Q14566 (MCM6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA replication licensing factor MCM6
EC=3.6.4.12

Alternative name(s):
p105MCM

Gene names

Name:

MCM6

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	821 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. 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.22
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.21
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 process	Cell cycle DNA replication
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Helicase Hydrolase
PTM	Acetylation Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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 replication Inferred from electronic annotation. Source: Compara G1/S transition of mitotic cell cycle Traceable author statement. Source: Reactome M/G1 transition of mitotic cell cycle Traceable author statement. Source: Reactome S phase of mitotic cell cycle Traceable author statement. Source: Reactome cell cycle checkpoint Traceable author statement. Source: Reactome
Cellular_component	MCM complex Inferred from direct assay Ref.14. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	ATP binding Non-traceable author statement Ref.1. Source: UniProtKB DNA helicase activity Inferred from electronic annotation. Source: Compara single-stranded DNA binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-374900,EBI-374900
	Q76353	2	EBI-374900,EBI-6248077	From a different organism.
CDKN2A	P42771	4	EBI-374900,EBI-375053
CDT1	Q9H211	3	EBI-374900,EBI-456953
MCM10	Q7L590	2	EBI-374900,EBI-374912
MCM2	P49736	6	EBI-374900,EBI-374819
MCM3	P25205	2	EBI-374900,EBI-355153
MCM7	P33993	4	EBI-374900,EBI-355924

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 821

821

DNA replication licensing factor MCM6

PRO_0000194113

Regions

Domain

346 – 553

208

MCM

Nucleotide binding

396 – 403

8

ATP Potential

Motif

528 – 531

4

Arginine finger

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.19

Modified residue

13

1

Phosphoserine Ref.19

Modified residue

271

1

Phosphoserine Ref.12 Ref.17 Ref.18 Ref.19

Modified residue

762

1

Phosphoserine Ref.12 Ref.17 Ref.18 Ref.19

Modified residue

791

1

Phosphothreonine Ref.16

Natural variations

Natural variant

35

1

E → V.
Corresponds to variant rs3087355 [ dbSNP | Ensembl ].

VAR_014816

Natural variant

806

1

E → K. Ref.3
Corresponds to variant rs4988283 [ dbSNP | Ensembl ].

VAR_016340

Experimental info

Mutagenesis

757

1

E → A or D: Impairs interaction with CTD1. Ref.22

Mutagenesis

763

1

E → A or D: Impairs interaction with CTD1. Ref.22

Mutagenesis

766

1

L → A: Impairs interaction with CTD1. Ref.22

Sequence conflict

377 – 387

11

PKTTGEGTSLR → SKDNRRRDLSS in AAC50766. Ref.2

Sequence conflict

495

1

A → T in AAC50766. Ref.2

Sequence conflict

738

1

Missing in AAB48165. Ref.7

Sequence conflict

790

1

L → P in AAC50766. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

821

Helix Strand Turn

Details...

Helix

709 – 711

3

Beta strand

714 – 716

3

Helix

718 – 737

20

Beta strand

739 – 741

3

Helix

745 – 756

12

Turn

757 – 759

3

Helix

763 – 782

20

Helix

793 – 796

4

Sequences

	Sequence		Length	Mass (Da)
	Q14566 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: F94968EB25A3E501	FASTA	821	92,889
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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: MASS SPECTROMETRY, HELICASE ACTIVITY OF THE MCM2-3 COMPLEX, INTERACTION WITH MCMBP, IDENTIFICATION IN THE MCM2-7 COMPLEX.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"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].
[21]	"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.
[22]	"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

NIEHS-SNPs

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.

IPI

IPI00031517.

RefSeq

NP_005906.2. NM_005915.5.

UniGene

Hs.444118.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KLQ	NMR	-	A	708-821	[»]
2LE8	NMR	-	A	708-821	[»]

ProteinModelPortal

Q14566.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31727N.

IntAct

Q14566. 28 interactions.

MINT

MINT-5004576.

STRING

9606.ENSP00000264156.

PTM databases

PhosphoSite

Q14566.

Polymorphism databases

DMDM

2497824.

Proteomic databases

PaxDb

Q14566.

PeptideAtlas

Q14566.

PRIDE

Q14566.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000264156; ENSP00000264156; ENSG00000076003.

GeneID

4175.

KEGG

hsa:4175.

UCSC

uc002tuw.3. human.

Organism-specific databases

CTD

4175.

GeneCards

GC02M136619.

HGNC

HGNC:6949. MCM6.

HPA

CAB009577.
HPA004818.

MIM

223100. phenotype.
601806. gene.

neXtProt

NX_Q14566.

PharmGKB

PA30696.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1241.

HOGENOM

HOG000224130.

HOVERGEN

HBG006334.

InParanoid

Q14566.

KO

K02542.

OMA

CQKLFQD.

OrthoDB

EOG4PC9RF.

PhylomeDB

Q14566.

Enzyme and pathway databases

Reactome

REACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpress

Q14566.

Bgee

Q14566.

CleanEx

HS_MCM6.

Genevestigator

Q14566.

GermOnline

ENSG00000076003. Homo sapiens.

Family and domain databases

Gene3D

2.20.28.10. 1 hit.
2.40.50.140. 2 hits.

InterPro

IPR008049. MCM6.
IPR018525. MCM_CS.
IPR001208. MCM_DNA-dep_ATPase.
IPR012340. NA-bd_OB-fold.
IPR004039. Rubredoxin-type_fold.
[Graphical view]

PANTHER

PTHR11630:SF43. PTHR11630:SF43. 1 hit.

Pfam

PF00493. MCM. 1 hit.
[Graphical view]

PRINTS

PR01657. MCMFAMILY.
PR01662. MCMPROTEIN6.

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

ChiTaRS

MCM6. human.

DrugBank

DB01076. Atorvastatin.

EvolutionaryTrace

Q14566.

GenomeRNAi

4175.

NextBio

16446.

PMAP-CutDB

Q14566.

SOURCE

Search...

Entry information

Entry name

MCM6_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 126 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.