NCBP1_MOUSE
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 03-AUG-2022, entry version 132.
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; 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=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., 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].
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., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT 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/6J; 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION IN A U SNRNA EXPORT COMPLEX WITH PHAX/RNUXA; NCBP2; 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 [6]
RP INTERACTION WITH PHAX/RNUXA.
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 PHAX is
RT a novel RNA-binding domain that is essential for U snRNA export.";
RL RNA 7:351-360(2001).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION BY
RP 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 cell
RT 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21 AND SER-22, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC 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 [11]
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).
RN [12]
RP INTERACTION WITH TASOR, AND TISSUE SPECIFICITY.
RX PubMed=31112734; DOI=10.1016/j.yexcr.2019.05.018;
RA Gresakova V., Novosadova V., Prochazkova M., Bhargava S., Jenickova I.,
RA Prochazka J., Sedlacek R.;
RT "Fam208a orchestrates interaction protein network essential for early
RT embryonic development and cell division.";
RL Exp. Cell Res. 382:111437-111437(2019).
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 regulation,
CC nonsense-mediated mRNA decay, RNA-mediated gene silencing (RNAi) by
CC microRNAs (miRNAs) and mRNA export. The CBC complex is involved in mRNA
CC export from the nucleus via its interaction with ALYREF/THOC4/ALY,
CC leading to the recruitment of the mRNA export machinery to the 5'-end
CC of mRNA and to mRNA export in a 5' to 3' direction through the nuclear
CC pore. The CBC complex is also involved in mediating U snRNA and
CC intronless mRNAs export from the nucleus. The CBC complex is essential
CC for a pioneer round of mRNA translation, before steady state
CC translation when the CBC complex is replaced by cytoplasmic cap-binding
CC protein eIF4E. The pioneer round of mRNA translation mediated by the
CC CBC complex plays a central role in nonsense-mediated mRNA decay (NMD),
CC NMD only taking place in mRNAs bound to the CBC complex, but not on
CC eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs containing at
CC least one exon-junction complex (EJC) via its interaction with UPF1,
CC promoting the interaction between UPF1 and UPF2. The CBC complex is
CC also involved in 'failsafe' NMD, which is independent of the EJC
CC complex, while it does not participate in Staufen-mediated mRNA decay
CC (SMD). During cell proliferation, the CBC complex is also involved in
CC microRNAs (miRNAs) biogenesis via its interaction with SRRT/ARS2 and is
CC required for miRNA-mediated RNA interference. The CBC complex also acts
CC as a negative regulator of PARN, thereby acting as an inhibitor of mRNA
CC deadenylation. In the CBC complex, NCBP1/CBP80 does not bind directly
CC capped RNAs (m7GpppG-capped RNA) but is required to stabilize the
CC movement of the N-terminal loop of NCBP2/CBP20 and lock the CBC into a
CC high affinity cap-binding state with the cap structure. Associates with
CC NCBP3 to form an alternative cap-binding complex (CBC) which plays a
CC key role in mRNA export and is particularly important in cellular
CC stress situations such as virus infections. The conventional CBC with
CC NCBP2 binds both small nuclear RNA (snRNA) and messenger (mRNA) and is
CC involved in their export from the nucleus whereas the alternative CBC
CC with NCBP3 does not bind snRNA and associates only with mRNA thereby
CC playing a role only in mRNA export. NCBP1/CBP80 is required for cell
CC growth and viability (By similarity). {ECO:0000250|UniProtKB:Q09161,
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. Found in a U snRNA export complex containing
CC PHAX/RNUXA, NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-capped RNA.
CC Identified in a IGF2BP1-dependent mRNP granule complex containing
CC untranslated mRNAs. Interacts with PHAX/RNUXA, SRRT/ARS2, EIF4G2,
CC IGF2BP1, HNRNPF, HNRNPH1, KIAA0427/CTIF, PARN, DROSHA, UPF1 and
CC ALYREF/THOC4. May interact with EIF4G1; the interaction is however
CC controversial. The large PER complex involved in the repression of
CC transcriptional termination is composed of at least PER2, CDK9, DDX5,
CC DHX9, NCBP1/CBP80 and POLR2A (active). Component of an alternative
CC nuclear cap-binding complex (CBC) composed of NCBP1/CBP80 and NCBP3 (By
CC similarity). Interacts with METTL3 (By similarity). Interacts with
CC ZFC3H1 in a RNase-insensitive manner (By similarity). Interacts with
CC MTREX (By similarity). Interacts with TASOR (PubMed:31112734).
CC Interacts with DHX34; the interaction is RNA-dependent (By similarity).
