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MCM5 (minichromosome maintenance complex component 5)

Written2011-07Christos K Kontos, Maria-Angeliki S Pavlou, Constantinos Giaginis
Department of Biochemistry, Molecular Biology, Faculty of Biology, University of Athens, 15701, Panepistimiopolis, Athens, Greece (CKK, MASP); Department of Food Science, Nutrition, University of the Aegean, 81400, Lemnos, Greece (CG)

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Alias (NCBI)CDC46
HGNC (Hugo) MCM5
HGNC Previous nameCDC46
HGNC Previous nameminichromosome maintenance deficient (S. cerevisiae) 5 (cell division cycle 46)
 MCM5 minichromosome maintenance deficient 5, cell division cycle 46 (S. cerevisiae)
LocusID (NCBI) 4174
Atlas_Id 41321
Location 22q12.3  [Link to chromosome band 22q12]
Location_base_pair Starts at 35400140 and ends at 35425431 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping MCM5.png]
Local_order Telomere to centromere.
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
MCM5 (22q12.3)::HMOX1 (22q12.3)MCM5 (22q12.3)::LYN (8q12.1)MCM5 (22q12.3)::MCM5 (22q12.3)
MCM5 (22q12.3)::RALGAPB (20q11.23)MCM5 (22q12.3)::TOM1 (22q12.3)RPS16 (19q13.2)::MCM5 (22q12.3)


  Figure 1. Schematic representation of the MCM5 gene. Exons are shown as boxes and introns as connecting lines. The coding sequence is highlighted as red, while 5' and 3' untranslated regions (UTRs) are shown in white. The numbers inside boxes indicate exon lengths and the vertical connecting lines show the intron lengths. The arrows show the position of the start codon (ATG) and stop codon (TGA), and the asterisk shows the position of the polyadenylation signal (AATAAA). Roman numerals indicate intron phases. The intron phase refers to the location of the intron within the codon; I denotes that the intron occurs after the first nucleotide of the codon, II denotes that the intron occurs after the second nucleotide, and 0 means that the intron occurs between distinct codons.
Description Spanning 24,4 kb of genomic DNA, the MCM5 gene consists of 17 exons and 16 intervening introns.
Transcription The unique transcript of the MCM5 gene is 2546 nt. The human MCM5 gene was shown to be expressed widely in many normal tissues, but its mRNA levels vary a lot. The highest levels of MCM5 mRNA transcripts were detected in A-431 epidermoid carcinoma cells, U-2 OS osteosarcoma cells, and U-251 MG astrocytoma cells. Expression of all human genes of the MCM family is induced by growth stimulation and their mRNA levels peak at G1/S transition. The growth-regulated expression of MCM5 is primarily regulated by members of the E2F family through binding to multiple E2F sites of the MCM5 gene promoter.
Pseudogene Not identified so far.


