ID MCM10_HUMAN Reviewed; 875 AA. AC Q7L590; A8K9I6; B7ZKZ8; Q3MIR3; Q7LD55; Q96GX4; Q96NB6; Q9H0D7; Q9H3P9; AC Q9P177; DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 20-FEB-2007, sequence version 2. DT 27-MAR-2024, entry version 164. DE RecName: Full=Protein MCM10 homolog; DE Short=HsMCM10; GN Name=MCM10; ORFNames=PRO2249; 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] (ISOFORM 2), SUBCELLULAR LOCATION, FUNCTION, RP DEVELOPMENTAL STAGE, AND INTERACTION WITH ORC2; MCM2 AND MCM6. RX PubMed=11095689; DOI=10.1093/nar/28.23.4769; RA Izumi M., Yanagi K., Mizuno T., Yokoi M., Kawasaki Y., Moon K.Y., RA Hurwitz J., Yatagai F., Hanaoka F.; RT "The human homolog of Saccharomyces cerevisiae Mcm10 interacts with RT replication factors and dissociates from nuclease-resistant nuclear RT structures in G(2) phase."; RL Nucleic Acids Res. 28:4769-4777(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS PRO-195 RP AND SER-541. RC TISSUE=Testis; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ARG-134 RP AND PRO-195. RC TISSUE=Thymus; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS RP SER-541 AND ARG-669. RC TISSUE=Liver, 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 517-875. RC TISSUE=Fetal liver; RA Zhang C., Yu Y., Zhang S., Wei H., Zhang Y., Zhou G., Bi J., Liu M., He F.; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. RN [8] RP DEVELOPMENTAL STAGE, AND PHOSPHORYLATION. RX PubMed=11602595; DOI=10.1074/jbc.m107190200; RA Izumi M., Yatagai F., Hanaoka F.; RT "Cell cycle-dependent proteolysis and phosphorylation of human Mcm10."; RL J. Biol. Chem. 276:48526-48531(2001). RN [9] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=15136575; DOI=10.1074/jbc.m314017200; RA Izumi M., Yatagai F., Hanaoka F.; RT "Localization of human Mcm10 is spatially and temporally regulated during RT the S phase."; RL J. Biol. Chem. 279:32569-32577(2004). RN [10] RP INTERACTION WITH POLA1 AND WDHD1. RX PubMed=17761813; DOI=10.1101/gad.1585607; RA Zhu W., Ukomadu C., Jha S., Senga T., Dhar S.K., Wohlschlegel J.A., RA Nutt L.K., Kornbluth S., Dutta A.; RT "Mcm10 and And-1/CTF4 recruit DNA polymerase alpha to chromatin for RT initiation of DNA replication."; RL Genes Dev. 21:2288-2299(2007). RN [11] RP FUNCTION. RX PubMed=17699597; DOI=10.1091/mbc.e06-12-1148; RA Chattopadhyay S., Bielinsky A.K.; RT "Human Mcm10 regulates the catalytic subunit of DNA polymerase-alpha and RT prevents DNA damage during replication."; RL Mol. Biol. Cell 18:4085-4095(2007). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-85, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-85 AND SER-93, AND 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 [14] RP INTERACTION WITH RECQL4. RX PubMed=19696745; DOI=10.1038/emboj.2009.235; RA Xu X., Rochette P.J., Feyissa E.A., Su T.V., Liu Y.; RT "MCM10 mediates RECQ4 association with MCM2-7 helicase complex during DNA RT replication."; RL EMBO J. 28:3005-3014(2009). RN [15] RP FUNCTION. RX PubMed=19608746; DOI=10.1074/jbc.m109.020438; RA Warren E.M., Huang H., Fanning E., Chazin W.J., Eichman B.F.; RT "Physical interactions between Mcm10, DNA, and DNA polymerase alpha."; RL J. Biol. Chem. 