MCM9_HUMAN
ID MCM9_HUMAN Reviewed; 1143 AA.
AC Q9NXL9; B4DR30; B9DI77; Q2KHJ0; Q8N5S5; Q9HCV5;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 4.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=DNA helicase MCM9;
DE Short=hMCM9;
DE EC=3.6.4.12 {ECO:0000269|PubMed:26300262};
DE AltName: Full=Mini-chromosome maintenance deficient domain-containing protein 1;
DE AltName: Full=Minichromosome maintenance 9;
GN Name=MCM9; Synonyms=C6orf61, MCMDC1;
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 [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 865-1143 (ISOFORM L).
RC TISSUE=Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM S).
RC TISSUE=Brain;
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 [4]
RP IDENTIFICATION.
RX PubMed=16226853; DOI=10.1016/j.gene.2005.07.031;
RA Lutzmann M., Maiorano D., Mechali M.;
RT "Identification of full genes and proteins of MCM9, a novel, vertebrate-
RT specific member of the MCM2-8 protein family.";
RL Gene 362:51-56(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-762, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP ALTERNATIVE SPLICING (ISOFORM M), AND DEVELOPMENTAL STAGE.
RX PubMed=23403237; DOI=10.1016/j.gene.2013.01.054;
RA Jeffries E.P., Denq W.I., Bartko J.C., Trakselis M.A.;
RT "Identification, quantification, and evolutionary analysis of a novel
RT isoform of MCM9.";
RL Gene 519:41-49(2013).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-762; SER-802 AND SER-1109,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [9]
RP FUNCTION, IDENTIFICATION IN THE MCM8-MCM9 COMPLEX, INTERACTION WITH RAD51,
RP AND SUBCELLULAR LOCATION.
RX PubMed=23401855; DOI=10.1128/mcb.01503-12;
RA Park J., Long D.T., Lee K.Y., Abbas T., Shibata E., Negishi M., Luo Y.,
RA Schimenti J.C., Gambus A., Walter J.C., Dutta A.;
RT "The MCM8-MCM9 complex promotes RAD51 recruitment at DNA damage sites to
RT facilitate homologous recombination.";
RL Mol. Cell. Biol. 33:1632-1644(2013).
RN [10]
RP INVOLVEMENT IN ODG4.
RX PubMed=25480036; DOI=10.1016/j.ajhg.2014.11.002;
RA Wood-Trageser M.A., Gurbuz F., Yatsenko S.A., Jeffries E.P., Kotan L.D.,
RA Surti U., Ketterer D.M., Matic J., Chipkin J., Jiang H., Trakselis M.A.,
RA Topaloglu A.K., Rajkovic A.;
RT "MCM9 mutations are associated with ovarian failure, short stature, and
RT chromosomal instability.";
RL Am. J. Hum. Genet. 95:754-762(2014).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE MCM8-MCM9 COMPLEX,
RP INTERACTION WITH MMR COMPLEX, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-358 AND ARG-482.
RX PubMed=26300262; DOI=10.1016/j.molcel.2015.07.010;
RA Traver S., Coulombe P., Peiffer I., Hutchins J.R., Kitzmann M.,
RA Latreille D., Mechali M.;
RT "MCM9 Is Required for Mammalian DNA Mismatch Repair.";
RL Mol. Cell 59:831-839(2015).
RN [12]
RP FUNCTION, AND INTERACTION WITH MRN COMPLEX AND MCM8.
RX PubMed=26215093; DOI=10.1038/ncomms8744;
RA Lee K.Y., Im J.S., Shibata E., Park J., Handa N., Kowalczykowski S.C.,
RA Dutta A.;
RT "MCM8-9 complex promotes resection of double-strand break ends by MRE11-
RT RAD50-NBS1 complex.";
RL Nat. Commun. 6:7744-7744(2015).
CC -!- FUNCTION: Component of the MCM8-MCM9 complex, a complex involved in the
CC repair of double-stranded DNA breaks (DBSs) and DNA interstrand cross-
CC links (ICLs) by homologous recombination (HR) (PubMed:23401855).
