Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Nuclear cap-binding protein subunit 2

Gene

Ncbp2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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, thereby being 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, NCBP2/CBP20 recognizes and binds capped RNAs (m7GpppG-capped RNA) but requires NCBP1/CBP80 to stabilize the movement of its N-terminal loop and lock the CBC into a high affinity cap-binding state with the cap structure. The conventional cap-binding complex with NCBP2 binds both small nuclear RNA (snRNA) and messenger (mRNA) and is involved in their export from the nucleus (By similarity).By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei20mRNA capBy similarity1
Binding sitei43mRNA capBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA capping, mRNA processing, mRNA splicing, mRNA transport, Nonsense-mediated mRNA decay, RNA-mediated gene silencing, Translation regulation, Transport

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-109688. Cleavage of Growing Transcript in the Termination Region.
R-MMU-111367. SLBP independent Processing of Histone Pre-mRNAs.
R-MMU-112382. Formation of RNA Pol II elongation complex.
R-MMU-113418. Formation of the Early Elongation Complex.
R-MMU-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-MMU-191859. snRNP Assembly.
R-MMU-674695. RNA Polymerase II Pre-transcription Events.
R-MMU-6803529. FGFR2 alternative splicing.
R-MMU-6807505. RNA polymerase II transcribes snRNA genes.
R-MMU-72086. mRNA Capping.
R-MMU-72163. mRNA Splicing - Major Pathway.
R-MMU-72165. mRNA Splicing - Minor Pathway.
R-MMU-72187. mRNA 3'-end processing.
R-MMU-72203. Processing of Capped Intron-Containing Pre-mRNA.
R-MMU-77588. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
R-MMU-77595. Processing of Intronless Pre-mRNAs.
R-MMU-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-MMU-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear cap-binding protein subunit 2
Alternative name(s):
20 kDa nuclear cap-binding protein
NCBP 20 kDa subunit
Short name:
CBP20
Gene namesi
Name:Ncbp2
Synonyms:Cbp20
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1915342. Ncbp2.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000815002 – 156Nuclear cap-binding protein subunit 2Add BLAST155

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei13PhosphoserineCombined sources1
Modified residuei18PhosphoserineBy similarity1
Modified residuei146Omega-N-methylarginineCombined sources1

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiQ9CQ49.
MaxQBiQ9CQ49.
PaxDbiQ9CQ49.
PeptideAtlasiQ9CQ49.
PRIDEiQ9CQ49.

PTM databases

iPTMnetiQ9CQ49.
PhosphoSitePlusiQ9CQ49.

Expressioni

Gene expression databases

BgeeiENSMUSG00000022774.
CleanExiMM_NCBP2.
ExpressionAtlasiQ9CQ49. baseline and differential.
GenevisibleiQ9CQ49. MM.

Interactioni

Subunit structurei

Component of the nuclear cap-binding complex (CBC), a heterodimer composed of NCBP1/CBP80 and NCBP2/CBP20 that interacts with m7GpppG-capped RNA (By similarity). Found in a U snRNA export complex with PHAX/RNUXA, NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-capped RNA (PubMed:10786834). Interacts with PHAX/RNUXA, EIF4G1, HNRNPF, HNRNPH1 and ALYREF/THOC4/ALY (By similarity). Interacts with SRRT/ARS2 and KPNA3 (By similarity).By similarity1 Publication

Protein-protein interaction databases

BioGridi212651. 25 interactors.
IntActiQ9CQ49. 26 interactors.
MINTiMINT-4613350.
STRINGi10090.ENSMUSP00000023460.

Structurei

3D structure databases

ProteinModelPortaliQ9CQ49.
SMRiQ9CQ49.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini40 – 118RRMPROSITE-ProRule annotationAdd BLAST79

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni112 – 116mRNA cap-bindingBy similarity5
Regioni123 – 127mRNA cap-bindingBy similarity5
Regioni133 – 134mRNA cap-bindingBy similarity2

Sequence similaritiesi

Belongs to the RRM NCBP2 family.Curated
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0121. Eukaryota.
ENOG4111FJQ. LUCA.
GeneTreeiENSGT00390000003197.
HOGENOMiHOG000217589.
HOVERGENiHBG052581.
InParanoidiQ9CQ49.
KOiK12883.
OMAiGNRYEQE.
OrthoDBiEOG091G0RKX.
PhylomeDBiQ9CQ49.
TreeFamiTF313897.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR027157. NCBP2.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PANTHERiPTHR18847. PTHR18847. 1 hit.
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9CQ49-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGGLLKALR SDSYVELSEY RDQHFRGDNE EQEKLLKKSC TLYVGNLSFY
60 70 80 90 100
TTEEQIYELF SKSGDIKKII MGLDKMKKTA CGFCFVEYYS RADAENAMRY
110 120 130 140 150
INGTRLDDRI IRTDWDAGFK EGRQYGRGRS GGQVRDEYRE DYDAGRGGYG

