CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006357
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA replication licensing factor MCM5 
Protein Synonyms/Alias
 CDC46 homolog; P1-CDC46 
Gene Name
 MCM5 
Gene Synonyms/Alias
 CDC46 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
36SQLQRRFKEFLRQYRubiquitination[1]
54DRTGFTFKYRDELKRubiquitination[1]
141PSSIRSLKSDMMSHLubiquitination[1, 2]
150DMMSHLVKIPGIIIAubiquitination[1]
218PYFIMPDKCKCVDFQubiquitination[1]
220FIMPDKCKCVDFQTLubiquitination[1]
228CVDFQTLKLQELPDAubiquitination[1]
256CDRYLCDKVVPGNRVubiquitination[1]
273MGIYSIKKFGLTTSRubiquitination[1]
337NVYEVISKSIAPSIFubiquitination[1, 3]
351FGGTDMKKAIACLLFubiquitination[1]
363LLFGGSRKRLPDGLTubiquitination[1, 4]
387LGDPGTAKSQLLKFVubiquitination[1, 4]
392TAKSQLLKFVEKCSPacetylation[5]
392TAKSQLLKFVEKCSPubiquitination[1, 4]
396QLLKFVEKCSPIGVYacetylation[5]
396QLLKFVEKCSPIGVYubiquitination[1, 4]
407IGVYTSGKGSSAAGLubiquitination[1]
471QQTISIAKAGITTTLubiquitination[1, 2, 3, 6]
499FGRWDETKGEDNIDFubiquitination[1, 3, 6]
561IDLAKLKKFIAYCRVubiquitination[1]
581LSAEAAEKLKNRYIIubiquitination[1, 3]
583AEAAEKLKNRYIIMRubiquitination[1]
625RIAEALSKMKLQPFAubiquitination[1]
627AEALSKMKLQPFATEubiquitination[1, 3, 6]
696VSEHSIIKDFTKQKYacetylation[5]
696VSEHSIIKDFTKQKYubiquitination[1, 2]
702IKDFTKQKYPEHAIHubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [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] 
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 (By similarity). Interacts with MCMBP. 
Sequence Annotation
 DOMAIN 331 537 MCM.
 NP_BIND 381 388 ATP (Potential).
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 392 392 N6-acetyllysine.
 MOD_RES 396 396 N6-acetyllysine.
 MOD_RES 696 696 N6-acetyllysine.  
Keyword
 Acetylation; ATP-binding; Cell cycle; Complete proteome; DNA replication; DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 734 AA 
Protein Sequence
MSGFDDPGIF YSDSFGGDAQ ADEGQARKSQ LQRRFKEFLR QYRVGTDRTG FTFKYRDELK 60
RHYNLGEYWI EVEMEDLASF DEDLADYLYK QPAEHLQLLE EAAKEVADEV TRPRPSGEEV 120
LQDIQVMLKS DASPSSIRSL KSDMMSHLVK IPGIIIAASA VRAKATRISI QCRSCRNTLT 180
NIAMRPGLEG YALPRKCNTD QAGRPKCPLD PYFIMPDKCK CVDFQTLKLQ ELPDAVPHGE 240
MPRHMQLYCD RYLCDKVVPG NRVTIMGIYS IKKFGLTTSR GRDRVGVGIR SSYIRVLGIQ 300
VDTDGSGRSF AGAVSPQEEE EFRRLAALPN VYEVISKSIA PSIFGGTDMK KAIACLLFGG 360
SRKRLPDGLT RRGDINLLML GDPGTAKSQL LKFVEKCSPI GVYTSGKGSS AAGLTASVMR 420
DPSSRNFIME GGAMVLADGG VVCIDEFDKM REDDRVAIHE AMEQQTISIA KAGITTTLNS 480
RCSVLAAANS VFGRWDETKG EDNIDFMPTI LSRFDMIFIV KDEHNEERDV MLAKHVITLH 540
VSALTQTQAV EGEIDLAKLK KFIAYCRVKC GPRLSAEAAE KLKNRYIIMR SGARQHERDS 600
DRRSSIPITV RQLEAIVRIA EALSKMKLQP FATEADVEEA LRLFQVSTLD AALSGTLSGV 660
EGFTSQEDQE MLSRIEKQLK RRFAIGSQVS EHSIIKDFTK QKYPEHAIHK VLQLMLRRGE 720
IQHRMQRKVL YRLK 734 
Gene Ontology
 GO:0042555; C:MCM complex; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003678; F:DNA helicase activity; IEA:InterPro.
 GO:0032508; P:DNA duplex unwinding; IEA:GOC.
 GO:0006270; P:DNA replication initiation; IEA:InterPro.
 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
 IPR008048; MCM5.
 IPR018525; MCM_CS.
 IPR001208; MCM_DNA-dep_ATPase.
 IPR012340; NA-bd_OB-fold.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00493; MCM 
SMART
 SM00350; MCM 
PROSITE
 PS00847; MCM_1
 PS50051; MCM_2 
PRINTS
 PR01657; MCMFAMILY.
 PR01661; MCMPROTEIN5.