CC Required for DNA resection by the MRE11-RAD50-NBN/NBS1 (MRN) complex by
CC recruiting the MRN complex to the repair site and by promoting the
CC complex nuclease activity (PubMed:26215093). Probably by regulating the
CC localization of the MRN complex, indirectly regulates the recruitment
CC of downstream effector RAD51 to DNA damage sites including DBSs and
CC ICLs (PubMed:23401855). Acts as a helicase in DNA mismatch repair (MMR)
CC following DNA replication errors to unwind the mismatch containing DNA
CC strand (PubMed:26300262). In addition, recruits MLH1, a component of
CC the MMR complex, to chromatin (PubMed:26300262). The MCM8-MCM9 complex
CC is dispensable for DNA replication and S phase progression
CC (PubMed:23401855). Probably by regulating HR, plays a key role during
CC gametogenesis (By similarity). {ECO:0000250|UniProtKB:Q2KHI9,
CC ECO:0000269|PubMed:23401855, ECO:0000269|PubMed:26215093,
CC ECO:0000269|PubMed:26300262}.
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 Evidence={ECO:0000269|PubMed:26300262};
CC -!- SUBUNIT: Component of the MCM8-MCM9 complex, which forms a hexamer
CC composed of MCM8 and MCM9 (PubMed:23401855, PubMed:26300262,
CC PubMed:26215093). Interacts with the DNA mismatch repair (MMR) complex
CC composed at least of MSH2, MSH3, MSH6, PMS1 and MLH1 (PubMed:26300262).
CC Interacts with MLH1; the interaction recruits MLH1 to chromatin
CC (PubMed:26300262). Interacts with MSH2; the interaction recruits MCM9
CC to chromatin (PubMed:26300262). Interacts with MSH6 (PubMed:26300262).
CC Interacts with the MRN complex composed of MRE11, RAD50 and NBN/NBS1;
CC the interaction recruits the MRN complex to DNA damage sites
CC (PubMed:26215093). Interacts with RAD51; the interaction recruits RAD51
CC to DNA damage sites (PubMed:23401855). {ECO:0000269|PubMed:23401855,
CC ECO:0000269|PubMed:26215093, ECO:0000269|PubMed:26300262}.
CC -!- INTERACTION:
CC Q9NXL9; Q9UJA3: MCM8; NbExp=3; IntAct=EBI-2804985, EBI-8756095;
CC Q9NXL9; P40692: MLH1; NbExp=4; IntAct=EBI-2804985, EBI-744248;
CC Q9NXL9; P52701: MSH6; NbExp=2; IntAct=EBI-2804985, EBI-395529;
CC Q9NXL9-3; Q14696: MESD; NbExp=3; IntAct=EBI-18899369, EBI-6165891;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23401855,
CC ECO:0000269|PubMed:26300262}. Chromosome {ECO:0000269|PubMed:23401855,
CC ECO:0000269|PubMed:26300262}. Note=Colocalizes to nuclear foci with
CC RPA1 following DNA damage (PubMed:23401855). Localizes to double-
CC stranded DNA breaks (PubMed:23401855). Recruited to chromatin by MSH2
CC (PubMed:26300262). {ECO:0000269|PubMed:23401855,
CC ECO:0000269|PubMed:26300262}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=L;
CC IsoId=Q9NXL9-1; Sequence=Displayed;
CC Name=M;
CC IsoId=Q9NXL9-2; Sequence=VSP_047462, VSP_047463;
CC Name=S;
CC IsoId=Q9NXL9-3; Sequence=VSP_028013, VSP_028014;
CC Name=4;
CC IsoId=Q9NXL9-4; Sequence=VSP_044180, VSP_044181;
CC -!- DEVELOPMENTAL STAGE: The expression of isoform L and isoform M is cell
CC cycle regulated: induced in S-phase, decreases through G2/M, and
CC becomes constant through G1. {ECO:0000269|PubMed:23403237}.
