P29469 (MCM2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA replication licensing factor MCM2
EC=3.6.4.12

Alternative name(s):
Minichromosome maintenance protein 2

Gene names

Name:	MCM2
Ordered Locus Names:	YBL023C
ORF Names:	YBL0438

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	868 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.5 Ref.6
Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	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. Ref.5 Ref.6
Subcellular location	Nucleus.
Miscellaneous	Present with 1690 molecules/cell in log phase SD medium. 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.
Sequence similarities	Belongs to the MCM family. Contains 1 MCM domain.

Ontologies

Keywords
Biological process	Cell cycle DNA replication
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	ATP-binding DNA-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Helicase Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA duplex unwinding Inferred from direct assay Ref.4. Source: GOC DNA replication initiation Inferred from electronic annotation. Source: InterPro DNA strand elongation involved in DNA replication Inferred from mutant phenotype PubMed 10834843. Source: SGD S phase of mitotic cell cycle Inferred from mutant phenotype PubMed 10834843. Source: SGD double-strand break repair via break-induced replication Inferred from mutant phenotype PubMed 20516198. Source: SGD pre-replicative complex assembly Inferred from direct assay PubMed 16824194. Source: SGD
Cellular_component	DNA replication preinitiation complex Inferred from direct assay PubMed 9554851. Source: SGD MCM complex Inferred from direct assay PubMed 12480933. Source: SGD cytoplasm Inferred from direct assay PubMed 10704410PubMed 22842922. Source: SGD pre-replicative complex Inferred from direct assay PubMed 16824194PubMed 9335335. Source: SGD replication fork protection complex Inferred from direct assay PubMed 16531994. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA helicase activity Inferred from electronic annotation. Source: InterPro DNA replication origin binding Inferred from direct assay PubMed 11756674PubMed 16824194. Source: SGD chromatin binding Inferred from direct assay PubMed 10783164. Source: SGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MCM4	P30665	3	EBI-10533,EBI-4326