  Figure 2. Amino acid sequence and structural motifs of the MCM5 protein. The asterisks (*) indicate amino acid residues being fully conserved in the human MCM protein family, the colons (:) indicate residues with strongly similar properties among all members of the human MCM family, and periods (.) indicate residues with weakly similar properties among all members of the same family. Light blue denotes the cis-acting ATPase elements (Walker A motif, Walker B motif and sensor 1), while yellow highlights the trans-acting ATPase elements (arginine finger and sensor 2). When combined in the heterohexameric MCM complex, the cis and trans motifs of adjacent subunits act together as an ATPase domain. Moreover, the sequence IDEFDKM (shown in dark blue color) is characteristic of most MCM family members. The MCM5 protein also contains a zinc finger (highlighted in pink), comprising four cysteine residues (shown in red color). This zinc finger is considered to play a role in the assembly of the MCM complex and its ATPase activity.
Description The MCM5 protein is composed of 734 amino acid residues, with a calculated molecular mass of 82,3 kDa and a basal isoelectric point of 8,64. MCM5 is a member of the MCM family, a distinct subgroup of the AAA+ family, which consists of ATPases associated with various cellular activities. The MCM5 protein is one the six subunits composing the minichromosome maintenance (MCM) complex. The structural characteristic of MCM5 is an MCM box consisting of approximately 200 amino acids. This includes a Walker A motif containing the P-loop (phosphate-binding loop) of the active site and the invariant lysine residue found in all ATP-binding proteins, a hydrophobic Walker B element that is responsible for ATP hydrolysis, and an arginine finger. The Walker B motif is part of the sequence IDEFDKM, which is conserved in all MCM proteins and defines the MCM family.
MCM proteins form ATPase active sites at clefts between two subdomains: one containing a series of loops connecting adjacent parallel beta-strands (P-loop) and a second positioned C-terminal to the P-loop domain, called the lid. Both subdomains contain conserved active-site motifs: the P-loop contains motifs involved in binding ATP (Walker A motif) and orienting the nucleophilic water molecule (Walker B motif and sensor 1), while the lid domain contains motifs that contact the gamma-phosphate of ATP (arginine finger and sensor 2). Therefore, ATPase active sites of the heterohexameric MCM complex are formed at dimer interfaces, with one subunit contributing the P-loop (cis motifs), while the adjacent subunit contributes the lid (trans motifs). The MCM5 also possesses a zinc finger, located prior to the MCM box. This zinc finger is considered to play a role in the assembly of the MCM complex and its ATPase activity.
Expression MCM5 is upregulated in the transition from the G0 to G1/S phase of the cell cycle. This protein is mainly expressed in bone marrow hematopoietic cells, lymphocytes in tonsil, and trophoblastic cells in placenta. This DNA replication licensing factor is also expressed in a few other cell types, including colorectal glandular cells, epidermal cells of the skin and bronchus, urothelial cells of the urinary bladder, decidual cells of placenta, and glandular cells of the pre-menopause uterus, though at lower intensity. Recently, it was shown that MCM5 is downregulated in neuroblastoma cells by miR-885-5p, which binds to the 3'-UTR of the MCM5 mRNA.
Localisation The MCM5 protein is localized to the nucleus.
Function MCM5 is a member of the MCM family of chromatin-binding proteins, implicated in the initiation of DNA replication. This protein can interact with at least two other members of this family, namely MCM2 and MCM3. MCM5 participates in the formation of the heterohexameric MCM complex, which is loaded onto the chromatin at origins of DNA replication with the aid of the multimeric CDC6-CDT1-ORC-DNA, thus forming together the pre-replication complex (pre-RC). Except for being responsible for the initiation of replication, the proteins composing the MCM complex serve as DNA helicases that unwind the DNA double helix at the replication forks. Moreover, MCM5 may actively participate in cell cycle regulation. Finally, the MCM complex is responsible for genome stability, as it limits the replication to once per cell cycle.
MCM5, MCM3 and MCM2 constitute the peripheral subunits of the complex that negatively regulate the active MCM core subunits (MCM4, MCM6 and MCM7). It has been proposed that MCM2 and MCM5 form a gate in the MCM toroid. When the conformation is in a closed status, the dimer MCM2-MCM5 binds ATP; on the other hand, when the gate is open, the active site of the dimer is empty since no nucleotide is bound, and therefore no helicase activity is observed. Further studies suggest that the very existence of the gate, its topology, its conformation and the complex discontinuity that the MCM2/5 dimer causes, is capable of regulating the helicase activity of the MCM complex and/or is essential for the initial loading of the complex onto the origins of replication.
MCM5 was shown to interact with CDC45, a key molecule that regulates the stages of initiation and elongation in the eukaryotic DNA replication. Interestingly, the heterodimer MCM3-MCM5 can also interact with the transcription factor STAT1a (STAT1 alpha isoform), thus implying a possible role of MCM5 in transcription regulation. Increased levels of MCM5 are associated with activation of transcription. Another recent study showed that the MCM complex is co-localized with RNA polymerase II (RNA Pol II) on chromatin of genes being constitutively transcribed, and that MCM5 is required for transcription elongation of RNA Pol II. In fact, the integrity of the MCM heterohexameric complex and the DNA helicase domain of MCM5 are essential for the process of transcription. Additionally, human minichromosome maintenance proteins including MCM5 can bind to and interact with histones, such as H3 and H4.
Homology Human MCM5 shares 96% amino acid identity and 99% similarity with the mouse and rat Mcm5 protein. Moreover, it shows 35% identity and 53% similarity with the human MCM4 protein ("minichromosome maintenance complex component 4", also known as "CDC21 homolog"), and to quite the same extent with other minichromosome maintenance complex components, including MCM2, MCM3, MCM6, MCM7 isoforms 1 and 2, MCM8 isoforms 1 and 2, and MCM9 isoform 1. Moreover, MCM5 is structurally very similar to the CDC46 protein from Saccharomyces cerevisiae, a protein involved in the initiation of DNA replication.


Note A mutation in a conserved residue (P -->L) enables MCM5 to bypass CDC7 phosphorylation, which is otherwise essential for the DNA replication to ensue, while the same mutation in other subunits of the MCM complex does not have any effect. It has been suggested that the MCM5 protein bearing this mutation obtains an altered conformation that allows it to promote the unwinding of the double helix without the necessity of phosphorylation of the other subunits of the MCM complex. Furthermore, MCM5 was shown to directly interact with the hypoxia-inducible factor-1 alpha subunit (HIF1A), along with other MCM proteins, in order to inhibit the alterations occurring in gene expression by the basic helix-loop-helix transcription factor HIF1 under hypoxic conditions.

Implicated in

Entity Urothelial carcinoma, ovarian adenocarcinoma, cervical cancer
Prognosis MCM5 protein overexpression was significantly associated with advanced histopathological stage, low grade of differentiation and poor prognosis in muscle-invasive urothelial carcinoma. MCM5 protein expression was also found to be significantly higher in ovarian adenocarcinomas compared to tumors of low malignant potential. In ovarian adenocarcinoma, MCM5 upregulation was significantly associated with advanced tumor histopathological stage, low grade of differentiation, and presence of bulky residual disease, therefore constituting an unfavorable prognostic biomarker. MCM5 expression showed also a linear correlation with the grade of cervical dysplasia, being independent of HPV infection.
Entity Gastric adenocarcinoma, esophageal cancer, biliary cancer
Prognosis Elevated expression of the MCM5 protein is significantly associated with advanced tumor size, presence of lymph node metastases, advanced tumor histopathological stage, and poor prognosis in gastric adenocarcinoma. Interestingly, MCM5 overexpression was significantly associated with lymph node positivity and advanced histopathological stage in diffuse-type gastric adenocarcinoma, while it predicted poor prognosis in intestinal-type gastric adenocarcinoma. Furthermore, MCM5 protein expression levels in gastric aspirates were shown to possess high predictive value for esophageal cancer. MCM5 protein expression was also significantly higher in malignant biliary tissues, compared to benign ones.
Entity Laryngeal squamous cell carcinoma
Prognosis MCM5-positive cells were present in cytological preparations from laryngeal squamous cell carcinoma, but not in those presenting atypical hyperplasia or inflammation in non-neoplastic tissues, supporting the notion that liquid-based cytology enhanced by immunohistochemistry for MCM5 can distinguish between patients requiring further investigation and those who could be followed up without resort to biopsy.
Entity Anaplastic thyroid cancer
Prognosis MCM5 overexpression was noticed in anaplastic thyroid cancer, in contrast with normal thyroid tissue and/or papillary thyroid cancer. MCM5 gene expression was also reported to be up-regulated at the mRNA level in papillary thyroid carcinoma, the follicular variant of papillary thyroid carcinoma, and in follicular thyroid tumors, compared to hyperplastic nodules and follicular adenomas. However, MCM5 mRNA expression was not associated with tumor size, patients' age and gender, tumor histopathological stage, and lymph node metastasis, in malignant thyroid lesions.