284:24662-24672(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-85, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [17] RP FUNCTION. RX PubMed=24726359; DOI=10.1016/j.celrep.2014.03.030; RA Miotto B., Chibi M., Xie P., Koundrioukoff S., Moolman-Smook H., Pugh D., RA Debatisse M., He F., Zhang L., Defossez P.A.; RT "The RBBP6/ZBTB38/MCM10 axis regulates DNA replication and common fragile RT site stability."; RL Cell Rep. 7:575-587(2014). RN [18] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-762, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [19] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-493; LYS-627; LYS-762 AND RP LYS-763, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [20] RP INVOLVEMENT IN IMD80, VARIANTS IMD80 CYS-427 AND 583-ARG--LYS-875 DEL, RP CHARACTERIZATION OF VARIANTS IMD80 CYS-427 AND 583-ARG--LYS-875 DEL, RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=32865517; DOI=10.1172/jci134966; RA Mace E.M., Paust S., Conte M.I., Baxley R.M., Schmit M.M., Patil S.L., RA Guilz N.C., Mukherjee M., Pezzi A.E., Chmielowiec J., Tatineni S., RA Chinn I.K., Akdemir Z.C., Jhangiani S.N., Muzny D.M., Stray-Pedersen A., RA Bradley R.E., Moody M., Connor P.P., Heaps A.G., Steward C., Banerjee P.P., RA Gibbs R.A., Borowiak M., Lupski J.R., Jolles S., Bielinsky A.K., RA Orange J.S.; RT "Human NK cell deficiency as a result of biallelic mutations in MCM10."; RL J. Clin. Invest. 130:5272-5286(2020). CC -!- FUNCTION: Acts as a replication initiation factor that brings together CC the MCM2-7 helicase and the DNA polymerase alpha/primase complex in CC order to initiate DNA replication. Additionally, plays a role in CC preventing DNA damage during replication. Key effector of the RBBP6 and CC ZBTB38-mediated regulation of DNA-replication and common fragile sites CC stability; acts as a direct target of transcriptional repression by CC ZBTB38 (PubMed:24726359). {ECO:0000269|PubMed:11095689, CC ECO:0000269|PubMed:15136575, ECO:0000269|PubMed:17699597, CC ECO:0000269|PubMed:19608746, ECO:0000269|PubMed:24726359, CC ECO:0000269|PubMed:32865517}. CC -!- SUBUNIT: Self-associates (By similarity). Interacts with ORC2. May CC interact with MCM2 and MCM6. Interacts with the DNA polymerase alpha CC subunit POLA1. Interacts with RECQL4; this interaction regulates RECQL4 CC unwinding activity. Interacts with WDHD1. CC {ECO:0000250|UniProtKB:Q5EAW4, ECO:0000269|PubMed:11095689, CC ECO:0000269|PubMed:17761813, ECO:0000269|PubMed:19696745}. CC -!- INTERACTION: CC Q7L590; Q7L590: MCM10; NbExp=2; IntAct=EBI-374912, EBI-374912; CC Q7L590; Q14566: MCM6; NbExp=2; IntAct=EBI-374912, EBI-374900; CC Q7L590; Q13416: ORC2; NbExp=5; IntAct=EBI-374912, EBI-374957; CC Q7L590-2; Q08379: GOLGA2; NbExp=3; IntAct=EBI-10233517, EBI-618309; CC Q7L590-2; Q2TBA0: KLHL40; NbExp=4; IntAct=EBI-10233517, EBI-7851314; CC Q7L590-2; Q14566: MCM6; NbExp=4; IntAct=EBI-10233517, EBI-374900; CC Q7L590-2; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-10233517, EBI-79165; CC Q7L590-2; Q9BSL1: UBAC1; NbExp=3; IntAct=EBI-10233517, EBI-749370; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11095689, CC ECO:0000269|PubMed:15136575, ECO:0000269|PubMed:32865517}. CC Note=Colocalizes with ORC2 in nuclei foci. Associated with chromatin in CC S phase. From early to mid-S phase located in discrete nuclear foci. In CC early S phase, several hundred foci appeared throughout the nucleus. In CC mid-S phase, the foci appeared at the nuclear periphery and nucleolar CC regions. In the late S and G phases localized to nucleoli. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q7L590-1; Sequence=Displayed; CC Name=2; CC IsoId=Q7L590-2; Sequence=VSP_029951; CC -!- DEVELOPMENTAL STAGE: Expression is cell cycle regulated. Expression CC increases at the G1/S-boundary. Expression decreases in late M phase, CC remains low during G(1) phase, and starts to accumulate at the onset of CC S phase. {ECO:0000269|PubMed:11095689, ECO:0000269|PubMed:11602595}. CC -!- DOMAIN: Each zinc finger-like domain binds a zinc ion and is involved CC in both ssDNA and dsDNA binding, as is the OB-fold domain. CC {ECO:0000250|UniProtKB:Q5EAW4}. CC -!- DOMAIN: The N-terminal domain mediates homodimerization. CC {ECO:0000250|UniProtKB:Q5EAW4}. CC -!- DISEASE: Immunodeficiency 80 with or without congenital cardiomyopathy CC (IMD80) [MIM:619313]: An autosomal recessive immunologic disorder with CC variable manifestations including decreased B and T cells, reduced CC effector and memory T cells, NK cell deficiency, chronic CC cytomegalovirus infection. Restrictive cardiomyopathy and hypoplasia of CC the spleen and thymus have also been reported in some patients. CC {ECO:0000269|PubMed:32865517}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the MCM10 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF69623.1; Type=Erroneous initiation; Note=Truncated N-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; AB042719; BAB18723.1; -; mRNA. DR EMBL; AL136840; CAB66774.2; -; mRNA. DR EMBL; AK055695; BAB70988.1; -; mRNA. DR EMBL; AK292701; BAF85390.1; -; mRNA. DR EMBL; AL355355; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL138764; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471072; EAW86297.1; -; Genomic_DNA. DR EMBL; BC004876; AAH04876.2; -; mRNA. DR EMBL; BC101727; AAI01728.1; -; mRNA. DR EMBL; BC143490; AAI43491.1; -; mRNA. DR EMBL; AF119869; AAF69623.1; ALT_INIT; mRNA. DR CCDS; CCDS7095.1; -. [Q7L590-2] DR CCDS; CCDS7096.1; -. [Q7L590-1] DR RefSeq; NP_060988.3; NM_018518.4. [Q7L590-2] DR RefSeq; NP_877428.1; NM_182751.2. [Q7L590-1] DR RefSeq; XP_011517840.1; XM_011519538.2. [Q7L590-1] DR AlphaFoldDB; Q7L590; -. DR SMR; Q7L590; -. DR BioGRID; 120654; 129. DR IntAct; Q7L590; 57. DR MINT; Q7L590; -. DR STRING; 9606.ENSP00000418268; -. DR GlyGen; Q7L590; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q7L590; -. DR MetOSite; Q7L590; -. DR PhosphoSitePlus; Q7L590; -. DR BioMuta; MCM10; -. DR DMDM; 126215746; -. DR CPTAC; CPTAC-1210; -. DR CPTAC; CPTAC-1211; -. DR EPD; Q7L590; -. DR jPOST; Q7L590; -. DR MassIVE; Q7L590; -. DR MaxQB; Q7L590; -. DR PaxDb; 9606-ENSP00000418268; -. DR PeptideAtlas; Q7L590; -. DR ProteomicsDB; 68795; -. [Q7L590-1] DR ProteomicsDB; 68796; -. [Q7L590-2] DR Pumba; Q7L590; -. DR Antibodypedia; 11355; 168 antibodies from 25 providers. DR DNASU; 55388; -. DR