 | electron microscopy | 3.80 | 2 | 1-868 | [»] | |
3JC5 | electron microscopy | 4.70 | 2 | 1-868 | [»] | |
3JC6 | electron microscopy | 3.70 | 2 | 1-868 | [»] | |
3JC7 | electron microscopy | 4.80 | 2 | 1-868 | [»] | |
5BK4 | electron microscopy | 3.90 | 2/A | 1-868 | [»] | |
5U8S | electron microscopy | 6.10 | 2 | 1-868 | [»] | |
5U8T | electron microscopy | 4.90 | 2 | 1-868 | [»] | |
5V8F | electron microscopy | 3.90 | 2 | 1-868 | [»] | |
5XF8 | electron microscopy | 7.10 | 2 | 1-868 | [»] | |
6EYC | electron microscopy | 3.80 | 2 | 1-868 | [»] | |
6F0L | electron microscopy | 4.77 | 2/A | 1-868 | [»] | |
6HV9 | electron microscopy | 4.98 | 2 | 1-868 | [»] | |
6PTJ | electron microscopy | 3.80 | 2 | 1-868 | [»] | |
6PTN | electron microscopy | 5.80 | 2/i | 1-868 | [»] | |
6PTO | electron microscopy | 7.00 | 2/F/h | 1-868 | [»] | |
6RQC | electron microscopy | 4.40 | 2 | 1-868 | [»] | |
6SKL | electron microscopy | 3.70 | 2 | 1-868 | [»] | |
6SKO | electron microscopy | 3.40 | 2 | 1-868 | [»] | |
6U0M | electron microscopy | 3.90 | 2 | 201-864 | [»] | |
6WGF | electron microscopy | 7.70 | 2 | 1-868 | [»] | |
6WGG | electron microscopy | 8.10 | 2 | 1-868 | [»] | |
6WGI | electron microscopy | 10.00 | 2 | 1-868 | [»] | |
SMRi | P29469 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 32675, 202 interactors |
ComplexPortali | CPX-2944, MCM complex |
DIPi | DIP-2291N |
IntActi | P29469, 53 interactors |
MINTi | P29469 |
STRINGi | 4932.YBL023C |
PTM databases
iPTMneti | P29469 |
Proteomic databases
MaxQBi | P29469 |
PaxDbi | P29469 |
PRIDEi | P29469 |
Genome annotation databases
EnsemblFungii | YBL023C_mRNA; YBL023C; YBL023C |
GeneIDi | 852258 |
KEGGi | sce:YBL023C |
Organism-specific databases
SGDi | S000000119, MCM2 |
VEuPathDBi | FungiDB:YBL023C |
Phylogenomic databases
eggNOGi | KOG0477, Eukaryota |
GeneTreei | ENSGT01040000240460 |
HOGENOMi | CLU_000995_0_0_1 |
InParanoidi | P29469 |
OMAi | DCVKCGY |
Enzyme and pathway databases
Reactomei | 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 |
Miscellaneous databases
PROi | PR:P29469 |
RNActi | P29469, protein |
Family and domain databases
Gene3Di | 3.40.50.300, 1 hit |
InterProi | View protein in InterPro IPR031327, MCM IPR008045, MCM2 IPR018525, MCM_CS IPR001208, MCM_dom IPR041562, MCM_lid IPR027925, MCM_N IPR033762, MCM_OB IPR012340, NA-bd_OB-fold IPR027417, P-loop_NTPase |
PANTHERi | PTHR11630, PTHR11630, 1 hit PTHR11630:SF44, PTHR11630:SF44, 1 hit |
Pfami | View protein in Pfam PF00493, MCM, 1 hit PF12619, MCM2_N, 1 hit PF17855, MCM_lid, 1 hit PF14551, MCM_N, 1 hit PF17207, MCM_OB, 1 hit |
PRINTSi | PR01657, MCMFAMILY PR01658, MCMPROTEIN2 |
SMARTi | View protein in SMART SM00350, MCM, 1 hit |
SUPFAMi | SSF50249, SSF50249, 1 hit SSF52540, SSF52540, 1 hit |
PROSITEi | View protein in PROSITE PS00847, MCM_1, 1 hit PS50051, MCM_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | MCM2_YEAST | |
Accessioni | P29469Primary (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: | February 23, 2022 | |
This is version 204 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome II
Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families