NCBP2_MOUSE
ID NCBP2_MOUSE Reviewed; 156 AA.
AC Q9CQ49; Q0VF93; Q3UI86;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion, Embryo, Forelimb, and Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION IN A U SNRNA EXPORT COMPLEX WITH PHAX/RNUXA; NCBP1; RAN;
RP XPO1 AND M7G-CAPPED RNA.
RX PubMed=10786834; DOI=10.1016/s0092-8674(00)80829-6;
RA Ohno M., Segref A., Bachi A., Wilm M., Mattaj I.W.;
RT "PHAX, a mediator of U snRNA nuclear export whose activity is regulated by
RT phosphorylation.";
RL Cell 101:187-198(2000).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP FUNCTION IN MIRNAS BIOGENESIS.
RX PubMed=19632182; DOI=10.1016/j.cell.2009.04.046;
RA Gruber J.J., Zatechka D.S., Sabin L.R., Yong J., Lum J.J., Kong M.,
RA Zong W.-X., Zhang Z., Lau C.-K., Rawlings J., Cherry S., Ihle J.N.,
RA Dreyfuss G., Thompson C.B.;
RT "Ars2 links the nuclear cap-binding complex to RNA interference and cell
RT proliferation.";
RL Cell 138:328-339(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-146, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Component of the cap-binding complex (CBC), which binds co-
CC transcriptionally to the 5' cap of pre-mRNAs and is involved in various
CC processes such as pre-mRNA splicing, translation regulation, nonsense-
CC mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs
CC (miRNAs) and mRNA export. The CBC complex is involved in mRNA export
CC from the nucleus via its interaction with ALYREF/THOC4/ALY, leading to
CC the recruitment of the mRNA export machinery to the 5' end of mRNA and
CC to mRNA export in a 5' to 3' direction through the nuclear pore. The
CC CBC complex is also involved in mediating U snRNA and intronless mRNAs
CC export from the nucleus. The CBC complex is essential for a pioneer
CC round of mRNA translation, before steady state translation when the CBC
CC complex is replaced by cytoplasmic cap-binding protein eIF4E. The
CC pioneer round of mRNA translation mediated by the CBC complex plays a
CC central role in nonsense-mediated mRNA decay (NMD), NMD only taking
CC place in mRNAs bound to the CBC complex, but not on eIF4E-bound mRNAs.
CC The CBC complex enhances NMD in mRNAs containing at least one exon-
CC junction complex (EJC) via its interaction with UPF1, promoting the
CC interaction between UPF1 and UPF2. The CBC complex is also involved in
CC 'failsafe' NMD, which is independent of the EJC complex, while it does
CC not participate in Staufen-mediated mRNA decay (SMD). During cell
CC proliferation, the CBC complex is also involved in microRNAs (miRNAs)
CC biogenesis via its interaction with SRRT/ARS2, thereby being required
CC for miRNA-mediated RNA interference. The CBC complex also acts as a
CC negative regulator of PARN, thereby acting as an inhibitor of mRNA
CC deadenylation. In the CBC complex, NCBP2/CBP20 recognizes and binds
CC capped RNAs (m7GpppG-capped RNA) but requires NCBP1/CBP80 to stabilize
CC the movement of its N-terminal loop and lock the CBC into a high
CC affinity cap-binding state with the cap structure. The conventional
CC cap-binding complex with NCBP2 binds both small nuclear RNA (snRNA) and
CC messenger (mRNA) and is involved in their export from the nucleus (By
CC similarity). {ECO:0000250|UniProtKB:P52298,
CC ECO:0000269|PubMed:19632182}.
CC -!- SUBUNIT: Component of the nuclear cap-binding complex (CBC), a
CC heterodimer composed of NCBP1/CBP80 and NCBP2/CBP20 that interacts with
CC m7GpppG-capped RNA (By similarity). Found in a U snRNA export complex
CC with PHAX/RNUXA, NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-capped RNA
CC (PubMed:10786834). Interacts with PHAX/RNUXA, EIF4G1, HNRNPF, HNRNPH1
CC and ALYREF/THOC4/ALY (By similarity). Interacts with SRRT/ARS2 and
CC KPNA3 (By similarity). {ECO:0000250|UniProtKB:P52298,
CC ECO:0000269|PubMed:10786834}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P52298}. Cytoplasm
CC {ECO:0000250|UniProtKB:P52298}.
CC -!- SIMILARITY: Belongs to the RRM NCBP2 family. {ECO:0000305}.
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DR EMBL; AK008980; BAB26004.1; -; mRNA.
DR EMBL; AK012659; BAB28389.1; -; mRNA.
DR EMBL; AK077841; BAC37030.1; -; mRNA.
DR EMBL; AK147027; BAE27620.1; -; mRNA.
DR EMBL; CH466521; EDK97760.1; -; Genomic_DNA.
DR EMBL; BC118926; AAI18927.1; -; mRNA.
DR CCDS; CCDS28110.1; -.
