CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020523
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cleavage and polyadenylation specificity factor subunit 5 
Protein Synonyms/Alias
 Nucleoside diphosphate-linked moiety X motif 21; Nudix motif 21 
Gene Name
 Nudt21 
Gene Synonyms/Alias
 Cpsf5 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
23GVNQFGNKYIQQTKPacetylation[1, 2, 3, 4, 5]
23GVNQFGNKYIQQTKPubiquitination[6]
29NKYIQQTKPLTLERTubiquitination[6]
56TKEPLYEKDSSVAARubiquitination[6]
167YIPAHITKPKEHKKLacetylation[2]
189KALFAVPKNYKLVAAubiquitination[6]
Reference
 [1] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [4] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
 [5] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [6] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional Description
 Component of the cleavage factor Im (CFIm) complex that plays a key role in pre-mRNA 3'-processing. Involved in association with CPSF6 or CPSF7 in pre-MRNA 3'-end poly(A) site cleavage and poly(A) addition. NUDT21/CPSF5 binds to cleavage and polyadenylation RNA substrates. The homodimer mediates simultaneous sequence-specific recognition of two 5'-UGUA-3' elements within the pre-mRNA. Binds to, but does not hydrolyze mono- and di-adenosine nucleotides. May have a role in mRNA export (By similarity). 
Sequence Annotation
 DOMAIN 76 201 Nudix hydrolase.
 REGION 2 147 Necessary for RNA-binding (By
 REGION 81 160 Necessary for interactions with PAPOLA
 REGION 102 104 Interaction with RNA (By similarity).
 MOTIF 109 130 Nudix box.
 MOD_RES 2 2 N-acetylserine (By similarity).
 MOD_RES 23 23 N6-acetyllysine (By similarity).
 MOD_RES 29 29 N6-acetyllysine (By similarity).
 MOD_RES 40 40 Phosphotyrosine (By similarity).
 MOD_RES 56 56 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Complete proteome; mRNA processing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 227 AA 
Protein Sequence
MSVVPPNRSQ TGWPRGVNQF GNKYIQQTKP LTLERTINLY PLTNYTFGTK EPLYEKDSSV 60
AARFQRMREE FDKIGMRRTV EGVLIVHEHR LPHVLLLQLG TTFFKLPGGE LNPGEDEVEG 120
LKRLMTEILG RQDGVLQDWV IDDCIGNWWR PNFEPPQYPY IPAHITKPKE HKKLFLVQLQ 180
EKALFAVPKN YKLVAAPLFE LYDNAPGYGP IISSLPQLLS RFNFIYN 227 
Gene Ontology
 GO:0005813; C:centrosome; IEA:Compara.
 GO:0005849; C:mRNA cleavage factor complex; ISS:UniProtKB.
 GO:0042382; C:paraspeckles; ISS:UniProtKB.
 GO:0017091; F:AU-rich element binding; ISS:UniProtKB.
 GO:0016787; F:hydrolase activity; IEA:InterPro.
 GO:0003729; F:mRNA binding; ISS:UniProtKB.
 GO:0006378; P:mRNA polyadenylation; ISS:UniProtKB.
 GO:0051262; P:protein tetramerization; IEA:Compara. 
Interpro
 IPR016706; Cleav_polyA_spec_factor_su5.
 IPR000086; NUDIX_hydrolase_dom.
 IPR015797; NUDIX_hydrolase_dom-like. 
Pfam
 PF13869; NUDIX_2 
SMART
  
PROSITE
 PS51462; NUDIX
 PS00893; NUDIX_BOX 
PRINTS