Full text data of NCBP1
NCBP1
(CBP80, NCBP)
[Confidence: low (only semi-automatic identification from reviews)]
Nuclear cap-binding protein subunit 1 (80 kDa nuclear cap-binding protein; CBP80; NCBP 80 kDa subunit)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Nuclear cap-binding protein subunit 1 (80 kDa nuclear cap-binding protein; CBP80; NCBP 80 kDa subunit)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q09161
ID NCBP1_HUMAN Reviewed; 790 AA.
AC Q09161; B2R718; Q59G76; Q5T1V0; Q5T7X2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 141.
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, NCBP;
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], PROTEIN SEQUENCE OF 119-128; 513-522 AND
RP 687-693, AND FUNCTION IN MRNA SPLICING.
RX PubMed=8069914; DOI=10.1016/0092-8674(94)90530-4;
RA Izaurralde E., Lewis J., McGuigan C., Jankowska E., Darzynkiewicz E.,
RA Mattaj I.W.;
RT "A nuclear cap binding protein complex involved in pre-mRNA
RT splicing.";
RL Cell 78:657-668(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7937105; DOI=10.1093/nar/22.19.3861;
RA Kataoka N., Ohno M., Kangawa K., Tokoro Y., Shimura Y.;
RT "Cloning of a complementary DNA encoding an 80 kilodalton nuclear cap
RT binding protein.";
RL Nucleic Acids Res. 22:3861-3865(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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].
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [7]
RP FUNCTION.
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 [8]
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 [9]
RP PHOSPHORYLATION AT SER-7; THR-21 AND SER-22, AND MUTAGENESIS OF SER-7;
RP 17-LYS-ARG-18 AND 21-THR-SER-22.
RX PubMed=10973943; DOI=10.1074/jbc.C000482200;
RA Wilson K.F., Wu W.J., Cerione R.A.;
RT "Cdc42 stimulates RNA splicing via the S6 kinase and a novel S6 kinase
RT target, the nuclear cap-binding complex.";
RL J. Biol. Chem. 275:37307-37310(2000).
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 INTERACTION WITH EIF4G1.
RX PubMed=11340157; DOI=10.1128/MCB.21.11.3632-3641.2001;
RA McKendrick L., Thompson E., Ferreira J., Morley S.J., Lewis J.D.;
RT "Interaction of eukaryotic translation initiation factor 4G with the
RT nuclear cap-binding complex provides a link between nuclear and
RT cytoplasmic functions of the m(7) guanosine cap.";
RL Mol. Cell. Biol. 21:3632-3641(2001).
RN [12]
RP FUNCTION.
RX PubMed=12093754; DOI=10.1093/emboj/cdf345;
RA Lejeune F., Ishigaki Y., Li X., Maquat L.E.;
RT "The exon junction complex is detected on CBP80-bound but not eIF4E-
RT bound mRNA in mammalian cells: dynamics of mRNP remodeling.";
RL EMBO J. 21:3536-3545(2002).
RN [13]
RP FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION, AND INTERACTION WITH
RP EIF4G1.
RX PubMed=15059963; DOI=10.1101/gad.1170204;
RA Chiu S.-Y., Lejeune F., Ranganathan A.C., Maquat L.E.;
RT "The pioneer translation initiation complex is functionally distinct
RT from but structurally overlaps with the steady-state translation
RT initiation complex.";
RL Genes Dev. 18:745-754(2004).
RN [14]
RP FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION, AND INTERACTION WITH
RP EIF4G1 AND EIF4G2.
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 [15]
RP FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, AND INTERACTION WITH UPF1.
RX PubMed=16186820; DOI=10.1038/nsmb995;
RA Hosoda N., Kim Y.K., Lejeune F., Maquat L.E.;
RT "CBP80 promotes interaction of Upf1 with Upf2 during nonsense-mediated
RT mRNA decay in mammalian cells.";
RL Nat. Struct. Mol. Biol. 12:893-901(2005).
RN [16]
RP FUNCTION IN MRNA EXPORT, AND INTERACTION WITH ALYREF/THOC4.
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 [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [18]
RP FUNCTION IN MRNA DEADENYLATION, AND INTERACTION WITH PARN.
RX PubMed=16317009; DOI=10.1074/jbc.M508590200;
RA Balatsos N.A.A., Nilsson P., Mazza C., Cusack S., Virtanen A.;
RT "Inhibition of mRNA deadenylation by the nuclear cap binding complex
RT (CBC).";
RL J. Biol. Chem. 281:4517-4522(2006).
