CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008348
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Poly(A) polymerase alpha 
Protein Synonyms/Alias
 PAP-alpha; Polynucleotide adenylyltransferase alpha 
Gene Name
 PAPOLA 
Gene Synonyms/Alias
 PAP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
67RRILILGKLNNLVKEubiquitination[1]
83IREISESKNLPQSVIubiquitination[1]
110YRLGVHTKGADIDALubiquitination[1]
136FFTSFYDKLKLQEEVubiquitination[2, 3]
138TSFYDKLKLQEEVKDubiquitination[1]
144LKLQEEVKDLRAVEEubiquitination[1, 3]
191LRDDSLLKNLDIRCIubiquitination[3]
360LSKAEWSKLFEAPNFubiquitination[1, 2]
370EAPNFFQKYKHYIVLubiquitination[1]
372PNFFQKYKHYIVLLAubiquitination[1]
641TSGNAATKIPTPIVGacetylation[4]
650PTPIVGVKRTSSPHKacetylation[4]
736ANPIPVIKNSIKLRLacetylation[4]
740PVIKNSIKLRLNR**acetylation[4]
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] 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]
 [4] Multiple histone deacetylases and the CREB-binding protein regulate pre-mRNA 3'-end processing.
 Shimazu T, Horinouchi S, Yoshida M.
 J Biol Chem. 2007 Feb 16;282(7):4470-8. [PMID: 17172643] 
Functional Description
 Polymerase that creates the 3'-poly(A) tail of mRNA's. Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CPSF) at its C-terminus. 
Sequence Annotation
 NP_BIND 100 102 ATP (By similarity).
 NP_BIND 113 115 ATP (By similarity).
 NP_BIND 246 247 ATP (By similarity).
 REGION 508 643 Ser/Thr-rich.
 REGION 677 745 Required for interaction with NUDT21.
 MOTIF 490 507 Nuclear localization signal 1 (By
 MOTIF 650 665 Nuclear localization signal 2 (By
 METAL 113 113 Magnesium 1; catalytic (By similarity).
 METAL 113 113 Magnesium 2; catalytic (By similarity).
 METAL 115 115 Magnesium 1; catalytic (By similarity).
 METAL 115 115 Magnesium 2; catalytic (By similarity).
 METAL 167 167 Magnesium 2; catalytic (By similarity).
 BINDING 109 109 ATP (By similarity).
 BINDING 167 167 ATP (By similarity).
 BINDING 228 228 ATP (By similarity).
 BINDING 237 237 ATP (By similarity).
 MOD_RES 24 24 Phosphoserine.
 MOD_RES 537 537 Phosphoserine (By similarity).
 MOD_RES 641 641 N6-acetyllysine (By similarity).
 MOD_RES 650 650 N6-acetyllysine (By similarity).
 MOD_RES 736 736 N6-acetyllysine; alternate (By
 MOD_RES 740 740 N6-acetyllysine; alternate (By
 CROSSLNK 444 444 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 445 445 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 506 506 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 507 507 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 736 736 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 740 740 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Acetylation; Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; Isopeptide bond; Magnesium; Manganese; Metal-binding; mRNA processing; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Transferase; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 745 AA 
Protein Sequence
MPFPVTTQGS QQTQPPQKHY GITSPISLAA PKETDCVLTQ 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
FPAPKENPDK EEFRTMWVIG LVFKKTENSE NLSVDLTYDI QSFTDTVYRQ AINSKMFEVD 480
MKIAAMHVKR KQLHQLLPNH VLQKKKKHST EGVKLTALND SSLDLSMDSD NSMSVPSPTS 540
ATKTSPLNSS GSSQGRNSPA PAVTAASVTN IQATEVSVPQ VNSSESSGGT SSESIPQTAT 600
QPAISPPPKP TVSRVVSSTR LVNPPPRSSG NAATSGNAAT KIPTPIVGVK RTSSPHKEES 660
PKKTKTEEDE TSEDANCLAL SGHDKTEAKE QLDTETSTTQ SETIQTAASL LASQKTSSTD 720
LSDIPALPAN PIPVIKNSIK LRLNR 745 
Gene Ontology
 GO:0005737; C:cytoplasm; TAS:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005524; F:ATP binding; ISS:UniProtKB.
 GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
 GO:0030145; F:manganese ion binding; ISS:UniProtKB.
 GO:0004652; F:polynucleotide adenylyltransferase activity; ISS:UniProtKB.
 GO:0003723; F:RNA binding; NAS:UniProtKB.
 GO:0006378; P:mRNA polyadenylation; NAS:UniProtKB.
 GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
 GO:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome. 
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