(data stored in ACNUC27637 zone)

SWISSPROT: NCBP2_DANRE

ID   NCBP2_DANRE             Reviewed;         155 AA.
AC   Q8JGR6; Q1MT38; Q5XIY9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   07-JUN-2017, entry version 96.
DE   RecName: Full=Nuclear cap-binding protein subunit 2;
DE   AltName: Full=20 kDa nuclear cap-binding protein;
DE   AltName: Full=NCBP 20 kDa subunit;
DE            Short=CBP20;
GN   Name=ncbp2; Synonyms=cbp20; ORFNames=ch211-258l4.5;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RX   PubMed=12006978; DOI=10.1038/ng896;
RA   Golling G., Amsterdam A., Sun Z., Antonelli M., Maldonado E., Chen W.,
RA   Burgess S., Haldi M., Artzt K., Farrington S., Lin S.-Y., Nissen R.M.,
RA   Hopkins N.;
RT   "Insertional mutagenesis in zebrafish rapidly identifies genes
RT   essential for early vertebrate development.";
RL   Nat. Genet. 31:135-140(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
RA   Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
RA   McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
RA   Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
RA   Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
RA   Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
RA   Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
RA   Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G.,
RA   Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B.,
RA   Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S.,
RA   Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C.,
RA   Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H.,
RA   Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C.,
RA   Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J.,
RA   Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S.,
RA   Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R.,
RA   Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R.,
RA   Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R.,
RA   Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A.,
RA   Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S.,
RA   Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J.,
RA   Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
RA   Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
RA   Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
RA   Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the
RT   human genome.";
RL   Nature 496:498-503(2013).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the cap-binding complex (CBC), which binds
CC       co-transcriptionally to the 5' cap of pre-mRNAs and is involved in
CC       various processes such as pre-mRNA splicing, translation
CC       regulation, nonsense-mediated mRNA decay, RNA-mediated gene
CC       silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC
CC       complex is involved in mRNA export from the nucleus, leading to
CC       the recruitment of the mRNA export machinery to the 5' end of mRNA
CC       and to mRNA export in a 5' to 3' direction through the nuclear
CC       pore. The CBC complex is also involved in mediating U snRNA and
CC       intronless mRNAs export from the nucleus. The CBC complex is
CC       essential for a pioneer round of mRNA translation, before steady
CC       state translation when the CBC complex is replaced by cytoplasmic
CC       cap-binding protein eIF4E. The pioneer round of mRNA translation
CC       mediated by the CBC complex plays a central role in nonsense-
CC       mediated mRNA decay (NMD), NMD only taking place in mRNAs bound to
CC       the CBC complex, but not on eIF4E-bound mRNAs. The CBC complex
CC       enhances NMD in mRNAs containing at least one exon-junction
CC       complex (EJC), promoting the interaction between upf1 and upf2.
CC       The CBC complex is also involved in 'failsafe' NMD, which is
CC       independent of the EJC complex, while it does not participate in
CC       Staufen-mediated mRNA decay (SMD). During cell proliferation, the
CC       CBC complex is also involved in microRNAs (miRNAs) biogenesis via
CC       its interaction with srrt/ars2, thereby being required for miRNA-
CC       mediated RNA interference. The CBC complex also acts as a negative
CC       regulator of parn, thereby acting as an inhibitor of mRNA
CC       deadenylation. In the CBC complex, ncbp2/cbp20 recognizes and
CC       binds capped RNAs (m7GpppG-capped RNA) but requires ncbp1/cbp80 to
CC       stabilize the movement of its N-terminal loop and lock the CBC
CC       into a high affinity cap-binding state with the cap structure. The
CC       conventional cap-binding complex with NCBP2 binds both small