RN [19]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [20]
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 [21]
RP INTERACTION WITH POLDIP3.
RX PubMed=18423201; DOI=10.1016/j.cell.2008.02.031;
RA Ma X.M., Yoon S.O., Richardson C.J., Julich K., Blenis J.;
RT "SKAR links pre-mRNA splicing to mTOR/S6K1-mediated enhanced
RT translation efficiency of spliced mRNAs.";
RL Cell 133:303-313(2008).
RN [22]
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 [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21 AND SER-22, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [25]
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 [26]
RP FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION, INTERACTION WITH
RP KIAA0427, AND SUBCELLULAR LOCATION.
RX PubMed=19648179; DOI=10.1101/gad.1823409;
RA Kim K.M., Cho H., Choi K., Kim J., Kim B.-W., Ko Y.-G., Jang S.K.,
RA Kim Y.K.;
RT "A new MIF4G domain-containing protein, CTIF, directs nuclear cap-
RT binding protein CBP80/20-dependent translation.";
RL Genes Dev. 23:2033-2045(2009).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND MASS
RP SPECTROMETRY.
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 [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-204 AND LYS-698, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [29]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [30]
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 [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 20-790 IN COMPLEX WITH NCBP2.
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 [33]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 20-790 IN COMPLEX WITH
RP NCBP2.
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 [34]
RP X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) IN COMPLEX WITH NCBP2.
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 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.
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 since it is reported by
CC PubMed:11340157, PubMed:15059963 and PubMed:15361857, but is not
CC observed by PubMed:19648179.
CC -!- INTERACTION:
CC P52298:NCBP2; NbExp=6; IntAct=EBI-464743, EBI-464729;
CC O95453:PARN; NbExp=2; IntAct=EBI-464743, EBI-372832;
CC Q9BY77:POLDIP3; NbExp=3; IntAct=EBI-464743, EBI-1776152;
CC P62753:RPS6; NbExp=3; IntAct=EBI-464743, EBI-356625;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Localized in
CC cytoplasmic mRNP granules containing untranslated mRNAs.
CC -!- SIMILARITY: Belongs to the NCBP1 family.
CC -!- SIMILARITY: Contains 1 MIF4G domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92470.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=CAI12863.1; Type=Erroneous gene model prediction;
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DR EMBL; X80030; CAA56334.1; -; mRNA.
DR EMBL; D32002; BAA06769.1; -; mRNA.
DR EMBL; AK312807; BAG35665.1; -; mRNA.
DR EMBL; AB209233; BAD92470.1; ALT_INIT; mRNA.
DR EMBL; AL445531; CAI15431.1; -; Genomic_DNA.
DR EMBL; AL162385; CAI15431.1; JOINED; Genomic_DNA.
DR EMBL; AL162385; CAI12861.1; -; Genomic_DNA.
DR EMBL; AL445531; CAI12861.1; JOINED; Genomic_DNA.
DR EMBL; AL162385; CAI12863.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC001450; AAH01450.1; -; mRNA.
DR PIR; S50082; S50082.
DR RefSeq; NP_002477.1; NM_002486.4.
DR UniGene; Hs.595669; -.
DR UniGene; Hs.686479; -.
DR PDB; 1H2T; X-ray; 2.15 A; C=20-790.
DR PDB; 1H2U; X-ray; 2.40 A; A/B=20-790.
DR PDB; 1H2V; X-ray; 2.00 A; C=20-790.
DR PDB; 1H6K; X-ray; 2.00 A; A/B/C=20-790.
DR PDB; 1N52; X-ray; 2.11 A; A=1-790.
DR PDB; 1N54; X-ray; 2.72 A; A=1-790.
DR PDB; 3FEX; X-ray; 3.55 A; A=1-790.
DR PDB; 3FEY; X-ray; 2.20 A; A=1-790.
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; DP00392; -.
DR ProteinModelPortal; Q09161; -.
DR SMR; Q09161; 2-790.
DR DIP; DIP-33244N; -.
DR IntAct; Q09161; 28.
DR MINT; MINT-248693; -.
DR STRING; 9606.ENSP00000364289; -.
DR TCDB; 9.A.60.1.1; the small nuclear rna exporter (snrna-e).
DR PhosphoSite; Q09161; -.
DR DMDM; 1705654; -.
DR PaxDb; Q09161; -.
DR PeptideAtlas; Q09161; -.
