MCM10_YEAST
ID MCM10_YEAST Reviewed; 571 AA.
AC P32354; D6VVD7;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Minichromosome maintenance protein 10;
DE AltName: Full=Protein DNA43;
GN Name=MCM10; Synonyms=DNA43; OrderedLocusNames=YIL150C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1514326; DOI=10.1002/yea.320080405;
RA Solomon N.A., Wright M.B., Chang S., Buckley A.M., Dumas L.B., Gaber R.F.;
RT "Genetic and molecular analysis of DNA43 and DNA52: two new cell-cycle
RT genes in Saccharomyces cerevisiae.";
RL Yeast 8:273-289(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MCM2; MCM3; MCM4; MCM6
RP AND MCM7.
RX PubMed=9154825; DOI=10.1128/mcb.17.6.3261;
RA Merchant A.M., Kawasaki Y., Chen Y., Lei M., Tye B.K.;
RT "A lesion in the DNA replication initiation factor Mcm10 induces pausing of
RT elongation forks through chromosomal replication origins in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 17:3261-3271(1997).
RN [5]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 449-ARG--ARG-451.
RX PubMed=13680157; DOI=10.1007/s00294-003-0443-y;
RA Burich R., Lei M.;
RT "Two bipartite NLSs mediate constitutive nuclear localization of Mcm10.";
RL Curr. Genet. 44:195-201(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ORC1 AND ORC2.
RX PubMed=11168584; DOI=10.1046/j.1365-2443.2000.00387.x;
RA Kawasaki Y., Hiraga S., Sugino A.;
RT "Interactions between Mcm10p and other replication factors are required for
RT proper initiation and elongation of chromosomal DNA replication in
RT Saccharomyces cerevisiae.";
RL Genes Cells 5:975-989(2000).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTANTS MCM10-1 AND MCM10-43.
RX PubMed=10783164;
RA Homesley L., Lei M., Kawasaki Y., Sawyer S., Christensen T., Tye B.K.;
RT "Mcm10 and the MCM2-7 complex interact to initiate DNA synthesis and to
RT release replication factors from origins.";
RL Genes Dev. 14:913-926(2000).
RN [9]
RP ZINC-BINDING, SELF-ASSOCIATION, AND MUTAGENESIS OF CYS-320; CYS-332 AND
RP HIS-335.
RX PubMed=12844493; DOI=10.1074/jbc.m306049200;
RA Cook C.R., Kung G., Peterson F.C., Volkman B.F., Lei M.;
RT "A novel zinc finger is required for Mcm10 homocomplex assembly.";
RL J. Biol. Chem. 278:36051-36058(2003).
RN [10]
RP FUNCTION, AND INTERACTION WITH CDC45.
RX PubMed=15201046; DOI=10.1016/j.jmb.2004.04.066;
RA Sawyer S.L., Cheng I.H., Chai W., Tye B.K.;
RT "Mcm10 and Cdc45 cooperate in origin activation in Saccharomyces
RT cerevisiae.";
RL J. Mol. Biol. 340:195-202(2004).
RN [11]
RP FUNCTION, AND INTERACTION WITH PRI2 AND RFA2.
RX PubMed=15494305; DOI=10.1016/j.molcel.2004.09.017;
RA Ricke R.M., Bielinsky A.-K.;
RT "Mcm10 regulates the stability and chromatin association of DNA polymerase-
RT alpha.";
RL Mol. Cell 16:173-185(2004).
RN [12]
RP FUNCTION.
RX PubMed=16085704; DOI=10.1534/genetics.105.042333;
RA Liachko I., Tye B.K.;
RT "Mcm10 is required for the maintenance of transcriptional silencing in
RT Saccharomyces cerevisiae.";
RL Genetics 171:503-515(2005).
RN [13]
RP FUNCTION IN TRANSCRIPTIONAL SILENCING, AND INTERACTION WITH SIR2 AND SIR3.
RX PubMed=16328881; DOI=10.1007/s11033-005-2312-x;
RA Douglas N.L., Dozier S.K., Donato J.J.;
RT "Dual roles for Mcm10 in DNA replication initiation and silencing at the
RT mating-type loci.";
RL Mol. Biol. Rep. 32:197-204(2005).
RN [14]
RP FUNCTION, INTERACTION WITH POL1; PRI2 AND POL12, AND MUTAGENESIS OF GLY-261
RP AND ASN-268.
RX PubMed=16675460; DOI=10.1074/jbc.m513551200;
RA Ricke R.M., Bielinsky A.-K.;
RT "A conserved Hsp10-like domain in Mcm10 is required to stabilize the
RT catalytic subunit of DNA polymerase-alpha in budding yeast.";
RL J. Biol. Chem. 281:18414-18425(2006).
