CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010409
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribonuclease P protein subunit p30 
Protein Synonyms/Alias
 RNaseP protein p30; RNase P subunit 2 
Gene Name
 RPP30 
Gene Synonyms/Alias
 RNASEP2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
16LRAGSDLKALRGLVEubiquitination[1, 2, 3]
45IVDFKEKKQEIEKPVubiquitination[2]
50EKKQEIEKPVAVSELubiquitination[2]
108DVVAVFPKTEKLFHIubiquitination[2]
138EKLPFYFKRPPINVAubiquitination[1, 2, 4]
161LVYSPAIKDSTMRRYubiquitination[2, 5, 6]
181LNLMQICKGKNVIISubiquitination[2]
183LMQICKGKNVIISSAubiquitination[2, 3, 5]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [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] 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]
 [6] 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
Functional Description
 Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. 
Sequence Annotation
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 251 251 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; Hydrolase; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; tRNA processing. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 268 AA 
Protein Sequence
MAVFADLDLR AGSDLKALRG LVETAAHLGY SVVAINHIVD FKEKKQEIEK PVAVSELFTT 60
LPIVQGKSRP IKILTRLTII VSDPSHCNVL RATSSRARLY DVVAVFPKTE KLFHIACTHL 120
DVDLVCITVT EKLPFYFKRP PINVAIDRGL AFELVYSPAI KDSTMRRYTI SSALNLMQIC 180
KGKNVIISSA AERPLEIRGP YDVANLGLLF GLSESDAKAA VSTNCRAALL HGETRKTAFG 240
IISTVKKPRP SEGDEDCLPA SKKAKCEG 268 
Gene Ontology
 GO:0005655; C:nucleolar ribonuclease P complex; TAS:ProtInc.
 GO:0004526; F:ribonuclease P activity; TAS:ProtInc.
 GO:0008033; P:tRNA processing; IEA:UniProtKB-KW. 
Interpro
 IPR016195; Pol/histidinol_Pase-like.
 IPR002738; RNase_P_p30. 
Pfam
 PF01876; RNase_P_p30 
SMART
  
PROSITE
  
PRINTS