Ensembl; ENST00000378714.8; ENSP00000367986.3; ENSG00000065328.17. [Q7L590-2] DR Ensembl; ENST00000484800.6; ENSP00000418268.1; ENSG00000065328.17. [Q7L590-1] DR GeneID; 55388; -. DR KEGG; hsa:55388; -. DR MANE-Select; ENST00000378714.8; ENSP00000367986.3; NM_018518.5; NP_060988.3. [Q7L590-2] DR UCSC; uc001ima.4; human. [Q7L590-1] DR AGR; HGNC:18043; -. DR CTD; 55388; -. DR DisGeNET; 55388; -. DR GeneCards; MCM10; -. DR HGNC; HGNC:18043; MCM10. DR HPA; ENSG00000065328; Tissue enhanced (bone marrow, lymphoid tissue). DR MalaCards; MCM10; -. DR MIM; 609357; gene. DR MIM; 619313; phenotype. DR neXtProt; NX_Q7L590; -. DR OpenTargets; ENSG00000065328; -. DR PharmGKB; PA30689; -. DR VEuPathDB; HostDB:ENSG00000065328; -. DR eggNOG; KOG3056; Eukaryota. DR GeneTree; ENSGT00390000007134; -. DR HOGENOM; CLU_014680_0_0_1; -. DR InParanoid; Q7L590; -. DR OMA; VFGLRMI; -. DR OrthoDB; 5354902at2759; -. DR PhylomeDB; Q7L590; -. DR TreeFam; TF313330; -. DR PathwayCommons; Q7L590; -. DR Reactome; R-HSA-176187; Activation of ATR in response to replication stress. DR Reactome; R-HSA-68962; Activation of the pre-replicative complex. DR SignaLink; Q7L590; -. DR SIGNOR; Q7L590; -. DR BioGRID-ORCS; 55388; 362 hits in 1168 CRISPR screens. DR ChiTaRS; MCM10; human. DR GeneWiki; MCM10; -. DR GenomeRNAi; 55388; -. DR Pharos; Q7L590; Tbio. DR PRO; PR:Q7L590; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q7L590; Protein. DR Bgee; ENSG00000065328; Expressed in secondary oocyte and 117 other cell types or tissues. DR ExpressionAtlas; Q7L590; baseline and differential. DR Genevisible; Q7L590; HS. DR GO; GO:0043596; C:nuclear replication fork; IBA:GO_Central. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central. DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central. DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl. DR GO; GO:0006974; P:DNA damage response; IMP:UniProtKB. DR GO; GO:0006270; P:DNA replication initiation; IMP:UniProtKB. DR Gene3D; 1.20.5.420; Immunoglobulin FC, subunit C; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR InterPro; IPR040184; Mcm10. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR015411; Rep_factor_Mcm10_C. DR InterPro; IPR015408; Znf_Mcm10/DnaG. DR PANTHER; PTHR13454; PROTEIN MCM10 HOMOLOG; 1. DR PANTHER; PTHR13454:SF11; PROTEIN MCM10 HOMOLOG; 1. DR Pfam; PF09332; Mcm10; 1. DR Pfam; PF09329; zf-primase; 1. DR SMART; SM01280; Mcm10; 1. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Disease variant; DNA damage; KW DNA replication; DNA-binding; Isopeptide bond; Metal-binding; Nucleus; KW Phosphoprotein; Reference proteome; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..875 FT /note="Protein MCM10 homolog" FT /id="PRO_0000278320" FT REGION 1..156 FT /note="N-terminal domain" FT /evidence="ECO:0000250" FT REGION 31..120 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 137..167 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 179..228 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 238..389 FT /note="OB-fold domain" FT /evidence="ECO:0000250" FT REGION 390..415 FT /note="Zinc finger-like 1" FT REGION 567..630 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 