CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-042518
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 DNA replication licensing factor MCM2 
Protein Synonyms/Alias
  
Gene Name
 MCM2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
41IENLEDLKGHSVREWubiquitination[1, 2, 3]
63LEIHHRFKNFLRTHVubiquitination[3]
79SHGHNVFKERISDMCacetylation[4, 5, 6]
79SHGHNVFKERISDMCubiquitination[3]
87ERISDMCKENRESLVubiquitination[3]
189LPQLSMVKYNCNKCNubiquitination[3]
247RIQESPGKVAAGRLPubiquitination[3, 6]
310LANHVAKKDNKVAVGubiquitination[3]
313HVAKKDNKVAVGELTubiquitination[3]
325ELTDEDVKMITSLSKubiquitination[1, 3, 6]
332KMITSLSKDQQIGEKubiquitination[3, 6, 7, 8]
339KDQQIGEKESSRNASmethylation[9]
424IYGHEDIKRGLALALubiquitination[3, 6, 7]
437ALFGGEPKNPGGKHKubiquitination[3]
461CGDPGTAKSQFLKYIubiquitination[3]
470QFLKYIEKVSSRAIFubiquitination[3]
523CLIDEFDKMNDQDRTubiquitination[2, 3, 6, 10]
545QQSISISKAGIVTSLubiquitination[1, 2, 3, 6, 7]
653PLPQEVLKKYIIYAKubiquitination[3]
654LPQEVLKKYIIYAKEubiquitination[3, 6]
660KKYIIYAKERVHPKLubiquitination[3]
666AKERVHPKLNQMDQDubiquitination[3]
674LNQMDQDKVAKMYSDubiquitination[3]
684KMYSDLRKESMATGSubiquitination[3, 6]
795DTIEVPEKDLVDKARacetylation[5]
795DTIEVPEKDLVDKARubiquitination[3]
800PEKDLVDKARQINIHubiquitination[3]
828NKFSHDLKRKMILQQubiquitination[6]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [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] 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]
 [9] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510]
 [10] 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
  
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; DNA replication; DNA-binding; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 836 AA 
Protein Sequence
XSDEEDEERP ARKRRQVERA TEDGEEDEEM IESIENLEDL KGHSVREWVS MAGPRLEIHH 60
RFKNFLRTHV DSHGHNVFKE RISDMCKENR ESLVVNYEDL AAREHVLAYF LPEAPAELLQ 120
IFDEAALEVV LAMYPKYDRI TNHIHVRISH LPLVEELRSL RQLHLNQLIR TSGVVTSCTG 180
VLPQLSMVKY NCNKCNFVLG PFCQSQNQEV KPGSCPECQS AGPFEVNMEE TIYQNYQRIR 240
IQESPGKVAA GRLPRSKDAI LLADLVDSCK PGDEIELTGI YHNNYDGSLN TANGFPVFAT 300
VILANHVAKK DNKVAVGELT DEDVKMITSL SKDQQIGEKE SSRNASLAEA GIGAIPSQLL 360
AIEPSLRRSG VPIGEVGVSQ RQEARSFSSA NTHWFLEDLL GPSCRDTMIF ASIAPSIYGH 420
EDIKRGLALA LFGGEPKNPG GKHKVRGDIN VLLCGDPGTA KSQFLKYIEK VSSRAIFTTG 480
QGASAVGLTA YVQRHPVSRE WTLEAGALVL ADRGVCLIDE FDKMNDQDRT SIHEAMEQQS 540
ISISKAGIVT SLQARCTVIA AANPIGGRYD PSLTFSENVD LTEPIISRFD ILCVVRDTVD 600
PVQDEMLARF VVGSHVRHHP SNKEEEGLAN GSAAEPAMPN TYGVEPLPQE VLKKYIIYAK 660
ERVHPKLNQM DQDKVAKMYS DLRKESMATG SIPITVRHIE SMIRMAEAHA RIHLRDYVIE 720
DDVNMAIRVM LESFIDTQKF SVMRSMRKTF ARYLSFRRDN NELLLFILKQ LVAEQVTYQR 780
NRFGAQQDTI EVPEKDLVDK ARQINIHNLS AFYDSELFRM NKFSHDLKRK MILQQF 836 
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:0032508; P:DNA duplex unwinding; IEA:GOC.
 GO:0006270; P:DNA replication initiation; IEA:InterPro. 
Interpro
 IPR008045; MCM2.
 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.
 PR01658; MCMPROTEIN2.