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Minichromosome maintenance protein 10 (Protein DNA43)

 MCM10_YEAST             Reviewed;         571 AA.
P32354; D6VVD7;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 2.
22-NOV-2017, entry version 140.
RecName: Full=Minichromosome maintenance protein 10;
AltName: Full=Protein DNA43;
Name=MCM10; Synonyms=DNA43; OrderedLocusNames=YIL150C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1514326; DOI=10.1002/yea.320080405;
Solomon N.A., Wright M.B., Chang S., Buckley A.M., Dumas L.B.,
Gaber R.F.;
"Genetic and molecular analysis of DNA43 and DNA52: two new cell-cycle
genes in Saccharomyces cerevisiae.";
Yeast 8:273-289(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169870;
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N.,
Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G.,
Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Rowley N.,
Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
Nature 387:84-87(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MCM2; MCM3; MCM4;
MCM6 AND MCM7.
PubMed=9154825; DOI=10.1128/MCB.17.6.3261;
Merchant A.M., Kawasaki Y., Chen Y., Lei M., Tye B.K.;
"A lesion in the DNA replication initiation factor Mcm10 induces
pausing of elongation forks through chromosomal replication origins in
Saccharomyces cerevisiae.";
Mol. Cell. Biol. 17:3261-3271(1997).
[5]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF 449-ARG--ARG-451.
PubMed=13680157; DOI=10.1007/s00294-003-0443-y;
Burich R., Lei M.;
"Two bipartite NLSs mediate constitutive nuclear localization of
Mcm10.";
Curr. Genet. 44:195-201(2003).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ORC1 AND ORC2.
PubMed=11168584; DOI=10.1046/j.1365-2443.2000.00387.x;
Kawasaki Y., Hiraga S., Sugino A.;
"Interactions between Mcm10p and other replication factors are
required for proper initiation and elongation of chromosomal DNA
replication in Saccharomyces cerevisiae.";
Genes Cells 5:975-989(2000).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND MUTANTS MCM10-1 AND MCM10-43.
PubMed=10783164;
Homesley L., Lei M., Kawasaki Y., Sawyer S., Christensen T., Tye B.K.;
"Mcm10 and the MCM2-7 complex interact to initiate DNA synthesis and
to release replication factors from origins.";
Genes Dev. 14:913-926(2000).
[9]
ZINC-BINDING, SELF-ASSOCIATION, AND MUTAGENESIS OF CYS-320; CYS-332
AND HIS-335.
PubMed=12844493; DOI=10.1074/jbc.M306049200;
Cook C.R., Kung G., Peterson F.C., Volkman B.F., Lei M.;
"A novel zinc finger is required for Mcm10 homocomplex assembly.";
J. Biol. Chem. 278:36051-36058(2003).
[10]
FUNCTION, AND INTERACTION WITH CDC45.
PubMed=15201046; DOI=10.1016/j.jmb.2004.04.066;
Sawyer S.L., Cheng I.H., Chai W., Tye B.K.;
"Mcm10 and Cdc45 cooperate in origin activation in Saccharomyces
cerevisiae.";
J. Mol. Biol. 340:195-202(2004).
[11]
FUNCTION, AND INTERACTION WITH PRI2 AND RFA2.
PubMed=15494305; DOI=10.1016/j.molcel.2004.09.017;
Ricke R.M., Bielinsky A.-K.;
"Mcm10 regulates the stability and chromatin association of DNA
polymerase-alpha.";
Mol. Cell 16:173-185(2004).
[12]
FUNCTION.
PubMed=16085704; DOI=10.1534/genetics.105.042333;
Liachko I., Tye B.K.;
"Mcm10 is required for the maintenance of transcriptional silencing in
Saccharomyces cerevisiae.";
Genetics 171:503-515(2005).
[13]
FUNCTION IN TRANSCRIPTIONAL SILENCING, AND INTERACTION WITH SIR2 AND
SIR3.
PubMed=16328881; DOI=10.1007/s11033-005-2312-x;
Douglas N.L., Dozier S.K., Donato J.J.;
"Dual roles for Mcm10 in DNA replication initiation and silencing at
the mating-type loci.";
Mol. Biol. Rep. 32:197-204(2005).
[14]
FUNCTION, INTERACTION WITH POL1; PRI2 AND POL12, AND MUTAGENESIS OF
GLY-261 AND ASN-268.
PubMed=16675460; DOI=10.1074/jbc.M513551200;
Ricke R.M., Bielinsky A.-K.;
"A conserved Hsp10-like domain in Mcm10 is required to stabilize the
catalytic subunit of DNA polymerase-alpha in budding yeast.";
J. Biol. Chem. 281:18414-18425(2006).
[15]
INTERACTION WITH POL30, UBIQUITINATION, AND MUTAGENESIS OF TYR-245.
PubMed=16782870; DOI=10.1128/MCB.02062-05;
Das-Bradoo S., Ricke R.M., Bielinsky A.-K.;
"Interaction between PCNA and diubiquitinated Mcm10 is essential for
cell growth in budding yeast.";
Mol. Cell. Biol. 26:4806-4817(2006).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453 AND SER-454, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-17 AND SER-18, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Required for DNA synthesis. Required for entry into or
completion of S phase. Involved in DNA replication and seems to
participate in the activation of the pre-replication complex (pre-
RC) and in transcription elongation. May play a role as a key
coordinator in assembling the replication fork. Proposed to
function at replication origins following the binding of the MCM2-
7 complex prior to the recruitment of CDC45. Probably is required
to stimulate phosphorylation of the MCM2-7 complex by the CDC7-
DBF4 kinase complex. May recruit the DNA polymerase alpha:primase
complex to replication origins and is required to maintain it on
chromatin independently of CDC45. May also play a role in
transcriptional silencing. {ECO:0000269|PubMed:10783164,
ECO:0000269|PubMed:11168584, ECO:0000269|PubMed:15201046,
ECO:0000269|PubMed:15494305, ECO:0000269|PubMed:16085704,
ECO:0000269|PubMed:16328881, ECO:0000269|PubMed:16675460,
ECO:0000269|PubMed:9154825}.
-!- SUBUNIT: Self-associates; assembles into large homomultimeric
complexes of approximately 800 kDa. Associates with the MCM2-7
complex and the DNA polymerase alpha:primase complex. Interacts
with ORC1, ORC2, MCM2, MCM3, CDC54/MCM4, MCM6, CDC47/MCM7, RFA2,
CDC45, POL1, PRI2, POL12, SIR2 and SIR3. The diubiquitinated form
interacts with POL30/PCNA C-terminus.
{ECO:0000269|PubMed:11168584, ECO:0000269|PubMed:15201046,
ECO:0000269|PubMed:15494305, ECO:0000269|PubMed:16328881,
ECO:0000269|PubMed:16675460, ECO:0000269|PubMed:16782870,
ECO:0000269|PubMed:9154825}.
-!- INTERACTION:
P30665:MCM4; NbExp=3; IntAct=EBI-5965, EBI-4326;
P53091:MCM6; NbExp=5; IntAct=EBI-5965, EBI-10556;
P15873:POL30; NbExp=4; IntAct=EBI-5965, EBI-12993;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10783164,
ECO:0000269|PubMed:11168584, ECO:0000269|PubMed:13680157,
ECO:0000269|PubMed:9154825}. Note=Colocalizes with ORC1 on
chromatin independent from cell cycle. According to
PubMed:15494305 is recruited to replication origins in a cell
cycle regulated manner.
-!- DOMAIN: The zinc finger-like domain binds a zinc ion and is
involved in self-association.
-!- PTM: Diubiquitinated in a cell cycle-regulated manner.
Ubiquitination first appears in late G(1) and persists throughout
S phase. {ECO:0000269|PubMed:16782870}.
-!- MISCELLANEOUS: Present with 1860 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the MCM10 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Z38059; CAA86128.1; -; Genomic_DNA.
EMBL; M83540; AAA34574.1; -; Genomic_DNA.
EMBL; BK006942; DAA08403.1; -; Genomic_DNA.
PIR; S48384; S48384.
RefSeq; NP_012116.1; NM_001179498.1.
ProteinModelPortal; P32354; -.
BioGrid; 34842; 354.
DIP; DIP-1293N; -.
IntAct; P32354; 18.
MINT; MINT-397002; -.
STRING; 4932.YIL150C; -.
iPTMnet; P32354; -.
MaxQB; P32354; -.
PRIDE; P32354; -.
EnsemblFungi; YIL150C; YIL150C; YIL150C.
GeneID; 854656; -.
KEGG; sce:YIL150C; -.
EuPathDB; FungiDB:YIL150C; -.
SGD; S000001412; MCM10.
GeneTree; ENSGT00390000007134; -.
HOGENOM; HOG000000960; -.
InParanoid; P32354; -.
KO; K10736; -.
OMA; CDIHLDM; -.
OrthoDB; EOG092C19KH; -.
BioCyc; YEAST:G3O-31399-MONOMER; -.
Reactome; R-SCE-68962; Activation of the pre-replicative complex.
PRO; PR:P32354; -.
Proteomes; UP000002311; Chromosome IX.
GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0005657; C:replication fork; IMP:SGD.
GO; GO:0031298; C:replication fork protection complex; IDA:SGD.
GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003697; F:single-stranded DNA binding; IDA:SGD.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0030466; P:chromatin silencing at silent mating-type cassette; IMP:SGD.
GO; GO:0006348; P:chromatin silencing at telomere; IMP:SGD.
GO; GO:0006270; P:DNA replication initiation; IMP:SGD.
GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IMP:SGD.
GO; GO:0000727; P:double-strand break repair via break-induced replication; IMP:SGD.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR015408; Znf_Mcm10/DnaG.
Pfam; PF09329; zf-primase; 1.
SUPFAM; SSF50249; SSF50249; 1.
1: Evidence at protein level;
Cell cycle; Complete proteome; DNA replication; Metal-binding;
Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation; Zinc;
Zinc-finger.
CHAIN 1 571 Minichromosome maintenance protein 10.
/FTId=PRO_0000079949.
REGION 309 335 Zinc finger-like.
REGION 435 512 Sufficient for nuclear localization.
REGION 453 553 Sufficient for nuclear localization.
MOTIF 435 451 Bipartite nuclear localization signal.
{ECO:0000250}.
MOTIF 512 527 Bipartite nuclear localization signal.
{ECO:0000250}.
MOD_RES 17 17 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 18 18 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 453 453 Phosphoserine.
{ECO:0000244|PubMed:17287358}.
MOD_RES 454 454 Phosphoserine.
{ECO:0000244|PubMed:17287358}.
MUTAGEN 245 245 Y->A: Inhibits interaction with
POL30/PCNA and abolishes cell
proliferation.
{ECO:0000269|PubMed:16782870}.
MUTAGEN 261 261 G->A,D: Temperature sensitive; loss of
CDC17 stabilization.
{ECO:0000269|PubMed:16675460}.
MUTAGEN 268 268 N->D,I: Temperature sensitive; loss of
CDC17 stabilization.
{ECO:0000269|PubMed:16675460}.
MUTAGEN 269 269 P->L: In mcm10-1; diminishes interaction
with MCM7.
MUTAGEN 320 320 C->Y: In mcm10-43; abolishes self-
association and diminishes interaction
with MCM7. {ECO:0000269|PubMed:12844493}.
MUTAGEN 332 332 C->G: Abolishes self-association; when
associated with L-335.
{ECO:0000269|PubMed:12844493}.
MUTAGEN 335 335 H->L: Abolishes self-association; when
associated with G-332.
{ECO:0000269|PubMed:12844493}.
MUTAGEN 449 451 RRR->GGG: No effect on nuclear
localization.
{ECO:0000269|PubMed:13680157}.
CONFLICT 38 38 Q -> H (in Ref. 1; AAA34574).
{ECO:0000305}.
CONFLICT 458 458 D -> H (in Ref. 1; AAA34574).
{ECO:0000305}.
CONFLICT 492 571 ISQVLKSSVSGSEPKNNLLGKKKTVINDLLHYKKEKVILAP
SKNEWFKKRSHREEVWQKHFGSKETKETSDGSASDLEII
-> NFPKYSSLLYQGANLRTTYSVKKKLL (in Ref.
1). {ECO:0000305}.
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


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