UniProt Accession

 MCM7_HUMAN; P33993; A4D2A1; A4D2A2; E9PGN9; Q15076; Q96D34; Q96GL1 

Genbank Protein ID

 D55716; AK055379; AC073842; CH236956; CH236956; CH471091; CH471091; BC009398; BC013375; X74796; D28480 

Genbank Nucleotide ID

 BAA09534.1; BAG51508.1; EAL23855.1; EAL23856.1; EAW76598.1; EAW76599.1; AAH09398.1; AAH13375.1; CAA52803.1; BAA05839.1 

Protein Name

 DNA replication licensing factor MCM7 

Protein Synonyms/Alias

 CDC47 homolog; P1.1-MCM3 

Gene Name

 MCM7 

Gene Synonyms/Alias

 CDC47; MCM2 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
4	****MALKDYALEKE	ubiquitination	[1, 2, 3]
10	LKDYALEKEKVKKFL	ubiquitination	[1, 2, 3, 4, 5, 6]
12	DYALEKEKVKKFLQE	ubiquitination	[2]
15	LEKEKVKKFLQEFYQ	ubiquitination	[2, 3, 4, 6, 7, 8]
28	YQDDELGKKQFKYGN	acetylation	[3, 9]
28	YQDDELGKKQFKYGN	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8]
29	QDDELGKKQFKYGNQ	ubiquitination	[1, 2, 3, 4, 6, 7, 8, 10]
32	ELGKKQFKYGNQLVR	ubiquitination	[1, 2]
75	ENARRYAKLFADAVQ	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8, 11]
89	QELLPQYKEREVVNK	ubiquitination	[1, 2, 3, 4, 5, 6, 12]
96	KEREVVNKDVLDVYI	ubiquitination	[1, 2, 3]
145	FQGPSSNKPRVIREV	ubiquitination	[1, 2, 4, 6, 7, 8, 11, 13]
159	VRADSVGKLVTVRGI	ubiquitination	[1, 2, 4, 6]
231	TRGSRFIKFQEMKMQ	ubiquitination	[1, 2, 4, 7, 8, 12]
236	FIKFQEMKMQEHSDQ	ubiquitination	[1, 2, 4, 6]
305	LEAHRIVKMNKSEDD	ubiquitination	[2, 4, 5]
308	HRIVKMNKSEDDESG	ubiquitination	[1, 2, 3, 4, 5, 6]
335	AEEDFYEKLAASIAP	ubiquitination	[2, 4, 5]
351	IYGHEDVKKALLLLL	ubiquitination	[1, 4, 5, 6]
352	YGHEDVKKALLLLLV	ubiquitination	[2, 3]
387	MGDPGVAKSQLLSYI	ubiquitination	[2, 4, 5, 12, 13]
449	CCIDEFDKMAEADRT	methylation	[14]
471	QQTISIAKAGILTTL	ubiquitination	[2, 3, 4, 5, 6, 13]
557	QFEPLDMKLMRRYIA	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8, 12]
569	YIAMCREKQPMVPES	ubiquitination	[2, 3, 4, 6]
596	RREAWASKDATYTSA	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8]
627	RMVDVVEKEDVNEAI	ubiquitination	[1, 2, 3, 4, 5, 6]
641	IRLMEMSKDSLLGDK	ubiquitination	[1, 2, 3, 4, 5, 6]
648	KDSLLGDKGQTARTQ	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8, 13]

Reference

 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [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] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] 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]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [11] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [12] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [13] 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]
 [14] A general molecular affinity strategy for global detection and proteomic analysis of lysine methylation.
 Moore KE, Carlson SM, Camp ND, Cheung P, James RG, Chua KF, Wolf-Yadlin A, Gozani O.
 Mol Cell. 2013 May 9;50(3):444-56. [PMID: 23583077] 

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 S-phase checkpoint activation upon UV-induced damage. 

Sequence Annotation

 DOMAIN 332 538 MCM.
 NP_BIND 381 388 ATP (Potential).
 REGION 521 564 Interaction with RAD17.
 REGION 577 719 Interaction with ATRIP.
 MOTIF 513 516 Arginine finger.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 121 121 Phosphoserine.
 MOD_RES 365 365 Phosphoserine.
 MOD_RES 500 500 Phosphoserine.  

Keyword

 Acetylation; Alternative splicing; ATP-binding; Cell cycle; Complete proteome; Direct protein sequencing; DNA replication; DNA-binding; Glycoprotein; Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 719 AA 

Protein Sequence

Gene Ontology

 GO:0000785; C:chromatin; TAS:ProtInc.
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0042555; C:MCM complex; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003678; F:DNA helicase activity; IEA:Compara.
 GO:0003697; F:single-stranded DNA binding; IEA:Compara.
 GO:0008283; P:cell proliferation; IEA:Compara.
 GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Compara.
 GO:0006270; P:DNA replication initiation; IEA:InterPro.
 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:0042325; P:regulation of phosphorylation; IMP:UniProtKB.
 GO:0006974; P:response to DNA damage stimulus; IMP:UniProtKB.
 GO:0042493; P:response to drug; IEA:Compara. 

Interpro

 IPR003593; AAA+_ATPase.
 IPR008050; MCM7.
 IPR018525; MCM_CS.
 IPR001208; MCM_DNA-dep_ATPase.
 IPR012340; NA-bd_OB-fold.
 IPR027417; P-loop_NTPase. 

Pfam

 PF00493; MCM 

SMART

 SM00382; AAA
 SM00350; MCM 

PROSITE

 PS00847; MCM_1
 PS50051; MCM_2 

PRINTS

 PR01657; MCMFAMILY.
 PR01663; MCMPROTEIN7.