DR RefSeq; NP_080830.1; NM_026554.4.
DR AlphaFoldDB; Q9CQ49; -.
DR SMR; Q9CQ49; -.
DR BioGRID; 212651; 38.
DR ComplexPortal; CPX-923; Nuclear cap-binding complex.
DR IntAct; Q9CQ49; 27.
DR MINT; Q9CQ49; -.
DR STRING; 10090.ENSMUSP00000023460; -.
DR iPTMnet; Q9CQ49; -.
DR PhosphoSitePlus; Q9CQ49; -.
DR EPD; Q9CQ49; -.
DR MaxQB; Q9CQ49; -.
DR PaxDb; Q9CQ49; -.
DR PeptideAtlas; Q9CQ49; -.
DR PRIDE; Q9CQ49; -.
DR ProteomicsDB; 286154; -.
DR Antibodypedia; 33952; 194 antibodies from 28 providers.
DR DNASU; 68092; -.
DR Ensembl; ENSMUST00000023460; ENSMUSP00000023460; ENSMUSG00000022774.
DR GeneID; 68092; -.
DR KEGG; mmu:68092; -.
DR UCSC; uc007yxz.2; mouse.
DR CTD; 22916; -.
DR MGI; MGI:1915342; Ncbp2.
DR VEuPathDB; HostDB:ENSMUSG00000022774; -.
DR eggNOG; KOG0121; Eukaryota.
DR GeneTree; ENSGT00390000003197; -.
DR HOGENOM; CLU_070952_2_0_1; -.
DR InParanoid; Q9CQ49; -.
DR OMA; AENCMRY; -.
DR OrthoDB; 1421503at2759; -.
DR PhylomeDB; Q9CQ49; -.
DR TreeFam; TF313897; -.
DR Reactome; R-MMU-111367; SLBP independent Processing of Histone Pre-mRNAs.
DR Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-MMU-113418; Formation of the Early Elongation Complex.
DR Reactome; R-MMU-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-MMU-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-MMU-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-6803529; FGFR2 alternative splicing.
DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-MMU-72086; mRNA Capping.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-MMU-72187; mRNA 3'-end processing.
DR Reactome; R-MMU-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-MMU-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
DR Reactome; R-MMU-77595; Processing of Intronless Pre-mRNAs.
DR Reactome; R-MMU-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR BioGRID-ORCS; 68092; 28 hits in 76 CRISPR screens.
DR ChiTaRS; Ncbp2; mouse.
DR PRO; PR:Q9CQ49; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9CQ49; protein.
DR Bgee; ENSMUSG00000022774; Expressed in pigmented layer of retina and 267 other tissues.
DR ExpressionAtlas; Q9CQ49; baseline and differential.
DR Genevisible; Q9CQ49; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
DR GO; GO:0005846; C:nuclear cap binding complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0034518; C:RNA cap binding complex; ISO:MGI.
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:0000380; P:alternative mRNA splicing, via spliceosome; IC:ComplexPortal.
DR GO; GO:0002191; P:cap-dependent translational initiation; IC:ComplexPortal.
DR GO; GO:0008334; P:histone mRNA metabolic process; IMP:ComplexPortal.
DR GO; GO:0035195; P:miRNA-mediated gene silencing; IC:ComplexPortal.
DR GO; GO:0031124; P:mRNA 3'-end processing; IC:ComplexPortal.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; ISO:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISS:UniProtKB.
DR GO; GO:0031442; P:positive regulation of mRNA 3'-end processing; ISO:MGI.
DR GO; GO:1901409; P:positive regulation of phosphorylation of RNA polymerase II C-terminal domain; IC:ComplexPortal.
DR GO; GO:0046833; P:positive regulation of RNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IC:ComplexPortal.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; ISO:MGI.
DR GO; GO:0031053; P:primary miRNA processing; IC:ComplexPortal.
DR GO; GO:0006446; P:regulation of translational initiation; ISS:UniProtKB.
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 Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR027157; NCBP2.
DR InterPro; IPR034148; NCBP2_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Methylation; mRNA processing; mRNA splicing;
KW mRNA transport; Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; RNA-mediated gene silencing;
KW Translation regulation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P52298"
FT CHAIN 2..156
FT /note="Nuclear cap-binding protein subunit 2"
FT /id="PRO_0000081500"
FT DOMAIN 40..118
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 124..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 20
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 112..116
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 123..127
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 133..134
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P52298"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52298"
FT MOD_RES 146
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
SQ SEQUENCE 156 AA; 18017 MW; C6DF61E0C6A2CC2C CRC64;
MSGGLLKALR SDSYVELSEY RDQHFRGDNE EQEKLLKKSC TLYVGNLSFY TTEEQIYELF
SKSGDIKKII MGLDKMKKTA CGFCFVEYYS RADAENAMRY INGTRLDDRI IRTDWDAGFK
EGRQYGRGRS GGQVRDEYRE DYDAGRGGYG KLAQKQ