KLAQKQ
Length:156
Mass (Da):18,017
Last modified:June 1, 2001 - v1
Checksum:iC6DF61E0C6A2CC2C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008980 mRNA. Translation: BAB26004.1.
AK012659 mRNA. Translation: BAB28389.1.
AK077841 mRNA. Translation: BAC37030.1.
AK147027 mRNA. Translation: BAE27620.1.
CH466521 Genomic DNA. Translation: EDK97760.1.
BC118926 mRNA. Translation: AAI18927.1.
CCDSiCCDS28110.1.
RefSeqiNP_080830.1. NM_026554.4.
UniGeneiMm.290027.
Mm.456900.

Genome annotation databases

EnsembliENSMUST00000023460; ENSMUSP00000023460; ENSMUSG00000022774.
GeneIDi68092.
KEGGimmu:68092.
UCSCiuc007yxz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008980 mRNA. Translation: BAB26004.1.
AK012659 mRNA. Translation: BAB28389.1.
AK077841 mRNA. Translation: BAC37030.1.
AK147027 mRNA. Translation: BAE27620.1.
CH466521 Genomic DNA. Translation: EDK97760.1.
BC118926 mRNA. Translation: AAI18927.1.
CCDSiCCDS28110.1.
RefSeqiNP_080830.1. NM_026554.4.
UniGeneiMm.290027.
Mm.456900.

3D structure databases

ProteinModelPortaliQ9CQ49.
SMRiQ9CQ49.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212651. 25 interactors.
IntActiQ9CQ49. 26 interactors.
MINTiMINT-4613350.
STRINGi10090.ENSMUSP00000023460.

PTM databases

iPTMnetiQ9CQ49.
PhosphoSitePlusiQ9CQ49.

Proteomic databases

EPDiQ9CQ49.
MaxQBiQ9CQ49.
PaxDbiQ9CQ49.
PeptideAtlasiQ9CQ49.
PRIDEiQ9CQ49.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023460; ENSMUSP00000023460; ENSMUSG00000022774.
GeneIDi68092.
KEGGimmu:68092.
UCSCiuc007yxz.2. mouse.

Organism-specific databases

CTDi22916.
MGIiMGI:1915342. Ncbp2.

Phylogenomic databases

eggNOGiKOG0121. Eukaryota.
ENOG4111FJQ. LUCA.
GeneTreeiENSGT00390000003197.
HOGENOMiHOG000217589.
HOVERGENiHBG052581.
InParanoidiQ9CQ49.
KOiK12883.
OMAiGNRYEQE.
OrthoDBiEOG091G0RKX.
PhylomeDBiQ9CQ49.
TreeFamiTF313897.

Enzyme and pathway databases

ReactomeiR-MMU-109688. Cleavage of Growing Transcript in the Termination Region.
R-MMU-111367. SLBP independent Processing of Histone Pre-mRNAs.
R-MMU-112382. Formation of RNA Pol II elongation complex.
R-MMU-113418. Formation of the Early Elongation Complex.
R-MMU-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-MMU-191859. snRNP Assembly.
R-MMU-674695. RNA Polymerase II Pre-transcription Events.
R-MMU-6803529. FGFR2 alternative splicing.
R-MMU-6807505. RNA polymerase II transcribes snRNA genes.
R-MMU-72086. mRNA Capping.
R-MMU-72163. mRNA Splicing - Major Pathway.
R-MMU-72165. mRNA Splicing - Minor Pathway.
R-MMU-72187. mRNA 3'-end processing.
R-MMU-72203. Processing of Capped Intron-Containing Pre-mRNA.
R-MMU-77588. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
R-MMU-77595. Processing of Intronless Pre-mRNAs.
R-MMU-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-MMU-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

PROiQ9CQ49.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000022774.
CleanExiMM_NCBP2.
ExpressionAtlasiQ9CQ49. baseline and differential.
GenevisibleiQ9CQ49. MM.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR027157. NCBP2.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PANTHERiPTHR18847. PTHR18847. 1 hit.
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNCBP2_MOUSE
AccessioniPrimary (citable) accession number: Q9CQ49
Secondary accession number(s): Q0VF93, Q3UI86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: June 1, 2001
Last modified: November 2, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.