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 868	868	DNA replication licensing factor MCM2		PRO_0000194091
Regions
	Domain	493 – 700	208	MCM
	Zinc finger	341 – 367	27	C4-type Potential
	Nucleotide binding	543 – 550	8	ATP Potential
	Motif	675 – 678	4	Arginine finger
Natural variations
	Natural variant	392	1	E → K in allele MCM2-1.
Experimental info
	Mutagenesis	364	1	C → Y, F, S or H: Loss of activity. Ref.1
	Mutagenesis	367	1	C → Y, F, S or H: Loss of activity. Ref.1
	Mutagenesis	549	1	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. Ref.4
	Mutagenesis	676	1	R → A: Loss of MCM2-7 complex helicase activity. Ref.4
	Sequence conflict	164	1	S → T in CAA37615. Ref.1
	Sequence conflict	172 – 173	2	MD → IH in CAA37615. Ref.1
	Sequence conflict	529	1	G → P in CAA37615. Ref.1
	Sequence conflict	578	1	A → R in CAA37615. Ref.1
	Sequence conflict	583	1	D → H in CAA37615. Ref.1
	Sequence conflict	712	1	E → Q in CAA37615. Ref.1
	Sequence conflict	733 – 747	15	Missing in CAA37615. Ref.1
	Sequence conflict	859 – 868	10	RSFAIYTLGH → SLSQFIPWVTKTLLFLRISG YEDKKFSVSIHVLAILFSIY KFPLFFV in CAA37615. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P29469 [UniParc]. Last modified October 1, 1994. Version 2. Checksum: F38FF682581B0EC0	FASTA	868	98,780
	10 20 30 40 50 60 MSDNRRRRRE EDDSDSENEL PPSSPQQHFR GGMNPVSSPI GSPDMINPEG DDNEVDDVPD 70 80 90 100 110 120 IDEVEEQMNE VDLMDDNMYE DYAADHNRDR YDPDQVDDRE QQELSLSERR RIDAQLNERD 130 140 150 160 170 180 RLLRNVAYID DEDEEQEGAA QLDEMGLPVQ RRRRRRQYED LENSDDDLLS DMDIDPLREE 190 200 210 220 230 240 LTLESLSNVK ANSYSEWITQ PNVSRTIARE LKSFLLEYTD ETGRSVYGAR IRTLGEMNSE 250 260 270 280 290 300 SLEVNYRHLA ESKAILALFL AKCPEEMLKI FDLVAMEATE LHYPDYARIH SEIHVRISDF 310 320 330 340 350 360 PTIYSLRELR ESNLSSLVRV TGVVTRRTGV FPQLKYVKFN CLKCGSILGP FFQDSNEEIR 370 380 390 400 410 420 ISFCTNCKSK GPFRVNGEKT VYRNYQRVTL QEAPGTVPPG RLPRHREVIL LADLVDVSKP 430 440 450 460 470 480 GEEVEVTGIY KNNYDGNLNA KNGFPVFATI IEANSIKRRE GNTANEGEEG LDVFSWTEEE 490 500 510 520 530 540 EREFRKISRD RGIIDKIISS MAPSIYGHRD IKTAVACSLF GGVPKNVNGK HSIRGDINVL 550 560 570 580 590 600 LLGDPGTAKS QILKYVEKTA HRAVFATGQG ASAVGLTASV RKDPITKEWT LEGGALVLAD 610 620 630 640 650 660 KGVCLIDEFD KMNDQDRTSI HEAMEQQSIS ISKAGIVTTL QARCSIIAAA NPNGGRYNST 670 680 690 700 710 720 LPLAQNVSLT EPILSRFDIL CVVRDLVDEE ADERLATFVV DSHVRSHPEN DEDREGEELK 730 740 750 760 770 780 NNGESAIEQG EDEINEQLNA RQRRLQRQRK KEEEISPIPQ ELLMKYIHYA RTKIYPKLHQ 790 800 810 820 830 840 MDMDKVSRVY ADLRRESIST GSFPITVRHL ESILRIAESF AKMRLSEFVS SYDLDRAIKV 850 860 VVDSFVDAQK VSVRRQLRRS FAIYTLGH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mcm2 and Mcm3, two proteins important for ARS activity, are related in structure and function." Yan H., Gibson S., Tye B.K. Genes Dev. 5:944-957(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF CYS-364 AND CYS-367.
[2]	"Analysis of a 17.4 kb DNA segment of yeast chromosome II encompassing the ribosomal protein L19 as well as proteins with homologies to components of the hnRNP and snRNP complexes and to the human proliferation-associated p120 antigen." van Dyck L., Jonniaux J.-L., Barreiros T.D.M., Kleine K., Goffeau A. Yeast 10:1663-1673(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K. EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"The Mcm2-7 complex has in vitro helicase activity." Bochman M.L., Schwacha A. Mol. Cell 31:287-293(2008) [PubMed] [Europe PMC] [Abstract] Cited for: RECONSTITUTION OF THE MCM2-7 COMPLEX, HELICASE ACTIVITY OF THE MCM2-7 COMPLEX, MUTAGENESIS OF LYS-549 AND ARG-676.
[5]	"Concerted loading of Mcm2-7 double hexamers around DNA during DNA replication origin licensing." Remus D., Beuron F., Tolun G., Griffith J.D., Morris E.P., Diffley J.F. Cell 139:719-730(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE MCM2-7 COMPLEX, FUNCTION OF THE MCM2-7 COMPLEX, ELECTRON MICROSCOPY OF THE MCM2-7 COMPLEX.
[6]	"A double-hexameric MCM2-7 complex is loaded onto origin DNA during licensing of eukaryotic DNA replication." Evrin C., Clarke P., Zech J., Lurz R., Sun J., Uhle S., Li H., Stillman B., Speck C. Proc. Natl. Acad. Sci. U.S.A. 106:20240-20245(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE MCM2-7 COMPLEX, FUNCTION OF THE MCM2-7 COMPLEX, ELECTRON MICROSCOPY OF THE MCM2-7 COMPLEX.
[7]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[8]	"PIM1 encodes a mitochondrial ATP-dependent protease that is required for mitochondrial function in the yeast Saccharomyces cerevisiae." van Dyck L., Pearce D.A., Sherman F. J. Biol. Chem. 269:238-242(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-85. Strain: ATCC 204508 / S288c.
[9]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
PIR	S45757.
RefSeq	NP_009530.1. NM_001178263.1.
3D structure databases
ProteinModelPortal	P29469.
SMR	P29469. Positions 214-841.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2291N.
IntAct	P29469. 45 interactions.
MINT	MINT-469073.
STRING	4932.YBL023C.
Proteomic databases
PaxDb	P29469.
PeptideAtlas	P29469.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YBL023C; YBL023C; YBL023C.
GeneID	852258.
KEGG	sce:YBL023C.
Organism-specific databases
CYGD	YBL023c.
SGD	S000000119. MCM2.
Phylogenomic databases
eggNOG	COG1241.
GeneTree	ENSGT00700000104566.
HOGENOM	HOG000224124.
KO	K02540.
OMA	NMEETVY.
OrthoDB	EOG4PZNFS.
Enzyme and pathway databases
Reactome	REACT_101785. DNA Replication. REACT_118473. Cell Cycle.
Gene expression databases
Genevestigator	P29469.
GermOnline	YBL023C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	2.40.50.140. 2 hits.
InterPro	IPR008045. MCM2. IPR018525. MCM_CS. IPR001208. MCM_DNA-dep_ATPase. IPR012340. NA-bd_OB-fold. [Graphical view]
Pfam	PF00493. MCM. 1 hit. PF12619. MCM2_N. 1 hit. [Graphical view]
PRINTS	PR01657. MCMFAMILY. PR01658. MCMPROTEIN2.
SMART	SM00350. MCM. 1 hit. [Graphical view]
SUPFAM	SSF50249. Nucleic_acid_OB. 1 hit.
PROSITE	PS00847. MCM_1. 1 hit. PS50051. MCM_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	970844.

Entry information

Entry name

MCM2_YEAST

Accession

Primary (citable) accession number: P29469
Secondary accession number(s): D6VPX7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	October 1, 1994
Last modified:	May 1, 2013
This is version 127 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program