UniProt Accession

 MCM3_HUMAN; P25205; Q92660; Q9BTR3; Q9NUE7 

Genbank Protein ID

 X62153; D38073; AY621074; AL034343; BC001626; BC003509 

Genbank Nucleotide ID

 CAA44078.2; BAA07267.1; AAT27321.1; CAB75298.1; AAH01626.1; AAH03509.2 

Protein Name

 DNA replication licensing factor MCM3 

Protein Synonyms/Alias

 DNA polymerase alpha holoenzyme-associated protein P1; P1-MCM3; RLF subunit beta; p102 

Gene Name

 MCM3 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
35	DQGIYQSKVRELISD	ubiquitination	[1, 2, 3]
81	VAFQRALKDFVASID	ubiquitination	[2]
140	KCSLVRPKVVRSVHY	ubiquitination	[2]
177	SSSVYPTKDEENNPL	ubiquitination	[1]
207	TIQEMPEKAPAGQLP	ubiquitination	[1]
228	LDDDLVDKAKPGDRV	ubiquitination	[2]
230	DDLVDKAKPGDRVQV	ubiquitination	[2]
248	YRCLPGKKGGYTSGT	ubiquitination	[2]
266	VLIACNVKQMSKDAQ	ubiquitination	[2, 4]
270	CNVKQMSKDAQPSFS	ubiquitination	[2]
293	KFSKTRSKDIFDQLA	ubiquitination	[2, 4]
301	DIFDQLAKSLAPSIH	ubiquitination	[4]
315	HGHDYVKKAILCLLL	ubiquitination	[2]
351	IGDPSVAKSQLLRYV	ubiquitination	[1, 4, 5, 6]
413	VCIDEFDKMSDMDRT	ubiquitination	[2]
435	QGRVTIAKAGIHARL	ubiquitination	[2, 3, 4, 6]
463	YGRYDQYKTPMENIG	ubiquitination	[1, 2, 3]
569	MVSAAFMKKYIHVAK	acetylation	[7]
570	VSAAFMKKYIHVAKI	ubiquitination	[2]
579	IHVAKIIKPVLTQES	ubiquitination	[4]
732	TADSQETKESQKVEL	ubiquitination	[1, 2]
736	QETKESQKVELSESR	ubiquitination	[2]
748	ESRLKAFKVALLDVF	ubiquitination	[4]

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] 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]
 [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] 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]
 [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]
 [7] 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] 

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 DNA replication and cell proliferation. 

Sequence Annotation

 DOMAIN 295 502 MCM.
 NP_BIND 345 352 ATP (Potential).
 MOTIF 477 480 Arginine finger.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 160 160 Phosphoserine.
 MOD_RES 535 535 Phosphoserine; by ATM.
 MOD_RES 668 668 Phosphoserine.
 MOD_RES 672 672 Phosphoserine.
 MOD_RES 674 674 Phosphothreonine.
 MOD_RES 681 681 Phosphoserine.
 MOD_RES 708 708 Phosphotyrosine.
 MOD_RES 711 711 Phosphoserine.
 MOD_RES 713 713 Phosphothreonine.
 MOD_RES 722 722 Phosphothreonine.
 MOD_RES 725 725 Phosphothreonine.  

Keyword

 Acetylation; 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

 808 AA 

Protein Sequence

Gene Ontology

 GO:0005658; C:alpha DNA polymerase:primase complex; TAS:ProtInc.
 GO:0005813; C:centrosome; IDA:HPA.
 GO:0042555; C:MCM complex; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; TAS:ProtInc.
 GO:0003678; F:DNA helicase activity; IEA:InterPro.
 GO:0032508; P:DNA duplex unwinding; IEA:GOC.
 GO:0006270; P:DNA replication initiation; TAS:ProtInc.
 GO:0006271; P:DNA strand elongation involved in DNA replication; TAS:Reactome.
 GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome. 

Interpro

 IPR003593; AAA+_ATPase.
 IPR008046; Mcm3.
 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.
 PR01659; MCMPROTEIN3.