CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-038135
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Poly(A) polymerase alpha 
Protein Synonyms/Alias
  
Gene Name
 Papola 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
360LSKAEWSKLFEAPNFubiquitination[1]
635PSGNTATKVPNPIVGacetylation[2]
644PNPIVGVKRTSSPNKacetylation[2, 3, 4]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] 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]
 [4] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 693 AA 
Protein Sequence
MPFPVTTQGS QQTQPPQRHY GITSPISLAA PKETDCLLTQ KLIETLKPFG VFEEEEELQR 60
RILILGKLNN LVKEWIREIS ESKNLPQSVI ENVGGKIFTF GSYRLGVHTK GADIDALCVA 120
PRHVDRSDFF TSFYDKLKLQ EEVKDLRAVE EAFVPVIKLC FDGIEIDILF ARLALQTIPE 180
DLDLRDDSLL KNLDIRCIRS LNGCRVTDEI LHLVPNIDNF RLTLRAIKLW AKRHNIYSNI 240
LGFLGGVSWA MLVARTCQLY PNAIASTLVH KFFLVFSKWE WPNPVLLKQP EECNLNLPVW 300
DPRVNPSDRY HLMPIITPAY PQQNSTYNVS VSTRMVMVEE FKQGLAITDE ILLSKAEWSK 360
LFEAPNFFQK YKHYIVLLAS APTEKQRLEW VGLVESKIRI LVGSLEKNEF ITLAHVNPQS 420
FPAPKESPDR EEFRTMWVIG LVFKKTENSE NLSVDLTYDI QSFTDTVYRQ AINSKMFELD 480
MKIAAMHVKR KQLHQLLPSH VLQKRKKHST EGVKLTALND SSLDLSMDSD NSMSVPSPTS 540
AMKTSPLNSS GSSQGRNSPA PAVTAASVTS IQASEVSVPQ ANSSESPGGP SSESIPQTAT 600
QPAISPPPKP TVSRVVSSTR LVNPSPRPSG NTATKVPNPI VGVKRTSSPN KEESPKKTKT 660
EEKTSSTDLS DIPALPANPI PVIKNSIKLR LNR 693 
Gene Ontology
 GO:0005737; C:cytoplasm; IBA:RefGenome.
 GO:0005634; C:nucleus; IBA:RefGenome.
 GO:0004652; F:polynucleotide adenylyltransferase activity; IDA:MGI.
 GO:0003723; F:RNA binding; IEA:InterPro.
 GO:0006378; P:mRNA polyadenylation; IBA:RefGenome.
 GO:0000398; P:mRNA splicing, via spliceosome; IBA:RefGenome.
 GO:0006369; P:termination of RNA polymerase II transcription; IBA:RefGenome. 
Interpro
 IPR002934; Nucleotidyltransferase.
 IPR011068; NuclTrfase_I_C.
 IPR007012; PolA_pol_cen_dom.
 IPR007010; PolA_pol_RNA-bd_dom.
 IPR014492; PolyA_polymerase. 
Pfam
 PF01909; NTP_transf_2
 PF04928; PAP_central
 PF04926; PAP_RNA-bind 
SMART
  
PROSITE
  
PRINTS