RN [15]
RP INTERACTION WITH POL30, UBIQUITINATION, AND MUTAGENESIS OF TYR-245.
RX PubMed=16782870; DOI=10.1128/mcb.02062-05;
RA Das-Bradoo S., Ricke R.M., Bielinsky A.-K.;
RT "Interaction between PCNA and diubiquitinated Mcm10 is essential for cell
RT growth in budding yeast.";
RL Mol. Cell. Biol. 26:4806-4817(2006).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453 AND SER-454, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-17 AND SER-18, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Required for DNA synthesis. Required for entry into or
CC completion of S phase. Involved in DNA replication and seems to
CC participate in the activation of the pre-replication complex (pre-RC)
CC and in transcription elongation. May play a role as a key coordinator
CC in assembling the replication fork. Proposed to function at replication
CC origins following the binding of the MCM2-7 complex prior to the
CC recruitment of CDC45. Probably is required to stimulate phosphorylation
CC of the MCM2-7 complex by the CDC7-DBF4 kinase complex. May recruit the
CC DNA polymerase alpha:primase complex to replication origins and is
CC required to maintain it on chromatin independently of CDC45. May also
CC play a role in transcriptional silencing. {ECO:0000269|PubMed:10783164,
CC ECO:0000269|PubMed:11168584, ECO:0000269|PubMed:15201046,
CC ECO:0000269|PubMed:15494305, ECO:0000269|PubMed:16085704,
CC ECO:0000269|PubMed:16328881, ECO:0000269|PubMed:16675460,
CC ECO:0000269|PubMed:9154825}.
CC -!- SUBUNIT: Self-associates; assembles into large homomultimeric complexes
CC of approximately 800 kDa. Associates with the MCM2-7 complex and the
CC DNA polymerase alpha:primase complex. Interacts with ORC1, ORC2, MCM2,
CC MCM3, CDC54/MCM4, MCM6, CDC47/MCM7, RFA2, CDC45, POL1, PRI2, POL12,
CC SIR2 and SIR3. The diubiquitinated form interacts with POL30/PCNA C-
CC terminus. {ECO:0000269|PubMed:11168584, ECO:0000269|PubMed:15201046,
CC ECO:0000269|PubMed:15494305, ECO:0000269|PubMed:16328881,
CC ECO:0000269|PubMed:16675460, ECO:0000269|PubMed:16782870,
CC ECO:0000269|PubMed:9154825}.
CC -!- INTERACTION:
CC P32354; P30665: MCM4; NbExp=3; IntAct=EBI-5965, EBI-4326;
CC P32354; P53091: MCM6; NbExp=5; IntAct=EBI-5965, EBI-10556;
CC P32354; P15873: POL30; NbExp=4; IntAct=EBI-5965, EBI-12993;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10783164,
CC ECO:0000269|PubMed:11168584, ECO:0000269|PubMed:13680157,
CC ECO:0000269|PubMed:9154825}. Note=Colocalizes with ORC1 on chromatin
CC independent from cell cycle. According to PubMed:15494305 is recruited
CC to replication origins in a cell cycle regulated manner.
CC -!- DOMAIN: The zinc finger-like domain binds a zinc ion and is involved in
CC self-association.
CC -!- PTM: Diubiquitinated in a cell cycle-regulated manner. Ubiquitination
CC first appears in late G(1) and persists throughout S phase.
CC {ECO:0000269|PubMed:16782870}.
CC -!- MISCELLANEOUS: Present with 1860 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MCM10 family. {ECO:0000305}.
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DR EMBL; Z38059; CAA86128.1; -; Genomic_DNA.
DR EMBL; M83540; AAA34574.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08403.1; -; Genomic_DNA.
DR PIR; S48384; S48384.
DR RefSeq; NP_012116.1; NM_001179498.1.
DR AlphaFoldDB; P32354; -.
DR SMR; P32354; -.
DR BioGRID; 34842; 383.
DR DIP; DIP-1293N; -.
DR IntAct; P32354; 18.
DR MINT; P32354; -.
DR STRING; 4932.YIL150C; -.
DR iPTMnet; P32354; -.
DR MaxQB; P32354; -.
DR PaxDb; P32354; -.
DR PRIDE; P32354; -.
DR EnsemblFungi; YIL150C_mRNA; YIL150C; YIL150C.
DR GeneID; 854656; -.
DR KEGG; sce:YIL150C; -.
DR SGD; S000001412; MCM10.
DR VEuPathDB; FungiDB:YIL150C; -.
DR eggNOG; KOG3056; Eukaryota.
DR GeneTree; ENSGT00390000007134; -.
DR HOGENOM; CLU_036499_0_0_1; -.
DR InParanoid; P32354; -.
DR OMA; YYNLRVG; -.
DR BioCyc; YEAST:G3O-31399-MON; -.
DR Reactome; R-SCE-68962; Activation of the pre-replicative complex.
DR PRO; PR:P32354; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P32354; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005657; C:replication fork; IMP:SGD.
DR GO; GO:0031298; C:replication fork protection complex; IDA:SGD.
DR GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IMP:SGD.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IMP:SGD.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IMP:SGD.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IMP:SGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR040184; Mcm10.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR015408; Znf_Mcm10/DnaG.
DR PANTHER; PTHR13454; PTHR13454; 1.
DR Pfam; PF09329; zf-primase; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 1: Evidence at protein level;
KW Cell cycle; DNA replication; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..571
FT /note="Minichromosome maintenance protein 10"
FT /id="PRO_0000079949"
FT REGION 309..335
FT /note="Zinc finger-like"
FT REGION 435..512
FT /note="Sufficient for nuclear localization"
FT REGION 451..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..553
FT /note="Sufficient for nuclear localization"
FT REGION 548..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 435..451
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 512..527
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 451..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MUTAGEN 245
FT /note="Y->A: Inhibits interaction with POL30/PCNA and
FT abolishes cell proliferation."
FT /evidence="ECO:0000269|PubMed:16782870"
FT MUTAGEN 261
FT /note="G->A,D: Temperature sensitive; loss of CDC17
FT stabilization."
FT /evidence="ECO:0000269|PubMed:16675460"
FT MUTAGEN 268
FT /note="N->D,I: Temperature sensitive; loss of CDC17
FT stabilization."
FT /evidence="ECO:0000269|PubMed:16675460"
FT MUTAGEN 269
FT /note="P->L: In mcm10-1; diminishes interaction with MCM7."
FT MUTAGEN 320
FT /note="C->Y: In mcm10-43; abolishes self-association and
FT diminishes interaction with MCM7."
FT /evidence="ECO:0000269|PubMed:12844493"
FT MUTAGEN 332
FT /note="C->G: Abolishes self-association; when associated
FT with L-335."
FT /evidence="ECO:0000269|PubMed:12844493"
FT MUTAGEN 335
FT /note="H->L: Abolishes self-association; when associated
FT with G-332."
FT /evidence="ECO:0000269|PubMed:12844493"
FT MUTAGEN 449..451
FT /note="RRR->GGG: No effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:13680157"
FT CONFLICT 38
FT /note="Q -> H (in Ref. 1; AAA34574)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="D -> H (in Ref. 1; AAA34574)"
FT /evidence="ECO:0000305"
FT CONFLICT 492..571
FT /note="ISQVLKSSVSGSEPKNNLLGKKKTVINDLLHYKKEKVILAPSKNEWFKKRSH
FT REEVWQKHFGSKETKETSDGSASDLEII -> NFPKYSSLLYQGANLRTTYSVKKKLL
FT (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 571 AA; 65815 MW; D32CFF4A94FD9B2A CRC64;
MNDPREILAV DPYNNITSDE EDEQAIAREL EFMERKRQAL VERLKRKQEF KKPQDPNFEA
IEVPQSPTKN RVKVGSHNAT QQGTKFEGSN INEVRLSQLQ QQPKPPASTT TYFMEKFQNA
KKNEDKQIAK FESMMNARVH TFSTDEKKYV PIITNELESF SNLWVKKRYI PEDDLKRALH
EIKILRLGKL FAKIRPPKFQ EPEYANWATV GLISHKSDIK FTSSEKPVKF FMFTITDFQH
TLDVYIFGKK GVERYYNLRL GDVIAILNPE VLPWRPSGRG NFIKSFNLRI SHDFKCILEI
GSSRDLGWCP IVNKKTHKKC GSPINISLHK CCDYHREVQF RGTSAKRIEL NGGYALGAPT
KVDSQPSLYK AKGENGFNII KGTRKRLSEE EERLKKSSHN FTNSNSAKAF FDEKFQNPDM
LANLDNKRRK IIETKKSTAL SRELGKIMRR RESSGLEDKS VGERQKMKRT TESALQTGLI
QRLGFDPTHG KISQVLKSSV SGSEPKNNLL GKKKTVINDL LHYKKEKVIL APSKNEWFKK
RSHREEVWQK HFGSKETKET SDGSASDLEI I
