CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016189
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Polyadenylate-binding protein 2 
Protein Synonyms/Alias
 PABP-2; Poly(A)-binding protein 2; Nuclear poly(A)-binding protein 1; Poly(A)-binding protein II; PABII; Polyadenylate-binding nuclear protein 1 
Gene Name
 PABPN1 
Gene Synonyms/Alias
 PAB2; PABP2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
123DPELEAIKARVREMEubiquitination[1, 2, 3]
137EEEAEKLKELQNEVEubiquitination[1, 3, 4, 5]
145ELQNEVEKQMNMSPPubiquitination[1]
207RVTILCDKFSGHPKGubiquitination[3]
223AYIEFSDKESVRTSLubiquitination[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] 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]
 [3] 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]
 [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] 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] 
Functional Description
 Involved in the 3'-end formation of mRNA precursors (pre-mRNA) by the addition of a poly(A) tail of 200-250 nt to the upstream cleavage product. Stimulates poly(A) polymerase (PAPOLA) conferring processivity on the poly(A) tail elongation reaction and controls also the poly(A) tail length. Increases the affinity of poly(A) polymerase for RNA. Is also present at various stages of mRNA metabolism including nucleocytoplasmic trafficking and nonsense-mediated decay (NMD) of mRNA. Cooperates with SKIP to synergistically activate E-box-mediated transcription through MYOD1 and may regulate the expression of muscle-specific genes. Binds to poly(A) and to poly(G) with high affinity. May protect the poly(A) tail from degradation (By similarity). 
Sequence Annotation
 DOMAIN 172 249 RRM.
 REGION 2 145 Interacts with SKIP.
 REGION 119 147 Stimulates PAPOLA (By similarity).
 REGION 155 306 Necessary for homooligomerization.
 REGION 286 306 Interacts with PAPOLA (By similarity).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 19 19 Phosphoserine.
 MOD_RES 95 95 Phosphoserine.
 MOD_RES 150 150 Phosphoserine.
 MOD_RES 238 238 Asymmetric dimethylarginine; alternate
 MOD_RES 238 238 Omega-N-methylarginine; alternate (By
 MOD_RES 259 259 Asymmetric dimethylarginine (By
 MOD_RES 263 263 Asymmetric dimethylarginine (By
 MOD_RES 265 265 Asymmetric dimethylarginine (By
 MOD_RES 267 267 Asymmetric dimethylarginine (By
 MOD_RES 269 269 Asymmetric dimethylarginine (By
 MOD_RES 277 277 Asymmetric dimethylarginine (By
 MOD_RES 279 279 Asymmetric dimethylarginine (By
 MOD_RES 287 287 Asymmetric dimethylarginine (By
 MOD_RES 289 289 Asymmetric dimethylarginine (By
 MOD_RES 291 291 Asymmetric dimethylarginine (By
 MOD_RES 294 294 Asymmetric dimethylarginine (By
 MOD_RES 296 296 Asymmetric dimethylarginine (By
 MOD_RES 298 298 Asymmetric dimethylarginine (By  
Keyword
 3D-structure; Acetylation; Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; Direct protein sequencing; Disease mutation; Methylation; mRNA processing; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; RNA-binding; Triplet repeat expansion. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 306 AA 
Protein Sequence
MAAAAAAAAA AGAAGGRGSG PGRRRHLVPG AGGEAGEGAP GGAGDYGNGL ESEELEPEEL 60
LLEPEPEPEP EEEPPRPRAP PGAPGPGPGS GAPGSQEEEE EPGLVEGDPG DGAIEDPELE 120
AIKARVREME EEAEKLKELQ NEVEKQMNMS PPPGNAGPVI MSIEEKMEAD ARSIYVGNVD 180
YGATAEELEA HFHGCGSVNR VTILCDKFSG HPKGFAYIEF SDKESVRTSL ALDESLFRGR 240
QIKVIPKRTN RPGISTTDRG FPRARYRART TNYNSSRSRF YSGFNSRPRG RVYRGRARAT 300
SWYSPY 306 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; TAS:ProtInc.
 GO:0046778; P:modification by virus of host mRNA processing; TAS:Reactome.
 GO:0031124; P:mRNA 3'-end processing; TAS:Reactome.
 GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
 GO:0006936; P:muscle contraction; TAS:ProtInc.
 GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:UniProtKB.
 GO:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome.
 GO:0019058; P:viral infectious cycle; TAS:Reactome. 
Interpro
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 
Pfam
 PF00076; RRM_1 
SMART
 SM00360; RRM 
PROSITE
 PS50102; RRM 
PRINTS