CC -!- DISEASE: Ovarian dysgenesis 4 (ODG4) [MIM:616185]: A form of ovarian
CC dysgenesis, a disorder characterized by lack of spontaneous pubertal
CC development, primary amenorrhea, uterine hypoplasia, and
CC hypergonadotropic hypogonadism as a result of streak gonads. ODG4 is an
CC autosomal recessive condition. {ECO:0000269|PubMed:25480036}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: [Isoform L]: Most abundant isoform.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA90991.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG61142.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK299076; BAG61142.1; ALT_SEQ; mRNA.
DR EMBL; AK000177; BAA90991.1; ALT_INIT; mRNA.
DR EMBL; AL132874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031658; AAH31658.1; -; mRNA.
DR EMBL; BN000882; CAJ70648.1; -; mRNA.
DR CCDS; CCDS5121.1; -. [Q9NXL9-3]
DR CCDS; CCDS56447.1; -. [Q9NXL9-1]
DR RefSeq; NP_060166.2; NM_017696.2. [Q9NXL9-1]
DR RefSeq; NP_694987.1; NM_153255.4. [Q9NXL9-3]
DR PDB; 7DPD; X-ray; 2.55 A; A/B=1-277.
DR PDBsum; 7DPD; -.
DR AlphaFoldDB; Q9NXL9; -.
DR SMR; Q9NXL9; -.
DR BioGRID; 129033; 46.
DR ComplexPortal; CPX-7113; MCM8-MCM9 DNA helicase complex.
DR IntAct; Q9NXL9; 34.
DR STRING; 9606.ENSP00000314505; -.
DR iPTMnet; Q9NXL9; -.
DR PhosphoSitePlus; Q9NXL9; -.
DR BioMuta; MCM9; -.
DR DMDM; 387912921; -.
DR EPD; Q9NXL9; -.
DR jPOST; Q9NXL9; -.
DR MassIVE; Q9NXL9; -.
DR MaxQB; Q9NXL9; -.
DR PaxDb; Q9NXL9; -.
DR PeptideAtlas; Q9NXL9; -.
DR PRIDE; Q9NXL9; -.
DR ProteomicsDB; 83112; -. [Q9NXL9-1]
DR ProteomicsDB; 83113; -. [Q9NXL9-2]
DR Antibodypedia; 34788; 94 antibodies from 24 providers.
DR DNASU; 254394; -.
DR Ensembl; ENST00000316068.7; ENSP00000312870.3; ENSG00000111877.18. [Q9NXL9-3]
DR Ensembl; ENST00000316316.10; ENSP00000314505.5; ENSG00000111877.18. [Q9NXL9-1]
DR Ensembl; ENST00000619706.5; ENSP00000480469.1; ENSG00000111877.18. [Q9NXL9-1]
DR GeneID; 254394; -.
DR KEGG; hsa:254394; -.
DR MANE-Select; ENST00000619706.5; ENSP00000480469.1; NM_017696.3; NP_060166.2.
DR UCSC; uc003pyh.4; human. [Q9NXL9-1]
DR CTD; 254394; -.
DR DisGeNET; 254394; -.
DR GeneCards; MCM9; -.
DR HGNC; HGNC:21484; MCM9.
DR HPA; ENSG00000111877; Low tissue specificity.
DR MalaCards; MCM9; -.
DR MIM; 610098; gene.
DR MIM; 616185; phenotype.
DR neXtProt; NX_Q9NXL9; -.
DR OpenTargets; ENSG00000111877; -.
DR Orphanet; 444048; 46,XX ovarian dysgenesis-short stature syndrome.
DR PharmGKB; PA162395071; -.
DR VEuPathDB; HostDB:ENSG00000111877; -.
DR eggNOG; KOG0477; Eukaryota.
DR GeneTree; ENSGT01050000244972; -.
DR HOGENOM; CLU_000995_7_2_1; -.
DR InParanoid; Q9NXL9; -.
DR OMA; RKSFQLH; -.
