CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012369
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribosomal RNA processing protein 1 homolog B 
Protein Synonyms/Alias
 RRP1-like protein B 
Gene Name
 RRP1B 
Gene Synonyms/Alias
 KIAA0179 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
182ELSKVGGKELLADQNubiquitination[1, 2]
191LLADQNLKFIDPFCKubiquitination[2]
198KFIDPFCKIAAKTKDubiquitination[2, 3]
204CKIAAKTKDHTLVQTubiquitination[2]
652FDTPFLPKPLFFRRAacetylation[4, 5]
652FDTPFLPKPLFFRRAubiquitination[6]
720VAFDPEQKPLHGVLKacetylation[3]
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] 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] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [5] 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]
 [6] 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
Functional Description
  
Sequence Annotation
 MOD_RES 245 245 Phosphoserine.
 MOD_RES 350 350 Phosphoserine.
 MOD_RES 392 392 Phosphoserine.
 MOD_RES 394 394 Phosphoserine.
 MOD_RES 395 395 Phosphoserine.
 MOD_RES 452 452 Phosphoserine.
 MOD_RES 458 458 Phosphoserine.
 MOD_RES 513 513 Phosphoserine.
 MOD_RES 652 652 N6-acetyllysine.
 MOD_RES 702 702 Phosphoserine.
 MOD_RES 706 706 Phosphoserine.
 MOD_RES 728 728 Phosphothreonine.
 MOD_RES 732 732 Phosphoserine.
 MOD_RES 735 735 Phosphoserine.
 MOD_RES 736 736 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Nucleus; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 758 AA 
Protein Sequence
MAPAMQPAEI QFAQRLASSE KGIRDRAVKK LRQYISVKTQ RETGGFSQEE LLKIWKGLFY 60
CMWVQDEPLL QEELANTIAQ LVHAVNNSAA QHLFIQTFWQ TMNREWKGID RLRLDKYYML 120
IRLVLRQSFE VLKRNGWEES RIKVFLDVLM KEVLCPESQS PNGVRFHFID IYLDELSKVG 180
GKELLADQNL KFIDPFCKIA AKTKDHTLVQ TIARGVFEAI VDQSPFVPEE TMEEQKTKVG 240
DGDLSAEEIP ENEVSLRRAV SKKKTALGKN HSRKDGLSDE RGRDDCGTFE DTGPLLQFDY 300
KAVADRLLEM TSRKNTPHFN RKRLSKLIKK FQDLSEGSSI SQLSFAEDIS ADEDDQILSQ 360
GKHKKKGNKL LEKTNLEKEK GSRVFCVEEE DSESSLQKRR RKKKKKHHLQ PENPGPGGAA 420
PSLEQNRGRE PEASGLKALK ARVAEPGAEA TSSTGEESGS EHPPAVPMHN KRKRPRKKSP 480
RAHREMLESA VLPPEDMSQS GPSGSHPQGP RGSPTGGAQL LKRKRKLGVV PVNGSGLSTP 540
AWPPLQQEGP PTGPAEGANS HTTLPQRRRL QKKKAGPGSL ELCGLPSQKT ASLKKRKKMR 600
VMSNLVEHNG VLESEAGQPQ ALGSSGTCSS LKKQKLRAES DFVKFDTPFL PKPLFFRRAK 660
SSTATHPPGP AVQLNKTPSS SKKVTFGLNR NMTAEFKKTD KSILVSPTGP SRVAFDPEQK 720
PLHGVLKTPT SSPASSPLVA KKPLTTTPRR RPRAMDFF 758 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0000791; C:euchromatin; IEA:Compara.
 GO:0000792; C:heterochromatin; IEA:Compara.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0030688; C:preribosome, small subunit precursor; IEA:InterPro.
 GO:0010923; P:negative regulation of phosphatase activity; IDA:UniProtKB.
 GO:0006364; P:rRNA processing; IEA:InterPro. 
Interpro
 IPR010301; Nop52. 
Pfam
 PF05997; Nop52 
SMART
  
PROSITE
  
PRINTS