CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019698
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nuclear polyadenylated RNA-binding protein 4 
Protein Synonyms/Alias
 Cleavage factor IB; CFIB 
Gene Name
 HRP1 
Gene Synonyms/Alias
 NAB4; NAB5; YOL123W 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
192VTDLKIMKDPATGRSubiquitination[1]
209FGFLSFEKPSSVDEVubiquitination[1]
218SSVDEVVKTQHILDGacetylation[2]
226TQHILDGKVIDPKRAacetylation[2]
304VDRVCQNKFIDFKDRacetylation[2]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [2] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919] 
Functional Description
 RNA-binding protein, which is involved in the polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with the cleavage factor CFIA complex and the cleavage and polyadenylation factor (CPF) complex. May be involved in regulation of poly(A) site selection. Is involved in nonsense- mediated mRNA decay. Seems to bind to a RNA downstream sequence element (DSE) located 3' of a nonsense codon and may mark the transcript for decay. 
Sequence Annotation
 DOMAIN 159 241 RRM 1.
 DOMAIN 243 320 RRM 2.
 MOD_RES 2 2 Phosphoserine.
 MOD_RES 3 3 Phosphoserine.
 MOD_RES 206 206 Phosphoserine.
 MOD_RES 458 458 Phosphothreonine.
 MOD_RES 462 462 Phosphoserine.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; mRNA processing; Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 534 AA 
Protein Sequence
MSSDEEDFND IYGDDKPTTT EEVKKEEEQN KAGSGTSQLD QLAALQALSS SLNKLNNPNS 60
NNSSSNNSNQ DTSSSKQDGT ANDKEGSNED TKNEKKQESA TSANANANAS SAGPSGLPWE 120
QLQQTMSQFQ QPSSQSPPQQ QVTQTKEERS KADLSKESCK MFIGGLNWDT TEDNLREYFG 180
KYGTVTDLKI MKDPATGRSR GFGFLSFEKP SSVDEVVKTQ HILDGKVIDP KRAIPRDEQD 240
KTGKIFVGGI GPDVRPKEFE EFFSQWGTII DAQLMLDKDT GQSRGFGFVT YDSADAVDRV 300
CQNKFIDFKD RKIEIKRAEP RHMQQKSSNN GGNNGGNNMN RRGGNFGNQG DFNQMYQNPM 360
MGGYNPMMNP QAMTDYYQKM QEYYQQMQKQ TGMDYTQMYQ QQMQQMAMMM PGFAMPPNAM 420
TLNQPQQDSN ATQGSPAPSD SDNNKSNDVQ TIGNTSNTDS GSPPLNLPNG PKGPSQYNDD 480
HNSGYGYNRD RGDRDRNDRD RDYNHRSGGN HRRNGRGGRG GYNRRNNGYH PYNR 534 
Gene Ontology
 GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
 GO:0005849; C:mRNA cleavage factor complex; IPI:SGD.
 GO:0003729; F:mRNA binding; IDA:SGD.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0006379; P:mRNA cleavage; IDA:SGD.
 GO:0006378; P:mRNA polyadenylation; IDA:SGD.
 GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW. 
Interpro
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 
Pfam
 PF00076; RRM_1 
SMART
 SM00360; RRM 
PROSITE
 PS50102; RRM 
PRINTS