CC {ECO:0000250|UniProtKB:Q09161, ECO:0000269|PubMed:10786834,
CC ECO:0000269|PubMed:11333016, ECO:0000269|PubMed:19632182,
CC ECO:0000269|PubMed:22767893, ECO:0000269|PubMed:31112734}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22767893}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q09161}. Note=Localized in cytoplasmic mRNP
CC granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:Q09161}.
CC -!- TISSUE SPECIFICITY: Expressed in the spermatogonia, spermatocytes and
CC granular cells within the cerebellum. {ECO:0000269|PubMed:31112734}.
CC -!- SIMILARITY: Belongs to the NCBP1 family. {ECO:0000305}.
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DR EMBL; AK134334; BAE22102.1; -; mRNA.
DR EMBL; AK169557; BAE41227.1; -; mRNA.
DR EMBL; AL732615; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL929438; -; NOT_ANNOTATED_CDS; 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 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 AlphaFoldDB; Q3UYV9; -.
DR SMR; Q3UYV9; -.
DR BioGRID; 241386; 43.
DR ComplexPortal; CPX-3661; Alternative nuclear cap-binding complex.
DR ComplexPortal; CPX-923; Nuclear cap-binding complex.
DR STRING; 10090.ENSMUSP00000030014; -.
DR iPTMnet; Q3UYV9; -.
DR PhosphoSitePlus; Q3UYV9; -.
DR SwissPalm; Q3UYV9; -.
DR EPD; Q3UYV9; -.
DR jPOST; Q3UYV9; -.
DR MaxQB; Q3UYV9; -.
DR PaxDb; Q3UYV9; -.
DR PeptideAtlas; Q3UYV9; -.
DR PRIDE; Q3UYV9; -.
DR ProteomicsDB; 252647; -.
DR Antibodypedia; 28868; 241 antibodies from 33 providers.
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 VEuPathDB; HostDB:ENSMUSG00000028330; -.
DR eggNOG; KOG1104; Eukaryota.
DR GeneTree; ENSGT00390000001733; -.
DR HOGENOM; CLU_013207_0_0_1; -.
DR InParanoid; Q3UYV9; -.
DR OMA; QPFKIPF; -.
DR OrthoDB; 270650at2759; -.
DR PhylomeDB; Q3UYV9; -.
DR TreeFam; TF313400; -.
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; 433702; 30 hits in 72 CRISPR screens.
DR ChiTaRS; Ncbp1; mouse.
DR PRO; PR:Q3UYV9; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q3UYV9; protein.
DR Bgee; ENSMUSG00000028330; Expressed in spermatid and 255 other tissues.
DR Genevisible; Q3UYV9; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; 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; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0034518; C:RNA cap binding complex; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; ISO:MGI.
DR GO; GO:0000339; F:RNA cap binding; IBA:GO_Central.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; 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:0051607; P:defense response to virus; ISO:MGI.
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:0006406; P:mRNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:ComplexPortal.
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:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0031442; P:positive regulation of mRNA 3'-end processing; ISS:UniProtKB.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; ISO:MGI.
DR GO; GO:1901409; P:positive regulation of phosphorylation of RNA polymerase II C-terminal domain; IC:ComplexPortal.
DR GO; GO:1905216; P:positive regulation of RNA binding; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0031053; P:primary miRNA processing; IC:ComplexPortal.
DR GO; GO:0050684; P:regulation of mRNA processing; IBA:GO_Central.
DR GO; GO:0006446; P:regulation of translational initiation; ISS:UniProtKB.
DR GO; GO:0006401; P:RNA catabolic process; ISO:MGI.
DR GO; GO:0006408; P:snRNA export from nucleus; ISO:MGI.
DR GO; GO:0000245; P:spliceosomal complex assembly; ISO:MGI.
DR IDEAL; IID50179; -.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR027159; CBP80.
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; Cytoplasm; Isopeptide bond;
KW mRNA capping; mRNA processing; mRNA splicing; mRNA transport;
KW Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-mediated gene silencing; Translation regulation; Transport;
KW Ubl conjugation.
FT CHAIN 1..790
FT /note="Nuclear cap-binding protein subunit 1"
FT /id="PRO_0000239779"
FT DOMAIN 28..240
FT /note="MIF4G"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 643..713
FT /evidence="ECO:0000255"
FT MOTIF 3..20
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q09161"
FT MOD_RES 21
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q09161"
FT MOD_RES 204
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q09161"
FT MOD_RES 698
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q09161"
FT CROSSLNK 684
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q09161"
FT CONFLICT 319
FT /note="H -> R (in Ref. 1; BAE22102)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="S -> R (in Ref. 1; BAE22102)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="L -> I (in Ref. 1; BAE22102)"
FT /evidence="ECO:0000305"
FT CONFLICT 574
FT /note="K -> Q (in Ref. 1; BAE22102)"
FT /evidence="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
