ID NCBP1_MOUSE Reviewed; 790 AA. AC Q3UYV9; B1AWH4; Q3TEM1; Q7TNE8; DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 13-JUN-2006, sequence version 2. DT 24-JUN-2015, entry version 87. DE RecName: Full=Nuclear cap-binding protein subunit 1; DE AltName: Full=80 kDa nuclear cap-binding protein; DE Short=CBP80; DE Short=NCBP 80 kDa subunit; GN Name=Ncbp1; Synonyms=Cbp80; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Testis, and Thymus; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; 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 [5] RP IDENTIFICATION IN A U SNRNA EXPORT COMPLEX WITH RNUXA/PHAX; NCBP2; RP RAN; 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 RT regulated by phosphorylation."; RL Cell 101:187-198(2000). RN [6] RP INTERACTION WITH RNUXA/PHAX. RX PubMed=11333016; DOI=10.1017/S1355838201002278; RA Segref A., Mattaj I.W., Ohno M.; RT "The evolutionarily conserved region of the U snRNA export mediator RT PHAX is a novel RNA-binding domain that is essential for U snRNA RT export."; RL RNA 7:351-360(2001). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION RP 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 [8] RP FUNCTION IN MIRNAS BIOGENESIS, AND INTERACTION WITH SRRT AND DROSHA. 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 [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [10] RP IDENTIFICATION IN A LARGE PER COMPLEX, AND SUBCELLULAR LOCATION. RX PubMed=22767893; DOI=10.1126/science.1221592; RA Padmanabhan K., Robles M.S., Westerling T., Weitz C.J.; RT "Feedback regulation of transcriptional termination by the mammalian RT circadian clock PERIOD complex."; RL Science 337:599-602(2012). CC -!- FUNCTION: Component of the cap-binding complex (CBC), which binds CC cotranscriptionally 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 and is required for miRNA-mediated CC 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, NCBP1/CBP80 does not bind CC directly capped RNAs (m7GpppG-capped RNA) but is required to CC stabilize the movement of the N-terminal loop of NCBP2/CBP20 and CC lock the CBC into a high affinity cap-binding state with the cap CC structure. {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 CC with m7GpppG-capped RNA. Found in a U snRNA export complex CC containing RNUXA/PHAX, NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and CC m7G-capped RNA. Identified in a IGF2BP1-dependent mRNP granule CC complex containing untranslated mRNAs. Interacts with RNUXA/PHAX, CC SRRT/ARS2, EIF4G2, IGF2BP1, HNRNPF, HNRNPH1, KIAA0427/CTIF, PARN, CC DROSHA, UPF1 and ALYREF/THOC4. May interact with EIF4G1; the CC interaction is however controversial. The large PER complex CC involved in the repression of transcriptional termination is CC composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A CC (active). {ECO:0000269|PubMed:10786834, CC ECO:0000269|PubMed:11333016, ECO:0000269|PubMed:19632182, CC ECO:0000269|PubMed:22767893}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22767893}. CC Cytoplasm {ECO:0000250}. Note=Localized in cytoplasmic mRNP CC granules containing untranslated mRNAs. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the NCBP1 family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 MIF4G domain. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK134334; BAE22102.1; -; mRNA. DR EMBL; AK169557; BAE41227.1; -; mRNA. DR EMBL; AL929438; CAM14995.1; -; Genomic_DNA. DR EMBL; AL732615; CAM14995.1; JOINED; Genomic_DNA. DR EMBL; AL732615; CAM17033.1; -; Genomic_DNA. DR EMBL; AL929438; CAM17033.1; JOINED; Genomic_DNA. DR EMBL; CH466565; EDL02380.1; -; Genomic_DNA. DR EMBL; BC055777; AAH55777.1; -; mRNA. DR EMBL; BC138898; AAI38899.1; -; mRNA. DR CCDS; CCDS18145.1; -. DR RefSeq; NP_001028373.2; NM_001033201.3. DR UniGene; Mm.389536; -. DR PDB; 3UKZ; X-ray; 2.30 A; C=1-23. DR PDB; 3UL0; X-ray; 2.00 A; C=1-23. DR PDBsum; 3UKZ; -. DR PDBsum; 3UL0; -. DR ProteinModelPortal; Q3UYV9; -. DR SMR; Q3UYV9; 2-790. DR BioGrid; 241386; 1. DR STRING; 10090.ENSMUSP00000030014; -. DR PhosphoSite; Q3UYV9; -. DR MaxQB; Q3UYV9; -. DR PaxDb; Q3UYV9; -. DR PRIDE; Q3UYV9; -. DR Ensembl; ENSMUST00000030014; ENSMUSP00000030014; ENSMUSG00000028330. DR GeneID; 433702; -. DR KEGG; mmu:433702; -. DR UCSC; uc008stk.1; mouse. DR CTD; 4686; -. DR MGI; MGI:1891840; Ncbp1. DR eggNOG; NOG303489; -. DR GeneTree; ENSGT00390000001733; -. DR HOGENOM; HOG000007990; -. DR HOVERGEN; HBG080328; -. DR InParanoid; Q3UYV9; -. DR KO; K12882; -. DR OMA; IMLLTEH; -. DR OrthoDB; EOG7K9K28; -. DR PhylomeDB; Q3UYV9; -. DR TreeFam; TF313400; -. DR Reactome; REACT_271571; mRNA Splicing - Minor Pathway. DR Reactome; REACT_278946; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs. DR Reactome; REACT_279505; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC). DR Reactome; REACT_282911; RNA Polymerase II Pre-transcription Events. DR Reactome; REACT_291263; mRNA 3'-end processing. DR Reactome; REACT_302277; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC). DR Reactome; REACT_305017; Processing of Intronless Pre-mRNAs. DR Reactome; REACT_307866; mRNA Splicing - Major Pathway. DR Reactome; REACT_308057; Formation of the Early Elongation Complex. DR Reactome; REACT_321120; Transport of Mature mRNA derived from an Intron-Containing Transcript. DR Reactome; REACT_326102; Formation of RNA Pol II elongation complex. DR Reactome; REACT_328741; Transport of Mature mRNA Derived from an Intronless Transcript. DR Reactome; REACT_333207; snRNP Assembly. DR Reactome; REACT_338828; mRNA Capping. DR Reactome; REACT_340895; Processing of Capped Intron-Containing Pre-mRNA. DR Reactome; REACT_343355; SLBP independent Processing of Histone Pre-mRNAs. DR Reactome; REACT_347720; Transport of the SLBP independent Mature mRNA. DR Reactome; REACT_351784; Cleavage of Growing Transcript in the Termination Region. DR Reactome; REACT_353355; Transport of the SLBP Dependant Mature mRNA. DR ChiTaRS; Ncbp1; mouse. DR NextBio; 408905; -. DR PRO; PR:Q3UYV9; -. DR Proteomes; UP000000589; Chromosome 4. DR Bgee; Q3UYV9; -. DR Genevisible; Q3UYV9; MM. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005739; C:mitochondrion; ISO:MGI. DR GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB. DR GO; GO:0005846; C:nuclear cap binding complex; IEA:InterPro. