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P53091

- MCM6_YEAST

UniProt

P53091 - MCM6_YEAST

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Protein

DNA replication licensing factor MCM6

Gene

MCM6

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. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity. Required for the entry in S phase and for cell division.2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi575 – 5828ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA helicase activity Source: InterPro
  3. DNA replication origin binding Source: SGD
  4. single-stranded DNA-dependent ATPase activity Source: SGD

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. DNA replication initiation Source: SGD
  3. DNA strand elongation involved in DNA replication Source: SGD
  4. DNA unwinding involved in DNA replication Source: SGD
  5. double-strand break repair via break-induced replication Source: SGD
  6. nuclear cell cycle DNA replication Source: SGD
  7. 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, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30681-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA replication licensing factor MCM6 (EC:3.6.4.12)
Alternative name(s):
Minichromosome maintenance protein 6
Gene namesi
Name:MCM6
Ordered Locus Names:YGL201C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

SGDiS000003169. MCM6.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi581 – 5811K → A: Loss of MCM2-7 complex helicase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10171017DNA replication licensing factor MCM6PRO_0000194117Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei78 – 781Phosphoserine1 Publication
Modified residuei249 – 2491Phosphoserine1 Publication
Modified residuei372 – 3721Phosphoserine1 Publication
Modified residuei766 – 7661Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53091.
PaxDbiP53091.
PeptideAtlasiP53091.
PRIDEiP53091.

Expressioni

Gene expression databases

GenevestigatoriP53091.

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. Interacts with MCM10.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MCM10P323545EBI-10556,EBI-5965
MCM4P306655EBI-10556,EBI-4326

Protein-protein interaction databases

BioGridi33056. 65 interactions.
DIPiDIP-1294N.
IntActiP53091. 54 interactions.
MINTiMINT-397018.
STRINGi4932.YGL201C.

Structurei

3D structure databases

ProteinModelPortaliP53091.
SMRiP53091. Positions 258-404, 508-832.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini525 – 732208MCMAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi707 – 7104Arginine finger

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1241.
GeneTreeiENSGT00550000074860.
HOGENOMiHOG000224130.
InParanoidiP53091.
KOiK02542.
OMAiLHNMIAK.
OrthoDBiEOG7Z69MX.

Family and domain databases

Gene3Di2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR008049. MCM6.
IPR018525. MCM_CS.
IPR001208. MCM_DNA-dep_ATPase.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11630:SF43. PTHR11630:SF43. 1 hit.
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01662. MCMPROTEIN6.
SMARTiSM00350. MCM. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 2 hits.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53091-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSPFPADTP SSNRPSNSSP PPSSIGAGFG SSSGLDSQIG SRLHFPSSSQ
60 70 80 90 100
PHVSNSQTGP FVNDSTQFSS QRLQTDGSAT NDMEGNEPAR SFKSRALNHV
110 120 130 140 150
KKVDDVTGEK VREAFEQFLE DFSVQSTDTG EVEKVYRAQI EFMKIYDLNT
160 170 180 190 200
IYIDYQHLSM RENGALAMAI SEQYYRFLPF LQKGLRRVVR KYAPELLNTS
210 220 230 240 250
DSLKRSEGDE GQADEDEQQD DDMNGSSLPR DSGSSAAPGN GTSAMATRSI
260 270 280 290 300
TTSTSPEQTE RVFQISFFNL PTVHRIRDIR SEKIGSLLSI SGTVTRTSEV
310 320 330 340 350
RPELYKASFT CDMCRAIVDN VEQSFKYTEP TFCPNPSCEN RAFWTLNVTR
360 370 380 390 400
SRFLDWQKVR IQENANEIPT GSMPRTLDVI LRGDSVERAK PGDRCKFTGV
410 420 430 440 450
EIVVPDVTQL GLPGVKPSST LDTRGISKTT EGLNSGVTGL RSLGVRDLTY
460 470 480 490 500
KISFLACHVI SIGSNIGASS PDANSNNRET ELQMAANLQA NNVYQDNERD
510 520 530 540 550
QEVFLNSLSS DEINELKEMV KDEHIYDKLV RSIAPAVFGH EAVKKGILLQ
560 570 580 590 600
MLGGVHKSTV EGIKLRGDIN ICVVGDPSTS KSQFLKYVVG FAPRSVYTSG
610 620 630 640 650
KASSAAGLTA AVVRDEEGGD YTIEAGALML ADNGICCIDE FDKMDISDQV
660 670 680 690 700
AIHEAMEQQT ISIAKAGIHA TLNARTSILA AANPVGGRYN RKLSLRGNLN
710 720 730 740 750
MTAPIMSRFD LFFVILDDCN EKIDTELASH IVDLHMKRDE AIEPPFSAEQ
760 770 780 790 800
LRRYIKYART FKPILTKEAR SYLVEKYKEL RKDDAQGFSR SSYRITVRQL
810 820 830 840 850
ESMIRLSEAI ARANCVDEIT PSFIAEAYDL LRQSIIRVDV DDVEMDEEFD
860 870 880 890 900
NIESQSHAAS GNNDDNDDGT GSGVITSEPP ADIEEGQSEA TARPGTSEKK
910 920 930 940 950
KTTVTYDKYV SMMNMIVRKI AEVDREGAEE LTAVDIVDWY LLQKENDLGS
960 970 980 990 1000
LAEYWEERRL AFKVIKRLVK DRILMEIHGT RHNLRDLENE ENENNKTVYV
1010
IHPNCEVLDQ LEPQDSS
Length:1,017
Mass (Da):112,978
Last modified:October 5, 2010 - v2
Checksum:i03AB793134E64A50
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti179 – 1791P → A in CAA96913. (PubMed:9169869)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY258324 Genomic DNA. Translation: AAO89010.1.
Z72723 Genomic DNA. Translation: CAA96913.1.
Y13624 Genomic DNA. Translation: CAA73947.1.
BK006941 Genomic DNA. Translation: DAA07914.1.
PIRiS64219.
RefSeqiNP_011314.2. NM_001181066.1.