DR OrthoDB; 266497at2759; -.
DR PhylomeDB; Q9NXL9; -.
DR TreeFam; TF329421; -.
DR PathwayCommons; Q9NXL9; -.
DR SignaLink; Q9NXL9; -.
DR BioGRID-ORCS; 254394; 29 hits in 1079 CRISPR screens.
DR ChiTaRS; MCM9; human.
DR GenomeRNAi; 254394; -.
DR Pharos; Q9NXL9; Tbio.
DR PRO; PR:Q9NXL9; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9NXL9; protein.
DR Bgee; ENSG00000111877; Expressed in secondary oocyte and 151 other tissues.
DR ExpressionAtlas; Q9NXL9; baseline and differential.
DR Genevisible; Q9NXL9; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0042555; C:MCM complex; IBA:GO_Central.
DR GO; GO:0097362; C:MCM8-MCM9 complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; IMP:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0032406; F:MutLbeta complex binding; IDA:UniProtKB.
DR GO; GO:0032407; F:MutSalpha complex binding; IDA:UniProtKB.
DR GO; GO:0032408; F:MutSbeta complex binding; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0032508; P:DNA duplex unwinding; IDA:ComplexPortal.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:UniProtKB.
DR GO; GO:0007292; P:female gamete generation; ISS:UniProtKB.
DR GO; GO:0070716; P:mismatch repair involved in maintenance of fidelity involved in DNA-dependent DNA replication; IMP:UniProtKB.
DR GO; GO:0071168; P:protein localization to chromatin; IMP:UniProtKB.
DR GO; GO:0036298; P:recombinational interstrand cross-link repair; IMP:UniProtKB.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR001208; MCM_dom.
DR InterPro; IPR041562; MCM_lid.
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; PF17207; MCM_OB; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00350; MCM; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50051; MCM_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Chromosome; DNA damage;
KW DNA repair; DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1143
FT /note="DNA helicase MCM9"
FT /id="PRO_0000089513"
FT DOMAIN 300..505
FT /note="MCM"
FT /evidence="ECO:0000255"
FT REGION 656..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..901
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1011
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1099
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 352..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 762
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 802
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..381
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044180"
FT VAR_SEQ 382..383
FT /note="SA -> MS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044181"
FT VAR_SEQ 383..391
FT /note="AGLTVTAVK -> AGIVCDNFK (in isoform S)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028013"
FT VAR_SEQ 392..1143
FT /note="Missing (in isoform S)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028014"
FT VAR_SEQ 606..648
FT /note="GGALLGGVNALHTSFPENPGEQYQRQCELILEKLELQSLLSEE -> VTESE
FT CAPIPTTGIGGRDYSRILEKWSRGRIKLQNFITAGNQL (in isoform M)"
FT /evidence="ECO:0000305"
FT /id="VSP_047462"
FT VAR_SEQ 649..1143
FT /note="Missing (in isoform M)"
FT /evidence="ECO:0000305"
FT /id="VSP_047463"
FT MUTAGEN 358
FT /note="K->A: Loss of helicase activity and DNA mismatch
FT repair function but does not affect the interaction with
FT MCM8, MSH2 or chromatin; when associated with A-482."
FT /evidence="ECO:0000269|PubMed:26300262"
FT MUTAGEN 482
FT /note="R->A: Loss of helicase activity and DNA mismatch
FT repair function but does not affect the interaction with
FT MCM8, MSH2 or chromatin; when associated with A-358."