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0030529; C:ribonucleoprotein complex; ISS:UniProtKB. DR GO; GO:0044822; F:poly(A) RNA binding; ISO:MGI. DR GO; GO:0000339; F:RNA cap binding; IEA:InterPro. DR GO; GO:0006370; P:7-methylguanosine mRNA capping; ISS:UniProtKB. DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW. DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:InterPro. DR GO; GO:0006379; P:mRNA cleavage; ISS:UniProtKB. DR GO; GO:0006406; P:mRNA export from nucleus; ISS:UniProtKB. 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; ISS:UniProtKB. DR GO; GO:0006446; P:regulation of translational initiation; ISS:UniProtKB. DR Gene3D; 1.25.40.180; -; 4. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR027159; CBP80. DR InterPro; IPR016021; MIF4-like_typ_1/2/3. DR InterPro; IPR015172; MIF4G-like_typ-1. DR InterPro; IPR015174; MIF4G-like_typ-2. DR InterPro; IPR003890; MIF4G-like_typ-3. DR PANTHER; PTHR12412; PTHR12412; 1. DR Pfam; PF02854; MIF4G; 1. DR Pfam; PF09088; MIF4G_like; 1. DR Pfam; PF09090; MIF4G_like_2; 1. DR SMART; SM00543; MIF4G; 1. DR SUPFAM; SSF48371; SSF48371; 3. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Coiled coil; Complete proteome; Cytoplasm; KW mRNA capping; mRNA processing; mRNA splicing; mRNA transport; KW Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein; KW Reference proteome; RNA-mediated gene silencing; KW Translation regulation; Transport. FT CHAIN 1 790 Nuclear cap-binding protein subunit 1. FT /FTId=PRO_0000239779. FT DOMAIN 28 240 MIF4G. FT COILED 643 713 {ECO:0000255}. FT MOTIF 3 20 Nuclear localization signal. FT {ECO:0000255}. FT MOD_RES 7 7 Phosphoserine. FT {ECO:0000250|UniProtKB:Q09161}. FT MOD_RES 21 21 Phosphothreonine. FT {ECO:0000250|UniProtKB:Q09161}. FT MOD_RES 22 22 Phosphoserine. FT {ECO:0000269|PubMed:17242355}. FT MOD_RES 204 204 N6-acetyllysine. FT {ECO:0000250|UniProtKB:Q09161}. FT MOD_RES 698 698 N6-acetyllysine. FT {ECO:0000250|UniProtKB:Q09161}. FT CONFLICT 319 319 H -> R (in Ref. 1; BAE22102). FT {ECO:0000305}. FT CONFLICT 443 443 S -> R (in Ref. 1; BAE22102). FT {ECO:0000305}. FT CONFLICT 453 453 L -> I (in Ref. 1; BAE22102). FT {ECO:0000305}. FT CONFLICT 574 574 K -> Q (in Ref. 1; BAE22102). FT {ECO:0000305}. SQ SEQUENCE 790 AA; 91927 MW; BE27F89BDBC19CF2 CRC64; MSRRRHSYEN DGGQPHKRRK TSDANETEDH LESLICKVGE KSACSLESNL EGLAGVLEAD LPNYKSKILR LLCTVARLLP EKLTIYTTLV GLLNARNYNF GGEFVEAMIR QLKESLKANN YNEAVYLVRF LSDLVNCHVI AAPSMVAMFE NFVSVTQEED VPQVRRDWYV YAFLSSLPWV GKELYEKKDA EMDRIFSTTE SYLKRRQKTH VPMLQVWTAD KPHPQEEYLD CLWAQIQKLK KDRWQERHIL RPYLAFDSIL CEALQHNLPP FTPPPHTEDS VYPMPRVIFR MFDYTDDPEG PVMPGSHSVE RFVIEENLHC IIKSYWKERK TCAAQLVSYP GKNKIPLNYH IVEVIFAELF QLPAPPHIDV MYTTLLIELC KLQPGSLPQV LAQATEMLYM RLDTMSTTCV DRFINWFSHH LSNFQFRWSW EDWSDCLTQD LESPKPKFVR EVLEKCMRLS YHQHILDIVP PTFSALCPAN PTCIYKYGDE SSNSLPGHSV ALCLSVAFKS KATNDEIFSI LKDVPNPNQV DDDDEGFRFN PLKIEVFVQT LLHLAAKSFS HSFSALAKFH EVFKTLAESD KGKLHVLRVM FEVWRNHPQM IAVLVDKMIR TQIVDCAAVA NWIFSSELSR DFTRLFVWEI LHSTIRKMNK HVLKIQKELE EAKEKLARQH KRRSDDDDRS SDRKDGALEE QIERLQEKVE AAQSEQKNLF LVIFQRFIMI LTEHLVRCET DGTSILTPWY KNCIERLQQI FLQHHQTIQQ YMVTLENLLF TAELDPHILA VFQQFCALQA //