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 27-MAR-2024, entry version 163. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7WI7; X-ray; 6.60 A; B=1-684. DR PDB; 7YOX; EM; 3.95 A; B/D/E=1-276. DR PDB; 8S91; EM; 4.30 A; D/E/F=1-1143. DR PDB; 8S92; EM; 4.06 A; D/E/F=1-1143. DR PDB; 8S94; EM; 3.94 A; D/E/F=1-1143. DR PDBsum; 7DPD; -. DR PDBsum; 7WI7; -. DR PDBsum; 7YOX; -. DR PDBsum; 8S91; -. DR PDBsum; 8S92; -. DR PDBsum; 8S94; -. DR AlphaFoldDB; Q9NXL9; -. DR EMDB; EMD-33989; -. DR EMDB; EMD-40234; -. DR EMDB; EMD-40235; -. DR EMDB; EMD-40236; -. DR EMDB; EMD-40237; -. DR SMR; Q9NXL9; -. DR BioGRID; 129033; 53. DR ComplexPortal; CPX-7113; MCM8-MCM9 DNA helicase complex. DR IntAct; Q9NXL9; 33. DR MINT; Q9NXL9; -. 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; 9606-ENSP00000314505; -. DR PeptideAtlas; Q9NXL9; -. DR ProteomicsDB; 83112; -. [Q9NXL9-1] DR ProteomicsDB; 83113; -. [Q9NXL9-2] DR Pumba; Q9NXL9; -. DR Antibodypedia; 34788; 108 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 AGR; HGNC:21484; -. 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; ENSGT01090000260080; -. DR HOGENOM; CLU_000995_7_2_1; -. DR InParanoid; Q9NXL9; -. DR OMA; CNKCKYV; -. DR OrthoDB; 1342948at2759; -. DR PhylomeDB; Q9NXL9; -. DR TreeFam; TF329421; -. DR PathwayCommons; Q9NXL9; -. DR SignaLink; Q9NXL9; -. DR BioGRID-ORCS; 254394; 35 hits in 1157 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 152 other cell types or tissues. DR ExpressionAtlas; Q9NXL9; baseline and differential. 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:InterPro. 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:DNA damage response; 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 CDD; cd17760; MCM9; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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:SF48; DNA HELICASE MCM9; 1. DR PANTHER; PTHR11630; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 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; Nucleic acid-binding proteins; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS50051; MCM_2; 1. DR Genevisible; Q9NXL9; HS. 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 //