CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012059
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]
186REAELGAKAKEFTNVubiquitination[1]
216ELFSQFGKTLSVKVMubiquitination[1]
284KRKFEQLKQERISRYubiquitination[1]
375AQRKEERKAHLTNQYubiquitination[1]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661
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 TLRHLAPTGN APASRGLPTT 480
TQRVGVPTAV QNLAPRAAVA AAAPRAVAPY KYASSVRSPH PAIQPLQAPQ PAVHVQGQEP 540
LTASMLAAAP PQEQKQMLGE RLFPLIQTMH SNLAGKITGM LLEIDNSELL HMLESPESLR 600
SKVDEAVAVL QAHHAKKEAA QKVGAVAAAT S 631 
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