MicroRNA miR-885-5p targets CDK2 and MCM5, activates p53 and inhibits proliferation and survival.
Afanasyeva EA, Mestdagh P, Kumps C, Vandesompele J, Ehemann V, Theissen J, Fischer M, Zapatka M, Brors B, Savelyeva L, Sagulenko V, Speleman F, Schwab M, Westermann F.
Cell Death Differ. 2011 Jun;18(6):974-84. Epub 2011 Jan 14.
PMID 21233845
MCM proteins: DNA damage, mutagenesis and repair.
Bailis JM, Forsburg SL.
Curr Opin Genet Dev. 2004 Feb;14(1):17-21. (REVIEW)
PMID 15108800
The Mcm complex: unwinding the mechanism of a replicative helicase.
Bochman ML, Schwacha A.
Microbiol Mol Biol Rev. 2009 Dec;73(4):652-83. (REVIEW)
PMID 19946136
Regulation of Cdc45 in the cell cycle and after DNA damage.
Broderick R, Nasheuer HP.
Biochem Soc Trans. 2009 Aug;37(Pt 4):926-30. (REVIEW)
PMID 19614620
Interactions of human nuclear proteins P1Mcm3 and P1Cdc46.
Burkhart R, Schulte D, Hu D, Musahl C, Gohring F, Knippers R.
Eur J Biochem. 1995 Mar 1;228(2):431-8.
PMID 7705359
Eukaryotic MCM proteins: beyond replication initiation.
Forsburg SL.
Microbiol Mol Biol Rev. 2004 Mar;68(1):109-31. (REVIEW)
PMID 15007098
Minichromosome maintenance proteins as biological markers of dysplasia and malignancy.
Freeman A, Morris LS, Mills AD, Stoeber K, Laskey RA, Williams GH, Coleman N.
Clin Cancer Res. 1999 Aug;5(8):2121-32.
PMID 10473096
MCM-2 and MCM-5 expression in gastric adenocarcinoma: clinical significance and comparison with Ki-67 proliferative marker.
Giaginis C, Giagini A, Tsourouflis G, Gatzidou E, Agapitos E, Kouraklis G, Theocharis S.
Dig Dis Sci. 2011 Mar;56(3):777-85. Epub 2010 Aug 6.
PMID 20694513
The P1 family: a new class of nuclear mammalian proteins related to the yeast Mcm replication proteins.
Hu B, Burkhart R, Schulte D, Musahl C, Knippers R.
Nucleic Acids Res. 1993 Nov 25;21(23):5289-93.
PMID 8265339
MCM proteins are negative regulators of hypoxia-inducible factor 1.
Hubbi ME, Luo W, Baek JH, Semenza GL.
Mol Cell. 2011 Jun 10;42(5):700-12.
PMID 21658608
Binding of human minichromosome maintenance proteins with histone H3.
Ishimi Y, Ichinose S, Omori A, Sato K, Kimura H.
J Biol Chem. 1996 Sep 27;271(39):24115-22.
PMID 8798650
MCM proteins: evolution, properties, and role in DNA replication.
Kearsey SE, Labib K.
Biochim Biophys Acta. 1998 Jun 16;1398(2):113-36. (REVIEW)
PMID 9689912
MCM proteins and DNA replication.
Maiorano D, Lutzmann M, Mechali M.
Curr Opin Cell Biol. 2006 Apr;18(2):130-6. Epub 2006 Feb 21. (REVIEW)
PMID 16495042
Coding sequence and chromosome mapping of the human gene (CDC46) for replication protein hCdc46/Mcm5.
Paul R, Hu B, Musahl C, Hameister H, Knippers R.
Cytogenet Cell Genet. 1996;73(4):317-21.
PMID 8751386
Analysis of interaction partners of H4 histone by a new proteomics approach.
Saade E, Mechold U, Kulyyassov A, Vertut D, Lipinski M, Ogryzko V.
Proteomics. 2009 Nov;9(21):4934-43.
PMID 19862764
The mcm5-bob1 bypass of Cdc7p/Dbf4p in DNA replication depends on both Cdk1-independent and Cdk1-dependent steps in Saccharomyces cerevisiae.
Sclafani RA, Tecklenburg M, Pierce A.
Genetics. 2002 May;161(1):47-57.
PMID 12019222
The minichromosome maintenance proteins 2-7 (MCM2-7) are necessary for RNA polymerase II (Pol II)-mediated transcription.
Snyder M, Huang XY, Zhang JJ.
J Biol Chem. 2009 May 15;284(20):13466-72. Epub 2009 Mar 23.
PMID 19318354
Expression, nuclear localization and interactions of human MCM/P1 proteins.
Tsuruga H, Yabuta N, Hashizume K, Ikeda M, Endo Y, Nojima H.
Biochem Biophys Res Commun. 1997 Jul 9;236(1):118-25.
PMID 9223437


