CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011673
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nuclear cap-binding protein subunit 1 
Protein Synonyms/Alias
 80 kDa nuclear cap-binding protein; CBP80; NCBP 80 kDa subunit 
Gene Name
 NCBP1 
Gene Synonyms/Alias
 CBP80; NCBP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
117RQLKESLKANNYNEAubiquitination[1, 2]
204ANTESYLKRRQKTHVacetylation[3]
204ANTESYLKRRQKTHVubiquitination[1, 4, 5, 6]
323ENLHCIIKSHWKERKubiquitination[5]
455FVREVLEKCMRLSYHubiquitination[5, 7]
583LAESDEGKLHVLRVMubiquitination[7]
698QIERLQEKVESAQSEacetylation[3, 8]
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] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [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] 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]
 [6] 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]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [8] 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] 
Functional Description
 Component of the cap-binding complex (CBC), which binds cotranscriptionally to the 5'-cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing, translation regulation, nonsense-mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC complex is involved in mRNA export from the nucleus via its interaction with ALYREF/THOC4/ALY, leading to the recruitment of the mRNA export machinery to the 5'-end of mRNA and to mRNA export in a 5' to 3' direction through the nuclear pore. The CBC complex is also involved in mediating U snRNA and intronless mRNAs export from the nucleus. The CBC complex is essential for a pioneer round of mRNA translation, before steady state translation when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. The pioneer round of mRNA translation mediated by the CBC complex plays a central role in nonsense-mediated mRNA decay (NMD), NMD only taking place in mRNAs bound to the CBC complex, but not on eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs containing at least one exon-junction complex (EJC) via its interaction with UPF1, promoting the interaction between UPF1 and UPF2. The CBC complex is also involved in 'failsafe' NMD, which is independent of the EJC complex, while it does not participate in Staufen-mediated mRNA decay (SMD). During cell proliferation, the CBC complex is also involved in microRNAs (miRNAs) biogenesis via its interaction with SRRT/ARS2 and is required for miRNA-mediated RNA interference. The CBC complex also acts as a negative regulator of PARN, thereby acting as an inhibitor of mRNA deadenylation. In the CBC complex, NCBP1/CBP80 does not bind directly capped RNAs (m7GpppG-capped RNA) but is required to stabilize the movement of the N-terminal loop of NCBP2/CBP20 and lock the CBC into a high affinity cap-binding state with the cap structure. 
Sequence Annotation
 DOMAIN 28 240 MIF4G.
 MOTIF 3 20 Nuclear localization signal (Potential).
 MOD_RES 7 7 Phosphoserine; by RPS6KB1.
 MOD_RES 21 21 Phosphothreonine; by RPS6KB1.
 MOD_RES 22 22 Phosphoserine; by RPS6KB1.
 MOD_RES 204 204 N6-acetyllysine.
 MOD_RES 698 698 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Coiled coil; Complete proteome; Cytoplasm; Direct protein sequencing; mRNA capping; mRNA processing; mRNA splicing; mRNA transport; Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein; Reference proteome; RNA-mediated gene silencing; Translation regulation; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 790 AA 
Protein Sequence
MSRRRHSDEN DGGQPHKRRK TSDANETEDH LESLICKVGE KSACSLESNL EGLAGVLEAD 60
LPNYKSKILR LLCTVARLLP EKLTIYTTLV GLLNARNYNF GGEFVEAMIR QLKESLKANN 120
YNEAVYLVRF LSDLVNCHVI AAPSMVAMFE NFVSVTQEED VPQVRRDWYV YAFLSSLPWV 180
GKELYEKKDA EMDRIFANTE SYLKRRQKTH VPMLQVWTAD KPHPQEEYLD CLWAQIQKLK 240
KDRWQERHIL RPYLAFDSIL CEALQHNLPP FTPPPHTEDS VYPMPRVIFR MFDYTDDPEG 300
PVMPGSHSVE RFVIEENLHC IIKSHWKERK TCAAQLVSYP GKNKIPLNYH IVEVIFAELF 360
QLPAPPHIDV MYTTLLIELC KLQPGSLPQV LAQATEMLYM RLDTMNTTCV DRFINWFSHH 420
LSNFQFRWSW EDWSDCLSQD PESPKPKFVR EVLEKCMRLS YHQRILDIVP PTFSALCPAN 480
PTCIYKYGDE SSNSLPGHSV ALCLAVAFKS KATNDEIFSI LKDVPNPNQD DDDDEGFSFN 540
PLKIEVFVQT LLHLAAKSFS HSFSALAKFH EVFKTLAESD EGKLHVLRVM FEVWRNHPQM 600
IAVLVDKMIR TQIVDCAAVA NWIFSSELSR DFTRLFVWEI LHSTIRKMNK HVLKIQKELE 660
EAKEKLARQH KRRSDDDDRS SDRKDGVLEE QIERLQEKVE SAQSEQKNLF LVIFQRFIMI 720
LTEHLVRCET DGTSVLTPWY KNCIERLQQI FLQHHQIIQQ YMVTLENLLF TAELDPHILA 780
VFQQFCALQA 790 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005845; C:mRNA cap binding complex; IDA:UniProtKB.
 GO:0005846; C:nuclear cap binding complex; IEA:InterPro.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0000339; F:RNA cap binding; TAS:ProtInc.
 GO:0006370; P:7-methylguanosine mRNA capping; IDA:UniProtKB.
 GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
 GO:0008334; P:histone mRNA metabolic process; TAS:Reactome.
 GO:0031124; P:mRNA 3'-end processing; TAS:Reactome.
 GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:InterPro.
 GO:0006379; P:mRNA cleavage; IDA:UniProtKB.
 GO:0006406; P:mRNA export from nucleus; IMP:UniProtKB.
 GO:0034660; P:ncRNA metabolic process; TAS:Reactome.
 GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:UniProtKB.
 GO:0031442; P:positive regulation of mRNA 3'-end processing; IDA:UniProtKB.
 GO:0050434; P:positive regulation of viral transcription; TAS:Reactome.
 GO:0006446; P:regulation of translational initiation; IDA:UniProtKB.
 GO:0000387; P:spliceosomal snRNP assembly; TAS:Reactome.
 GO:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome.
 GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
 GO:0022415; P:viral reproductive process; TAS:Reactome. 
Interpro
 IPR016024; ARM-type_fold.
 IPR027159; CBP80.
 IPR016021; MIF4-like_typ_1/2/3.
 IPR015172; MIF4G-like_typ-1.
 IPR015174; MIF4G-like_typ-2.
 IPR003890; MIF4G-like_typ-3. 
Pfam
 PF02854; MIF4G
 PF09088; MIF4G_like
 PF09090; MIF4G_like_2 
SMART
 SM00543; MIF4G 
PROSITE
  
PRINTS