FT /evidence="ECO:0000269|PubMed:26300262"
FT CONFLICT 433
FT /note="Q -> R (in Ref. 1; BAG61142)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="C -> S (in Ref. 1; BAG61142)"
FT /evidence="ECO:0000305"
FT CONFLICT 1063
FT /note="F -> V (in Ref. 1; BAA90991)"
FT /evidence="ECO:0000305"
FT CONFLICT 1136
FT /note="D -> G (in Ref. 1; BAA90991)"
FT /evidence="ECO:0000305"
FT HELIX 3..20
FT /evidence="ECO:0007829|PDB:7DPD"
FT HELIX 22..30
FT /evidence="ECO:0007829|PDB:7DPD"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:7DPD"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:7DPD"
FT HELIX 44..50
FT /evidence="ECO:0007829|PDB:7DPD"
FT HELIX 52..60
FT /evidence="ECO:0007829|PDB:7DPD"
FT HELIX 62..82
FT /evidence="ECO:0007829|PDB:7DPD"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:7DPD"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:7DPD"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:7DPD"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:7DPD"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:7DPD"
FT STRAND 123..133
FT /evidence="ECO:0007829|PDB:7DPD"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:7DPD"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:7DPD"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:7DPD"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:7DPD"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:7DPD"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:7DPD"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:7DPD"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:7DPD"
FT STRAND 196..205
FT /evidence="ECO:0007829|PDB:7DPD"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:7DPD"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:7DPD"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:7DPD"
FT STRAND 237..249
FT /evidence="ECO:0007829|PDB:7DPD"
FT STRAND 258..270
FT /evidence="ECO:0007829|PDB:7DPD"
SQ SEQUENCE 1143 AA; 127313 MW; 3C35C8B3476A470F CRC64;
MNSDQVTLVG QVFESYVSEY HKNDILLILK ERDEDAHYPV VVNAMTLFET NMEIGEYFNM
FPSEVLTIFD SALRRSALTI LQSLSQPEAV SMKQNLHARI SGLPVCPELV REHIPKTKDV
GHFLSVTGTV IRTSLVKVLE FERDYMCNKC KHVFVIKADF EQYYTFCRPS SCPSLESCDS
SKFTCLSGLS SSPTRCRDYQ EIKIQEQVQR LSVGSIPRSM KVILEDDLVD SCKSGDDLTI
YGIVMQRWKP FQQDVRCEVE IVLKANYIQV NNEQSSGIIM DEEVQKEFED FWEYYKSDPF
AGRNVILASL CPQVFGMYLV KLAVAMVLAG GIQRTDATGT RVRGESHLLL VGDPGTGKSQ
FLKYAAKITP RSVLTTGIGS TSAGLTVTAV KDSGEWNLEA GALVLADAGL CCIDEFNSLK
EHDRTSIHEA MEQQTISVAK AGLVCKLNTR TTILAATNPK GQYDPQESVS VNIALGSPLL
SRFDLILVLL DTKNEDWDRI ISSFILENKG YPSKSEKLWS MEKMKTYFCL IRNLQPTLSD
VGNQVLLRYY QMQRQSDCRN AARTTIRLLE SLIRLAEAHA RLMFRDTVTL EDAITVVSVM
ESSMQGGALL GGVNALHTSF PENPGEQYQR QCELILEKLE LQSLLSEELR RLERLQNQSV
HQSQPRVLEV ETTPGSLRNG PGEESNFRTS SQQEINYSTH IFSPGGSPEG SPVLDPPPHL
EPNRSTSRKH SAQHKNNRDD SLDWFDFMAT HQSEPKNTVV VSPHPKTSGE NMASKISNST
SQGKEKSEPG QRSKVDIGLL PSPGETGVPW RADNVESNKK KRLALDSEAA VSADKPDSVL
THHVPRNLQK LCKERAQKLC RNSTRVPAQC TVPSHPQSTP VHSPDRMLDS PKRKRPKSLA
QVEEPAIENV KPPGSPVAKL AKFTFKQKSK LIHSFEDHSH VSPGATKIAV HSPKISQRRT
RRDAALPVKR PGKLTSTPGN QISSQPQGET KEVSQQPPEK HGPREKVMCA PEKRIIQPEL
ELGNETGCAH LTCEGDKKEE VSGSNKSGKV HACTLARLAN FCFTPPSESK SKSPPPERKN
RGERGPSSPP TTTAPMRVSK RKSFQLRGST EKLIVSKESL FTLPELGDEA FDCDWDEEMR
KKS