This paper should be referenced as such :
Kontos, CK ; Pavlou, MAS ; Giaginis, C
MCM5 (minichromosome maintenance complex component 5)
Atlas Genet Cytogenet Oncol Haematol. 2011;15(12):1045-1049.
Free journal version : [ pdf ]   [ DOI ]

External links


HGNC (Hugo)MCM5   6948
Entrez_Gene (NCBI)MCM5    minichromosome maintenance complex component 5
AliasesCDC46; MGORS8; P1-CDC46
GeneCards (Weizmann)MCM5
Ensembl hg19 (Hinxton)ENSG00000100297 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000100297 [Gene_View]  ENSG00000100297 [Sequence]  chr22:35400140-35425431 [Contig_View]  MCM5 [Vega]
ICGC DataPortalENSG00000100297
TCGA cBioPortalMCM5
AceView (NCBI)MCM5
Genatlas (Paris)MCM5
SOURCE (Princeton)MCM5
Genetics Home Reference (NIH)MCM5
Genomic and cartography
GoldenPath hg38 (UCSC)MCM5  -     chr22:35400140-35425431 +  22q12.3   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)MCM5  -     22q12.3   [Description]    (hg19-Feb_2009)
GoldenPathMCM5 - 22q12.3 [CytoView hg19]  MCM5 - 22q12.3 [CytoView hg38]
Genome Data Viewer NCBIMCM5 [Mapview hg19]  
OMIM602696   617564   
Gene and transcription
Genbank (Entrez)AB209612 AK122853 AK130620 AK223323 AK291136
RefSeq transcript (Entrez)NM_006739
Consensus coding sequences : CCDS (NCBI)MCM5
Gene ExpressionMCM5 [ NCBI-GEO ]   MCM5 [ EBI - ARRAY_EXPRESS ]   MCM5 [ SEEK ]   MCM5 [ MEM ]
Gene Expression Viewer (FireBrowse)MCM5 [ Firebrowse - Broad ]
GenevisibleExpression of MCM5 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)4174
GTEX Portal (Tissue expression)MCM5
Human Protein AtlasENSG00000100297-MCM5 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP33992   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP33992  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP33992
Catalytic activity : Enzyme3.6.4.12 [ Enzyme-Expasy ] [ IntEnz-EBI ] [ BRENDA ] [ KEGG ]   [ MEROPS ]
Domaine pattern : Prosite (Expaxy)MCM_1 (PS00847)    MCM_2 (PS50051)   
Domains : Interpro (EBI)MCM    MCM5    MCM_CS    MCM_dom    MCM_lid    MCM_N    MCM_OB    NA-bd_OB-fold    P-loop_NTPase   
Domain families : Pfam (Sanger)MCM (PF00493)    MCM_lid (PF17855)    MCM_N (PF14551)    MCM_OB (PF17207)   
Domain families : Pfam (NCBI)pfam00493    pfam17855    pfam14551    pfam17207   
Domain families : Smart (EMBL)MCM (SM00350)  
Conserved Domain (NCBI)MCM5
PDB Europe6XTX    6XTY   
PDB (PDBSum)6XTX    6XTY   
PDB (IMB)6XTX    6XTY   
Structural Biology KnowledgeBase6XTX    6XTY   
SCOP (Structural Classification of Proteins)6XTX    6XTY   
CATH (Classification of proteins structures)6XTX    6XTY   
AlphaFold pdb e-kbP33992   
Human Protein Atlas [tissue]ENSG00000100297-MCM5 [tissue]
Protein Interaction databases
IntAct (EBI)P33992
Complex Portal (EBI)P33992 CPX-2940 MCM complex
Ontologies - Pathways
