Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P25206 (MCM3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA replication licensing factor MCM3

EC=3.6.4.12
Alternative name(s):
DNA polymerase alpha holoenzyme-associated protein P1
P1-MCM3
Gene names
Name:Mcm3
Synonyms:Mcmd, Mcmd3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length812 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Required for DNA replication and cell proliferation.

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Component of the MCM2-7 complex. The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5. Associated with the replication-specific DNA polymerase alpha. Interacts with MCMBP (By simililarity).

Subcellular location

Nucleus.

Post-translational modification

O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner By similarity.

Sequence similarities

Belongs to the MCM family.

Contains 1 MCM domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 812811DNA replication licensing factor MCM3
PRO_0000194094

Regions

Domain295 – 502208MCM
Nucleotide binding345 – 3528ATP Potential
Motif477 – 4804Arginine finger

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue1601Phosphoserine By similarity
Modified residue2931N6-acetyllysine Ref.6
Modified residue5471N6-acetyllysine Ref.6
Modified residue6681Phosphoserine Ref.4
Modified residue6721Phosphoserine Ref.4 Ref.5
Modified residue6811Phosphoserine By similarity
Modified residue7051Phosphotyrosine By similarity
Modified residue7081Phosphoserine By similarity
Modified residue7191Phosphothreonine By similarity
Modified residue7221Phosphothreonine By similarity

Experimental info

Sequence conflict18 – 225DYLDF → RLLGL in CAA44079. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P25206 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 3C8653CF13D0F140

FASTA81291,546
        10         20         30         40         50         60 
MAGTVVLDDV ELREAQRDYL DFLDDEEDQG IYQNKVRELI SDNQYRLIVS VNDLRRKNEK 

        70         80         90        100        110        120 
RANRLLNNAF EELVAFQRAL KDFVASIDAT YAKQYEEFYI GLEGSFGSKH VSPRTLTSCF 

       130        140        150        160        170        180 
LSCVVCVEGI VTKCSLVRPK VVRSVHYCPA TKKTIERRYS DLTTLVAFPS SSVYPTKDEE 

       190        200        210        220        230        240 
NNPLETEYGL SVYKDHQTIT IQEMPEKAPA GQLPRSVDVI LDDDLVDKVK PGDRIQVVGT 

       250        260        270        280        290        300 
YRCLPGKKGC YTSGTFRTVL IACNVKQMSK DIQPAFSADD IAKIKKFSKT RSKDVFEQLA 

       310        320        330        340        350        360 
RSLAPSIHGH DYVKKAILCL LLGGVERELE NGSHIRGDIN ILLIGDPSVA KSQLLRYVLC 

       370        380        390        400        410        420 
TAPRAIPTTG RGSSGVGLTA AVTTDQETGE RRLEAGAMVL ADRGVVCIDE FDKMSDMDRT 

       430        440        450        460        470        480 
AIHEVMEQGR VTIAKAGIHA RLNARCSVLA AANPVYGRYD QYKTPMENIG LQDSLLSRFD 

       490        500        510        520        530        540 
LLFIMLDQMD PEQDREISDH VLRMHQYRAP GEQDGDALPL GSSVDILATD DPDFTQDDQQ 

       550        560        570        580        590        600 
DTRIYEKHDS LLHGTKKKKE KMVSAAFMKK YIHVAKIIKP TLTQESAAYI AEEYSRLRSQ 

       610        620        630        640        650        660 
DSMSSDTART SPVTARTLET LIRLATAHAK ARMSKTVDLQ DAEEAVELVQ YAYFKKVLEK 

       670        680        690        700        710        720 
EKKRKKASED ESDLEDEEEK SQEDTEQKRK RRKTHAKDGE SYDPYDFSEA ETQMPQVHTP 

       730        740        750        760        770        780 
KTDDSQEKTD DSQETQDSQK VELSEPRLKA FKAALLEVFQ EAHEQSVGML HLTESINRNR 

       790        800        810 
EEPFSSEEIQ ACLSRMQDDN QVMVSEGIVF LI 

« Hide

References

« Hide 'large scale' references
[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N-3.
Tissue: Mammary gland.
[2]"Properties of the nuclear P1 protein, a mammalian homologue of the yeast Mcm3 replication protein."
Thoemmes P., Fett R., Schray B., Burkhart R., Barnes M., Kennedy C., Brown N.C., Knippers R.
Nucleic Acids Res. 20:1069-1074(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 18-812.
[3]"DNA polymerase alpha associated protein P1, a murine homolog of yeast MCM3, changes its intranuclear distribution during the DNA synthetic period."
Kimura H., Nozaki N., Sugimoto K.
EMBO J. 13:4311-4320(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
[4]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-668 AND SER-672, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[5]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[6]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-293 AND LYS-547, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC031700 mRNA. Translation: AAH31700.1.
X62154 mRNA. Translation: CAA44079.1.
D26088 Genomic DNA. Translation: BAA05081.1.
CCDSCCDS14843.1.
PIRS22804.
S51615.
RefSeqNP_032589.1. NM_008563.2.
UniGeneMm.4502.

3D structure databases

ProteinModelPortalP25206.
SMRP25206. Positions 10-650.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201345. 4 interactions.
DIPDIP-45878N.
IntActP25206. 1 interaction.
MINTMINT-4101604.

PTM databases

PhosphoSiteP25206.

Proteomic databases

MaxQBP25206.
PaxDbP25206.
PRIDEP25206.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000053266; ENSMUSP00000059192; ENSMUSG00000041859.
GeneID17215.
KEGGmmu:17215.
UCSCuc007alc.1. mouse.

Organism-specific databases

CTD4172.
MGIMGI:101845. Mcm3.

Phylogenomic databases

eggNOGCOG1241.
HOGENOMHOG000224126.
HOVERGENHBG104962.
InParanoidP25206.
KOK02541.
OMARMISEHV.
OrthoDBEOG7V1FQ3.
PhylomeDBP25206.
TreeFamTF106459.

Gene expression databases

ArrayExpressP25206.
BgeeP25206.
GenevestigatorP25206.

Family and domain databases

Gene3D2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR008046. Mcm3.
IPR018525. MCM_CS.
IPR001208. MCM_DNA-dep_ATPase.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSPR01657. MCMFAMILY.
PR01659. MCMPROTEIN3.
SMARTSM00382. AAA. 1 hit.
SM00350. MCM. 1 hit.
[Graphical view]
SUPFAMSSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMCM3. mouse.
NextBio291602.
PMAP-CutDBP25206.
PROP25206.
SOURCESearch...

Entry information

Entry nameMCM3_MOUSE
AccessionPrimary (citable) accession number: P25206
Secondary accession number(s): Q61492
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot