MCM10_MOUSE
ID MCM10_MOUSE Reviewed; 885 AA.
AC Q0VBD2; Q505F3; Q8BMJ1; Q8BYA7;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Protein MCM10 homolog;
GN Name=Mcm10;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-85 AND SER-656, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). {ECO:0000250|UniProtKB:Q7L590}.
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q5EAW4, ECO:0000250|UniProtKB:Q7L590}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7L590}.
CC Note=Colocalizes with ORC2 in nuclei foci. Associated with chromatin in
CC S phase (By similarity). {ECO:0000250|UniProtKB:Q7L590}.
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 -!- SIMILARITY: Belongs to the MCM10 family. {ECO:0000305}.
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DR EMBL; AK030780; BAC27135.1; -; mRNA.
DR EMBL; AK041406; BAC30933.1; -; mRNA.
DR EMBL; AL928662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC094576; AAH94576.1; -; mRNA.
DR EMBL; BC120689; AAI20690.1; -; mRNA.
DR EMBL; BC120687; AAI20688.1; -; mRNA.
DR CCDS; CCDS15662.1; -.
DR RefSeq; NP_001292188.1; NM_001305259.1.
DR RefSeq; NP_081566.2; NM_027290.3.
DR AlphaFoldDB; Q0VBD2; -.
DR SMR; Q0VBD2; -.
DR BioGRID; 213824; 2.
DR STRING; 10090.ENSMUSP00000027980; -.
DR iPTMnet; Q0VBD2; -.
DR PhosphoSitePlus; Q0VBD2; -.
DR EPD; Q0VBD2; -.
DR MaxQB; Q0VBD2; -.
DR PaxDb; Q0VBD2; -.
DR PeptideAtlas; Q0VBD2; -.
DR PRIDE; Q0VBD2; -.
DR ProteomicsDB; 295707; -.
DR Antibodypedia; 11355; 153 antibodies from 25 providers.
DR Ensembl; ENSMUST00000027980; ENSMUSP00000027980; ENSMUSG00000026669.
DR Ensembl; ENSMUST00000102985; ENSMUSP00000100050; ENSMUSG00000026669.
DR GeneID; 70024; -.
DR KEGG; mmu:70024; -.
DR UCSC; uc008ifh.2; mouse.
DR CTD; 55388; -.
DR MGI; MGI:1917274; Mcm10.
DR VEuPathDB; HostDB:ENSMUSG00000026669; -.
DR eggNOG; KOG3056; Eukaryota.
DR GeneTree; ENSGT00390000007134; -.
DR HOGENOM; CLU_014680_0_0_1; -.
DR InParanoid; Q0VBD2; -.
DR OMA; VFGLRMI; -.
DR OrthoDB; 758449at2759; -.
DR PhylomeDB; Q0VBD2; -.
DR TreeFam; TF313330; -.
DR Reactome; R-MMU-176187; Activation of ATR in response to replication stress.
DR Reactome; R-MMU-68962; Activation of the pre-replicative complex.
DR BioGRID-ORCS; 70024; 12 hits in 73 CRISPR screens.
DR PRO; PR:Q0VBD2; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q0VBD2; protein.
DR Bgee; ENSMUSG00000026669; Expressed in animal zygote and 166 other tissues.
DR Genevisible; Q0VBD2; MM.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS: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; IPI:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
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; IMP:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006270; P:DNA replication initiation; ISO:MGI.
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 Coiled coil; DNA damage; DNA replication; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..885
FT /note="Protein MCM10 homolog"
FT /id="PRO_0000278321"
FT REGION 1..153
FT /note="N-terminal domain"
FT /evidence="ECO:0000250"
FT REGION 23..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..405
FT /note="OB-fold domain"
FT /evidence="ECO:0000250"
FT REGION 406..431
FT /note="Zinc finger-like 1"
FT REGION 579..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..812
FT /note="Zinc finger-like 2"
FT /evidence="ECO:0000250"
FT REGION 826..846
FT /note="Zinc finger-like 3"
FT /evidence="ECO:0000250"
FT COILED 101..139
FT /evidence="ECO:0000255"
FT COMPBIAS 38..58
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 85
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 656
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 639
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7L590"
FT CROSSLNK 772
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7L590"
FT CROSSLNK 773
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7L590"
FT CONFLICT 50
FT /note="G -> R (in Ref. 3; AAH94576)"
FT /evidence="ECO:0000305"
FT CONFLICT 673
FT /note="A -> V (in Ref. 1; BAC27135)"
FT /evidence="ECO:0000305"
FT CONFLICT 873
FT /note="R -> I (in Ref. 3; AAH94576)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 885 AA; 98406 MW; CF2F91AC0A8A18B1 CRC64;
MDVEEDDLCL LTSLLEENEA VLPCSSEKDK SLSLGDGDPD EFDELFDADG DGESYTEEAG
SGEEGKTGNQ EERLATLFGD VEDLTDDEVA TSKVGNSGPP PAPSQEKTSE ELQDELKKLQ
EQMKSLQEQL KAASIKQPPG TAPLQEPPDS SLQPLLKEKR IRRIQESACF SAELDVPTLP
KAKRVARKPK TPAESSSRMR TPAQPLQVSS SFLEPNHSSS SRSSTPSPQA VPGNKCSRTI
RNQNTVSPGN SGDRPQQVSQ VSVEAFSGLR LRRPRVSSTE MSRKMAGRKL IRLPQIKEKM
ATENLEETDW VTFGVILRKV TPQSATSGQT FSIWKLNDLH DLTQCVSLFL FGDVHKDLWK
TEQGTVIGLL NANPMKPKDG LKEVCLSIDH PQKVLIMGEA MDLGACKAKK KNGEPCTQTV
NLHDCEYCQY HIQAQYKKLS AKRTDLQSTF SGGRIPKKFR KGTSLKERLC QDGFYYGGVS
SESFAASRAA AIAPKKKVQT TLTNLVVRGT NSIIQETKQK LGIPQKSLSC SEEFRELMAL
PTFGARNLQK HLARAKASGS SKPAIQSISA SALLKQQKQQ MLEMRKRRSE DIQKRFLQSS
SEVQSPAVPS SSRQAAAQSP RTGAEFPRLE GTATPRMPKL GRGISEGDDV LFFDDSPPPR
PKLSAAAEAK KLAAIAKLRA KGQILTKVDP NNTVRKQMDG RAMLGVKERV ENSNTVSPEE
ELEPARKKRR EQLAYLESEE FQKILKAKSK HTDILKEAEA ELQKSYFEPL VKKEQMEEKM
RATREVKCRV VTCRTCTYTH FKPLETCVSE QHNLHWHDGV KRFFKCPCGN RTISLDKLPN
KHCRNCGLYK WERDGMLKEK TGPKIGGETL LPRGEEHAKF LNSLK
