MCM5_HUMAN
ID MCM5_HUMAN Reviewed; 734 AA.
AC P33992; O60785; Q14578; Q9BTJ4; Q9BWL8;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 5.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=DNA replication licensing factor MCM5 {ECO:0000303|Ref.3};
DE EC=3.6.4.12;
DE AltName: Full=CDC46 homolog {ECO:0000250|UniProtKB:P49718};
DE AltName: Full=P1-CDC46 {ECO:0000303|PubMed:8265339};
GN Name=MCM5; Synonyms=CDC46;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cervix carcinoma;
RA Hu B.;
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SEQUENCE REVISION.
RA Goehring F., Jehnichen P., Hemmer W.H.;
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Mimura S., Nishimoto S., Kubota Y., Takisawa H., Nojima H.;
RT "Homo sapiens DNA replication licensing factor (huMCM5).";
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-136; SER-180 AND
RP ILE-258.
RG NIEHS SNPs program;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 352-590.
RC TISSUE=Cervix;
RX PubMed=8265339; DOI=10.1093/nar/21.23.5289-a;
RA Hu B., Burkhart R., Schulte D., Musahl C., Knippers R.;
RT "The P1 family: a new class of nuclear mammalian proteins related to the
RT yeast Mcm replication proteins.";
RL Nucleic Acids Res. 21:5289-5293(1993).
RN [9]
RP IDENTIFICATION IN THE MCM2-7 COMPLEX, AND FUNCTION.
RX PubMed=16899510; DOI=10.1091/mbc.e06-03-0241;
RA Tsuji T., Ficarro S.B., Jiang W.;
RT "Essential role of phosphorylation of MCM2 by Cdc7/Dbf4 in the initiation
RT of DNA replication in mammalian cells.";
RL Mol. Biol. Cell 17:4459-4472(2006).
RN [10]
RP INTERACTION WITH MCMBP, IDENTIFICATION IN THE MCM2-7 COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17296731; DOI=10.1128/mcb.02384-06;
RA Sakwe A.M., Nguyen T., Athanasopoulos V., Shire K., Frappier L.;
RT "Identification and characterization of a novel component of the human
RT minichromosome maintenance complex.";
RL Mol. Cell. Biol. 27:3044-3055(2007).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-392; LYS-396 AND LYS-696, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP INTERACTION WITH ANKRD17.
RX PubMed=23711367; DOI=10.1016/j.febslet.2013.05.037;
RA Menning M., Kufer T.A.;
RT "A role for the Ankyrin repeat containing protein Ankrd17 in Nod1- and
RT Nod2-mediated inflammatory responses.";
RL FEBS Lett. 587:2137-2142(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315 AND SER-605, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP INTERACTION WITH TONSL.
RX PubMed=26527279; DOI=10.1016/j.molcel.2015.08.005;
RA Campos E.I., Smits A.H., Kang Y.H., Landry S., Escobar T.M., Nayak S.,
RA Ueberheide B.M., Durocher D., Vermeulen M., Hurwitz J., Reinberg D.;
RT "Analysis of the histone H3.1 interactome: a suitable chaperone for the
RT right event.";
RL Mol. Cell 60:697-709(2015).
RN [19]
RP INVOLVEMENT IN MGORS8, VARIANT MGORS8 ILE-466, AND SUBCELLULAR LOCATION.
RX PubMed=28198391; DOI=10.1038/ejhg.2017.5;
RA Vetro A., Savasta S., Russo Raucci A., Cerqua C., Sartori G.,
RA Limongelli I., Forlino A., Maruelli S., Perucca P., Vergani D., Mazzini G.,
RA Mattevi A., Stivala L.A., Salviati L., Zuffardi O.;
RT "MCM5: a new actor in the link between DNA replication and Meier-Gorlin
RT syndrome.";
RL Eur. J. Hum. Genet. 25:646-650(2017).
CC -!- FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which
CC is the putative replicative helicase essential for 'once per cell
CC cycle' DNA replication initiation and elongation in eukaryotic cells.
CC The active ATPase sites in the MCM2-7 ring are formed through the
CC interaction surfaces of two neighboring subunits such that a critical
CC structure of a conserved arginine finger motif is provided in trans
CC relative to the ATP-binding site of the Walker A box of the adjacent
CC subunit. The six ATPase active sites, however, are likely to contribute
CC differentially to the complex helicase activity.
CC {ECO:0000269|PubMed:16899510}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBUNIT: Component of the MCM2-7 complex (PubMed:17296731,
CC PubMed:16899510). The complex forms a toroidal hexameric ring with the
CC proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5 (PubMed:17296731,
CC PubMed:16899510). Interacts with ANKRD17 (PubMed:23711367). Interacts
CC with MCMBP (PubMed:17296731). Component of the CMG helicase complex,
CC composed of the MCM2-7 complex, the GINS complex and CDC45 (By
CC similarity). Interacts with TONSL; the interaction is direct
CC (PubMed:26527279). {ECO:0000250|UniProtKB:P55862,
CC ECO:0000269|PubMed:16899510, ECO:0000269|PubMed:17296731,
CC ECO:0000269|PubMed:23711367, ECO:0000269|PubMed:26527279}.
CC -!- INTERACTION:
CC P33992; P62805: H4C9; NbExp=2; IntAct=EBI-359410, EBI-302023;
CC P33992; Q9Y468: L3MBTL1; NbExp=2; IntAct=EBI-359410, EBI-1265089;
CC P33992; P49736: MCM2; NbExp=5; IntAct=EBI-359410, EBI-374819;
CC P33992; P25205: MCM3; NbExp=5; IntAct=EBI-359410, EBI-355153;
CC P33992; P33993: MCM7; NbExp=8; IntAct=EBI-359410, EBI-355924;
CC P33992; Q9BTE3: MCMBP; NbExp=13; IntAct=EBI-359410, EBI-749378;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28198391}. Chromosome
CC {ECO:0000250|UniProtKB:P55862}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:28198391}. Note=Associated with chromatin before
CC the formation of nuclei and detaches from it as DNA replication
CC progresses. {ECO:0000250|UniProtKB:P55862}.
CC -!- DISEASE: Meier-Gorlin syndrome 8 (MGORS8) [MIM:617564]: A form of
CC Meier-Gorlin syndrome, a syndrome characterized by bilateral microtia,
CC aplasia/hypoplasia of the patellae, and severe intrauterine and
CC postnatal growth retardation with short stature and poor weight gain.
CC Additional clinical findings include anomalies of cranial sutures,
CC microcephaly, apparently low-set and simple ears, microstomia, full
CC lips, highly arched or cleft palate, micrognathia, genitourinary tract
CC anomalies, and various skeletal anomalies. While almost all cases have
CC primordial dwarfism with substantial prenatal and postnatal growth
CC retardation, not all cases have microcephaly, and microtia and
CC absent/hypoplastic patella are absent in some. Despite the presence of
CC microcephaly, intellect is usually normal. MGORS8 inheritance is
CC autosomal recessive. {ECO:0000269|PubMed:28198391}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Early fractionation of eukaryotic MCM proteins yielded a
CC variety of dimeric, trimeric and tetrameric complexes with unclear
CC biological significance. The MCM2-7 hexamer is the proposed
CC physiological active complex.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/mcm5/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MCM5ID41321ch22q12.html";
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DR EMBL; X74795; CAA52802.2; -; mRNA.
DR EMBL; D83986; BAA12176.1; -; mRNA.
DR EMBL; CR456517; CAG30403.1; -; mRNA.
DR EMBL; AY212028; AAO21127.1; -; Genomic_DNA.
DR EMBL; Z82244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000142; AAH00142.1; -; mRNA.
DR EMBL; BC003656; AAH03656.1; -; mRNA.
DR CCDS; CCDS13915.1; -.
DR PIR; I38080; I38080.
