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Q14566

- MCM6_HUMAN

UniProt

Q14566 - MCM6_HUMAN

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Protein

DNA replication licensing factor MCM6

Gene
MCM6
Organism
Homo sapiens (Human)
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.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi396 – 4038ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. DNA helicase activity Source: Ensembl
  3. identical protein binding Source: IntAct
  4. protein binding Source: UniProtKB
  5. single-stranded DNA binding Source: Ensembl

GO - Biological processi

  1. DNA replication Source: UniProtKB
  2. DNA replication initiation Source: InterPro
  3. DNA strand elongation involved in DNA replication Source: Reactome
  4. DNA unwinding involved in DNA replication Source: Ensembl
  5. G1/S transition of mitotic cell cycle Source: Reactome
  6. mitotic cell cycle Source: Reactome
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

ReactomeiREACT_1095. Activation of the pre-replicative complex.
REACT_1156. Orc1 removal from chromatin.
REACT_207. Removal of licensing factors from origins.
REACT_2148. Switching of origins to a post-replicative state.
REACT_2243. Assembly of the pre-replicative complex.
REACT_6769. Activation of ATR in response to replication stress.
REACT_6776. Unwinding of DNA.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA replication licensing factor MCM6 (EC:3.6.4.12)
Alternative name(s):
p105MCM
Gene namesi
Name:MCM6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:6949. MCM6.

Subcellular locationi

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

GO - Cellular componenti

  1. MCM complex Source: UniProtKB
  2. nucleoplasm Source: Reactome
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi757 – 7571E → A or D: Impairs interaction with CTD1. 1 Publication
Mutagenesisi763 – 7631E → A or D: Impairs interaction with CTD1. 1 Publication
Mutagenesisi766 – 7661L → A: Impairs interaction with CTD1. 1 Publication

Organism-specific databases

MIMi223100. phenotype.
Orphaneti319681. Lactase non-persistence in adulthood.
PharmGKBiPA30696.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 821821DNA replication licensing factor MCM6PRO_0000194113Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine4 Publications
Modified residuei13 – 131Phosphoserine1 Publication
Modified residuei271 – 2711Phosphoserine4 Publications
Modified residuei643 – 6431N6-acetyllysine By similarity
Modified residuei762 – 7621Phosphoserine4 Publications
Modified residuei791 – 7911Phosphothreonine1 Publication

Post-translational modificationi

O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ14566.
PaxDbiQ14566.
PeptideAtlasiQ14566.
PRIDEiQ14566.

PTM databases

PhosphoSiteiQ14566.

Miscellaneous databases

PMAP-CutDBQ14566.

Expressioni

Gene expression databases

ArrayExpressiQ14566.
BgeeiQ14566.
CleanExiHS_MCM6.
GenevestigatoriQ14566.

Organism-specific databases

HPAiCAB009577.
HPA004818.

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 (By simililarity). May interact with MCM10. Interacts with TIPIN. Interacts with CDT1. Interacts with MCMBP.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-374900,EBI-374900
Q763532EBI-374900,EBI-6248077From a different organism.
CDKN2AP427714EBI-374900,EBI-375053
CDT1Q9H2113EBI-374900,EBI-456953
MCM10Q7L5902EBI-374900,EBI-374912
MCM2P497369EBI-374900,EBI-374819
MCM3P252052EBI-374900,EBI-355153
MCM7P339935EBI-374900,EBI-355924
MCMBPQ9BTE314EBI-374900,EBI-749378
SSRP1Q089452EBI-374900,EBI-353771

Protein-protein interaction databases

BioGridi110343. 74 interactions.
DIPiDIP-31727N.
IntActiQ14566. 33 interactions.
MINTiMINT-5004576.
STRINGi9606.ENSP00000264156.

Structurei

Secondary structure

1
821
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi709 – 7113
Beta strandi714 – 7163
Helixi718 – 73720
Beta strandi739 – 7413
Helixi745 – 75612
Turni757 – 7593
Helixi763 – 78220
Helixi793 – 7964

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KLQNMR-A708-821[»]
2LE8NMR-A708-821[»]
ProteinModelPortaliQ14566.
SMRiQ14566. Positions 27-652, 708-821.

Miscellaneous databases

EvolutionaryTraceiQ14566.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini346 – 553208MCMAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi528 – 5314Arginine finger

Sequence similaritiesi

Belongs to the MCM family.
Contains 1 MCM domain.

Phylogenomic databases

eggNOGiCOG1241.
HOGENOMiHOG000224130.
HOVERGENiHBG006334.
InParanoidiQ14566.
KOiK02542.
OMAiGTNIRGE.
OrthoDBiEOG7CCBQC.
PhylomeDBiQ14566.
TreeFamiTF105646.

Family and domain databases

Gene3Di2.20.28.10. 1 hit.
2.40.50.140. 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.
IPR004039. Rubredoxin-type_fold.
[Graphical view]
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01662. MCMPROTEIN6.
SMARTiSM00350. MCM. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q14566-1 [UniParc]FASTAAdd to Basket

