Welcome! Click here to login or here to register.
Catalytic RNA molecules
Enzymatic complexes
Draw a picture

Bujnicki Lab Homepage

Nuclear cap-binding protein subunit 1

Known also as: 80 kDa nuclear cap-binding protein

Known abbreviations: NCBP1, CBP80, NCBP


Component of the cap-binding complex (CBC), which binds co-transcriptionally 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. 
Component of the nuclear cap-binding complex (CBC), a heterodimer composed of NCBP1/CBP80 and NCBP2/CBP20 that interacts with m7GpppG-capped RNA. Found in a U snRNA export complex with RNUXA/PHAX, NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-capped RNA. Interaction with RNUXA/PHAX By similarity. Heterodimer with NCBP2. Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Is part of the exon junction complex (EJC) containing NCBP1, NCBP2, RNPS1, RBM8A, SRRM1, NXF1, UPF3B, UPF2, ALYREF/THOC4 and/or REFBP2. Interacts with SRRT/ARS2, EIF4G2, IGF2BP1, HNRNPF, HNRNPH1, KIAA0427/CTIF, PARN, DROSHA, UPF1 and ALYREF/THOC4. May interact with EIF4G1; (the interaction is however controversial) 
Nucleus. Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.

This protein can be a part of a given complexes: Activities in which Nuclear cap-binding protein subunit 1 is involved: Pathways in which Nuclear cap-binding protein subunit 1 is involved:

NCBI GI number(s): 4505343
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot Q09161 Q09161
KEGG hsa:4686 hsa:4686
PFAM: PF02854
InterPro: IPR016024
CATH: - -
SCOP: - -
Solved crystal structures: 3FEY
[PDB] [details]
[PDB] [details]
[PDB] [details]
[PDB] [details]
[PDB] [details]
[PDB] [details]
[PDB] [details]
[PDB] [details]

Protein sequence:

Nuclear cap-binding protein subunit 1 (Homo sapiens) is product of expression of NCBP1 gene.


