CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-030563
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Double-strand break repair protein MRE11A 
Protein Synonyms/Alias
 cDNA FLJ38069 fis, clone CTONG2015434, highly similar to DOUBLE-STRAND BREAK REPAIR PROTEIN MRE11A 
Gene Name
 MRE11A 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
73HENKPSRKTLHTCLEubiquitination[1]
164GRSMSVEKIDISPVLubiquitination[1]
174ISPVLLQKGSTKIALubiquitination[1, 2]
258ECKIAPTKNEQQLFYubiquitination[3]
363GNSHQPEKPLVRLRVubiquitination[1]
387SVLRFSQKFVDRVANubiquitination[1, 2, 4, 5]
396VDRVANPKDIIHFFRubiquitination[1, 2, 4, 5, 6]
410RHREQKEKTGEEINFubiquitination[1]
419GEEINFGKLITKPSEacetylation[2, 7]
419GEEINFGKLITKPSEubiquitination[1, 4, 5]
423NFGKLITKPSEGTTLubiquitination[1, 2]
437LRVEDLVKQYFQTAEubiquitination[1, 4, 5]
445QYFQTAEKNVQLSLLubiquitination[1, 4, 5, 6]
478DAIEELVKYQLEKTQubiquitination[4, 5]
483LVKYQLEKTQRFLKEubiquitination[1]
676WSSTSSSKIMSQSQVubiquitination[4, 5]
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] 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]
 [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] 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]
 [6] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [7] 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
 Complete proteome; DNA damage; DNA repair; Endonuclease; Exonuclease; Hydrolase; Manganese; Meiosis; Nuclease; Nucleus; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 711 AA 
Protein Sequence
MNRNISHQKG DDENTFKILV ATDIHLGFME KDAVRGNDTF VTLDEILRLA QENEVDFILL 60
GGDLFHENKP SRKTLHTCLE LLRKYCMGDR PVQFEILSDQ SVNFGFSKFP WVNYQDGNLN 120
ISIPVFSIHG NHDDPTGADA LCALDILSCA GFVNHFGRSM SVEKIDISPV LLQKGSTKIA 180
LYGLGSIPDE RLYRMFVNKK VTMLRPKEDE NSWFNLFVIH QNRSKHGSTN FIPEQFLDDF 240
IDLVIWGHEH ECKIAPTKNE QQLFYISQPG SSVVTSLSPG EAVKKHVGLL RIKGRKMNMH 300
KIPLHTVRQF FMEDIVLANH PDIFNPDNPK VTQAIQSFCL EKIEEMLENA ERERLGNSHQ 360
PEKPLVRLRV DYSGGFEPFS VLRFSQKFVD RVANPKDIIH FFRHREQKEK TGEEINFGKL 420
ITKPSEGTTL RVEDLVKQYF QTAEKNVQLS LLTERGMGEA VQEFVDKEEK DAIEELVKYQ 480
LEKTQRFLKE RHIDALEDKI DEEVRRFRET RQKNTNEEDD EVREAMTRAR ALRSQSEESA 540
SAFSADDLMS IDLAEQMAND SDDSISAATN KGRGRGRGRR GGRGQNSASR GGSQRGRADT 600
GLETSTRSRN SKTAVSASRN MSIIDAFKST RQQPSRNVTT KNYSEVIEVD ESDVEEDIFP 660
TTSKTDQRWS STSSSKIMSQ SQVSKGVDFE SSEDDDDDPF MNTSSLRRNR R 711 
Gene Ontology
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
 GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
 GO:0030145; F:manganese ion binding; IEA:InterPro.
 GO:0006302; P:double-strand break repair; IEA:InterPro.
 GO:0007126; P:meiosis; IEA:UniProtKB-KW.
 GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC. 
Interpro
 IPR003701; DNA_repair_Mre11.
 IPR004843; Metallo_PEstase_dom.
 IPR007281; Mre11_DNA-bd. 
Pfam
 PF00149; Metallophos
 PF04152; Mre11_DNA_bind 
SMART
  
PROSITE
  
PRINTS