DR PRIDE; Q09161; -.
DR DNASU; 4686; -.
DR Ensembl; ENST00000375147; ENSP00000364289; ENSG00000136937.
DR GeneID; 4686; -.
DR KEGG; hsa:4686; -.
DR UCSC; uc004axq.3; human.
DR CTD; 4686; -.
DR GeneCards; GC09P100395; -.
DR HGNC; HGNC:7658; NCBP1.
DR MIM; 600469; gene.
DR neXtProt; NX_Q09161; -.
DR PharmGKB; PA31461; -.
DR eggNOG; NOG303489; -.
DR HOGENOM; HOG000007990; -.
DR HOVERGEN; HBG080328; -.
DR InParanoid; Q09161; -.
DR KO; K12882; -.
DR OMA; LICRVGE; -.
DR OrthoDB; EOG7K9K28; -.
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; NCBP1; human.
DR EvolutionaryTrace; Q09161; -.
DR GenomeRNAi; 4686; -.
DR NextBio; 18072; -.
DR PRO; PR:Q09161; -.
DR ArrayExpress; Q09161; -.
DR Bgee; Q09161; -.
DR CleanEx; HS_NCBP1; -.
DR Genevestigator; Q09161; -.
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; TAS:Reactome.
DR GO; GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0000339; F:RNA cap binding; TAS:ProtInc.
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; IEA:InterPro.
DR GO; GO:0006379; P:mRNA cleavage; IDA:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:UniProtKB.
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:0031442; P:positive regulation of mRNA 3'-end processing; IDA: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: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; 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 Direct protein sequencing; mRNA capping; mRNA processing;
KW mRNA splicing; mRNA transport; Nonsense-mediated mRNA decay; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-mediated gene silencing;
KW Translation regulation; Transport.
FT CHAIN 1 790 Nuclear cap-binding protein subunit 1.
FT /FTId=PRO_0000089364.
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 RPS6KB1.
FT MOD_RES 21 21 Phosphothreonine; by RPS6KB1.
FT MOD_RES 22 22 Phosphoserine; by RPS6KB1.
FT MOD_RES 204 204 N6-acetyllysine.
FT MOD_RES 698 698 N6-acetyllysine.
FT MUTAGEN 7 7 S->A: Reduced phosphorylation by RPS6KB1.
FT Abolishes phosphorylation by RPS6KB1;
FT when associated with 21-A-A-22.
FT MUTAGEN 17 18 KR->AA: Abolishes nuclear localization
FT and phosphorylation by RPS6KB1.
FT MUTAGEN 21 22 TS->A: Reduced phosphorylation by
FT RPS6KB1. Abolishes phosphorylation by
FT RPS6KB1; when associated with A-7.
FT CONFLICT 80 80 P -> S (in Ref. 3; BAG35665).
FT CONFLICT 159 159 E -> D (in Ref. 4; BAD92470).
FT CONFLICT 674 674 S -> G (in Ref. 3; BAG35665).
FT HELIX 30 36
FT TURN 37 39
FT HELIX 46 59
FT HELIX 61 78
FT HELIX 80 82
FT HELIX 83 94
FT HELIX 98 117
FT HELIX 121 136
FT STRAND 138 140
FT HELIX 142 154
FT HELIX 155 157
FT HELIX 163 174
FT HELIX 177 204
FT HELIX 211 214
FT STRAND 216 218
FT STRAND 221 223
FT HELIX 228 241
FT TURN 242 244
FT STRAND 247 249
FT HELIX 252 256
FT TURN 257 259
FT HELIX 262 264
FT HELIX 294 296
FT STRAND 298 301
FT HELIX 309 325
FT HELIX 329 337
FT HELIX 347 359
FT HELIX 369 382
FT TURN 384 386
FT HELIX 387 400
FT HELIX 402 404
FT HELIX 407 421
FT TURN 422 426
FT HELIX 430 436
FT HELIX 444 458
FT HELIX 462 468
FT HELIX 471 476
FT STRAND 488 490
FT STRAND 493 495
FT HELIX 498 509
FT HELIX 514 520
FT HELIX 521 523
FT HELIX 541 554
