CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012058
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Polyadenylate-binding protein 4 
Protein Synonyms/Alias
 PABP-4; Poly(A)-binding protein 4; Activated-platelet protein 1; APP-1; Inducible poly(A)-binding protein; iPABP 
Gene Name
 PABPC4 
Gene Synonyms/Alias
 APP1; PABP4 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
78TMNFDVIKGKPIRIMubiquitination[1, 2]
95QRDPSLRKSGVGNVFubiquitination[1]
104GVGNVFIKNLDKSIDacetylation[3]
104GVGNVFIKNLDKSIDubiquitination[1]
157AADKAIEKMNGMLLNubiquitination[2]
186REAELGAKAKEFTNVubiquitination[1]
188AELGAKAKEFTNVYIubiquitination[2]
196EFTNVYIKNFGEEVDubiquitination[1, 4]
208EVDDESLKELFSQFGubiquitination[1]
216ELFSQFGKTLSVKVMubiquitination[1, 2, 4]
254AVEEMNGKEISGKIIubiquitination[1]
279RQAELKRKFEQLKQEubiquitination[1]
284KRKFEQLKQERISRYubiquitination[1]
299QGVNLYIKNLDDTIDubiquitination[4]
309DDTIDDEKLRKEFSPubiquitination[1]
312IDDEKLRKEFSPFGSubiquitination[1, 2, 4]
333MLEDGRSKGFGFVCFubiquitination[2]
361NGRIVGSKPLYVALAmethylation[5]
361NGRIVGSKPLYVALAubiquitination[1, 2, 4]
375AQRKEERKAHLTNQYubiquitination[1, 2, 4]
635AKKEAAQKVGAVAAAubiquitination[1]
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] 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]
 [3] 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]
 [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] Update on activities at the Universal Protein Resource (UniProt) in 2013.
 e="String">UniProt Consortium.
 Nucleic Acids Res. 2013 Jan;41(Database issue):D43-7. [PMID: 23161681] 
Functional Description
 Binds the poly(A) tail of mRNA. May be involved in cytoplasmic regulatory processes of mRNA metabolism. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo (By similarity). 
Sequence Annotation
 DOMAIN 11 89 RRM 1.
 DOMAIN 99 175 RRM 2.
 DOMAIN 191 268 RRM 3.
 DOMAIN 294 370 RRM 4.
 DOMAIN 551 628 PABC.
 MOD_RES 140 140 Phosphotyrosine.
 MOD_RES 315 315 Phosphoserine.
 MOD_RES 361 361 N6,N6-dimethyllysine.
 MOD_RES 518 518 Dimethylated arginine; alternate.
 MOD_RES 518 518 Omega-N-methylated arginine; alternate.
 MOD_RES 531 531 Phosphoserine.  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Methylation; Phosphoprotein; Polymorphism; Reference proteome; Repeat; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 644 AA 
Protein Sequence
MNAAASSYPM ASLYVGDLHS DVTEAMLYEK FSPAGPVLSI RVCRDMITRR SLGYAYVNFQ 60
QPADAERALD TMNFDVIKGK PIRIMWSQRD PSLRKSGVGN VFIKNLDKSI DNKALYDTFS 120
AFGNILSCKV VCDENGSKGY AFVHFETQEA ADKAIEKMNG MLLNDRKVFV GRFKSRKERE 180
AELGAKAKEF TNVYIKNFGE EVDDESLKEL FSQFGKTLSV KVMRDPNGKS KGFGFVSYEK 240
HEDANKAVEE MNGKEISGKI IFVGRAQKKV ERQAELKRKF EQLKQERISR YQGVNLYIKN 300
LDDTIDDEKL RKEFSPFGSI TSAKVMLEDG RSKGFGFVCF SSPEEATKAV TEMNGRIVGS 360
KPLYVALAQR KEERKAHLTN QYMQRVAGMR ALPANAILNQ FQPAAGGYFV PAVPQAQGRP 420
PYYTPNQLAQ MRPNPRWQQG GRPQGFQGMP SAIRQSGPRP TLRHLAPTGS ECPDRLAMDF 480
GGAGAAQQGL TDSCQSGGVP TAVQNLAPRA AVAAAAPRAV APYKYASSVR SPHPAIQPLQ 540
APQPAVHVQG QEPLTASMLA AAPPQEQKQM LGERLFPLIQ TMHSNLAGKI TGMLLEIDNS 600
ELLHMLESPE SLRSKVDEAV AVLQAHHAKK EAAQKVGAVA AATS 644 
Gene Ontology
 GO:0010494; C:cytoplasmic stress granule; IDA:MGI.
 GO:0005634; C:nucleus; IDA:MGI.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0008143; F:poly(A) RNA binding; IDA:MGI.
 GO:0008266; F:poly(U) RNA binding; IDA:MGI.
 GO:0007596; P:blood coagulation; TAS:ProtInc.
 GO:0006401; P:RNA catabolic process; TAS:ProtInc.
 GO:0006396; P:RNA processing; TAS:ProtInc.
 GO:0006412; P:translation; TAS:ProtInc. 
Interpro
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR006515; PABP_1234.
 IPR002004; PABP_HYD.
 IPR000504; RRM_dom. 
Pfam
 PF00658; PABP
 PF00076; RRM_1 
SMART
 SM00517; PolyA
 SM00360; RRM 
PROSITE
 PS51309; PABC
 PS50102; RRM 
PRINTS