MCM10_HUMAN
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 03-AUG-2022, entry version 155.
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};
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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; 113.
DR IntAct; Q7L590; 54.
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; Q7L590; -.
DR PeptideAtlas; Q7L590; -.
DR PRIDE; Q7L590; -.
DR ProteomicsDB; 68795; -. [Q7L590-1]
DR ProteomicsDB; 68796; -. [Q7L590-2]
DR Antibodypedia; 11355; 153 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 CTD; 55388; -.
DR DisGeNET; 55388; -.
DR GeneCards; MCM10; -.
DR HGNC; HGNC:18043; MCM10.
DR HPA; ENSG00000065328; Tissue enhanced (bone marrow, lymphoid tissue).
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; 758449at2759; -.
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; 341 hits in 1088 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 116 other tissues.
DR ExpressionAtlas; Q7L590; baseline and differential.
DR Genevisible; Q7L590; HS.
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:0031298; C:replication fork protection complex; IBA:GO_Central.
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:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0006270; P:DNA replication initiation; IMP:UniProtKB.
DR Gene3D; 2.40.50.140; -; 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; PTHR13454; 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
