CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-029757
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA replication licensing factor MCM5 
Protein Synonyms/Alias
 MCM5 minichromosome maintenance deficient 5, cell division cycle 46 (S. cerevisiae), isoform CRA_c 
Gene Name
 MCM5 
Gene Synonyms/Alias
 hCG_41525 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
54DRTGFTFKYRDELKRubiquitination[1]
175PYFIMPDKCKCVDFQubiquitination[1, 2]
177FIMPDKCKCVDFQTLacetylation[2]
177FIMPDKCKCVDFQTLubiquitination[1, 2]
185CVDFQTLKLQELPDAubiquitination[1, 2]
213CDRYLCDKVVPGNRVubiquitination[1, 2]
230MGIYSIKKFGLTTSRubiquitination[1]
294NVYEVISKSIAPSIFubiquitination[1, 3]
308FGGTDMKKAIACLLFubiquitination[1, 2]
320LLFGGSRKRLPDGLTubiquitination[1, 2, 4]
344LGDPGTAKSQLLKFVubiquitination[1, 2, 4]
349TAKSQLLKFVEKCSPacetylation[2, 5]
349TAKSQLLKFVEKCSPubiquitination[1, 2, 4]
353QLLKFVEKCSPIGVYacetylation[2]
353QLLKFVEKCSPIGVYubiquitination[1, 2, 4]
364IGVYTSGKGSSAAGLubiquitination[1]
428QQTISIAKAGITTTLubiquitination[1, 2, 3, 6, 7, 8]
456FGRWDETKGEDNIDFubiquitination[1, 2, 3, 8]
518IDLAKLKKFIAYCRVubiquitination[1]
538LSAEAAEKLKNRYIIacetylation[2]
538LSAEAAEKLKNRYIIubiquitination[1, 2]
540AEAAEKLKNRYIIMRubiquitination[1]
582RIAEALSKMKLQPFAubiquitination[1]
584AEALSKMKLQPFATEubiquitination[1, 2, 3, 8]
653VSEHSIIKDFTKQKYacetylation[2, 9]
653VSEHSIIKDFTKQKYubiquitination[1, 2, 6]
659IKDFTKQKYPEHAIHubiquitination[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] 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]
 [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] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [6] 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]
 [7] 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]
 [8] 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]
 [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] 
Functional Description
  
Sequence Annotation
  
Keyword
 ATP-binding; Cell cycle; Cell division; Complete proteome; DNA replication; DNA-binding; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 691 AA 
Protein Sequence
MSGFDDPGIF YSDSFGGDAQ ADEGQARKSQ LQRRFKEFLR QYRVGTDRTG FTFKYRDELK 60
RHYNLGEYWI EVEMEDLASF DEDLADYLYK QPAEHLQLSD MMSHLVKIPG IIIAASAVRA 120
KATRISIQCR SCRNTLTNIA MRPGLEGYAL PRKCNTDQAG RPKCPLDPYF IMPDKCKCVD 180
FQTLKLQELP DAVPHGEMPR HMQLYCDRYL CDKVVPGNRV TIMGIYSIKK FGLTTSRGRD 240
RVGVGIRSSY IRVLGIQVDT DGSGRSFAGA VSPQEEEEFR RLAALPNVYE VISKSIAPSI 300
FGGTDMKKAI ACLLFGGSRK RLPDGLTRRG DINLLMLGDP GTAKSQLLKF VEKCSPIGVY 360
TSGKGSSAAG LTASVMRDPS SRNFIMEGGA MVLADGGVVC IDEFDKMRED DRVAIHEAME 420
QQTISIAKAG ITTTLNSRCS VLAAANSVFG RWDETKGEDN IDFMPTILSR FDMIFIVKDE 480
HNEERDVMLA KHVITLHVSA LTQTQAVEGE IDLAKLKKFI AYCRVKCGPR LSAEAAEKLK 540
NRYIIMRSGA RQHERDSDRR SSIPITVRQL EAIVRIAEAL SKMKLQPFAT EADVEEALRL 600
FQVSTLDAAL SGTLSGVEGF TSQEDQEMLS RIEKQLKRRF AIGSQVSEHS IIKDFTKQKY 660
PEHAIHKVLQ LMLRRGEIQH RMQRKVLYRL K 691 
Gene Ontology
 GO:0042555; C:MCM complex; IEA:InterPro.
 GO:0005634; C:nucleus; IEA:InterPro.
 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:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0032508; P:DNA duplex unwinding; IEA:GOC.
 GO:0006270; P:DNA replication initiation; IEA:InterPro. 
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.