DR RefSeq; NP_006730.2; NM_006739.3.
DR PDB; 6XTX; EM; 3.29 A; 5=1-734.
DR PDB; 6XTY; EM; 6.77 A; 5=1-734.
DR PDB; 7PFO; EM; 3.20 A; 5=1-734.
DR PDB; 7PLO; EM; 2.80 A; 5=1-734.
DR PDBsum; 6XTX; -.
DR PDBsum; 6XTY; -.
DR PDBsum; 7PFO; -.
DR PDBsum; 7PLO; -.
DR AlphaFoldDB; P33992; -.
DR SMR; P33992; -.
DR BioGRID; 110342; 372.
DR ComplexPortal; CPX-2940; MCM complex.
DR CORUM; P33992; -.
DR DIP; DIP-27578N; -.
DR IntAct; P33992; 81.
DR MINT; P33992; -.
DR STRING; 9606.ENSP00000216122; -.
DR ChEMBL; CHEMBL4630815; -.
DR GlyGen; P33992; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P33992; -.
DR MetOSite; P33992; -.
DR PhosphoSitePlus; P33992; -.
DR SwissPalm; P33992; -.
DR BioMuta; MCM5; -.
DR DMDM; 19858646; -.
DR EPD; P33992; -.
DR jPOST; P33992; -.
DR MassIVE; P33992; -.
DR MaxQB; P33992; -.
DR PaxDb; P33992; -.
DR PeptideAtlas; P33992; -.
DR PRIDE; P33992; -.
DR ProteomicsDB; 54935; -.
DR Antibodypedia; 244; 923 antibodies from 38 providers.
DR DNASU; 4174; -.
DR Ensembl; ENST00000216122.9; ENSP00000216122.3; ENSG00000100297.16.
DR GeneID; 4174; -.
DR KEGG; hsa:4174; -.
DR MANE-Select; ENST00000216122.9; ENSP00000216122.3; NM_006739.4; NP_006730.2.
DR UCSC; uc003anu.5; human.
DR CTD; 4174; -.
DR DisGeNET; 4174; -.
DR GeneCards; MCM5; -.
DR HGNC; HGNC:6948; MCM5.
DR HPA; ENSG00000100297; Tissue enhanced (bone).
DR MalaCards; MCM5; -.
DR MIM; 602696; gene.
DR MIM; 617564; phenotype.
DR neXtProt; NX_P33992; -.
DR OpenTargets; ENSG00000100297; -.
DR PharmGKB; PA30695; -.
DR VEuPathDB; HostDB:ENSG00000100297; -.
DR eggNOG; KOG0481; Eukaryota.
DR GeneTree; ENSGT01050000244824; -.
DR InParanoid; P33992; -.
DR OMA; ITYCKTR; -.
DR OrthoDB; 266497at2759; -.
DR PhylomeDB; P33992; -.
DR TreeFam; TF105653; -.
DR PathwayCommons; P33992; -.
DR Reactome; R-HSA-176187; Activation of ATR in response to replication stress.
DR Reactome; R-HSA-176974; Unwinding of DNA.
DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-68962; Activation of the pre-replicative complex.
DR Reactome; R-HSA-69052; Switching of origins to a post-replicative state.
DR SignaLink; P33992; -.
DR SIGNOR; P33992; -.
DR BioGRID-ORCS; 4174; 794 hits in 1094 CRISPR screens.
DR ChiTaRS; MCM5; human.
DR GeneWiki; MCM5; -.
DR GenomeRNAi; 4174; -.
DR Pharos; P33992; Tbio.
DR PRO; PR:P33992; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P33992; protein.
DR Bgee; ENSG00000100297; Expressed in ventricular zone and 163 other tissues.
DR ExpressionAtlas; P33992; baseline and differential.
DR Genevisible; P33992; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; HDA:BHF-UCL.
DR GO; GO:0071162; C:CMG complex; IPI:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0042555; C:MCM complex; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003688; F:DNA replication origin binding; IEA:InterPro.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; TAS:ProtInc.
DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IDA:ComplexPortal.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IC:ComplexPortal.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008048; MCM5.
DR InterPro; IPR018525; MCM_CS.
DR InterPro; IPR001208; MCM_dom.
DR InterPro; IPR041562; MCM_lid.
DR InterPro; IPR027925; MCM_N.
DR InterPro; IPR033762; MCM_OB.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11630; PTHR11630; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF17855; MCM_lid; 1.
DR Pfam; PF14551; MCM_N; 1.
DR Pfam; PF17207; MCM_OB; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR PRINTS; PR01661; MCMPROTEIN5.
DR SMART; SM00350; MCM; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00847; MCM_1; 1.
DR PROSITE; PS50051; MCM_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cell cycle; Chromosome; Cytoplasm;
KW Disease variant; DNA replication; DNA-binding; Dwarfism; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..734
FT /note="DNA replication licensing factor MCM5"
FT /id="PRO_0000194107"
FT DOMAIN 331..537
FT /note="MCM"
FT BINDING 381..388
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 392
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 396
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 696
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 136
FT /note="S -> T (in dbSNP:rs2307334)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_014813"
FT VARIANT 180
FT /note="T -> S (in dbSNP:rs2307340)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_014814"
FT VARIANT 258
FT /note="V -> I (in dbSNP:rs2230933)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_014815"
FT VARIANT 466
FT /note="T -> I (in MGORS8; dbSNP:rs1131692169)"
FT /evidence="ECO:0000269|PubMed:28198391"
FT /id="VAR_079198"
FT CONFLICT 41
FT /note="Q -> R (in Ref. 7; AAH03656)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="M -> W (in Ref. 8)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="E -> V (in Ref. 3; BAA12176)"
FT /evidence="ECO:0000305"
FT CONFLICT 591
FT /note="S -> T (in Ref. 3; BAA12176)"
FT /evidence="ECO:0000305"
FT CONFLICT 593..603
FT /note="ARQHERDSDRR -> PVSTRGTVTA (in Ref. 3; BAA12176)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 734 AA; 82286 MW; A80280E61749998D CRC64;
MSGFDDPGIF YSDSFGGDAQ ADEGQARKSQ LQRRFKEFLR QYRVGTDRTG FTFKYRDELK
RHYNLGEYWI EVEMEDLASF DEDLADYLYK QPAEHLQLLE EAAKEVADEV TRPRPSGEEV
LQDIQVMLKS DASPSSIRSL KSDMMSHLVK IPGIIIAASA VRAKATRISI QCRSCRNTLT
NIAMRPGLEG YALPRKCNTD QAGRPKCPLD PYFIMPDKCK CVDFQTLKLQ ELPDAVPHGE
MPRHMQLYCD RYLCDKVVPG NRVTIMGIYS IKKFGLTTSR GRDRVGVGIR SSYIRVLGIQ
VDTDGSGRSF AGAVSPQEEE EFRRLAALPN VYEVISKSIA PSIFGGTDMK KAIACLLFGG
SRKRLPDGLT RRGDINLLML GDPGTAKSQL LKFVEKCSPI GVYTSGKGSS AAGLTASVMR
DPSSRNFIME GGAMVLADGG VVCIDEFDKM REDDRVAIHE AMEQQTISIA KAGITTTLNS
RCSVLAAANS VFGRWDETKG EDNIDFMPTI LSRFDMIFIV KDEHNEERDV MLAKHVITLH
VSALTQTQAV EGEIDLAKLK KFIAYCRVKC GPRLSAEAAE KLKNRYIIMR SGARQHERDS
DRRSSIPITV RQLEAIVRIA EALSKMKLQP FATEADVEEA LRLFQVSTLD AALSGTLSGV
EGFTSQEDQE MLSRIEKQLK RRFAIGSQVS EHSIIKDFTK QKYPEHAIHK VLQLMLRRGE
IQHRMQRKVL YRLK