FT TURN 555 557
FT HELIX 559 568
FT HELIX 570 576
FT HELIX 580 594
FT HELIX 598 610
FT HELIX 616 623
FT HELIX 626 628
FT TURN 629 633
FT HELIX 635 661
FT HELIX 693 731
FT HELIX 738 753
FT HELIX 755 758
FT HELIX 759 761
FT HELIX 762 768
FT HELIX 776 787
SQ SEQUENCE 790 AA; 91839 MW; F10DE7B9D16FDA0B CRC64;
MSRRRHSDEN DGGQPHKRRK TSDANETEDH LESLICKVGE KSACSLESNL EGLAGVLEAD
LPNYKSKILR LLCTVARLLP EKLTIYTTLV GLLNARNYNF GGEFVEAMIR QLKESLKANN
YNEAVYLVRF LSDLVNCHVI AAPSMVAMFE NFVSVTQEED VPQVRRDWYV YAFLSSLPWV
GKELYEKKDA EMDRIFANTE SYLKRRQKTH VPMLQVWTAD KPHPQEEYLD CLWAQIQKLK
KDRWQERHIL RPYLAFDSIL CEALQHNLPP FTPPPHTEDS VYPMPRVIFR MFDYTDDPEG
PVMPGSHSVE RFVIEENLHC IIKSHWKERK TCAAQLVSYP GKNKIPLNYH IVEVIFAELF
QLPAPPHIDV MYTTLLIELC KLQPGSLPQV LAQATEMLYM RLDTMNTTCV DRFINWFSHH
LSNFQFRWSW EDWSDCLSQD PESPKPKFVR EVLEKCMRLS YHQRILDIVP PTFSALCPAN
PTCIYKYGDE SSNSLPGHSV ALCLAVAFKS KATNDEIFSI LKDVPNPNQD DDDDEGFSFN
PLKIEVFVQT LLHLAAKSFS HSFSALAKFH EVFKTLAESD EGKLHVLRVM FEVWRNHPQM
IAVLVDKMIR TQIVDCAAVA NWIFSSELSR DFTRLFVWEI LHSTIRKMNK HVLKIQKELE
EAKEKLARQH KRRSDDDDRS SDRKDGVLEE QIERLQEKVE SAQSEQKNLF LVIFQRFIMI
LTEHLVRCET DGTSVLTPWY KNCIERLQQI FLQHHQIIQQ YMVTLENLLF TAELDPHILA
VFQQFCALQA
//
ID NCBP1_HUMAN Reviewed; 790 AA.
AC Q09161; B2R718; Q59G76; Q5T1V0; Q5T7X2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 141.
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, NCBP;
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], PROTEIN SEQUENCE OF 119-128; 513-522 AND
RP 687-693, AND FUNCTION IN MRNA SPLICING.
RX PubMed=8069914; DOI=10.1016/0092-8674(94)90530-4;
RA Izaurralde E., Lewis J., McGuigan C., Jankowska E., Darzynkiewicz E.,
RA Mattaj I.W.;
RT "A nuclear cap binding protein complex involved in pre-mRNA
RT splicing.";
RL Cell 78:657-668(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7937105; DOI=10.1093/nar/22.19.3861;
RA Kataoka N., Ohno M., Kangawa K., Tokoro Y., Shimura Y.;
RT "Cloning of a complementary DNA encoding an 80 kilodalton nuclear cap
RT binding protein.";
RL Nucleic Acids Res. 22:3861-3865(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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].
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [7]
RP FUNCTION.
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 [8]
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 [9]
RP PHOSPHORYLATION AT SER-7; THR-21 AND SER-22, AND MUTAGENESIS OF SER-7;
RP 17-LYS-ARG-18 AND 21-THR-SER-22.
RX PubMed=10973943; DOI=10.1074/jbc.C000482200;
RA Wilson K.F., Wu W.J., Cerione R.A.;
RT "Cdc42 stimulates RNA splicing via the S6 kinase and a novel S6 kinase
RT target, the nuclear cap-binding complex.";
RL J. Biol. Chem. 275:37307-37310(2000).
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 INTERACTION WITH EIF4G1.
RX PubMed=11340157; DOI=10.1128/MCB.21.11.3632-3641.2001;
RA McKendrick L., Thompson E., Ferreira J., Morley S.J., Lewis J.D.;
RT "Interaction of eukaryotic translation initiation factor 4G with the
RT nuclear cap-binding complex provides a link between nuclear and
RT cytoplasmic functions of the m(7) guanosine cap.";
RL Mol. Cell. Biol. 21:3632-3641(2001).
RN [12]
RP FUNCTION.
