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Q14566 (MCM6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA replication licensing factor MCM6

EC=3.6.4.12
Alternative name(s):
p105MCM
Gene names
Name:MCM6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length821 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Ref.8

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 (By simililarity). May interact with MCM10. Interacts with TIPIN. Interacts with CDT1. Interacts with MCMBP. Ref.8 Ref.9 Ref.11 Ref.13 Ref.14 Ref.25

Subcellular location

Nucleus. Note: Binds to chromatin during G1 and detach from it during S phase.

Post-translational modification

O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner. Ref.22

Polymorphism

Intronic variations in MCM6 upstream from the LCT gene are associated with adult-type hypolactasia [MIM:223100] leading to lactose intolerance, or with lactase persistance. Lactose intolerance is a normal physiological phenomenon caused by developmental down-regulation of lactase activity during childhood or early adulthood. A non-coding variation in MCM6 affects the transcriptional regulation of the LCT gene resulting in down-regulation of lactase activity. However, the majority of Northern Europeans and some African populations have the ability to maintain lactase activity and digest lactose throughout life (lactase persistence).

Miscellaneous

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 processCell cycle
DNA replication
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionHelicase
Hydrolase
   PTMAcetylation
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Non-traceable author statement Ref.1. Source: UniProtKB

DNA replication initiation

Inferred from electronic annotation. Source: InterPro

DNA strand elongation involved in DNA replication

Traceable author statement. Source: Reactome

DNA unwinding involved in DNA replication

Inferred from electronic annotation. Source: Ensembl

G1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

   Cellular_componentMCM complex

Inferred from direct assay Ref.14. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.11. Source: UniProtKB

   Molecular_functionATP binding

Non-traceable author statement Ref.1. Source: UniProtKB

DNA helicase activity

Inferred from electronic annotation. Source: Ensembl

identical protein binding

Inferred from physical interaction PubMed 15232106PubMed 16189514. Source: IntAct

protein binding

Inferred from physical interaction Ref.9PubMed 16438930. Source: UniProtKB

single-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 821821DNA replication licensing factor MCM6
PRO_0000194113

Regions

Domain346 – 553208MCM
Nucleotide binding396 – 4038ATP Potential
Motif528 – 5314Arginine finger

Amino acid modifications

Modified residue11N-acetylmethionine Ref.18 Ref.20 Ref.23 Ref.24
Modified residue131Phosphoserine Ref.20
Modified residue2711Phosphoserine Ref.12 Ref.17 Ref.19 Ref.20
Modified residue6431N6-acetyllysine By similarity
Modified residue7621Phosphoserine Ref.12 Ref.17 Ref.19 Ref.20
Modified residue7911Phosphothreonine Ref.16

Natural variations

Natural variant351E → V.
Corresponds to variant rs3087355 [ dbSNP | Ensembl ].
VAR_014816
Natural variant8061E → K. Ref.3
Corresponds to variant rs4988283 [ dbSNP | Ensembl ].
VAR_016340

Experimental info

Mutagenesis7571E → A or D: Impairs interaction with CTD1. Ref.25
Mutagenesis7631E → A or D: Impairs interaction with CTD1. Ref.25
Mutagenesis7661L → A: Impairs interaction with CTD1. Ref.25
Sequence conflict377 – 38711PKTTGEGTSLR → SKDNRRRDLSS in AAC50766. Ref.2
Sequence conflict4951A → T in AAC50766. Ref.2
Sequence conflict7381Missing in AAB48165. Ref.7
Sequence conflict7901L → P in AAC50766. Ref.2

Secondary structure

................ 821
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q14566 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: F94968EB25A3E501

FASTA82192,889
        10         20         30         40         50         60 
MDLAAAAEPG AGSQHLEVRD EVAEKCQKLF LDFLEEFQSS DGEIKYLQLA EELIRPERNT 

        70         80         90        100        110        120 
LVVSFVDLEQ FNQQLSTTIQ EEFYRVYPYL CRALKTFVKD RKEIPLAKDF YVAFQDLPTR 

       130        140        150        160        170        180 
HKIRELTSSR IGLLTRISGQ VVRTHPVHPE LVSGTFLCLD CQTVIRDVEQ QFKYTQPNIC 

       190        200        210        220        230        240 
RNPVCANRRR FLLDTNKSRF VDFQKVRIQE TQAELPRGSI PRSLEVILRA EAVESAQAGD 

