Full text data of NCBP2
NCBP2
(CBP20)
[Confidence: low (only semi-automatic identification from reviews)]
Nuclear cap-binding protein subunit 2 (20 kDa nuclear cap-binding protein; Cell proliferation-inducing gene 55 protein; NCBP 20 kDa subunit; CBP20; NCBP-interacting protein 1; NIP1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Nuclear cap-binding protein subunit 2 (20 kDa nuclear cap-binding protein; Cell proliferation-inducing gene 55 protein; NCBP 20 kDa subunit; CBP20; NCBP-interacting protein 1; NIP1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P52298
ID NCBP2_HUMAN Reviewed; 156 AA.
AC P52298; B2RE91; B4DMK7; Q14924; Q2TS50;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 146.
DE RecName: Full=Nuclear cap-binding protein subunit 2;
DE AltName: Full=20 kDa nuclear cap-binding protein;
DE AltName: Full=Cell proliferation-inducing gene 55 protein;
DE AltName: Full=NCBP 20 kDa subunit;
DE Short=CBP20;
DE AltName: Full=NCBP-interacting protein 1;
DE Short=NIP1;
GN Name=NCBP2; Synonyms=CBP20; ORFNames=PIG55;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 9-25
RP AND 113-145.
RX PubMed=7651522; DOI=10.1038/376709a0;
RA Izaurralde E., Lewis J., Gamberi C., Jarmolowski A., McGuigan C.,
RA Mattaj A.W.;
RT "A cap-binding protein complex mediating U snRNA export.";
RL Nature 376:709-712(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Cervix carcinoma;
RX PubMed=7478990; DOI=10.1093/nar/23.18.3638;
RA Kataoka N., Ohno M., Moda I., Shimura Y.;
RT "Identification of the factors that interact with NCBP, an 80 kDa
RT nuclear cap binding protein.";
RL Nucleic Acids Res. 23:3638-3641(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kim J.W.;
RT "Identification of a human cell proliferation gene.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=8601613; DOI=10.1083/jcb.133.1.5;
RA Visa N., Izaurralde E., Ferreira J., Daneholt B., Mattaj I.W.;
RT "A nuclear cap-binding complex binds Balbiani ring pre-mRNA
RT cotranscriptionally and accompanies the ribonucleoprotein particle
RT during nuclear export.";
RL J. Cell Biol. 133:5-14(1996).
RN [9]
RP INTERACTION WITH HNRNPF AND HNRNPH1.
RX PubMed=9111328;
RA Gamberi C., Izaurralde E., Beisel C., Mattaj I.W.;
RT "Interaction between the human nuclear cap-binding protein complex and
RT hnRNP F.";
RL Mol. Cell. Biol. 17:2587-2597(1997).
RN [10]
RP FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION.
RX PubMed=11551508; DOI=10.1016/S0092-8674(01)00475-5;
RA Ishigaki Y., Li X., Serin G., Maquat L.E.;
RT "Evidence for a pioneer round of mRNA translation: mRNAs subject to
RT nonsense-mediated decay in mammalian cells are bound by CBP80 and
RT CBP20.";
RL Cell 106:607-617(2001).
RN [11]
RP FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION, AND INTERACTION WITH
RP EIF4G1.
RX PubMed=15361857; DOI=10.1038/nsmb824;
RA Lejeune F., Ranganathan A.C., Maquat L.E.;
RT "eIF4G is required for the pioneer round of translation in mammalian
RT cells.";
RL Nat. Struct. Mol. Biol. 11:992-1000(2004).
RN [12]
RP FUNCTION IN MRNA EXPORT.
RX PubMed=17190602; DOI=10.1016/j.cell.2006.10.044;
RA Cheng H., Dufu K., Lee C.-S., Hsu J.L., Dias A., Reed R.;
RT "Human mRNA export machinery recruited to the 5' end of mRNA.";
RL Cell 127:1389-1400(2006).
RN [13]
RP FUNCTION IN MRNA EXPORT, AND INTERACTION WITH ALYREF/THOC4.
RX PubMed=17363367; DOI=10.1074/jbc.M700629200;
RA Nojima T., Hirose T., Kimura H., Hagiwara M.;
RT "The interaction between cap-binding complex and RNA export factor is
RT required for intronless mRNA export.";
RL J. Biol. Chem. 282:15645-15651(2007).
RN [14]
RP FUNCTION IN NONSENSE-MEDIATED MRNA DECAY.
RX PubMed=17873884; DOI=10.1038/nsmb1297;
RA Matsuda D., Hosoda N., Kim Y.K., Maquat L.E.;
RT "Failsafe nonsense-mediated mRNA decay does not detectably target
RT eIF4E-bound mRNA.";
RL Nat. Struct. Mol. Biol. 14:974-979(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [16]
RP FUNCTION IN NONSENSE-MEDIATED MRNA DECAY.