« Hide

MDLAAAAEPG AGSQHLEVRD EVAEKCQKLF LDFLEEFQSS DGEIKYLQLA    50
EELIRPERNT LVVSFVDLEQ FNQQLSTTIQ EEFYRVYPYL CRALKTFVKD 100
RKEIPLAKDF YVAFQDLPTR HKIRELTSSR IGLLTRISGQ VVRTHPVHPE 150
LVSGTFLCLD CQTVIRDVEQ QFKYTQPNIC RNPVCANRRR FLLDTNKSRF 200
VDFQKVRIQE TQAELPRGSI PRSLEVILRA EAVESAQAGD KCDFTGTLIV 250
VPDVSKLSTP GARAETNSRV SGVDGYETEG IRGLRALGVR DLSYRLVFLA 300
CCVAPTNPRF GGKELRDEEQ TAESIKNQMT VKEWEKVFEM SQDKNLYHNL 350
CTSLFPTIHG NDEVKRGVLL MLFGGVPKTT GEGTSLRGDI NVCIVGDPST 400
AKSQFLKHVE EFSPRAVYTS GKASSAAGLT AAVVRDEESH EFVIEAGALM 450
LADNGVCCID EFDKMDVRDQ VAIHEAMEQQ TISITKAGVK ATLNARTSIL 500
AAANPISGHY DRSKSLKQNI NLSAPIMSRF DLFFILVDEC NEVTDYAIAR 550
RIVDLHSRIE ESIDRVYSLD DIRRYLLFAR QFKPKISKES EDFIVEQYKH 600
LRQRDGSGVT KSSWRITVRQ LESMIRLSEA MARMHCCDEV QPKHVKEAFR 650
LLNKSIIRVE TPDVNLDQEE EIQMEVDEGA GGINGHADSP APVNGINGYN 700
EDINQESAPK ASLRLGFSEY CRISNLIVLH LRKVEEEEDE SALKRSELVN 750
WYLKEIESEI DSEEELINKK RIIEKVIHRL THYDHVLIEL TQAGLKGSTE 800
GSESYEEDPY LVVNPNYLLE D 821
Length:821
Mass (Da):92,889
Last modified:November 1, 1997 - v1
Checksum:iF94968EB25A3E501
GO

Polymorphismi

Intronic variations in MCM6 upstream from the LCT gene are associated with adult-type hypolactasia [MIMi: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).

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti35 – 351E → V.
Corresponds to variant rs3087355 [ dbSNP | Ensembl ].
VAR_014816
Natural varianti806 – 8061E → K.1 Publication
Corresponds to variant rs4988283 [ dbSNP | Ensembl ].
VAR_016340

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti377 – 38711PKTTGEGTSLR → SKDNRRRDLSS in AAC50766. 1 PublicationAdd
BLAST
Sequence conflicti495 – 4951A → T in AAC50766. 1 Publication
Sequence conflicti738 – 7381Missing in AAB48165. 1 Publication
Sequence conflicti790 – 7901L → P in AAC50766. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS2179.1.
RefSeqiNP_005906.2. NM_005915.5.
UniGeneiHs.444118.

Genome annotation databases

EnsembliENST00000264156; ENSP00000264156; ENSG00000076003.
GeneIDi4175.
KEGGihsa:4175.
UCSCiuc002tuw.4. human.

Polymorphism databases

DMDMi2497824.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS2179.1.
RefSeqi NP_005906.2. NM_005915.5.
UniGenei Hs.444118.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KLQ NMR - A 708-821 [» ]
2LE8 NMR - A 708-821 [» ]
ProteinModelPortali Q14566.
SMRi Q14566. Positions 27-652, 708-821.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110343. 74 interactions.
DIPi DIP-31727N.
IntActi Q14566. 33 interactions.
MINTi MINT-5004576.
STRINGi 9606.ENSP00000264156.

Chemistry

DrugBanki DB01076. Atorvastatin.

PTM databases

PhosphoSitei Q14566.

Polymorphism databases

DMDMi 2497824.

Proteomic databases

MaxQBi Q14566.
PaxDbi Q14566.
PeptideAtlasi Q14566.
PRIDEi Q14566.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264156 ; ENSP00000264156 ; ENSG00000076003 .
GeneIDi 4175.
KEGGi hsa:4175.
UCSCi uc002tuw.4. human.

Organism-specific databases

CTDi 4175.
GeneCardsi GC02M136619.
HGNCi HGNC:6949. MCM6.
HPAi CAB009577.
HPA004818.
MIMi 223100. phenotype.
601806. gene.
neXtProti NX_Q14566.
Orphaneti 319681. Lactase non-persistence in adulthood.
PharmGKBi PA30696.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1241.
HOGENOMi HOG000224130.
HOVERGENi HBG006334.
InParanoidi Q14566.
KOi K02542.
OMAi GTNIRGE.
OrthoDBi EOG7CCBQC.
PhylomeDBi Q14566.
TreeFami TF105646.

Enzyme and pathway databases

Reactomei REACT_1095. Activation of the pre-replicative complex.
REACT_1156. Orc1 removal from chromatin.
REACT_207. Removal of licensing factors from origins.
REACT_2148. Switching of origins to a post-replicative state.
REACT_2243. Assembly of the pre-replicative complex.
REACT_6769. Activation of ATR in response to replication stress.
REACT_6776. Unwinding of DNA.

Miscellaneous databases

ChiTaRSi MCM6. human.
EvolutionaryTracei Q14566.
GeneWikii MCM6.
GenomeRNAii 4175.
NextBioi 16446.
PMAP-CutDB Q14566.
PROi Q14566.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q14566.
Bgeei Q14566.
CleanExi HS_MCM6.
Genevestigatori Q14566.

Family and domain databases

Gene3Di 2.20.28.10. 1 hit.
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.
IPR004039. Rubredoxin-type_fold.
[Graphical view ]
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. 1 hit.
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. "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. 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.
    , 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. 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. Cited for: INVOLVEMENT IN ADULT-TYPE HYPOLACTASIA AND LACTASE PERSISTANCE.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-791, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  17. 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. 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. 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.

Entry informationi

Entry nameiMCM6_HUMAN
AccessioniPrimary (citable) accession number: Q14566
Secondary accession number(s): B2R6H2, Q13504, Q99859
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 3, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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