       250        260        270        280        290        300 
KCDFTGTLIV VPDVSKLSTP GARAETNSRV SGVDGYETEG IRGLRALGVR DLSYRLVFLA 

       310        320        330        340        350        360 
CCVAPTNPRF GGKELRDEEQ TAESIKNQMT VKEWEKVFEM SQDKNLYHNL CTSLFPTIHG 

       370        380        390        400        410        420 
NDEVKRGVLL MLFGGVPKTT GEGTSLRGDI NVCIVGDPST AKSQFLKHVE EFSPRAVYTS 

       430        440        450        460        470        480 
GKASSAAGLT AAVVRDEESH EFVIEAGALM LADNGVCCID EFDKMDVRDQ VAIHEAMEQQ 

       490        500        510        520        530        540 
TISITKAGVK ATLNARTSIL AAANPISGHY DRSKSLKQNI NLSAPIMSRF DLFFILVDEC 

       550        560        570        580        590        600 
NEVTDYAIAR RIVDLHSRIE ESIDRVYSLD DIRRYLLFAR QFKPKISKES EDFIVEQYKH 

       610        620        630        640        650        660 
LRQRDGSGVT KSSWRITVRQ LESMIRLSEA MARMHCCDEV QPKHVKEAFR LLNKSIIRVE 

       670        680        690        700        710        720 
TPDVNLDQEE EIQMEVDEGA GGINGHADSP APVNGINGYN EDINQESAPK ASLRLGFSEY 

       730        740        750        760        770        780 
CRISNLIVLH LRKVEEEEDE SALKRSELVN WYLKEIESEI DSEEELINKK RIIEKVIHRL 

       790        800        810        820 
THYDHVLIEL TQAGLKGSTE GSESYEEDPY LVVNPNYLLE D 

« Hide

References

« Hide 'large scale' references
[1]"HsMCM6: a new member of the human MCM/P1 family encodes a protein homologous to fission yeast Mis5."
Tsuruga H., Yabuta N., Hosoya S., Tamura K., Endo Y., Nojima H.
Genes Cells 2:381-399(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Human protein MCM6 on HeLa cell chromatin."
Holthoff H.P., Baack M., Richter A., Ritzi M., Knippers R.
J. Biol. Chem. 273:7320-7325(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]NIEHS SNPs program
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-806.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Cervix.
[7]"Characterisation of a human homologue of a yeast cell division cycle gene, MCM6, located adjacent to the 5' end of the lactase gene on chromosome 2q21."
Harvey C.B., Wang Y., Darmoul D., Phillips A., Mantei N., Swallow D.M.
FEBS Lett. 398:135-140(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 640-821.
[8]"A DNA helicase activity is associated with an MCM4, -6, and -7 protein complex."
Ishimi Y.
J. Biol. Chem. 272:24508-24513(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE MCM2-7 COMPLEX, FUNCTION.
[9]"The human homolog of Saccharomyces cerevisiae Mcm10 interacts with replication factors and dissociates from nuclease-resistant nuclear structures in G(2) phase."
Izumi M., Yanagi K., Mizuno T., Yokoi M., Kawasaki Y., Moon K.Y., Hurwitz J., Yatagai F., Hanaoka F.
Nucleic Acids Res. 28:4769-4777(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MCM10.
[10]"Identification of a variant associated with adult-type hypolactasia."
Enattah N.S., Sahi T., Savilahti E., Terwilliger J.D., Peltonen L., Jaervelae I.
Nat. Genet. 30:233-237(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN ADULT-TYPE HYPOLACTASIA.
[11]"Essential role of phosphorylation of MCM2 by Cdc7/Dbf4 in the initiation of DNA replication in mammalian cells."
Tsuji T., Ficarro S.B., Jiang W.
Mol. Biol. Cell 17:4459-4472(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE MCM2-7 COMPLEX, ATPASE ACTIVITY OF THE MCM2-7 COMPLEX.
[12]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271 AND SER-762, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Tipin and Timeless form a mutually protective complex required for genotoxic stress resistance and checkpoint function."
Chou D.M., Elledge S.J.
Proc. Natl. Acad. Sci. U.S.A. 103:18143-18147(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TIPIN.
[14]"Identification and characterization of a novel component of the human minichromosome maintenance complex."
Sakwe A.M., Nguyen T., Athanasopoulos V., Shire K., Frappier L.
Mol. Cell. Biol. 27:3044-3055(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: HELICASE ACTIVITY OF THE MCM2-3 COMPLEX, INTERACTION WITH MCMBP, IDENTIFICATION IN THE MCM2-7 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[15]"Convergent adaptation of human lactase persistence in Africa and Europe."
Tishkoff S.A., Reed F.A., Ranciaro A., Voight B.F., Babbitt C.C., Silverman J.S., Powell K., Mortensen H.M., Hirbo J.B., Osman M., Ibrahim M., Omar S.A., Lema G., Nyambo T.B., Ghori J., Bumpstead S., Pritchard J.K., Wray G.A., Deloukas P.
Nat. Genet. 39:31-40(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN ADULT-TYPE HYPOLACTASIA AND LACTASE PERSISTANCE.
[16]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-791, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[17]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271 AND SER-762, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271 AND SER-762, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[20]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-271 AND SER-762, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Characterization of O-GlcNAc cycling and proteomic identification of differentially O-GlcNAcylated proteins during G1/S transition."
Drougat L., Olivier-Van Stichelen S., Mortuaire M., Foulquier F., Lacoste A.S., Michalski J.C., Lefebvre T., Vercoutter-Edouart A.S.
Biochim. Biophys. Acta 1820:1839-1848(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION.
[23]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"Characterization and structure determination of the Cdt1 binding domain of human minichromosome maintenance (Mcm) 6."
Wei Z., Liu C., Wu X., Xu N., Zhou B., Liang C., Zhu G.
J. Biol. Chem. 285:12469-12473(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 708-821, INTERACTION WITH CDT1, MUTAGENESIS OF GLU-757; GLU-763 AND LEU-766.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D84557 mRNA. Translation: BAA12699.1.
U46838 mRNA. Translation: AAC50766.1.
AY220757 Genomic DNA. Translation: AAO26043.1.
AK312575 mRNA. Translation: BAG35469.1.
CH471058 Genomic DNA. Translation: EAX11621.1.
BC032374 mRNA. Translation: AAH32374.1.
AH005100 Genomic DNA. Translation: AAB48165.1.
CCDSCCDS2179.1.
RefSeqNP_005906.2. NM_005915.5.
UniGeneHs.444118.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KLQNMR-A708-821[»]
2LE8NMR-A708-821[»]
ProteinModelPortalQ14566.
SMRQ14566. Positions 27-652, 708-821.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110343. 74 interactions.
DIPDIP-31727N.
IntActQ14566. 33 interactions.
MINTMINT-5004576.
STRING9606.ENSP00000264156.