RX PubMed=18369367; DOI=10.1038/embor.2008.36;
RA Woeller C.F., Gaspari M., Isken O., Maquat L.E.;
RT "NMD resulting from encephalomyocarditis virus IRES-directed
RT translation initiation seems to be restricted to CBP80/20-bound
RT mRNA.";
RL EMBO Rep. 9:446-451(2008).
RN [17]
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
RT cell proliferation.";
RL Cell 138:328-339(2009).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 20-790 IN COMPLEX WITH NCBP1,
RP RNA-BINDING, AND MUTAGENESIS OF PHE-25; TYR-43; ASN-46; PHE-83;
RP ASP-114; ASP-116 AND PHE-119.
RX PubMed=11545740; DOI=10.1016/S1097-2765(01)00299-4;
RA Mazza C., Ohno M., Segref A., Mattaj I.W., Cusack S.;
RT "Crystal structure of the human nuclear cap binding complex.";
RL Mol. Cell 8:383-396(2001).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 20-790 IN COMPLEX WITH NCBP1
RP AND MRNA CAP, RNA-BINDING, AND MUTAGENESIS OF TYR-20; TYR-43; ARG-112
RP AND TYR-138.
RX PubMed=12374755; DOI=10.1093/emboj/cdf538;
RA Mazza C., Segref A., Mattaj I.W., Cusack S.;
RT "Large-scale induced fit recognition of an m(7)GpppG cap analogue by
RT the human nuclear cap-binding complex.";
RL EMBO J. 21:5548-5557(2002).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) IN COMPLEX WITH NCBP1 AND MRNA
RP CAP, AND RNA-BINDING.
RX PubMed=12434151; DOI=10.1038/nsb874;
RA Calero G., Wilson K.F., Ly T., Rios-Steiner J.L., Clardy J.C.,
RA Cerione R.A.;
RT "Structural basis of m7GpppG binding to the nuclear cap-binding
RT protein complex.";
RL Nat. Struct. Biol. 9:912-917(2002).
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 via its
CC interaction with ALYREF/THOC4/ALY, leading to the recruitment of
CC the mRNA export machinery to the 5' end of mRNA and to mRNA export
CC in a 5' to 3' direction through the nuclear pore. The CBC complex
CC is also involved in mediating U snRNA and intronless mRNAs export
CC from the nucleus. The CBC complex is essential for a pioneer round
CC 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
CC plays a central role in nonsense-mediated mRNA decay (NMD), NMD
CC only taking place in mRNAs bound to the CBC complex, but not on
CC eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs
CC containing at least one exon-junction complex (EJC) via its
CC interaction with UPF1, promoting the interaction between UPF1 and
CC UPF2. 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.
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. Found in a U snRNA export complex with
CC RNUXA/PHAX, NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-capped
CC RNA. Interacts with RNUXA/PHAX, EIF4G1, HNRNPF, HNRNPH1 and
CC ALYREF/THOC4/ALY.
CC -!- INTERACTION:
CC Q09161:NCBP1; NbExp=6; IntAct=EBI-464729, EBI-464743;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P52298-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P52298-2; Sequence=VSP_038125;
CC -!- SIMILARITY: Belongs to the RRM NCBP2 family.
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
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DR EMBL; X84157; CAA58962.1; -; mRNA.
DR EMBL; D59253; BAA09599.1; -; mRNA.
DR EMBL; AK297506; BAG59919.1; -; mRNA.
DR EMBL; AK315903; BAH14274.1; -; mRNA.
DR EMBL; AK316601; BAG38188.1; -; mRNA.
DR EMBL; AY644767; AAV85455.1; -; mRNA.
DR EMBL; BT006842; AAP35488.1; -; mRNA.
DR EMBL; CH471191; EAW53624.1; -; Genomic_DNA.
DR EMBL; BC001255; AAH01255.1; -; mRNA.
DR PIR; I37222; I37222.
DR PIR; S60109; S60109.
DR RefSeq; NP_001036005.1; NM_001042540.1.
DR RefSeq; NP_031388.2; NM_007362.3.
DR RefSeq; XP_005269370.1; XM_005269313.1.
DR UniGene; Hs.591671; -.
DR PDB; 1H2T; X-ray; 2.15 A; Z=1-156.
DR PDB; 1H2U; X-ray; 2.40 A; X/Y=1-156.
DR PDB; 1H2V; X-ray; 2.00 A; Z=1-156.
DR PDB; 1H6K; X-ray; 2.00 A; X/Y/Z=22-120.
DR PDB; 1N52; X-ray; 2.11 A; B=1-156.
DR PDB; 1N54; X-ray; 2.72 A; B=1-156.
