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 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 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
chromatin binding
Source: SGD
Inferred from direct assayⁱ
- 10783164
DNA replication origin binding
Source: SGD
Inferred from direct assayⁱ
- 11756674
- 16824194
helicase activity Source: UniProtKB-KW
metal ion binding Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cellular response to DNA damage stimulus
Source: SGD
Inferred from mutant phenotypeⁱ
- 22564307
DNA duplex unwinding Source: GOC
DNA strand elongation involved in DNA replication
Source: SGD
Inferred from mutant phenotypeⁱ
- 10834843
double-strand break repair via break-induced replication
Source: SGD
Inferred from mutant phenotypeⁱ
- 20516198
mitotic DNA replication initiation
Source: SGD
Inferred from mutant phenotypeⁱ
- 8224843
- 9407029
negative regulation of ATP-dependent DNA helicase activity
Source: SGD
Inferred from direct assayⁱ
- 13679365
pre-replicative complex assembly involved in nuclear cell cycle DNA replication
Source: SGD
Inferred from direct assayⁱ
- 16824194

View the complete GO annotation on QuickGO ...

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

BioCycⁱ	YEAST:G3O-28926-MONOMER
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	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae
Proteomesⁱ	UP000002311 Componentⁱ: Chromosome II

Organism-specific databases

EuPathDBⁱ	FungiDB:YBL023C
Saccharomyces Genome Database More...SGDⁱ	S000000119 MCM2

Keywords - Cellular componentⁱ

Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	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	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

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P29469
PaxDbⁱ	P29469
PRIDEⁱ	P29469

PTM databases

iPTMnetⁱ	P29469

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 Publications

Binary interactionsⁱ

With	Entry	#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, 187 interactors
ComplexPortalⁱ	CPX-2944 MCM complex
Database of interacting proteins More...DIPⁱ	DIP-2291N
IntActⁱ	P29469, 53 interactors
Molecular INTeraction database More...MINTⁱ	P29469
STRINGⁱ	4932.YBL023C

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P29469
SMRⁱ	P29469
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	493 – 700	MCMAdd BLAST		208

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	675 – 678	Arginine finger		4

Sequence similaritiesⁱ

Belongs to the MCM family.Curated

Zinc finger

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Zinc fingerⁱ	341 – 367	C4-typeSequence analysisAdd BLAST		27

Keywords - Domainⁱ

Zinc-finger

Phylogenomic databases

Ensembl GeneTree More...GeneTreeⁱ	ENSGT00920000149148
HOGENOMⁱ	HOG000224124
InParanoidⁱ	P29469
KEGG Orthology (KO) More...KOⁱ	K02540
OMAⁱ	KYDCVKC
Database of Orthologous Groups More...OrthoDBⁱ	EOG092C0VUM

Family and domain databases

InterProⁱ	View 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
PANTHERⁱ	PTHR11630 PTHR11630, 1 hit PTHR11630:SF44 PTHR11630:SF44, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00493 MCM, 1 hit PF12619 MCM2_N, 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, 2 hits
PROSITEⁱ	View protein in PROSITE PS00847 MCM_1, 1 hit PS50051 MCM_2, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P29469-1 [UniParc]FASTA Add 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 key	Position(s)	DescriptionActions	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
NCBI Reference Sequences More...RefSeqⁱ	NP_009530.1, NM_001178263.1

Genome annotation databases

EnsemblFungiⁱ	YBL023C; YBL023C; YBL023C
GeneIDⁱ	852258
KEGGⁱ	sce:YBL023C

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P29469	DNA helicase		YEASB		868	UniRef100_P29469
DNA helicase		YEAS1		868
DNA helicase		YEASK		868
DNA helicase		YEASC		868
DNA helicase		YEASV		868
+4

Protein	Similar proteins		Species	Score	Length	Source
P29469	DNA helicase		YEASB		868	UniRef90_P29469
DNA helicase		YEAS1		868
DNA helicase		YEASK		868
DNA helicase		YEASC		868
DNA helicase		YEASV		868
+9

Protein	Similar proteins		Species	Score	Length	Source
P29469	DNA replication licensing factor mcm2		SCHPO		830	UniRef50_P29469
DNA helicase		YEASB		868
DNA helicase		YEAS1		868
DNA helicase		YEASK		868
DNA helicase		YEASC		868
+239

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:	September 12, 2018
	This is version 182 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, Complete proteome, Reference proteome

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P29469 (MCM2_YEAST)

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DNA replication licensing factor MCM2

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Motif

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Zinc finger

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Sequence databases

Genome annotation databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