Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P29469

- MCM2_YEAST

UniProt

P29469 - MCM2_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

DNA replication licensing factor MCM2

Gene

MCM2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri341 – 36727C4-typeSequence AnalysisAdd
BLAST
Nucleotide bindingi543 – 5508ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. chromatin binding Source: SGD
  3. DNA helicase activity Source: InterPro
  4. DNA replication origin binding Source: SGD
  5. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: SGD
  2. DNA duplex unwinding Source: GOC
  3. DNA replication initiation Source: InterPro
  4. DNA strand elongation involved in DNA replication Source: SGD
  5. double-strand break repair via break-induced replication Source: SGD
  6. negative regulation of ATP-dependent DNA helicase activity Source: SGD
  7. nuclear cell cycle DNA replication Source: SGD
  8. 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.
ReactomeiREACT_241537. Switching of origins to a post-replicative state.
REACT_245084. Removal of licensing factors from origins.
REACT_255883. Unwinding of DNA.

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
ProteomesiUP000002311: Chromosome II

Organism-specific databases

CYGDiYBL023c.
SGDiS000000119. MCM2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. DNA replication preinitiation complex Source: SGD
  3. MCM complex Source: SGD
  4. nuclear pre-replicative complex Source: SGD
  5. nucleoplasm Source: Reactome
  6. nucleus Source: SGD
  7. replication fork protection complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi364 – 3641C → Y, F, S or H: Loss of activity. 1 Publication
Mutagenesisi367 – 3671C → Y, F, S or H: Loss of activity. 1 Publication
Mutagenesisi549 – 5491K → 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
Mutagenesisi676 – 6761R → A: Loss of MCM2-7 complex helicase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 868868DNA replication licensing factor MCM2PRO_0000194091Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141Phosphoserine1 Publication
Modified residuei16 – 161Phosphoserine1 Publication
Modified residuei23 – 231Phosphoserine1 Publication
Modified residuei164 – 1641Phosphoserine1 Publication
Modified residuei170 – 1701Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP29469.
PaxDbiP29469.
PeptideAtlasiP29469.

Expressioni

Gene expression databases

GenevestigatoriP29469.

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. 107 interactions.
DIPiDIP-2291N.
IntActiP29469. 47 interactions.
MINTiMINT-469073.
STRINGi4932.YBL023C.

Structurei

3D structure databases

ProteinModelPortaliP29469.
SMRiP29469. Positions 214-841.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini493 – 700208MCMAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi675 – 6784Arginine finger

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri341 – 36727C4-typeSequence AnalysisAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG1241.
GeneTreeiENSGT00740000115337.
HOGENOMiHOG000224124.
InParanoidiP29469.
KOiK02540.
OMAiNMEETVY.
OrthoDBiEOG7B5X4C.

Family and domain databases

Gene3Di2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR008045. MCM2.
IPR018525. MCM_CS.
IPR001208. MCM_DNA-dep_ATPase.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00493. MCM. 1 hit.
PF12619. MCM2_N. 1 hit.
PF14551. MCM_N. 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti164 – 1641S → T in CAA37615. (PubMed:2044961)Curated
Sequence conflicti172 – 1732MD → IH in CAA37615. (PubMed:2044961)Curated
Sequence conflicti529 – 5291G → P in CAA37615. (PubMed:2044961)Curated
Sequence conflicti578 – 5781A → R in CAA37615. (PubMed:2044961)Curated
Sequence conflicti583 – 5831D → H in CAA37615. (PubMed:2044961)Curated
Sequence conflicti712 – 7121E → Q in CAA37615. (PubMed:2044961)Curated
Sequence conflicti733 – 74715Missing in CAA37615. (PubMed:2044961)CuratedAdd
BLAST
Sequence conflicti859 – 86810RSFAIYTLGH → SLSQFIPWVTKTLLFLRISG YEDKKFSVSIHVLAILFSIY KFPLFFV in CAA37615. (PubMed:2044961)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti392 – 3921E → K in allele MCM2-1.

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 .
PIRi S45757.
RefSeqi NP_009530.1. NM_001178263.1.

3D structure databases

ProteinModelPortali P29469.
SMRi P29469. Positions 214-841.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32675. 107 interactions.
DIPi DIP-2291N.
IntActi P29469. 47 interactions.
MINTi MINT-469073.
STRINGi 4932.YBL023C.

Proteomic databases

MaxQBi P29469.
PaxDbi P29469.
PeptideAtlasi P29469.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

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

Organism-specific databases

CYGDi YBL023c.
SGDi S000000119. MCM2.

Phylogenomic databases

eggNOGi COG1241.
GeneTreei ENSGT00740000115337.
HOGENOMi HOG000224124.
InParanoidi P29469.
KOi K02540.
OMAi NMEETVY.
OrthoDBi EOG7B5X4C.

Enzyme and pathway databases

BioCyci YEAST:G3O-28926-MONOMER.
Reactomei REACT_241537. Switching of origins to a post-replicative state.
REACT_245084. Removal of licensing factors from origins.
REACT_255883. Unwinding of DNA.

Miscellaneous databases

NextBioi 970844.
PROi P29469.

Gene expression databases

Genevestigatori P29469.

Family and domain databases

Gene3Di 2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProi IPR008045. MCM2.
IPR018525. MCM_CS.
IPR001208. MCM_DNA-dep_ATPase.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF00493. MCM. 1 hit.
PF12619. MCM2_N. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view ]
PRINTSi PR01657. MCMFAMILY.
PR01658. MCMPROTEIN2.
SMARTi SM00350. MCM. 1 hit.
[Graphical view ]
SUPFAMi SSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEi PS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-16; SER-23; SER-164 AND SER-170, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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 26, 2014
This is version 144 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

External Data

Dasty 3