CC       nuclear RNA (snRNA) and messenger (mRNA) and is involved in their
CC       export from the nucleus (By similarity).
CC       {ECO:0000250|UniProtKB:P52298}.
CC   -!- SUBUNIT: Component of the nuclear cap-binding complex (CBC), a
CC       heterodimer composed of ncbp1/cbp80 and ncbp2/cbp20 that interacts
CC       with m7GpppG-capped RNA. {ECO:0000250|UniProtKB:P52298}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P52298}.
CC       Cytoplasm {ECO:0000250|UniProtKB:P52298}.
CC   -!- SIMILARITY: Belongs to the RRM NCBP2 family. {ECO:0000305}.
DR   EMBL; AY099530; AAM28218.1; -; mRNA.
DR   EMBL; AL953867; CAK04823.1; -; Genomic_DNA.
DR   EMBL; BC083529; AAH83529.1; -; mRNA.
DR   RefSeq; NP_775356.1; NM_173249.1.
DR   UniGene; Dr.83993; -.
DR   ProteinModelPortal; Q8JGR6; -.
DR   SMR; Q8JGR6; -.
DR   STRING; 7955.ENSDARP00000020688; -.
DR   PaxDb; Q8JGR6; -.
DR   PRIDE; Q8JGR6; -.
DR   Ensembl; ENSDART00000008365; ENSDARP00000020688; ENSDARG00000014898.
DR   GeneID; 192325; -.
DR   KEGG; dre:192325; -.
DR   CTD; 22916; -.
DR   ZFIN; ZDB-GENE-020419-31; ncbp2.
DR   eggNOG; KOG0121; Eukaryota.
DR   eggNOG; ENOG4111FJQ; LUCA.
DR   GeneTree; ENSGT00390000003197; -.
DR   HOGENOM; HOG000217589; -.
DR   InParanoid; Q8JGR6; -.
DR   KO; K12883; -.
DR   OMA; RQDYDPA; -.
DR   OrthoDB; EOG091G0RKX; -.
DR   PhylomeDB; Q8JGR6; -.
DR   TreeFam; TF313897; -.
DR   Reactome; R-DRE-113418; Formation of the Early Elongation Complex.
DR   Reactome; R-DRE-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR   Reactome; R-DRE-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-DRE-6803529; FGFR2 alternative splicing.
DR   Reactome; R-DRE-6807505; RNA polymerase II transcribes snRNA genes.
DR   Reactome; R-DRE-72163; mRNA Splicing - Major Pathway.
DR   Reactome; R-DRE-72165; mRNA Splicing - Minor Pathway.
DR   Reactome; R-DRE-72187; mRNA 3'-end processing.
DR   Reactome; R-DRE-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR   Reactome; R-DRE-77595; Processing of Intronless Pre-mRNAs.
DR   Reactome; R-DRE-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR   Reactome; R-DRE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   PRO; PR:Q8JGR6; -.
DR   Proteomes; UP000000437; Chromosome 22.
DR   Bgee; ENSDARG00000014898; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005846; C:nuclear cap binding complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR   GO; GO:0000340; F:RNA 7-methylguanosine cap binding; ISS:UniProtKB.
DR   GO; GO:0000339; F:RNA cap binding; IBA:GO_Central.
DR   GO; GO:0017069; F:snRNA binding; ISS:UniProtKB.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR   GO; GO:0045292; P:mRNA cis splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR   GO; GO:0046833; P:positive regulation of RNA export from nucleus; ISS:UniProtKB.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; ISS:UniProtKB.
DR   GO; GO:0006408; P:snRNA export from nucleus; ISS:UniProtKB.
DR   CDD; cd12240; RRM_NCBP2; 1.
DR   InterPro; IPR027157; NCBP2.
DR   InterPro; IPR034148; NCBP2_RRM.
DR   InterPro; IPR000504; RRM_dom.
DR   PANTHER; PTHR18847; PTHR18847; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; Q8JGR6.
DR   SWISS-2DPAGE; Q8JGR6.
KW   Complete proteome; Cytoplasm; mRNA processing; mRNA splicing;
KW   mRNA transport; Nonsense-mediated mRNA decay; Nucleus;
KW   Reference proteome; RNA-binding; RNA-mediated gene silencing;
KW   Translation regulation; Transport.
FT   CHAIN         1    155       Nuclear cap-binding protein subunit 2.
FT                                /FTId=PRO_0000385251.
FT   DOMAIN       39    117       RRM. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00176}.
FT   REGION      111    115       mRNA cap-binding. {ECO:0000250}.
FT   REGION      122    126       mRNA cap-binding. {ECO:0000250}.
FT   REGION      132    133       mRNA cap-binding. {ECO:0000250}.
FT   BINDING      19     19       mRNA cap. {ECO:0000250}.
FT   BINDING      42     42       mRNA cap. {ECO:0000250}.
FT   CONFLICT     12     12       S -> F (in Ref. 1; AAM28218).
FT                                {ECO:0000305}.
FT   CONFLICT     57     57       E -> V (in Ref. 1; AAM28218).
FT                                {ECO:0000305}.
FT   CONFLICT    126    126       R -> W (in Ref. 3; AAH83529).
FT                                {ECO:0000305}.
SQ   SEQUENCE   155 AA;  17932 MW;  A548E56498E98E3F CRC64;
     MSIKLNALFS DSYVDVSQYR DQHFKGNRYE QEKLLKQSAT LYVGNLSFYT TEEQVHELFA
     KCGDVKRIII GLDKIKKTAC GFCFVEYYTR ADAENAMRFV NGTRLDDRII RTDWDAGFKE
     GRQYGRGKSG GQVRDEYRQD YDPARGGYGK MVQKS
//

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