DR PDB; 3FEX; X-ray; 3.55 A; B=1-156.
DR PDB; 3FEY; X-ray; 2.20 A; B=1-156.
DR PDBsum; 1H2T; -.
DR PDBsum; 1H2U; -.
DR PDBsum; 1H2V; -.
DR PDBsum; 1H6K; -.
DR PDBsum; 1N52; -.
DR PDBsum; 1N54; -.
DR PDBsum; 3FEX; -.
DR PDBsum; 3FEY; -.
DR DisProt; DP00393; -.
DR ProteinModelPortal; P52298; -.
DR SMR; P52298; 5-149.
DR DIP; DIP-33246N; -.
DR IntAct; P52298; 8.
DR MINT; MINT-248711; -.
DR STRING; 9606.ENSP00000326806; -.
DR TCDB; 9.A.60.1.1; the small nuclear rna exporter (snrna-e).
DR PhosphoSite; P52298; -.
DR DMDM; 1705651; -.
DR PaxDb; P52298; -.
DR PRIDE; P52298; -.
DR DNASU; 22916; -.
DR Ensembl; ENST00000321256; ENSP00000326806; ENSG00000114503.
DR Ensembl; ENST00000452404; ENSP00000412785; ENSG00000114503.
DR GeneID; 22916; -.
DR KEGG; hsa:22916; -.
DR UCSC; uc003fxb.1; human.
DR CTD; 22916; -.
DR GeneCards; GC03M196662; -.
DR HGNC; HGNC:7659; NCBP2.
DR HPA; HPA044850; -.
DR MIM; 605133; gene.
DR neXtProt; NX_P52298; -.
DR PharmGKB; PA31462; -.
DR eggNOG; COG0724; -.
DR HOGENOM; HOG000217589; -.
DR HOVERGEN; HBG052581; -.
DR InParanoid; P52298; -.
DR KO; K12883; -.
DR OMA; KIAPNTD; -.
DR PhylomeDB; P52298; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_1675; mRNA Processing.
DR Reactome; REACT_1788; Transcription.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR Reactome; REACT_78; Post-Elongation Processing of the Transcript.
DR ChiTaRS; NCBP2; human.
DR EvolutionaryTrace; P52298; -.
DR GenomeRNAi; 22916; -.
DR NextBio; 43603; -.
DR PRO; PR:P52298; -.
DR ArrayExpress; P52298; -.
DR Bgee; P52298; -.
DR CleanEx; HS_NCBP2; -.
DR Genevestigator; P52298; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005845; C:mRNA cap binding complex; IDA:UniProtKB.
DR GO; GO:0005846; C:nuclear cap binding complex; IEA:InterPro.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IDA:UniProtKB.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IDA:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0008334; P:histone mRNA metabolic process; TAS:Reactome.
DR GO; GO:0031124; P:mRNA 3'-end processing; TAS:Reactome.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; TAS:Reactome.
DR GO; GO:0034660; P:ncRNA metabolic process; TAS:Reactome.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:UniProtKB.
DR GO; GO:0046833; P:positive regulation of RNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0050434; P:positive regulation of viral transcription; TAS:Reactome.
DR GO; GO:0006446; P:regulation of translational initiation; IDA:UniProtKB.
DR GO; GO:0006408; P:snRNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; TAS:Reactome.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR027157; NCBP2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR18847; PTHR18847; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Direct protein sequencing; mRNA capping; mRNA processing;
KW mRNA splicing; mRNA transport; Nonsense-mediated mRNA decay; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing; Translation regulation; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 156 Nuclear cap-binding protein subunit 2.
FT /FTId=PRO_0000081499.
FT DOMAIN 40 118 RRM.
FT REGION 112 116 mRNA cap-binding.
FT REGION 123 127 mRNA cap-binding.
FT REGION 133 134 mRNA cap-binding.
FT BINDING 20 20 mRNA cap.
FT BINDING 43 43 mRNA cap.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 18 18 Phosphoserine.
FT VAR_SEQ 1 26 MSGGLLKALRSDSYVELSQYRDQHFR -> MVLRKLYA
FT (in isoform 2).
FT /FTId=VSP_038125.
FT MUTAGEN 20 20 Y->A: Abolishes mRNA cap-binding.
FT MUTAGEN 20 20 Y->F: Strongly impairs mRNA cap-binding.
FT MUTAGEN 25 25 F->A: Does not affect mRNA cap-binding.
FT MUTAGEN 43 43 Y->A: Abolishes mRNA cap-binding.
FT MUTAGEN 43 43 Y->F: Does not affect mRNA cap-binding.
FT MUTAGEN 46 46 N->A: Does not affect mRNA cap-binding.
FT MUTAGEN 83 83 F->A: Abolishes mRNA cap-binding.
