UniProt Accession

 MCM2_HUMAN; P49736; Q14577; Q15023; Q8N2V1; Q969W7; Q96AE1; Q9BRM7 

Genbank Protein ID

 X67334; D21063; AY675259; BC006165; BC007670; BC007938; BC014272; BC017258; BC017490; BC030131; D83987; BT009734 

Genbank Nucleotide ID

 CAA47749.1; BAA04642.1; AAT70723.1; AAH06165.3; AAH07670.2; AAH07938.2; AAH14272.2; AAH17258.2; AAH17490.2; AAH30131.2; BAA12177.1; AAP88736.1 

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; CCNL1; CDCL1; KIAA0030 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
178	IENLEDLKGHSVREW	ubiquitination	[1, 2]
200	LEIHHRFKNFLRTHV	ubiquitination	[2]
216	SHGHNVFKERISDMC	acetylation	[3]
216	SHGHNVFKERISDMC	ubiquitination	[2]
224	ERISDMCKENRESLV	ubiquitination	[2]
326	LPQLSMVKYNCNKCN	ubiquitination	[2]
384	RIQESPGKVAAGRLP	ubiquitination	[2]
447	LANHVAKKDNKVAVG	ubiquitination	[2]
450	HVAKKDNKVAVGELT	ubiquitination	[2]
462	ELTDEDVKMITSLSK	ubiquitination	[1, 2]
469	KMITSLSKDQQIGEK	ubiquitination	[1, 2, 4, 5]
476	KDQQIGEKIFASIAP	ubiquitination	[2, 4, 5]
492	IYGHEDIKRGLALAL	ubiquitination	[2, 4, 5]
505	ALFGGEPKNPGGKHK	ubiquitination	[2]
529	CGDPGTAKSQFLKYI	ubiquitination	[2]
538	QFLKYIEKVSSRAIF	ubiquitination	[2]
591	CLIDEFDKMNDQDRT	ubiquitination	[2, 6]
613	QQSISISKAGIVTSL	ubiquitination	[1, 2, 4]
721	PLPQEVLKKYIIYAK	ubiquitination	[2]
722	LPQEVLKKYIIYAKE	ubiquitination	[2]
728	KKYIIYAKERVHPKL	ubiquitination	[2]
734	AKERVHPKLNQMDQD	ubiquitination	[2]
742	LNQMDQDKVAKMYSD	ubiquitination	[2]
752	KMYSDLRKESMATGS	ubiquitination	[2]
863	DTIEVPEKDLVDKAR	ubiquitination	[2]
868	PEKDLVDKARQINIH	ubiquitination	[2]
896	NKFSHDLKRKMILQQ	acetylation	[3]

Reference

 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931] 

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 473 679 MCM.
 ZN_FING 329 355 C4-type (Potential).
 NP_BIND 523 530 ATP (Potential).
 REGION 2 257 Interaction with KAT7 (By similarity).
 MOTIF 655 658 Arginine finger.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 12 12 Phosphoserine (By similarity).
 MOD_RES 13 13 Phosphoserine.
 MOD_RES 25 25 Phosphothreonine (By similarity).
 MOD_RES 26 26 Phosphoserine.
 MOD_RES 27 27 Phosphoserine.
 MOD_RES 39 39 Phosphothreonine.
 MOD_RES 40 40 Phosphoserine; by CDC7.
 MOD_RES 41 41 Phosphoserine.
 MOD_RES 53 53 Phosphoserine; by CDC7.
 MOD_RES 59 59 Phosphothreonine.
 MOD_RES 108 108 Phosphoserine; by ATR.
 MOD_RES 139 139 Phosphoserine.
 MOD_RES 216 216 N6-acetyllysine.
 MOD_RES 381 381 Phosphoserine.  

Keyword

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

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 904 AA 

Protein Sequence

Gene Ontology

 GO:0000785; C:chromatin; IDA:UniProtKB.
 GO:0042555; C:MCM complex; IDA:UniProtKB.
 GO:0005664; C:nuclear origin of replication recognition complex; IEA:Compara.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; TAS:ProtInc.
 GO:0003678; F:DNA helicase activity; IEA:InterPro.
 GO:0003688; F:DNA replication origin binding; IEA:Compara.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006270; P:DNA replication initiation; IMP:UniProtKB.
 GO:0006271; P:DNA strand elongation involved in DNA replication; TAS:Reactome.
 GO:0006268; P:DNA unwinding involved in replication; IEA:Compara.
 GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
 GO:0006334; P:nucleosome assembly; IEA:Compara. 

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.