Q3UYV9 · NCBP1_MOUSE
- ProteinNuclear cap-binding protein subunit 1
- GeneNcbp1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids790 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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. Associates with NCBP3 to form an alternative cap-binding complex (CBC) which plays a key role in mRNA export and is particularly important in cellular stress situations such as virus infections. The conventional CBC with NCBP2 binds both small nuclear RNA (snRNA) and messenger (mRNA) and is involved in their export from the nucleus whereas the alternative CBC with NCBP3 does not bind snRNA and associates only with mRNA thereby playing a role only in mRNA export. NCBP1/CBP80 is required for cell growth and viability (By similarity).
GO annotations
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNuclear cap-binding protein subunit 1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ3UYV9
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000239779 | 1-790 | Nuclear cap-binding protein subunit 1 | |||
Sequence: MSRRRHSYENDGGQPHKRRKTSDANETEDHLESLICKVGEKSACSLESNLEGLAGVLEADLPNYKSKILRLLCTVARLLPEKLTIYTTLVGLLNARNYNFGGEFVEAMIRQLKESLKANNYNEAVYLVRFLSDLVNCHVIAAPSMVAMFENFVSVTQEEDVPQVRRDWYVYAFLSSLPWVGKELYEKKDAEMDRIFSTTESYLKRRQKTHVPMLQVWTADKPHPQEEYLDCLWAQIQKLKKDRWQERHILRPYLAFDSILCEALQHNLPPFTPPPHTEDSVYPMPRVIFRMFDYTDDPEGPVMPGSHSVERFVIEENLHCIIKSYWKERKTCAAQLVSYPGKNKIPLNYHIVEVIFAELFQLPAPPHIDVMYTTLLIELCKLQPGSLPQVLAQATEMLYMRLDTMSTTCVDRFINWFSHHLSNFQFRWSWEDWSDCLTQDLESPKPKFVREVLEKCMRLSYHQHILDIVPPTFSALCPANPTCIYKYGDESSNSLPGHSVALCLSVAFKSKATNDEIFSILKDVPNPNQVDDDDEGFRFNPLKIEVFVQTLLHLAAKSFSHSFSALAKFHEVFKTLAESDKGKLHVLRVMFEVWRNHPQMIAVLVDKMIRTQIVDCAAVANWIFSSELSRDFTRLFVWEILHSTIRKMNKHVLKIQKELEEAKEKLARQHKRRSDDDDRSSDRKDGALEEQIERLQEKVEAAQSEQKNLFLVIFQRFIMILTEHLVRCETDGTSILTPWYKNCIERLQQIFLQHHQTIQQYMVTLENLLFTAELDPHILAVFQQFCALQA | ||||||
Modified residue | 7 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 21 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 22 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 201 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 204 | N6-acetyllysine | ||||
Sequence: K | ||||||
Cross-link | 684 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 698 | N6-acetyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in the spermatogonia, spermatocytes and granular cells within the cerebellum.
Gene expression databases
Interaction
Subunit
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 containing PHAX/RNUXA, NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-capped RNA. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with PHAX/RNUXA, SRRT/ARS2, EIF4G2, IGF2BP1, HNRNPF, HNRNPH1, KIAA0427/CTIF, PARN, DROSHA, UPF1 and ALYREF/THOC4. May interact with EIF4G1; the interaction is however controversial. The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1/CBP80 and POLR2A (active). Component of an alternative nuclear cap-binding complex (CBC) composed of NCBP1/CBP80 and NCBP3 (By similarity).
Interacts with METTL3 (By similarity).
Interacts with ZFC3H1 in a RNase-insensitive manner (By similarity).
Interacts with MTREX (By similarity).
Interacts with TASOR (PubMed:31112734).
Interacts with DHX34; the interaction is RNA-dependent (By similarity).
Interacts with KPNA3 (By similarity).
Interacts with METTL3 (By similarity).
Interacts with ZFC3H1 in a RNase-insensitive manner (By similarity).
Interacts with MTREX (By similarity).
Interacts with TASOR (PubMed:31112734).
Interacts with DHX34; the interaction is RNA-dependent (By similarity).
Interacts with KPNA3 (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, motif, domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-26 | Disordered | ||||
Sequence: MSRRRHSYENDGGQPHKRRKTSDANE | ||||||
Motif | 3-20 | Nuclear localization signal | ||||
Sequence: RRRHSYENDGGQPHKRRK | ||||||
Domain | 28-240 | MIF4G | ||||
Sequence: EDHLESLICKVGEKSACSLESNLEGLAGVLEADLPNYKSKILRLLCTVARLLPEKLTIYTTLVGLLNARNYNFGGEFVEAMIRQLKESLKANNYNEAVYLVRFLSDLVNCHVIAAPSMVAMFENFVSVTQEEDVPQVRRDWYVYAFLSSLPWVGKELYEKKDAEMDRIFSTTESYLKRRQKTHVPMLQVWTADKPHPQEEYLDCLWAQIQKLK | ||||||
Coiled coil | 643-713 | |||||
Sequence: STIRKMNKHVLKIQKELEEAKEKLARQHKRRSDDDDRSSDRKDGALEEQIERLQEKVEAAQSEQKNLFLVI | ||||||
Region | 666-685 | Disordered | ||||
Sequence: LARQHKRRSDDDDRSSDRKD |
Sequence similarities
Belongs to the NCBP1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length790
- Mass (Da)91,927
- Last updated2006-06-13 v2
- ChecksumBE27F89BDBC19CF2
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 319 | in Ref. 1; BAE22102 | ||||
Sequence: H → R | ||||||
Sequence conflict | 443 | in Ref. 1; BAE22102 | ||||
Sequence: S → R | ||||||
Sequence conflict | 453 | in Ref. 1; BAE22102 | ||||
Sequence: L → I | ||||||
Sequence conflict | 574 | in Ref. 1; BAE22102 | ||||
Sequence: K → Q |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK134334 EMBL· GenBank· DDBJ | BAE22102.1 EMBL· GenBank· DDBJ | mRNA | ||
AK169557 EMBL· GenBank· DDBJ | BAE41227.1 EMBL· GenBank· DDBJ | mRNA | ||
AL732615 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL929438 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH466565 EMBL· GenBank· DDBJ | EDL02380.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC055777 EMBL· GenBank· DDBJ | AAH55777.1 EMBL· GenBank· DDBJ | mRNA | ||
BC138898 EMBL· GenBank· DDBJ | AAI38899.1 EMBL· GenBank· DDBJ | mRNA |