783..802 FT /note="Zinc finger-like 2" FT /evidence="ECO:0000250" FT REGION 816..836 FT /note="Zinc finger-like 3" FT /evidence="ECO:0000250" FT COILED 104..142 FT /evidence="ECO:0000255" FT COMPBIAS 42..65 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 103..120 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 197..228 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 567..585 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 85 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17525332, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332" FT MOD_RES 93 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 644 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q0VBD2" FT CROSSLNK 493 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 627 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 762 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 763 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 152 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11095689, FT ECO:0000303|PubMed:11230166, ECO:0000303|PubMed:15489334" FT /id="VSP_029951" FT VARIANT 134 FT /note="K -> R (in dbSNP:rs17152897)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_030771" FT VARIANT 195 FT /note="A -> P (in dbSNP:rs34630110)" FT /evidence="ECO:0000269|PubMed:11230166, FT ECO:0000269|PubMed:14702039" FT /id="VAR_053836" FT VARIANT 418 FT /note="A -> V (in dbSNP:rs35114749)" FT /id="VAR_053837" FT VARIANT 427 FT /note="R -> C (in IMD80; no effect on the formation of the FT replisome)" FT /evidence="ECO:0000269|PubMed:32865517" FT /id="VAR_085769" FT VARIANT 541 FT /note="T -> S (in dbSNP:rs7905784)" FT /evidence="ECO:0000269|PubMed:11230166, FT ECO:0000269|PubMed:15489334" FT /id="VAR_030772" FT VARIANT 583..875 FT /note="Missing (in IMD80; cell cycle defect and replication FT stress in patient-derived cells; loss of nuclear FT localization)" FT /evidence="ECO:0000269|PubMed:32865517" FT /id="VAR_085770" FT VARIANT 669 FT /note="K -> R (in dbSNP:rs2274110)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_030773" FT CONFLICT 303 FT /note="K -> R (in Ref. 3; BAB70988)" FT /evidence="ECO:0000305" SQ SEQUENCE 875 AA; 98183 MW; DD87191FFF3729D4 CRC64; MDEEEDNLSL LTALLEENES ALDCNSEENN FLTRENGEPD AFDELFDADG DGESYTEEAD DGETGETRDE KENLATLFGD MEDLTDEEEV PASQSTENRV LPAPAPRREK TNEELQEELR NLQEQMKALQ EQLKVTTIKQ TASPARLQKS PVEKSPRPPL KERRVQRIQE STCFSAELDV PALPRTKRVA RTPKASPPDP KSSSSRMTSA PSQPLQTISR NKPSGITRGQ IVGTPGSSGE TTQPICVEAF SGLRLRRPRV SSTEMNKKMT GRKLIRLSQI KEKMAREKLE EIDWVTFGVI LKKVTPQSVN SGKTFSIWKL NDLRDLTQCV SLFLFGEVHK ALWKTEQGTV VGILNANPMK PKDGSEEVCL SIDHPQKVLI MGEALDLGTC KAKKKNGEPC TQTVNLRDCE YCQYHVQAQY KKLSAKRADL QSTFSGGRIP KKFARRGTSL KERLCQDGFY YGGVSSASYA ASIAAAVAPK KKIQTTLSNL VVKGTNLIIQ ETRQKLGIPQ KSLSCSEEFK ELMDLPTCGA RNLKQHLAKA TASGIMGSPK PAIKSISASA LLKQQKQRML EMRRRKSEEI QKRFLQSSSE VESPAVPSSS RQPPAQPPRT GSEFPRLEGA PATMTPKLGR GVLEGDDVLF YDESPPPRPK LSALAEAKKL AAITKLRAKG QVLTKTNPNS IKKKQKDPQD ILEVKERVEK NTMFSSQAED ELEPARKKRR EQLAYLESEE FQKILKAKSK HTGILKEAEA EMQERYFEPL VKKEQMEEKM RNIREVKCRV VTCKTCAYTH FKLLETCVSE QHEYHWHDGV KRFFKCPCGN RSISLDRLPN KHCSNCGLYK WERDGMLKEK TGPKIGGETL LPRGEEHAKF LNSLK //