UniProt Accession

 MCM2_MOUSE; P97310; O08971; O89057; Q8C2R0 

Genbank Protein ID

 D86725; AF004105; AK129039; AK088156; BC055318; U89403 

Genbank Nucleotide ID

 BAA22148.1; AAC16250.1; BAC97849.1; BAC40178.1; AAH55318.1; AAC36510.1 

Protein Name

 DNA replication licensing factor MCM2 

Protein Synonyms/Alias

 Minichromosome maintenance protein 2 homolog; Nuclear protein BM28 

Gene Name

 Mcm2 

Gene Synonyms/Alias

 Bm28; Cdcl1; Kiaa0030; Mcmd2 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
462	ELTDEDVKMITGLSK	acetylation	[1]
534	TAKSQFLKYIEKVSS	acetylation	[2]
538	QFLKYIEKVSSRAIF	acetylation	[2]
591	CLIDEFDKMNDQDRT	acetylation	[2]

Reference

 [1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441] 

Functional Description

 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 the entry in S phase and for cell division. 

Sequence Annotation

 DOMAIN 473 680 MCM.
 ZN_FING 329 355 C4-type (Potential).
 NP_BIND 523 530 ATP (Potential).
 REGION 2 257 Interaction with KAT7.
 MOTIF 655 658 Arginine finger.
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 12 12 Phosphoserine.
 MOD_RES 21 21 Phosphoserine.
 MOD_RES 25 25 Phosphothreonine.
 MOD_RES 26 26 Phosphoserine.
 MOD_RES 27 27 Phosphoserine.
 MOD_RES 39 39 Phosphothreonine (By similarity).
 MOD_RES 40 40 Phosphoserine; by CDC7 (By similarity).
 MOD_RES 41 41 Phosphoserine.
 MOD_RES 53 53 Phosphoserine; by CDC7 (By similarity).
 MOD_RES 59 59 Phosphothreonine (By similarity).
 MOD_RES 108 108 Phosphoserine (By similarity).
 MOD_RES 139 139 Phosphoserine.
 MOD_RES 140 140 Phosphoserine.
 MOD_RES 216 216 N6-acetyllysine (By similarity).
 MOD_RES 381 381 Phosphoserine (By similarity).  

Keyword

 Acetylation; ATP-binding; Cell cycle; Complete proteome; Direct protein sequencing; DNA replication; DNA-binding; Helicase; Hydrolase; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Zinc; Zinc-finger. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 904 AA 

Protein Sequence

Gene Ontology

 GO:0000785; C:chromatin; IEA:Compara.
 GO:0042555; C:MCM complex; ISS:UniProtKB.
 GO:0005664; C:nuclear origin of replication recognition complex; IDA:MGI.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003678; F:DNA helicase activity; IEA:InterPro.
 GO:0003688; F:DNA replication origin binding; IDA:MGI.
 GO:0042393; F:histone binding; IDA:MGI.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0071353; P:cellular response to interleukin-4; IDA:MGI.
 GO:0006270; P:DNA replication initiation; TAS:MGI.
 GO:0006268; P:DNA unwinding involved in replication; IDA:MGI.
 GO:0006334; P:nucleosome assembly; IDA:MGI. 

Interpro

 IPR008045; MCM2.
 IPR018525; MCM_CS.
 IPR001208; MCM_DNA-dep_ATPase.
 IPR012340; NA-bd_OB-fold.
 IPR027417; P-loop_NTPase. 

Pfam

 PF00493; MCM
 PF12619; MCM2_N 

SMART

 SM00350; MCM 

PROSITE

 PS00847; MCM_1
 PS50051; MCM_2 

PRINTS

 PR01657; MCMFAMILY.
 PR01658; MCMPROTEIN2.