ID NCBP1_MOUSE Reviewed; 790 AA. AC Q3UYV9; Q7TNE8; DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 13-JUN-2006, sequence version 2. DT 10-JUN-2008, entry version 25. DE Nuclear cap-binding protein subunit 1 (80 kDa nuclear cap-binding DE protein) (NCBP 80 kDa subunit) (CBP80). GN Name=Ncbp1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Testis; 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 MRNA] OF 79-790. 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 [3] 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 [4] 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 [5] 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). CC -!- FUNCTION: Involved in mediating U snRNA export from the nucleus. CC Binds to 5' capped mRNA (By similarity). CC -!- SUBUNIT: Heterodimer with NCBP2. Is part of the exon junction CC complex (EJC) containing NCBP1, NCBP2, RNPS1, RBM8A, SRRM1, NXF1, CC UPF3B, UPF2, THOC4 and/or REFBP2 (By similarity). Found in a U CC snRNA export complex with RNUXA/PHAX, NCBP1, NCBP2, RAN, XPO1 and CC m7G-capped RNA. Interaction with RNUXA/PHAX. CC -!- SUBCELLULAR LOCATION: Nucleus (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; BC055777; AAH55777.1; -; mRNA. DR RefSeq; NP_001028373.2; -. DR UniGene; Mm.389536; -. DR HSSP; Q09161; 1N52. DR SMR; Q3UYV9; 29-790. DR PhosphoSite; Q3UYV9; -. DR Ensembl; ENSMUSG00000028330; Mus musculus. DR GeneID; 433702; -. DR KEGG; mmu:433702; -. DR MGI; MGI:1891840; Ncbp1. DR HOVERGEN; Q3UYV9; -. DR ArrayExpress; Q3UYV9; -. DR GermOnline; ENSMUSG00000028330; Mus musculus. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005515; F:protein binding; ISS:UniProtKB. DR GO; GO:0006379; P:mRNA cleavage; ISS:UniProtKB. DR GO; GO:0031442; P:positive regulation of mRNA 3'-end processing; ISS:UniProtKB. 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; 3. DR Pfam; PF02854; MIF4G; 1. DR Pfam; PF09088; MIF4G_like; 1. DR Pfam; PF09090; MIF4G_like_2; 1. DR SMART; SM00543; MIF4G; 1. PE 1: Evidence at protein level; KW Coiled coil; mRNA transport; Nucleus; Phosphoprotein; RNA-binding; 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 21 21 Phosphothreonine (By similarity). FT MOD_RES 22 22 Phosphoserine. FT MOD_RES 674 674 Phosphoserine (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 //