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UniProtKB - P29469 (MCM2_YEAST)

Protein

DNA replication licensing factor MCM2

Gene

MCM2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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

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.

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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionDNA-binding, Helicase, Hydrolase
Biological processCell cycle, DNA replication
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-28926-MONOMER
ReactomeiR-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
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBL023C
SGDiS000000119 MCM2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
PaxDbiP29469
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

Protein-protein interaction databases

BioGridi32675, 187 interactors
ComplexPortaliCPX-2944 MCM complex
DIPiDIP-2291N
IntActiP29469, 53 interactors
MINTiP29469
STRINGi4932.YBL023C

Structurei

3D structure databases

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

Zinc finger

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

Keywords - Domaini

Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00920000149148
HOGENOMiHOG000224124
InParanoidiP29469
KOiK02540
OMAiKYDCVKC
OrthoDBiEOG092C0VUM

Family and domain databases

InterProiView protein in InterPro
IPR031327 MCM
IPR008045 MCM2
IPR018525 MCM_CS
IPR001208 MCM_dom
IPR027925 MCM_N
IPR033762 MCM_OB
IPR012340 NA-bd_OB-fold
IPR027417 P-loop_NTPase
PANTHERiPTHR11630 PTHR11630, 1 hit
PTHR11630:SF44 PTHR11630:SF44, 1 hit
PfamiView protein in Pfam
PF00493 MCM, 1 hit
PF12619 MCM2_N, 1 hit
PF14551 MCM_N, 1 hit
PF17207 MCM_OB, 1 hit
PRINTSiPR01657 MCMFAMILY
PR01658 MCMPROTEIN2
SMARTiView protein in SMART
SM00350 MCM, 1 hit
SUPFAMiSSF50249 SSF50249, 1 hit
SSF52540 SSF52540, 2 hits
PROSITEiView protein in PROSITE
PS00847 MCM_1, 1 hit
PS50051 MCM_2, 1 hit

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

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
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[»]
5BK4electron microscopy3.902/A1-868[»]
5H7Ielectron microscopy7.1021-868[»]
5U8Selectron microscopy6.1021-868[»]
5U8Telectron microscopy4.9021-868[»]
5UDBelectron microscopy3.9021-868[»]
5V8Felectron microscopy3.9021-868[»]
5XF8electron microscopy7.1021-868[»]
6EYCelectron microscopy3.8021-868[»]
6F0Lelectron microscopy4.772/A1-868[»]
ProteinModelPortaliP29469
SMRiP29469
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32675, 187 interactors
ComplexPortaliCPX-2944 MCM complex
DIPiDIP-2291N
IntActiP29469, 53 interactors
MINTiP29469
STRINGi4932.YBL023C

PTM databases

iPTMnetiP29469

Proteomic databases

MaxQBiP29469
PaxDbiP29469
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

GeneTreeiENSGT00920000149148
HOGENOMiHOG000224124
InParanoidiP29469
KOiK02540
OMAiKYDCVKC
OrthoDBiEOG092C0VUM

Enzyme and pathway databases

BioCyciYEAST:G3O-28926-MONOMER
ReactomeiR-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

PROiPR:P29469

Family and domain databases

InterProiView protein in InterPro
IPR031327 MCM
IPR008045 MCM2
IPR018525 MCM_CS
IPR001208 MCM_dom
IPR027925 MCM_N
IPR033762 MCM_OB
IPR012340 NA-bd_OB-fold
IPR027417 P-loop_NTPase
PANTHERiPTHR11630 PTHR11630, 1 hit
PTHR11630:SF44 PTHR11630:SF44, 1 hit
PfamiView protein in Pfam
PF00493 MCM, 1 hit
PF12619 MCM2_N, 1 hit
PF14551 MCM_N, 1 hit
PF17207 MCM_OB, 1 hit
PRINTSiPR01657 MCMFAMILY
PR01658 MCMPROTEIN2
SMARTiView protein in SMART
SM00350 MCM, 1 hit
SUPFAMiSSF50249 SSF50249, 1 hit
SSF52540 SSF52540, 2 hits
PROSITEiView protein in PROSITE
PS00847 MCM_1, 1 hit
PS50051 MCM_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiMCM2_YEAST
AccessioniPrimary (citable) accession number: P29469
Secondary accession number(s): D6VPX7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 1, 1994
Last modified: September 12, 2018
This is version 182 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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