Ontology : AmiGOdouble-strand break repair via break-induced replication  chromosome, telomeric region  DNA replication origin binding  single-stranded DNA binding  protein binding  ATP binding  nucleus  nucleoplasm  nucleoplasm  cytosol  DNA replication  pre-replicative complex assembly involved in nuclear cell cycle DNA replication  DNA replication initiation  DNA replication initiation  membrane  hydrolase activity  single-stranded DNA helicase activity  DNA duplex unwinding  pre-replicative complex assembly  MCM complex  MCM complex  3'-5' DNA helicase activity  CMG complex  
Ontology : EGO-EBIdouble-strand break repair via break-induced replication  chromosome, telomeric region  DNA replication origin binding  single-stranded DNA binding  protein binding  ATP binding  nucleus  nucleoplasm  nucleoplasm  cytosol  DNA replication  pre-replicative complex assembly involved in nuclear cell cycle DNA replication  DNA replication initiation  DNA replication initiation  membrane  hydrolase activity  single-stranded DNA helicase activity  DNA duplex unwinding  pre-replicative complex assembly  MCM complex  MCM complex  3'-5' DNA helicase activity  CMG complex  
Pathways : BIOCARTACDK Regulation of DNA Replication [Genes]   
Pathways : KEGGDNA replication    Cell cycle   
REACTOMEP33992 [protein]
REACTOME PathwaysR-HSA-69052 [pathway]   
NDEx NetworkMCM5
Atlas of Cancer Signalling NetworkMCM5
Wikipedia pathwaysMCM5
Orthology - Evolution
GeneTree (enSembl)ENSG00000100297
Phylogenetic Trees/Animal Genes : TreeFamMCM5
Homologs : HomoloGeneMCM5
Homology/Alignments : Family Browser (UCSC)MCM5
Gene fusions - Rearrangements
Fusion : MitelmanMCM5::HMOX1 [22q12.3/22q12.3]  
Fusion : MitelmanMCM5::LYN [22q12.3/8q12.1]  
Fusion : MitelmanMCM5::RALGAPB [22q12.3/20q11.23]  
Fusion : MitelmanMCM5::TOM1 [22q12.3/22q12.3]  
Fusion : QuiverMCM5
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerMCM5 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)MCM5
Exome Variant ServerMCM5
GNOMAD BrowserENSG00000100297
Varsome BrowserMCM5
ACMGMCM5 variants
Genomic Variants (DGV)MCM5 [DGVbeta]
DECIPHERMCM5 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisMCM5 
ICGC Data PortalMCM5 
TCGA Data PortalMCM5 
Broad Tumor PortalMCM5
OASIS PortalMCM5 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICMCM5  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DMCM5
Mutations and Diseases : HGMDMCM5
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)MCM5
DoCM (Curated mutations)MCM5
CIViC (Clinical Interpretations of Variants in Cancer)MCM5
NCG (London)MCM5
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
OMIM602696    617564   
Genetic Testing Registry MCM5
NextProtP33992 [Medical]
Target ValidationMCM5
Huge Navigator MCM5 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDMCM5
Pharm GKB GenePA30695
Clinical trialMCM5
DataMed IndexMCM5
PubMed190 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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