CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020032
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Zinc phosphodiesterase ELAC protein 2 
Protein Synonyms/Alias
 ElaC homolog protein 2; Heredity prostate cancer protein 2; Ribonuclease Z 2; RNase Z 2; tRNA 3 endonuclease 2; tRNase Z 2 
Gene Name
 ELAC2 
Gene Synonyms/Alias
 HPC2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
101LMQEHKLKVARLDNIubiquitination[1]
146SGPPQLEKYLEAIKIubiquitination[1]
152EKYLEAIKIFSGPLKubiquitination[1, 2, 3, 4]
258RGNFLVLKAKEMGLPubiquitination[1]
260NFLVLKAKEMGLPVGubiquitination[1, 5]
279APIIAAVKDGKSITHubiquitination[1, 5]
282IAAVKDGKSITHEGRubiquitination[1, 5]
332TFQRYQGKADAPVALubiquitination[1]
384VHNLRSHKIQTQLNLubiquitination[1]
407LTSFRCKKEGPTLSVubiquitination[1]
424VQGECLLKYQLRPRRubiquitination[1]
476DGPAPAEKRSQYPEIubiquitination[1, 5]
495TGSAIPMKIRNVSATubiquitination[1, 2, 4]
571RALASLGKPLHPLLVubiquitination[1, 2, 4]
608HISMIPAKCLQEGAEubiquitination[1]
678EALVRMGKDATLLIHubiquitination[1]
731HFSQRYAKVPLFSPNubiquitination[1, 2, 4]
742FSPNFSEKVGVAFDHubiquitination[1, 5]
751GVAFDHMKVCFGDFPubiquitination[1]
762GDFPTMPKLIPPLKAubiquitination[1]
768PKLIPPLKALFAGDIubiquitination[1]
811EDGEPQQKRAHTEEPubiquitination[1, 3, 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] 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] 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]
 [4] 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]
 [5] 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
Functional Description
 Zinc phosphodiesterase, which displays some tRNA 3'- processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA. 
Sequence Annotation
 MOD_RES 199 199 Phosphoserine.
 MOD_RES 208 208 Phosphoserine (By similarity).  
Keyword
 Alternative splicing; Complete proteome; Disease mutation; Endonuclease; Hydrolase; Metal-binding; Nuclease; Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene; Reference proteome; tRNA processing; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 826 AA 
Protein Sequence
MWALCSLLRS AAGRTMSQGR TISQAPARRE RPRKDPLRHL RTREKRGPSG CSGGPNTVYL 60
QVVAAGSRDS GAALYVFSEF NRYLFNCGEG VQRLMQEHKL KVARLDNIFL TRMHWSNVGG 120
LSGMILTLKE TGLPKCVLSG PPQLEKYLEA IKIFSGPLKG IELAVRPHSA PEYEDETMTV 180
YQIPIHSEQR RGKHQPWQSP ERPLSRLSPE RSSDSESNEN EPHLPHGVSQ RRGVRDSSLV 240
VAFICKLHLK RGNFLVLKAK EMGLPVGTAA IAPIIAAVKD GKSITHEGRE ILAEELCTPP 300
DPGAAFVVVE CPDESFIQPI CENATFQRYQ GKADAPVALV VHMAPASVLV DSRYQQWMER 360
FGPDTQHLVL NENCASVHNL RSHKIQTQLN LIHPDIFPLL TSFRCKKEGP TLSVPMVQGE 420
CLLKYQLRPR REWQRDAIIT CNPEEFIVEA LQLPNFQQSV QEYRRSAQDG PAPAEKRSQY 480
PEIIFLGTGS AIPMKIRNVS ATLVNISPDT SLLLDCGEGT FGQLCRHYGD QVDRVLGTLA 540
AVFVSHLHAD HHTGLPSILL QRERALASLG KPLHPLLVVA PNQLKAWLQQ YHNQCQEVLH 600
HISMIPAKCL QEGAEISSPA VERLISSLLR TCDLEEFQTC LVRHCKHAFG CALVHTSGWK 660
VVYSGDTMPC EALVRMGKDA TLLIHEATLE DGLEEEAVEK THSTTSQAIS VGMRMNAEFI 720
MLNHFSQRYA KVPLFSPNFS EKVGVAFDHM KVCFGDFPTM PKLIPPLKAL FAGDIEEMEE 780
RREKRELRQV RAALLSRELA GGLEDGEPQQ KRAHTEEPQA KKVRAQ 826 
Gene Ontology
 GO:0005739; C:mitochondrion; IEA:Compara.
 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:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
 GO:0008033; P:tRNA processing; IEA:UniProtKB-KW. 
Interpro
 IPR001279; Beta-lactamas-like. 
Pfam
  
SMART
 SM00849; Lactamase_B 
PROSITE
  
PRINTS