Title Authors Journal Publication date (Issue) PubMed ID
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, K Genome Res 2004-10-01 (14) 15489334
Complete sequencing and characterization of 21,243 full-length human cDNAs. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K Nat Genet 2004-02-01 (36) 14702039
NMD resulting from encephalomyocarditis virus IRES-directed translation initiation seems to be restricted to CBP80/20-bound mRNA. Woeller CF, Gaspari M, Isken O, Maquat LE EMBO Rep 2008-05-01 (9) 18369367
Structural basis of m7GpppG binding to the nuclear cap-binding protein complex. Calero G, Wilson KF, Ly T, Rios-Steiner JL, Clardy JC, Cerione RA Nat Struct Biol 2002-12-01 (9) 12434151
A cap-binding protein complex mediating U snRNA export. Izaurralde E, Lewis J, Gamberi C, Jarmolowski A, McGuigan C, Mattaj IW Nature 1995-08-24 (376) 7651522
Large-scale induced fit recognition of an m(7)GpppG cap analogue by the human nuclear cap-binding complex. Mazza C, Segref A, Mattaj IW, Cusack S EMBO J 2002-10-15 (21) 12374755
A nuclear cap binding protein complex involved in pre-mRNA splicing. Izaurralde E, Lewis J, McGuigan C, Jankowska M, Darzynkiewicz E, Mattaj IW Cell 1994-08-26 (78) 8069914
Human mRNA export machinery recruited to the 5' end of mRNA. Cheng H, Dufu K, Lee CS, Hsu JL, Dias A, Reed R Cell 2006-12-01 (127) 17190602
Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M Cell 2006-11-03 (127) 17081983
Initial characterization of the human central proteome. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J BMC Syst Biol 2011-01-01 (5) 21269460
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 2009-08-14 (325) 19608861
A quantitative atlas of mitotic phosphorylation. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP Proc Natl Acad Sci U S A 2008-08-05 (105) 18669648
Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK Sci Signal 2009-01-01 (2) 19690332
Molecular composition of IMP1 ribonucleoprotein granules. Jonson L, Vikesaa J, Krogh A, Nielsen LK, Hansen T, Borup R, Johnsen AH, Christiansen J, Nielsen FC Mol Cell Proteomics 2007-05-01 (6) 17289661
Interaction between the human nuclear cap-binding protein complex and hnRNP F. Gamberi C, Izaurralde E, Beisel C, Mattaj IW Mol Cell Biol 1997-05-01 (17) 9111328
Evidence for a pioneer round of mRNA translation: mRNAs subject to nonsense-mediated decay in mammalian cells are bound by CBP80 and CBP20. Ishigaki Y, Li X, Serin G, Maquat LE Cell 2001-09-07 (106) 11551508
The exon junction complex is detected on CBP80-bound but not eIF4E-bound mRNA in mammalian cells: dynamics of mRNP remodeling. Lejeune F, Ishigaki Y, Li X, Maquat LE EMBO J 2002-07-01 (21) 12093754
eIF4G is required for the pioneer round of translation in mammalian cells. Lejeune F, Ranganathan AC, Maquat LE Nat Struct Mol Biol 2004-10-01 (11) 15361857
Failsafe nonsense-mediated mRNA decay does not detectably target eIF4E-bound mRNA. Matsuda D, Hosoda N, Kim YK, Maquat LE Nat Struct Mol Biol 2007-10-01 (14) 17873884
Ars2 links the nuclear cap-binding complex to RNA interference and cell proliferation. Gruber JJ, Zatechka DS, Sabin LR, Yong J, Lum JJ, Kong M, Zong WX, Zhang Z, Lau CK, Rawlings J, Cherry S, Ihle JN, Dreyfuss G, Thompson CB Cell 2009-07-23 (138) 19632182
Crystal structure of the human nuclear cap binding complex. Mazza C, Ohno M, Segref A, Mattaj IW, Cusack S Mol Cell 2001-08-01 (8) 11545740
Cloning of a complementary DNA encoding an 80 kilodalton nuclear cap binding protein. Kataoka N, Ohno M, Kangawa K, Tokoro Y, Shimura Y Nucleic Acids Res 1994-09-25 (22) 7937105
DNA sequence and analysis of human chromosome 9. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE Nature 2004-05-27 (429) 15164053
Cdc42 stimulates RNA splicing via the S6 kinase and a novel S6 kinase target, the nuclear cap-binding complex. Wilson KF, Wu WJ, Cerione RA J Biol Chem 2000-12-01 (275) 10973943
Interaction of eukaryotic translation initiation factor 4G with the nuclear cap-binding complex provides a link between nuclear and cytoplasmic functions of the m(7) guanosine cap. McKendrick L, Thompson E, Ferreira J, Morley SJ, Lewis JD Mol Cell Biol 2001-06-01 (21) 11340157
The pioneer translation initiation complex is functionally distinct from but structurally overlaps with the steady-state translation initiation complex. Chiu SY, Lejeune F, Ranganathan AC, Maquat LE Genes Dev 2004-04-01 (18) 15059963
CBP80 promotes interaction of Upf1 with Upf2 during nonsense-mediated mRNA decay in mammalian cells. Hosoda N, Kim YK, Lejeune F, Maquat LE Nat Struct Mol Biol 2005-10-01 (12) 16186820
Inhibition of mRNA deadenylation by the nuclear cap binding complex (CBC). Balatsos NA, Nilsson P, Mazza C, Cusack S, Virtanen A J Biol Chem 2006-01-17 (281) 16317009
SKAR links pre-mRNA splicing to mTOR/S6K1-mediated enhanced translation efficiency of spliced mRNAs. Ma XM, Yoon SO, Richardson CJ, Julich K, Blenis J Cell 2008-04-18 (133) 18423201
A new MIF4G domain-containing protein, CTIF, directs nuclear cap-binding protein CBP80/20-dependent translation. Kim KM, Cho H, Choi K, Kim J, Kim BW, Ko YG, Jang SK, Kim YK Genes Dev 2009-09-01 (23) 19648179

Add your own comment!

There are no comments yet.

Last modification of this entry: Sept. 25, 2012.

Welcome stranger! Click here to login or here to register.