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 30-NOV-2010, entry version 47. 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 MEDLINE=20246506; 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 MASS RP SPECTROMETRY. 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 RNASEN. 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). 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 THOC4/ALY, leading to the recruitment of the mRNA CC export machinery to the 5' end of mRNA and to mRNA export in a 5' CC to 3' direction through the nuclear pore. The CBC complex is also CC involved in mediating U snRNA and intronless mRNAs export from the CC nucleus. The CBC complex is essential for a pioneer round of mRNA CC translation, before steady state translation when the CBC complex CC is replaced by cytoplasmic cap-binding protein eIF4E. The pioneer CC round of mRNA translation mediated by the CBC complex plays a CC central role in nonsense-mediated mRNA decay (NMD), NMD only CC taking place in mRNAs bound to the CBC complex, but not on eIF4E- CC bound mRNAs. The CBC complex enhances NMD in mRNAs containing at CC least one exon-junction complex (EJC) via its interaction with CC UPF1, promoting the interaction between UPF1 and UPF2. The CBC CC complex is also involved in 'failsafe' NMD, which is independent CC of the EJC complex, while it does not participate in Staufen- CC mediated mRNA decay (SMD). During cell proliferation, the CBC CC complex is also involved in microRNAs (miRNAs) biogenesis via its CC interaction with SRRT/ARS2 and is required for miRNA-mediated RNA CC interference. The CBC complex also acts as a negative regulator of CC PARN, thereby acting as an inhibitor of mRNA deadenylation. In the CC CBC complex, NCBP1/CBP80 does not bind directly capped RNAs CC (m7GpppG-capped RNA) but is required to stabilize the movement of CC the N-terminal loop of NCBP2/CBP20 and lock the CBC into a high CC 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. Heterodimer with NCBP2. Is part of the CC exon junction complex (EJC) containing NCBP1, NCBP2, RNPS1, RBM8A, CC SRRM1, NXF1, UPF3B, UPF2, THOC4 and/or REFBP2. Identified in a CC mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, CC HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, CC HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, CC PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, CC YBX1 and untranslated mRNAs. Interacts with SRRT/ARS2, EIF4G2, CC HNRNPF, IGF2BP1, HNRNPH1, KIAA0427/CTIF, PARN, RNASEN, UPF1 and CC THOC4. May interact with EIF4G1; the interaction is however CC controversial (By similarity). Found in a U snRNA export complex CC with RNUXA/PHAX, NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G- CC capped RNA. Interaction with RNUXA/PHAX. CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By CC similarity). Note=Localized in cytoplasmic mRNP granules CC containing untranslated mRNAs (By similarity). CC -!- SIMILARITY: Belongs to the NCBP1 family. CC -!- SIMILARITY: Contains 1 MIF4G domain. 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 IPI; IPI00458056; -. DR RefSeq; NP_001028373.2; NM_001033201.3. DR UniGene; Mm.389536; -. DR ProteinModelPortal; Q3UYV9; -. DR SMR; Q3UYV9; 2-790. DR STRING; Q3UYV9; -. DR PhosphoSite; Q3UYV9; -. DR PRIDE; Q3UYV9; -. DR Ensembl; ENSMUST00000030014; ENSMUSP00000030014; ENSMUSG00000028330. DR GeneID; 433702; -. DR KEGG; mmu:433702; -. DR UCSC; uc008stk.1; mouse. DR CTD; 433702; -. DR MGI; MGI:1891840; Ncbp1. DR HOGENOM; HBG378185; -. DR HOVERGEN; HBG080328; -. DR InParanoid; Q3UYV9; -. DR OMA; LICRVGE; -. DR OrthoDB; EOG95B41X; -. DR NextBio; 408905; -. DR ArrayExpress; Q3UYV9; -. DR Bgee; Q3UYV9; -. DR Genevestigator; Q3UYV9; -. DR GermOnline; ENSMUSG00000028330; Mus musculus. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0030529; C:ribonucleoprotein complex; ISS:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW. DR GO; GO:0006370; P:mRNA capping; ISS:UniProtKB. 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,...; 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 GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. DR InterPro; IPR016024; ARM-type_fold. 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 Gene3D; G3DSA:1.25.40.180; MIF4-like_typ_1/2/3; 4. 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; ARM-type_fold; 3. PE 1: Evidence at protein level; KW Acetylation; Coiled coil; Cytoplasm; mRNA capping; mRNA processing; KW mRNA splicing; mRNA transport; Nonsense-mediated mRNA decay; Nucleus; KW Phosphoprotein; RNA-mediated gene silencing; Translation regulation; KW Transport. FT CHAIN 1 790 Nuclear cap-binding protein subunit 1. FT /FTId=PRO_0000239779. FT DOMAIN 28 240 MIF4G. FT COILED 643 713 Potential. FT MOTIF 3 20 Nuclear localization signal (Potential). FT MOD_RES 7 7 Phosphoserine (By similarity). FT MOD_RES 21 21 Phosphothreonine (By similarity). FT MOD_RES 22 22 Phosphoserine. FT MOD_RES 204 204 N6-acetyllysine (By similarity). FT MOD_RES 674 674 Phosphoserine (By similarity). FT MOD_RES 698 698 N6-acetyllysine (By similarity). FT CONFLICT 319 319 H -> R (in Ref. 1; BAE22102). FT CONFLICT 443 443 S -> R (in Ref. 1; BAE22102). FT CONFLICT 453 453 L -> I (in Ref. 1; BAE22102). FT CONFLICT 574 574 K -> Q (in Ref. 1; BAE22102). 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 //