Genome annotation databases

EnsemblFungiiYGL201C; YGL201C; YGL201C.
GeneIDi852673.
KEGGisce:YGL201C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY258324 Genomic DNA. Translation: AAO89010.1 .
Z72723 Genomic DNA. Translation: CAA96913.1 .
Y13624 Genomic DNA. Translation: CAA73947.1 .
BK006941 Genomic DNA. Translation: DAA07914.1 .
PIRi S64219.
RefSeqi NP_011314.2. NM_001181066.1.

3D structure databases

ProteinModelPortali P53091.
SMRi P53091. Positions 258-404, 508-832.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33056. 65 interactions.
DIPi DIP-1294N.
IntActi P53091. 54 interactions.
MINTi MINT-397018.
STRINGi 4932.YGL201C.

Proteomic databases

MaxQBi P53091.
PaxDbi P53091.
PeptideAtlasi P53091.
PRIDEi P53091.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGL201C ; YGL201C ; YGL201C .
GeneIDi 852673.
KEGGi sce:YGL201C.

Organism-specific databases

SGDi S000003169. MCM6.

Phylogenomic databases

eggNOGi COG1241.
GeneTreei ENSGT00550000074860.
HOGENOMi HOG000224130.
InParanoidi P53091.
KOi K02542.
OMAi LHNMIAK.
OrthoDBi EOG7Z69MX.

Enzyme and pathway databases

BioCyci YEAST:G3O-30681-MONOMER.

Miscellaneous databases

NextBioi 971976.
PROi P53091.

Gene expression databases

Genevestigatori P53091.

Family and domain databases

Gene3Di 2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProi IPR008049. MCM6.
IPR018525. MCM_CS.
IPR001208. MCM_DNA-dep_ATPase.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR11630:SF43. PTHR11630:SF43. 1 hit.
Pfami PF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view ]
PRINTSi PR01657. MCMFAMILY.
PR01662. MCMPROTEIN6.
SMARTi SM00350. MCM. 1 hit.
[Graphical view ]
SUPFAMi SSF50249. SSF50249. 2 hits.
SSF52540. SSF52540. 1 hit.
PROSITEi PS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of the Saccharomyces cerevisiae MCM6 gene."
    Duina A.A., Winston F.
    Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-766, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  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-581.
  5. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78 AND SER-372, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "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.
  7. "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.
  8. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  9. "Characterisation of Saccharomyces cerevisiae ARO8 and ARO9 genes encoding aromatic aminotransferases I and II reveals a new aminotransferase subfamily."
    Iraqui I., Vissers S., Cartiaux M., Urrestarazu A.
    Mol. Gen. Genet. 257:238-248(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 456-1017.
    Strain: Sigma 1278B.
  10. "A lesion in the DNA replication initiation factor Mcm10 induces pausing of elongation forks through chromosomal replication origins in Saccharomyces cerevisiae."
    Merchant A.M., Kawasaki Y., Chen Y., Lei M., Tye B.K.
    Mol. Cell. Biol. 17:3261-3271(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MCM10.
  11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  12. "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-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMCM6_YEAST
AccessioniPrimary (citable) accession number: P53091
Secondary accession number(s): D6VTV3, Q870M9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 5, 2010
Last modified: October 29, 2014
This is version 127 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 13400 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 VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3