FT MUTAGEN 85 85 F->A: Impairs mRNA cap-binding.
FT MUTAGEN 112 112 R->A,T: Does not affect mRNA cap-binding.
FT MUTAGEN 114 114 D->A: Does not affect mRNA cap-binding.
FT MUTAGEN 116 116 D->A: Abolishes mRNA cap-binding.
FT MUTAGEN 119 119 F->A: Does not affect mRNA cap-binding.
FT MUTAGEN 138 138 Y->A: Does not affect mRNA cap-binding.
FT CONFLICT 97 97 A -> S (in Ref. 2; BAA09599).
FT HELIX 7 10
FT HELIX 13 15
FT STRAND 23 27
FT TURN 34 38
FT STRAND 41 46
FT HELIX 53 60
FT HELIX 61 63
FT STRAND 66 73
FT TURN 75 77
FT STRAND 80 90
FT HELIX 91 100
FT TURN 101 103
FT STRAND 104 106
FT STRAND 112 117
FT TURN 121 124
FT HELIX 134 137
FT HELIX 144 146
SQ SEQUENCE 156 AA; 18001 MW; B6C94F3182A2CC3D CRC64;
MSGGLLKALR SDSYVELSQY RDQHFRGDNE EQEKLLKKSC TLYVGNLSFY TTEEQIYELF
SKSGDIKKII MGLDKMKKTA CGFCFVEYYS RADAENAMRY INGTRLDDRI IRTDWDAGFK
EGRQYGRGRS GGQVRDEYRQ DYDAGRGGYG KLAQNQ
//
ID NCBP2_HUMAN Reviewed; 156 AA.
AC P52298; B2RE91; B4DMK7; Q14924; Q2TS50;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 146.
DE RecName: Full=Nuclear cap-binding protein subunit 2;
DE AltName: Full=20 kDa nuclear cap-binding protein;
DE AltName: Full=Cell proliferation-inducing gene 55 protein;
DE AltName: Full=NCBP 20 kDa subunit;
DE Short=CBP20;
DE AltName: Full=NCBP-interacting protein 1;
DE Short=NIP1;
GN Name=NCBP2; Synonyms=CBP20; ORFNames=PIG55;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 9-25
RP AND 113-145.
RX PubMed=7651522; DOI=10.1038/376709a0;
RA Izaurralde E., Lewis J., Gamberi C., Jarmolowski A., McGuigan C.,
RA Mattaj A.W.;
RT "A cap-binding protein complex mediating U snRNA export.";
RL Nature 376:709-712(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Cervix carcinoma;
RX PubMed=7478990; DOI=10.1093/nar/23.18.3638;
RA Kataoka N., Ohno M., Moda I., Shimura Y.;
RT "Identification of the factors that interact with NCBP, an 80 kDa
RT nuclear cap binding protein.";
RL Nucleic Acids Res. 23:3638-3641(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kim J.W.;
RT "Identification of a human cell proliferation gene.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=8601613; DOI=10.1083/jcb.133.1.5;
RA Visa N., Izaurralde E., Ferreira J., Daneholt B., Mattaj I.W.;
RT "A nuclear cap-binding complex binds Balbiani ring pre-mRNA
RT cotranscriptionally and accompanies the ribonucleoprotein particle
RT during nuclear export.";
RL J. Cell Biol. 133:5-14(1996).
RN [9]
RP INTERACTION WITH HNRNPF AND HNRNPH1.
RX PubMed=9111328;
RA Gamberi C., Izaurralde E., Beisel C., Mattaj I.W.;
RT "Interaction between the human nuclear cap-binding protein complex and
RT hnRNP F.";
RL Mol. Cell. Biol. 17:2587-2597(1997).
RN [10]
RP FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION.
RX PubMed=11551508; DOI=10.1016/S0092-8674(01)00475-5;
RA Ishigaki Y., Li X., Serin G., Maquat L.E.;
RT "Evidence for a pioneer round of mRNA translation: mRNAs subject to
RT nonsense-mediated decay in mammalian cells are bound by CBP80 and
RT CBP20.";
RL Cell 106:607-617(2001).
RN [11]
RP FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION, AND INTERACTION WITH
RP EIF4G1.
RX PubMed=15361857; DOI=10.1038/nsmb824;
RA Lejeune F., Ranganathan A.C., Maquat L.E.;
RT "eIF4G is required for the pioneer round of translation in mammalian
RT cells.";
RL Nat. Struct. Mol. Biol. 11:992-1000(2004).
RN [12]
RP FUNCTION IN MRNA EXPORT.
RX PubMed=17190602; DOI=10.1016/j.cell.2006.10.044;
RA Cheng H., Dufu K., Lee C.-S., Hsu J.L., Dias A., Reed R.;
RT "Human mRNA export machinery recruited to the 5' end of mRNA.";
RL Cell 127:1389-1400(2006).
RN [13]
RP FUNCTION IN MRNA EXPORT, AND INTERACTION WITH ALYREF/THOC4.
RX PubMed=17363367; DOI=10.1074/jbc.M700629200;
RA Nojima T., Hirose T., Kimura H., Hagiwara M.;
RT "The interaction between cap-binding complex and RNA export factor is
RT required for intronless mRNA export.";
RL J. Biol. Chem. 282:15645-15651(2007).
RN [14]
RP FUNCTION IN NONSENSE-MEDIATED MRNA DECAY.
RX PubMed=17873884; DOI=10.1038/nsmb1297;
RA Matsuda D., Hosoda N., Kim Y.K., Maquat L.E.;
RT "Failsafe nonsense-mediated mRNA decay does not detectably target
RT eIF4E-bound mRNA.";
RL Nat. Struct. Mol. Biol. 14:974-979(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [16]
RP FUNCTION IN NONSENSE-MEDIATED MRNA DECAY.
RX PubMed=18369367; DOI=10.1038/embor.2008.36;
RA Woeller C.F., Gaspari M., Isken O., Maquat L.E.;
RT "NMD resulting from encephalomyocarditis virus IRES-directed
RT translation initiation seems to be restricted to CBP80/20-bound
RT mRNA.";
RL EMBO Rep. 9:446-451(2008).
RN [17]
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
RT cell proliferation.";
RL Cell 138:328-339(2009).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 20-790 IN COMPLEX WITH NCBP1,
RP RNA-BINDING, AND MUTAGENESIS OF PHE-25; TYR-43; ASN-46; PHE-83;
RP ASP-114; ASP-116 AND PHE-119.
RX PubMed=11545740; DOI=10.1016/S1097-2765(01)00299-4;
RA Mazza C., Ohno M., Segref A., Mattaj I.W., Cusack S.;
RT "Crystal structure of the human nuclear cap binding complex.";
RL Mol. Cell 8:383-396(2001).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 20-790 IN COMPLEX WITH NCBP1
RP AND MRNA CAP, RNA-BINDING, AND MUTAGENESIS OF TYR-20; TYR-43; ARG-112
RP AND TYR-138.
RX PubMed=12374755; DOI=10.1093/emboj/cdf538;
RA Mazza C., Segref A., Mattaj I.W., Cusack S.;
RT "Large-scale induced fit recognition of an m(7)GpppG cap analogue by
RT the human nuclear cap-binding complex.";
RL EMBO J. 21:5548-5557(2002).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) IN COMPLEX WITH NCBP1 AND MRNA
RP CAP, AND RNA-BINDING.
RX PubMed=12434151; DOI=10.1038/nsb874;
RA Calero G., Wilson K.F., Ly T., Rios-Steiner J.L., Clardy J.C.,
RA Cerione R.A.;
RT "Structural basis of m7GpppG binding to the nuclear cap-binding
RT protein complex.";
RL Nat. Struct. Biol. 9:912-917(2002).
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 via its
CC interaction with ALYREF/THOC4/ALY, leading to the recruitment of
CC the mRNA export machinery to the 5' end of mRNA and to mRNA export
CC in a 5' to 3' direction through the nuclear pore. The CBC complex
CC is also involved in mediating U snRNA and intronless mRNAs export
CC from the nucleus. The CBC complex is essential for a pioneer round
CC 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
CC plays a central role in nonsense-mediated mRNA decay (NMD), NMD
CC only taking place in mRNAs bound to the CBC complex, but not on
CC eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs
CC containing at least one exon-junction complex (EJC) via its
CC interaction with UPF1, promoting the interaction between UPF1 and
CC UPF2. 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.
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. Found in a U snRNA export complex with
CC RNUXA/PHAX, NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-capped
CC RNA. Interacts with RNUXA/PHAX, EIF4G1, HNRNPF, HNRNPH1 and
CC ALYREF/THOC4/ALY.
CC -!- INTERACTION:
CC Q09161:NCBP1; NbExp=6; IntAct=EBI-464729, EBI-464743;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P52298-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P52298-2; Sequence=VSP_038125;
CC -!- SIMILARITY: Belongs to the RRM NCBP2 family.
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
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DR EMBL; X84157; CAA58962.1; -; mRNA.
DR EMBL; D59253; BAA09599.1; -; mRNA.
DR EMBL; AK297506; BAG59919.1; -; mRNA.
DR EMBL; AK315903; BAH14274.1; -; mRNA.
DR EMBL; AK316601; BAG38188.1; -; mRNA.
DR EMBL; AY644767; AAV85455.1; -; mRNA.
DR EMBL; BT006842; AAP35488.1; -; mRNA.
DR EMBL; CH471191; EAW53624.1; -; Genomic_DNA.
DR EMBL; BC001255; AAH01255.1; -; mRNA.
DR PIR; I37222; I37222.
DR PIR; S60109; S60109.
DR RefSeq; NP_001036005.1; NM_001042540.1.
DR RefSeq; NP_031388.2; NM_007362.3.
DR RefSeq; XP_005269370.1; XM_005269313.1.
DR UniGene; Hs.591671; -.
DR PDB; 1H2T; X-ray; 2.15 A; Z=1-156.
DR PDB; 1H2U; X-ray; 2.40 A; X/Y=1-156.
DR PDB; 1H2V; X-ray; 2.00 A; Z=1-156.
DR PDB; 1H6K; X-ray; 2.00 A; X/Y/Z=22-120.
DR PDB; 1N52; X-ray; 2.11 A; B=1-156.
DR PDB; 1N54; X-ray; 2.72 A; B=1-156.
DR PDB; 3FEX; X-ray; 3.55 A; B=1-156.
DR PDB; 3FEY; X-ray; 2.20 A; B=1-156.
DR PDBsum; 1H2T; -.
DR PDBsum; 1H2U; -.
DR PDBsum; 1H2V; -.
DR PDBsum; 1H6K; -.
DR PDBsum; 1N52; -.
DR PDBsum; 1N54; -.
DR PDBsum; 3FEX; -.
DR PDBsum; 3FEY; -.
DR DisProt; DP00393; -.
DR ProteinModelPortal; P52298; -.
DR SMR; P52298; 5-149.
DR DIP; DIP-33246N; -.
DR IntAct; P52298; 8.
DR MINT; MINT-248711; -.
DR STRING; 9606.ENSP00000326806; -.
DR TCDB; 9.A.60.1.1; the small nuclear rna exporter (snrna-e).
DR PhosphoSite; P52298; -.
DR DMDM; 1705651; -.
DR PaxDb; P52298; -.
DR PRIDE; P52298; -.
DR DNASU; 22916; -.
DR Ensembl; ENST00000321256; ENSP00000326806; ENSG00000114503.
DR Ensembl; ENST00000452404; ENSP00000412785; ENSG00000114503.
DR GeneID; 22916; -.
DR KEGG; hsa:22916; -.
DR UCSC; uc003fxb.1; human.
DR CTD; 22916; -.
DR GeneCards; GC03M196662; -.
DR HGNC; HGNC:7659; NCBP2.
DR HPA; HPA044850; -.
DR MIM; 605133; gene.
DR neXtProt; NX_P52298; -.
DR PharmGKB; PA31462; -.
DR eggNOG; COG0724; -.
DR HOGENOM; HOG000217589; -.
DR HOVERGEN; HBG052581; -.
DR InParanoid; P52298; -.
DR KO; K12883; -.
DR OMA; KIAPNTD; -.
DR PhylomeDB; P52298; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_1675; mRNA Processing.
DR Reactome; REACT_1788; Transcription.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR Reactome; REACT_78; Post-Elongation Processing of the Transcript.
DR ChiTaRS; NCBP2; human.
DR EvolutionaryTrace; P52298; -.
DR GenomeRNAi; 22916; -.
DR NextBio; 43603; -.
DR PRO; PR:P52298; -.
DR ArrayExpress; P52298; -.
DR Bgee; P52298; -.
DR CleanEx; HS_NCBP2; -.
DR Genevestigator; P52298; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005845; C:mRNA cap binding complex; IDA:UniProtKB.
DR GO; GO:0005846; C:nuclear cap binding complex; IEA:InterPro.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IDA:UniProtKB.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IDA:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0008334; P:histone mRNA metabolic process; TAS:Reactome.
DR GO; GO:0031124; P:mRNA 3'-end processing; TAS:Reactome.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; TAS:Reactome.
DR GO; GO:0034660; P:ncRNA metabolic process; TAS:Reactome.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:UniProtKB.
DR GO; GO:0046833; P:positive regulation of RNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0050434; P:positive regulation of viral transcription; TAS:Reactome.
DR GO; GO:0006446; P:regulation of translational initiation; IDA:UniProtKB.
DR GO; GO:0006408; P:snRNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; TAS:Reactome.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR027157; NCBP2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR18847; PTHR18847; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Direct protein sequencing; mRNA capping; mRNA processing;
KW mRNA splicing; mRNA transport; Nonsense-mediated mRNA decay; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing; Translation regulation; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 156 Nuclear cap-binding protein subunit 2.
FT /FTId=PRO_0000081499.
FT DOMAIN 40 118 RRM.
FT REGION 112 116 mRNA cap-binding.
FT REGION 123 127 mRNA cap-binding.
FT REGION 133 134 mRNA cap-binding.
FT BINDING 20 20 mRNA cap.
FT BINDING 43 43 mRNA cap.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 18 18 Phosphoserine.
FT VAR_SEQ 1 26 MSGGLLKALRSDSYVELSQYRDQHFR -> MVLRKLYA
FT (in isoform 2).
FT /FTId=VSP_038125.
FT MUTAGEN 20 20 Y->A: Abolishes mRNA cap-binding.
FT MUTAGEN 20 20 Y->F: Strongly impairs mRNA cap-binding.
FT MUTAGEN 25 25 F->A: Does not affect mRNA cap-binding.
FT MUTAGEN 43 43 Y->A: Abolishes mRNA cap-binding.
FT MUTAGEN 43 43 Y->F: Does not affect mRNA cap-binding.
FT MUTAGEN 46 46 N->A: Does not affect mRNA cap-binding.
FT MUTAGEN 83 83 F->A: Abolishes mRNA cap-binding.
FT MUTAGEN 85 85 F->A: Impairs mRNA cap-binding.
FT MUTAGEN 112 112 R->A,T: Does not affect mRNA cap-binding.
FT MUTAGEN 114 114 D->A: Does not affect mRNA cap-binding.
FT MUTAGEN 116 116 D->A: Abolishes mRNA cap-binding.
FT MUTAGEN 119 119 F->A: Does not affect mRNA cap-binding.
FT MUTAGEN 138 138 Y->A: Does not affect mRNA cap-binding.
FT CONFLICT 97 97 A -> S (in Ref. 2; BAA09599).
FT HELIX 7 10
FT HELIX 13 15
FT STRAND 23 27
FT TURN 34 38
FT STRAND 41 46
FT HELIX 53 60
FT HELIX 61 63
FT STRAND 66 73
FT TURN 75 77
FT STRAND 80 90
FT HELIX 91 100
FT TURN 101 103
FT STRAND 104 106
FT STRAND 112 117
FT TURN 121 124
FT HELIX 134 137
FT HELIX 144 146
SQ SEQUENCE 156 AA; 18001 MW; B6C94F3182A2CC3D CRC64;
MSGGLLKALR SDSYVELSQY RDQHFRGDNE EQEKLLKKSC TLYVGNLSFY TTEEQIYELF
SKSGDIKKII MGLDKMKKTA CGFCFVEYYS RADAENAMRY INGTRLDDRI IRTDWDAGFK
EGRQYGRGRS GGQVRDEYRQ DYDAGRGGYG KLAQNQ
//
MIM
605133
*RECORD*
*FIELD* NO
605133
*FIELD* TI
*605133 NUCLEAR CAP-BINDING PROTEIN 2; NCBP2
;;NUCLEAR CAP-BINDING PROTEIN, 20-KD;;
read moreCAP-BINDING PROTEIN, 20-KD; CBP20;;
NUCLEAR CAP-BINDING PROTEIN-INTERACTING PROTEIN 1; NIP1
*FIELD* TX
Monomethylated cap structures are added at the time of transcription to
RNAs transcribed by RNA polymerase II. The cap structure enhances
translation by facilitating binding of the mRNA to the ribosome in the
cytoplasm. It is also important in nuclear events, such as pre-mRNA
splicing and nuclear export of RNA, as well as in spliceosome formation.
An 80-kD nuclear cap-binding protein, NCBP1 (600469), is one factor
involved in cap-dependent nuclear processes.
CLONING
By screening a HeLa cell cDNA library using a yeast 2-hybrid interaction
trap system with NCBP1 as bait, Kataoka et al. (1995) isolated a cDNA
encoding NCBP2, which they called NIP1 (NCBP-interacting protein-1).
Izaurralde et al. (1995) isolated a cDNA encoding NCBP2, which they
called CBP20, by PCR analysis on a HeLa cell cDNA library using
oligonucleotide primers corresponding to a purified and microsequenced
20-kD cap-binding protein. Sequence analysis of the deduced 156-amino
acid NCBP2 protein, which shares 84% amino acid identity with the
Xenopus Ncbp2 protein, predicted that it contains an RNP motif with
highly conserved RNP1 and RNP2 domains. Northern blot analysis detected
a major 2.0- and a minor 0.8-kb NCBP2 transcript (Kataoka et al., 1995).
Kataoka et al. (1995) demonstrated that NCBP2 and NCBP1 bind to the cap
structure only when in complex with each other. Izaurralde et al. (1995)
showed that antibodies to NCBP1 and NCBP2 could inhibit their
interaction with capped RNAs.
BIOCHEMICAL FEATURES
Mazza et al. (2001) determined the 2-angstrom crystal structure of the
human nuclear cap-binding complex. The structure showed that the large
subunit, CBP80, has 3 domains, each containing consecutive helical
hairpins and resembling the so-called MIF4G domain found in several
other proteins involved in RNA metabolism. The small subunit, CBP20, has
an RNP fold and associates with the second and third domains of CBP80.
Site-directed mutagenesis revealed 4 residues of CBP20 that are critical
for cap binding.
*FIELD* RF
1. Izaurralde, E.; Lewis, J.; Gamberi, C.; Jarmolowski, A.; McGuigan,
C.; Mattaj, I. W.: A cap-binding protein complex mediating U snRNA
export. Nature 376: 709-712, 1995.
2. Kataoka, N.; Ohno, M.; Moda, I.; Shimura, Y.: Identification of
the factors that interact with NCBP, an 80 kDa nuclear cap binding
protein. Nucleic Acids Res. 23: 3638-3641, 1995.
3. Mazza, C.; Ohno, M.; Segref, A.; Mattaj, I. W.; Cusack, S.: Crystal
structure of the human nuclear cap binding complex. Molec. Cell 8:
383-396, 2001.
*FIELD* CN
Stylianos E. Antonarakis - updated: 10/30/2001
*FIELD* CD
Paul J. Converse: 7/12/2000
*FIELD* ED
mgross: 10/30/2001
mgross: 7/12/2000
*RECORD*
*FIELD* NO
605133
*FIELD* TI
*605133 NUCLEAR CAP-BINDING PROTEIN 2; NCBP2
;;NUCLEAR CAP-BINDING PROTEIN, 20-KD;;
read moreCAP-BINDING PROTEIN, 20-KD; CBP20;;
NUCLEAR CAP-BINDING PROTEIN-INTERACTING PROTEIN 1; NIP1
*FIELD* TX
Monomethylated cap structures are added at the time of transcription to
RNAs transcribed by RNA polymerase II. The cap structure enhances
translation by facilitating binding of the mRNA to the ribosome in the
cytoplasm. It is also important in nuclear events, such as pre-mRNA
splicing and nuclear export of RNA, as well as in spliceosome formation.
An 80-kD nuclear cap-binding protein, NCBP1 (600469), is one factor
involved in cap-dependent nuclear processes.
CLONING
By screening a HeLa cell cDNA library using a yeast 2-hybrid interaction
trap system with NCBP1 as bait, Kataoka et al. (1995) isolated a cDNA
encoding NCBP2, which they called NIP1 (NCBP-interacting protein-1).
Izaurralde et al. (1995) isolated a cDNA encoding NCBP2, which they
called CBP20, by PCR analysis on a HeLa cell cDNA library using
oligonucleotide primers corresponding to a purified and microsequenced
20-kD cap-binding protein. Sequence analysis of the deduced 156-amino
acid NCBP2 protein, which shares 84% amino acid identity with the
Xenopus Ncbp2 protein, predicted that it contains an RNP motif with
highly conserved RNP1 and RNP2 domains. Northern blot analysis detected
a major 2.0- and a minor 0.8-kb NCBP2 transcript (Kataoka et al., 1995).
Kataoka et al. (1995) demonstrated that NCBP2 and NCBP1 bind to the cap
structure only when in complex with each other. Izaurralde et al. (1995)
showed that antibodies to NCBP1 and NCBP2 could inhibit their
interaction with capped RNAs.
BIOCHEMICAL FEATURES
Mazza et al. (2001) determined the 2-angstrom crystal structure of the
human nuclear cap-binding complex. The structure showed that the large
subunit, CBP80, has 3 domains, each containing consecutive helical
hairpins and resembling the so-called MIF4G domain found in several
other proteins involved in RNA metabolism. The small subunit, CBP20, has
an RNP fold and associates with the second and third domains of CBP80.
Site-directed mutagenesis revealed 4 residues of CBP20 that are critical
for cap binding.
*FIELD* RF
1. Izaurralde, E.; Lewis, J.; Gamberi, C.; Jarmolowski, A.; McGuigan,
C.; Mattaj, I. W.: A cap-binding protein complex mediating U snRNA
export. Nature 376: 709-712, 1995.
2. Kataoka, N.; Ohno, M.; Moda, I.; Shimura, Y.: Identification of
the factors that interact with NCBP, an 80 kDa nuclear cap binding
protein. Nucleic Acids Res. 23: 3638-3641, 1995.
3. Mazza, C.; Ohno, M.; Segref, A.; Mattaj, I. W.; Cusack, S.: Crystal
structure of the human nuclear cap binding complex. Molec. Cell 8:
383-396, 2001.
*FIELD* CN
Stylianos E. Antonarakis - updated: 10/30/2001
*FIELD* CD
Paul J. Converse: 7/12/2000
*FIELD* ED
mgross: 10/30/2001
mgross: 7/12/2000