Chemistry

DrugBankDB01076. Atorvastatin.

PTM databases

PhosphoSiteQ14566.

Polymorphism databases

DMDM2497824.

Proteomic databases

MaxQBQ14566.
PaxDbQ14566.
PeptideAtlasQ14566.
PRIDEQ14566.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264156; ENSP00000264156; ENSG00000076003.
GeneID4175.
KEGGhsa:4175.
UCSCuc002tuw.4. human.

Organism-specific databases

CTD4175.
GeneCardsGC02M136619.
HGNCHGNC:6949. MCM6.
HPACAB009577.
HPA004818.
MIM223100. phenotype.
601806. gene.
neXtProtNX_Q14566.
Orphanet319681. Lactase non-persistence in adulthood.
PharmGKBPA30696.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1241.
HOGENOMHOG000224130.
HOVERGENHBG006334.
InParanoidQ14566.
KOK02542.
OMAGTNIRGE.
OrthoDBEOG7CCBQC.
PhylomeDBQ14566.
TreeFamTF105646.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpressQ14566.
BgeeQ14566.
CleanExHS_MCM6.
GenevestigatorQ14566.

Family and domain databases

Gene3D2.20.28.10. 1 hit.
2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProIPR008049. MCM6.
IPR018525. MCM_CS.
IPR001208. MCM_DNA-dep_ATPase.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
IPR004039. Rubredoxin-type_fold.
[Graphical view]
PfamPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSPR01657. MCMFAMILY.
PR01662. MCMPROTEIN6.
SMARTSM00350. MCM. 1 hit.
[Graphical view]
SUPFAMSSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMCM6. human.
EvolutionaryTraceQ14566.
GeneWikiMCM6.
GenomeRNAi4175.
NextBio16446.
PMAP-CutDBQ14566.
PROQ14566.
SOURCESearch...

Entry information

Entry nameMCM6_HUMAN
AccessionPrimary (citable) accession number: Q14566
Secondary accession number(s): B2R6H2, Q13504, Q99859
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM