Mcm3

Functionⁱ

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 activityⁱ

ATP + H₂O = ADP + phosphate.

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	345 – 352	ATPSequence analysis		8

GO - Molecular functionⁱ

ATP binding Source: UniProtKB-KW
DNA binding Source: UniProtKB-KW
helicase activity Source: UniProtKB-KW

Complete GO annotation...

GO - Biological processⁱ

cell cycle Source: UniProtKB-KW
DNA replication initiation Source: InterPro

Complete GO annotation...

Keywordsⁱ

Molecular function	DNA-binding, Helicase, Hydrolase
Biological process	Cell cycle, DNA replication
Ligand	ATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactomeⁱ	R-MMU-176187. Activation of ATR in response to replication stress. R-MMU-68867. Assembly of the pre-replicative complex. R-MMU-68949. Orc1 removal from chromatin. R-MMU-68962. Activation of the pre-replicative complex. R-MMU-69052. Switching of origins to a post-replicative state. R-MMU-69300. Removal of licensing factors from origins.

Reactomeⁱ

R-MMU-176187. Activation of ATR in response to replication stress.
R-MMU-68867. Assembly of the pre-replicative complex.
R-MMU-68949. Orc1 removal from chromatin.
R-MMU-68962. Activation of the pre-replicative complex.
R-MMU-69052. Switching of origins to a post-replicative state.
R-MMU-69300. Removal of licensing factors from origins.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: DNA replication licensing factor MCM3 (EC:3.6.4.12) Alternative name(s): DNA polymerase alpha holoenzyme-associated protein P1 P1-MCM3
Gene namesⁱ	Name:Mcm3 Synonyms:Mcmd, Mcmd3
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Chromosome 1

Organism-specific databases

MGIⁱ	MGI:101845. Mcm3.

Subcellular locationⁱ

Nucleus

GO - Cellular componentⁱ

centrosome Source: MGI
cytoplasm
Source: MGI
Inferred from direct assayⁱ
- 18590716
MCM complex Source: UniProtKB
membrane Source: MGI
nuclear chromosome, telomeric region Source: MGI
nucleoplasm Source: MGI
nucleus
Source: MGI
Inferred from direct assayⁱ
- 18590716
perinuclear region of cytoplasm Source: MGI

Complete GO annotation...

Keywords - Cellular componentⁱ

Nucleus

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		RemovedBy similarity
ChainⁱPRO_0000194094	2 – 812	DNA replication licensing factor MCM3Add BLAST		811

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	2	N-acetylalanineBy similarity	1
Modified residueⁱ	160	PhosphoserineCombined sources	1
Modified residueⁱ	293	N6-acetyllysineCombined sources	1
Modified residueⁱ	547	N6-acetyllysineCombined sources	1
Modified residueⁱ	611	PhosphoserineBy similarity	1
Modified residueⁱ	668	PhosphoserineCombined sources	1
Modified residueⁱ	672	PhosphoserineCombined sources	1
Modified residueⁱ	681	PhosphoserineBy similarity	1
Modified residueⁱ	705	PhosphotyrosineBy similarity	1
Modified residueⁱ	708	PhosphoserineCombined sources	1
Modified residueⁱ	719	PhosphothreonineCombined sources	1
Modified residueⁱ	722	PhosphothreonineBy similarity	1
Modified residueⁱ	729	PhosphothreonineCombined sources	1
Modified residueⁱ	732	PhosphoserineCombined sources	1
Modified residueⁱ	738	PhosphoserineCombined sources	1

Post-translational modificationⁱ

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

Keywords - PTMⁱ

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

EPDⁱ	P25206.
PaxDbⁱ	P25206.
PeptideAtlas More...PeptideAtlasⁱ	P25206.
PRIDEⁱ	P25206.

PTM databases

iPTMnetⁱ	P25206.
PhosphoSitePlusⁱ	P25206.
SwissPalmⁱ	P25206.

Miscellaneous databases

PMAP-CutDBⁱ	P25206.

PMAP-CutDBⁱ

P25206.

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSMUSG00000041859.
ExpressionAtlasⁱ	P25206. baseline and differential.
Genevisibleⁱ	P25206. MM.

Interactionⁱ

Subunit structureⁱ

Component of the MCM2-7 complex. The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5 (Probable). Associated with the replication-specific DNA polymerase alpha. Interacts with MCMBP. Interacts with ANKRD17.By similarityCurated

Protein-protein interaction databases

BioGridⁱ	201345. 29 interactors.
Database of interacting proteins More...DIPⁱ	DIP-45878N.
IntActⁱ	P25206. 27 interactors.
Molecular INTeraction database More...MINTⁱ	MINT-4101604.
STRINGⁱ	10090.ENSMUSP00000059192.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P25206.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	295 – 502	MCMAdd BLAST		208

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	477 – 480	Arginine finger		4

Sequence similaritiesⁱ

Belongs to the MCM family.Curated

Phylogenomic databases

eggNOGⁱ	KOG0479. Eukaryota. COG1241. LUCA.
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00550000075022.
HOGENOMⁱ	HOG000224126.
HOVERGENⁱ	HBG104962.
InParanoidⁱ	P25206.
KEGG Orthology (KO) More...KOⁱ	K02541.
OMAⁱ	NEKRANR.
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G02B0.
PhylomeDBⁱ	P25206.
TreeFamⁱ	TF106459.

Family and domain databases

InterProⁱ	View protein in InterPro IPR003593. AAA+_ATPase. IPR031327. MCM. IPR008046. Mcm3. IPR018525. MCM_CS. IPR001208. MCM_dom. IPR027925. MCM_N. IPR033762. MCM_OB. IPR012340. NA-bd_OB-fold. IPR027417. P-loop_NTPase.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00493. MCM. 1 hit. PF14551. MCM_N. 1 hit. PF17207. MCM_OB. 1 hit.
PRINTSⁱ	PR01657. MCMFAMILY. PR01659. MCMPROTEIN3.
SMARTⁱ	View protein in SMART SM00382. AAA. 1 hit. SM00350. MCM. 1 hit.
SUPFAMⁱ	SSF50249. SSF50249. 1 hit. SSF52540. SSF52540. 2 hits.
PROSITEⁱ	View protein in PROSITE PS00847. MCM_1. 1 hit. PS50051. MCM_2. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P25206-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MAGTVVLDDV ELREAQRDYL DFLDDEEDQG IYQNKVRELI SDNQYRLIVS 
        60         70         80         90        100
VNDLRRKNEK RANRLLNNAF EELVAFQRAL KDFVASIDAT YAKQYEEFYI 
       110        120        130        140        150
GLEGSFGSKH VSPRTLTSCF LSCVVCVEGI VTKCSLVRPK VVRSVHYCPA 
       160        170        180        190        200
TKKTIERRYS DLTTLVAFPS SSVYPTKDEE NNPLETEYGL SVYKDHQTIT 
       210        220        230        240        250
IQEMPEKAPA GQLPRSVDVI LDDDLVDKVK PGDRIQVVGT YRCLPGKKGC 
       260        270        280        290        300
YTSGTFRTVL IACNVKQMSK DIQPAFSADD IAKIKKFSKT RSKDVFEQLA 
       310        320        330        340        350
RSLAPSIHGH DYVKKAILCL LLGGVERELE NGSHIRGDIN ILLIGDPSVA 
       360        370        380        390        400
KSQLLRYVLC TAPRAIPTTG RGSSGVGLTA AVTTDQETGE RRLEAGAMVL 
       410        420        430        440        450
ADRGVVCIDE FDKMSDMDRT AIHEVMEQGR VTIAKAGIHA RLNARCSVLA 
       460        470        480        490        500
AANPVYGRYD QYKTPMENIG LQDSLLSRFD LLFIMLDQMD PEQDREISDH 
       510        520        530        540        550
VLRMHQYRAP GEQDGDALPL GSSVDILATD DPDFTQDDQQ DTRIYEKHDS 
       560        570        580        590        600
LLHGTKKKKE KMVSAAFMKK YIHVAKIIKP TLTQESAAYI AEEYSRLRSQ 
       610        620        630        640        650
DSMSSDTART SPVTARTLET LIRLATAHAK ARMSKTVDLQ DAEEAVELVQ 
       660        670        680        690        700
YAYFKKVLEK EKKRKKASED ESDLEDEEEK SQEDTEQKRK RRKTHAKDGE 
       710        720        730        740        750
SYDPYDFSEA ETQMPQVHTP KTDDSQEKTD DSQETQDSQK VELSEPRLKA 
       760        770        780        790        800
FKAALLEVFQ EAHEQSVGML HLTESINRNR EEPFSSEEIQ ACLSRMQDDN 
       810 
QVMVSEGIVF LI

Length:812

Mass (Da):91,546

Last modified:November 1, 1997 - v2

Checksum:ⁱ3C8653CF13D0F140

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	18 – 22	DYLDF → RLLGL in CAA44079 (PubMed:1549468).Curated		5

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	BC031700 mRNA. Translation: AAH31700.1. X62154 mRNA. Translation: CAA44079.1. D26088 Genomic DNA. Translation: BAA05081.1.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS14843.1.
PIRⁱ	S22804. S51615.
NCBI Reference Sequences More...RefSeqⁱ	NP_032589.1. NM_008563.2.
UniGeneⁱ	Mm.4502.

Genome annotation databases

Ensemblⁱ	ENSMUST00000053266; ENSMUSP00000059192; ENSMUSG00000041859.
GeneIDⁱ	17215.
KEGGⁱ	mmu:17215.
UCSC genome browser More...UCSCⁱ	uc007alc.1. mouse.

Similar proteinsⁱ

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:

100%	UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%	UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%	UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	BC031700 mRNA. Translation: AAH31700.1. X62154 mRNA. Translation: CAA44079.1. D26088 Genomic DNA. Translation: BAA05081.1.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS14843.1.
PIRⁱ	S22804. S51615.
NCBI Reference Sequences More...RefSeqⁱ	NP_032589.1. NM_008563.2.
UniGeneⁱ	Mm.4502.

3D structure databases

ProteinModelPortalⁱ	P25206.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	201345. 29 interactors.
Database of interacting proteins More...DIPⁱ	DIP-45878N.
IntActⁱ	P25206. 27 interactors.
Molecular INTeraction database More...MINTⁱ	MINT-4101604.
STRINGⁱ	10090.ENSMUSP00000059192.

PTM databases

iPTMnetⁱ	P25206.
PhosphoSitePlusⁱ	P25206.
SwissPalmⁱ	P25206.

Proteomic databases

EPDⁱ	P25206.
PaxDbⁱ	P25206.
PeptideAtlas More...PeptideAtlasⁱ	P25206.
PRIDEⁱ	P25206.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSMUST00000053266; ENSMUSP00000059192; ENSMUSG00000041859.
GeneIDⁱ	17215.
KEGGⁱ	mmu:17215.
UCSC genome browser More...UCSCⁱ	uc007alc.1. mouse.

Organism-specific databases

CTDⁱ	4172.
MGIⁱ	MGI:101845. Mcm3.

Phylogenomic databases

eggNOGⁱ	KOG0479. Eukaryota. COG1241. LUCA.
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00550000075022.
HOGENOMⁱ	HOG000224126.
HOVERGENⁱ	HBG104962.
InParanoidⁱ	P25206.
KEGG Orthology (KO) More...KOⁱ	K02541.
OMAⁱ	NEKRANR.
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G02B0.
PhylomeDBⁱ	P25206.
TreeFamⁱ	TF106459.

Enzyme and pathway databases

Reactomeⁱ	R-MMU-176187. Activation of ATR in response to replication stress. R-MMU-68867. Assembly of the pre-replicative complex. R-MMU-68949. Orc1 removal from chromatin. R-MMU-68962. Activation of the pre-replicative complex. R-MMU-69052. Switching of origins to a post-replicative state. R-MMU-69300. Removal of licensing factors from origins.

Reactomeⁱ

R-MMU-176187. Activation of ATR in response to replication stress.
R-MMU-68867. Assembly of the pre-replicative complex.
R-MMU-68949. Orc1 removal from chromatin.
R-MMU-68962. Activation of the pre-replicative complex.
R-MMU-69052. Switching of origins to a post-replicative state.
R-MMU-69300. Removal of licensing factors from origins.

Miscellaneous databases

ChiTaRSⁱ	Mcm3. mouse.
PMAP-CutDBⁱ	P25206.
Protein Ontology More...PROⁱ	PR:P25206.
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSMUSG00000041859.
ExpressionAtlasⁱ	P25206. baseline and differential.
Genevisibleⁱ	P25206. MM.

Family and domain databases

InterProⁱ	View protein in InterPro IPR003593. AAA+_ATPase. IPR031327. MCM. IPR008046. Mcm3. IPR018525. MCM_CS. IPR001208. MCM_dom. IPR027925. MCM_N. IPR033762. MCM_OB. IPR012340. NA-bd_OB-fold. IPR027417. P-loop_NTPase.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00493. MCM. 1 hit. PF14551. MCM_N. 1 hit. PF17207. MCM_OB. 1 hit.
PRINTSⁱ	PR01657. MCMFAMILY. PR01659. MCMPROTEIN3.
SMARTⁱ	View protein in SMART SM00382. AAA. 1 hit. SM00350. MCM. 1 hit.
SUPFAMⁱ	SSF50249. SSF50249. 1 hit. SSF52540. SSF52540. 2 hits.
PROSITEⁱ	View protein in PROSITE PS00847. MCM_1. 1 hit. PS50051. MCM_2. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	MCM3_MOUSE
Accessionⁱ	P25206Primary (citable) accession number: P25206 Secondary accession number(s): Q61492
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
	Last sequence update:	November 1, 1997
	Last modified:	July 5, 2017
	This is version 164 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

Documents

MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
SIMILARITY comments
Index of protein domains and families

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P25206 (MCM3_MOUSE)

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DNA replication licensing factor MCM3

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

Miscellaneous databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Motif

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