Minichromosome maintenance protein 10 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P32354 (MCM10_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 92. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Minichromosome maintenance protein 10

Alternative name(s):
Protein DNA43

Gene names

Name:	MCM10
Synonyms:	DNA43
Ordered Locus Names:	YIL150C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	571 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.4 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14
Subunit structure	Self-associates; assembles into large homomultimeric complexes of approximative 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. Ref.4 Ref.7 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15
Subcellular location	Nucleus. Note: Colocalizes with ORC1 on chromatin independent from cell cycle. According to Ref.11 is recruited to replication origins in a cell cycle regulated manner. Ref.4 Ref.5 Ref.7 Ref.8
Domain	The zinc finger-like domain binds a zinc ion and is involved in self-association.
Post-translational modification	Diubiquitinated in a cell cycle-regulated manner. Ubiquitination first appears in late G₁ and persists throughout S phase.
Miscellaneous	Present with 1860 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Belongs to the MCM10 family.

Ontologies

Keywords
Biological process	Cell cycle DNA replication
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	Metal-binding Zinc
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA strand elongation involved in DNA replication Inferred from mutant phenotype Ref.8 Ref.4. Source: SGD DNA-dependent DNA replication initiation Inferred from mutant phenotype Ref.8. Source: SGD S phase of mitotic cell cycle Inferred from mutant phenotype Ref.7 Ref.11. Source: SGD chromatin silencing at silent mating-type cassette Inferred from mutant phenotype Ref.12 Ref.13. Source: SGD chromatin silencing at telomere Inferred from mutant phenotype Ref.12. Source: SGD double-strand break repair via break-induced replication Inferred from mutant phenotype. Source: SGD
Cellular component	replication fork protection complex Inferred from direct assay. Source: SGD
Molecular function	DNA replication origin binding Inferred from direct assay Ref.8 Ref.11. Source: SGD double-stranded DNA binding Inferred from direct assay. Source: SGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.15 Ref.4. Source: IntAct single-stranded DNA binding Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MCM6	P53091	3	EBI-5965,EBI-10556
POL30	P15873	4	EBI-5965,EBI-12993

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 571

571

Minichromosome maintenance protein 10

PRO_0000079949

Regions

Region

309 – 335

Zinc finger-like

Region

435 – 512

Sufficient for nuclear localization

Region

453 – 553

101

Sufficient for nuclear localization

Motif

435 – 451

Bipartite nuclear localization signal By similarity

Motif

512 – 527

Bipartite nuclear localization signal By similarity

Amino acid modifications

Modified residue

Phosphothreonine Ref.17

Modified residue

Phosphoserine Ref.17

Modified residue

453

Phosphoserine Ref.16

Modified residue

454

Phosphoserine Ref.16

Experimental info

Mutagenesis

245

Y → A: Inhibits interaction with POL30/PCNA and abolishes cell proliferation. Ref.15

Mutagenesis

261

G → A or D: Temperature sensitive; loss of CDC17 stabilization. Ref.14

Mutagenesis

268

N → D or I: Temperature sensitive; loss of CDC17 stabilization. Ref.14

Mutagenesis

269

P → L in mcm10-1; diminishes interaction with MCM7.

Mutagenesis

320

C → Y in mcm10-43; abolishes self-association and diminishes interaction with MCM7. Ref.9

Mutagenesis

332

C → G: Abolishes self-association; when associated with L-335. Ref.9

Mutagenesis

335

H → L: Abolishes self-association; when associated with G-332. Ref.9

Mutagenesis

449 – 451

RRR → GGG: No effect on nuclear localization. Ref.5

Sequence conflict

Q → H in AAA34574. Ref.1

Sequence conflict

458

D → H in AAA34574. Ref.1

Sequence conflict

492 – 571

ISQVL…DLEII → NFPKYSSLLYQGANLRTTYS VKKKLL Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P32354 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: D32CFF4A94FD9B2A
Show »

FASTA

571

65,815

        10         20         30         40         50         60 
MNDPREILAV DPYNNITSDE EDEQAIAREL EFMERKRQAL VERLKRKQEF KKPQDPNFEA 

        70         80         90        100        110        120 
IEVPQSPTKN RVKVGSHNAT QQGTKFEGSN INEVRLSQLQ QQPKPPASTT TYFMEKFQNA 

       130        140        150        160        170        180 
KKNEDKQIAK FESMMNARVH TFSTDEKKYV PIITNELESF SNLWVKKRYI PEDDLKRALH 

       190        200        210        220        230        240 
EIKILRLGKL FAKIRPPKFQ EPEYANWATV GLISHKSDIK FTSSEKPVKF FMFTITDFQH 

       250        260        270        280        290        300 
TLDVYIFGKK GVERYYNLRL GDVIAILNPE VLPWRPSGRG NFIKSFNLRI SHDFKCILEI 

       310        320        330        340        350        360 
GSSRDLGWCP IVNKKTHKKC GSPINISLHK CCDYHREVQF RGTSAKRIEL NGGYALGAPT 

       370        380        390        400        410        420 
KVDSQPSLYK AKGENGFNII KGTRKRLSEE EERLKKSSHN FTNSNSAKAF FDEKFQNPDM 

       430        440        450        460        470        480 
LANLDNKRRK IIETKKSTAL SRELGKIMRR RESSGLEDKS VGERQKMKRT TESALQTGLI 

       490        500        510        520        530        540 
QRLGFDPTHG KISQVLKSSV SGSEPKNNLL GKKKTVINDL LHYKKEKVIL APSKNEWFKK 

       550        560        570 
RSHREEVWQK HFGSKETKET SDGSASDLEI I

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genetic and molecular analysis of DNA43 and DNA52: two new cell-cycle genes in Saccharomyces cerevisiae." Solomon N.A., Wright M.B., Chang S., Buckley A.M., Dumas L.B., Gaber R.F. Yeast 8:273-289(1992) [PubMed: 1514326] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX." 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. Barrell B.G. Nature 387:84-87(1997) [PubMed: 9169870] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"A lesion in the DNA replication initiation factor Mcm10 induces pausing of elongation forks through chromosomal replication origins in Saccharomyces cerevisiae." Merchant A.M., Kawasaki Y., Chen Y., Lei M., Tye B.K. Mol. Cell. Biol. 17:3261-3271(1997) [PubMed: 9154825] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MCM2; MCM3; MCM4; MCM6 AND MCM7.
[5]	"Two bipartite NLSs mediate constitutive nuclear localization of Mcm10." Burich R., Lei M. Curr. Genet. 44:195-201(2003) [PubMed: 13680157] [Abstract] Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF 449-ARG--ARG-451.
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"Interactions between Mcm10p and other replication factors are required for proper initiation and elongation of chromosomal DNA replication in Saccharomyces cerevisiae." Kawasaki Y., Hiraga S., Sugino A. Genes Cells 5:975-989(2000) [PubMed: 11168584] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ORC1 AND ORC2.
[8]	"Mcm10 and the MCM2-7 complex interact to initiate DNA synthesis and to release replication factors from origins." Homesley L., Lei M., Kawasaki Y., Sawyer S., Christensen T., Tye B.K. Genes Dev. 14:913-926(2000) [PubMed: 10783164] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTANTS MCM10-1 AND MCM10-43.
[9]	"A novel zinc finger is required for Mcm10 homocomplex assembly." Cook C.R., Kung G., Peterson F.C., Volkman B.F., Lei M. J. Biol. Chem. 278:36051-36058(2003) [PubMed: 12844493] [Abstract] Cited for: ZINC-BINDING, SELF-ASSOCIATION, MUTAGENESIS OF CYS-320; CYS-332 AND HIS-335.
[10]	"Mcm10 and Cdc45 cooperate in origin activation in Saccharomyces cerevisiae." Sawyer S.L., Cheng I.H., Chai W., Tye B.K. J. Mol. Biol. 340:195-202(2004) [PubMed: 15201046] [Abstract] Cited for: FUNCTION, INTERACTION WITH CDC45.
[11]	"Mcm10 regulates the stability and chromatin association of DNA polymerase-alpha." Ricke R.M., Bielinsky A.-K. Mol. Cell 16:173-185(2004) [PubMed: 15494305] [Abstract] Cited for: FUNCTION, INTERACTION WITH PRI2 AND RFA2.
[12]	"Mcm10 is required for the maintenance of transcriptional silencing in Saccharomyces cerevisiae." Liachko I., Tye B.K. Genetics 171:503-515(2005) [PubMed: 16085704] [Abstract] Cited for: FUNCTION.
[13]	"Dual roles for Mcm10 in DNA replication initiation and silencing at the mating-type loci." Douglas N.L., Dozier S.K., Donato J.J. Mol. Biol. Rep. 32:197-204(2005) [PubMed: 16328881] [Abstract] Cited for: FUNCTION IN TRANSCRIPTIONAL SILENCING, INTERACTION WITH SIR2 AND SIR3.
[14]	"A conserved Hsp10-like domain in Mcm10 is required to stabilize the catalytic subunit of DNA polymerase-alpha in budding yeast." Ricke R.M., Bielinsky A.-K. J. Biol. Chem. 281:18414-18425(2006) [PubMed: 16675460] [Abstract] Cited for: FUNCTION, INTERACTION WITH POL1; PRI2 AND POL12, MUTAGENESIS OF GLY-261 AND ASN-268.
[15]	"Interaction between PCNA and diubiquitinated Mcm10 is essential for cell growth in budding yeast." Das-Bradoo S., Ricke R.M., Bielinsky A.-K. Mol. Cell. Biol. 26:4806-4817(2006) [PubMed: 16782870] [Abstract] Cited for: INTERACTION WITH POL30, UBIQUITINATION, MUTAGENESIS OF TYR-245.
[16]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." 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. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453 AND SER-454, MASS SPECTROMETRY.
[17]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-17 AND SER-18, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z38059 Genomic DNA. Translation: CAA86128.1. M83540 Genomic DNA. Translation: AAA34574.1. BK006942 Genomic DNA. Translation: DAA08403.1.
PIR	S48384.
RefSeq	NP_012116.1. NM_001179498.1.
3D structure databases
ProteinModelPortal	P32354.
SMR	P32354. Positions 151-348.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1293N.
IntAct	P32354. 16 interactions.
MINT	MINT-397002.
STRING	P32354.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YIL150C; YIL150C; YIL150C.
GeneID	854656.
KEGG	sce:YIL150C.
NMPDR	fig\|4932.3.peg.1638.
Organism-specific databases
CYGD	YIL150c.
SGD	S000001412. MCM10.
Phylogenomic databases
eggNOG	fuNOG04350.
GeneTree	EFGT00050000004953.
HOGENOM	HBG203027.
OMA	NCILEIG.
OrthoDB	EOG4N07PV.
Gene expression databases
ArrayExpress	P32354.
Genevestigator	P32354.
GermOnline	YIL150C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. IPR015408. Znf_Mcm10/DnaG. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KO	K10736.
Pfam	PF09329. zf-primase. 1 hit. [Graphical view]
SUPFAM	SSF50249. Nucleic_acid_OB. 1 hit.
ProtoNet	Search...
Other
NextBio	977217.

Entry information

Entry name

MCM10_YEAST

Accession

Primary (citable) accession number: P32354
Secondary accession number(s): D6VVD7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	February 1, 1995
Last modified:	December 14, 2011
This is version 92 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome IX

Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents