CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020104
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein pelota homolog 
Protein Synonyms/Alias
  
Gene Name
 PELO 
Gene Synonyms/Alias
 CGI-17 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
46LRASTIRKVQTESSTubiquitination[1, 2, 3]
84QACQLRVKGTNIQENubiquitination[1, 3, 4, 5, 6]
95IQENEYVKMGAYHTIubiquitination[1, 5]
115RQFTLAKKQWDSVVLubiquitination[3]
162SMTLTRAKVEVNIPRubiquitination[3, 5, 6]
203HIHFDVVKCILVASPubiquitination[1, 3]
231QAVKTDNKLLLENRSubiquitination[1, 3]
254SGHKYSLKEALCDPTubiquitination[3, 4, 6, 7, 8]
270ASRLSDTKAAGEVKAubiquitination[1, 3, 4, 6, 7]
276TKAAGEVKALDDFYKubiquitination[1, 3, 5]
283KALDDFYKMLQHEPDubiquitination[1, 3, 6]
297DRAFYGLKQVEKANEubiquitination[1, 3, 4, 5]
301YGLKQVEKANEAMAIubiquitination[3]
337VRLVDSVKENAGTVRubiquitination[1, 3, 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] 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]
 [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] 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] 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]
 [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] 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] 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
Functional Description
 Required for normal chromosome segregation during cell division and genomic stability (By similarity). May function in recognizing stalled ribosomes and triggering endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and degrade damaged mRNAs. May have ribonuclease activity (Potential). 
Sequence Annotation
 MOD_RES 374 374 Phosphoserine.
 MOD_RES 380 380 Phosphoserine.
 MOD_RES 381 381 Phosphoserine.
 MOD_RES 382 382 Phosphoserine.  
Keyword
 3D-structure; Cell cycle; Cell division; Complete proteome; Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 385 AA 
Protein Sequence
MKLVRKNIEK DNAGQVTLVP EEPEDMWHTY NLVQVGDSLR ASTIRKVQTE SSTGSVGSNR 60
VRTTLTLCVE AIDFDSQACQ LRVKGTNIQE NEYVKMGAYH TIELEPNRQF TLAKKQWDSV 120
VLERIEQACD PAWSADVAAV VMQEGLAHIC LVTPSMTLTR AKVEVNIPRK RKGNCSQHDR 180
ALERFYEQVV QAIQRHIHFD VVKCILVASP GFVREQFCDY LFQQAVKTDN KLLLENRSKF 240
LQVHASSGHK YSLKEALCDP TVASRLSDTK AAGEVKALDD FYKMLQHEPD RAFYGLKQVE 300
KANEAMAIDT LLISDELFRH QDVATRSRYV RLVDSVKENA GTVRIFSSLH VSGEQLSQLT 360
GVAAILRFPV PELSDQEGDS SSEED 385 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0008283; P:cell proliferation; IEA:Compara.
 GO:0051276; P:chromosome organization; IEA:Compara.
 GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC. 
Interpro
 IPR005140; eRF1_1_Pelota.
 IPR005141; eRF1_2.
 IPR005142; eRF1_3.
 IPR004405; Transl_rel_pelota-like. 
Pfam
 PF03463; eRF1_1
 PF03464; eRF1_2
 PF03465; eRF1_3 
SMART
  
PROSITE
  
PRINTS