RX PubMed=12093754; DOI=10.1093/emboj/cdf345;
RA Lejeune F., Ishigaki Y., Li X., Maquat L.E.;
RT "The exon junction complex is detected on CBP80-bound but not eIF4E-
RT bound mRNA in mammalian cells: dynamics of mRNP remodeling.";
RL EMBO J. 21:3536-3545(2002).
RN [13]
RP FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION, AND INTERACTION WITH
RP EIF4G1.
RX PubMed=15059963; DOI=10.1101/gad.1170204;
RA Chiu S.-Y., Lejeune F., Ranganathan A.C., Maquat L.E.;
RT "The pioneer translation initiation complex is functionally distinct
RT from but structurally overlaps with the steady-state translation
RT initiation complex.";
RL Genes Dev. 18:745-754(2004).
RN [14]
RP FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION, AND INTERACTION WITH
RP EIF4G1 AND EIF4G2.
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 [15]
RP FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, AND INTERACTION WITH UPF1.
RX PubMed=16186820; DOI=10.1038/nsmb995;
RA Hosoda N., Kim Y.K., Lejeune F., Maquat L.E.;
RT "CBP80 promotes interaction of Upf1 with Upf2 during nonsense-mediated
RT mRNA decay in mammalian cells.";
RL Nat. Struct. Mol. Biol. 12:893-901(2005).
RN [16]
RP FUNCTION IN MRNA EXPORT, AND INTERACTION WITH ALYREF/THOC4.
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 [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [18]
RP FUNCTION IN MRNA DEADENYLATION, AND INTERACTION WITH PARN.
RX PubMed=16317009; DOI=10.1074/jbc.M508590200;
RA Balatsos N.A.A., Nilsson P., Mazza C., Cusack S., Virtanen A.;
RT "Inhibition of mRNA deadenylation by the nuclear cap binding complex
RT (CBC).";
RL J. Biol. Chem. 281:4517-4522(2006).
RN [19]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [20]
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 [21]
RP INTERACTION WITH POLDIP3.
RX PubMed=18423201; DOI=10.1016/j.cell.2008.02.031;
RA Ma X.M., Yoon S.O., Richardson C.J., Julich K., Blenis J.;
RT "SKAR links pre-mRNA splicing to mTOR/S6K1-mediated enhanced
RT translation efficiency of spliced mRNAs.";
RL Cell 133:303-313(2008).
RN [22]
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 [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21 AND SER-22, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [25]
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 [26]
RP FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION, INTERACTION WITH
RP KIAA0427, AND SUBCELLULAR LOCATION.
RX PubMed=19648179; DOI=10.1101/gad.1823409;
RA Kim K.M., Cho H., Choi K., Kim J., Kim B.-W., Ko Y.-G., Jang S.K.,
RA Kim Y.K.;
RT "A new MIF4G domain-containing protein, CTIF, directs nuclear cap-
RT binding protein CBP80/20-dependent translation.";
RL Genes Dev. 23:2033-2045(2009).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND MASS
RP SPECTROMETRY.
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 [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-204 AND LYS-698, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [29]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [30]
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 [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 20-790 IN COMPLEX WITH NCBP2.
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 [33]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 20-790 IN COMPLEX WITH
RP NCBP2.
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 [34]
RP X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) IN COMPLEX WITH NCBP2.
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 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.
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 since it is reported by
CC PubMed:11340157, PubMed:15059963 and PubMed:15361857, but is not
CC observed by PubMed:19648179.
CC -!- INTERACTION:
CC P52298:NCBP2; NbExp=6; IntAct=EBI-464743, EBI-464729;
CC O95453:PARN; NbExp=2; IntAct=EBI-464743, EBI-372832;
CC Q9BY77:POLDIP3; NbExp=3; IntAct=EBI-464743, EBI-1776152;
CC P62753:RPS6; NbExp=3; IntAct=EBI-464743, EBI-356625;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Localized in
CC cytoplasmic mRNP granules containing untranslated mRNAs.
CC -!- SIMILARITY: Belongs to the NCBP1 family.
CC -!- SIMILARITY: Contains 1 MIF4G domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92470.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=CAI12863.1; Type=Erroneous gene model prediction;
CC -----------------------------------------------------------------------
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DR EMBL; X80030; CAA56334.1; -; mRNA.
DR EMBL; D32002; BAA06769.1; -; mRNA.
DR EMBL; AK312807; BAG35665.1; -; mRNA.
DR EMBL; AB209233; BAD92470.1; ALT_INIT; mRNA.
DR EMBL; AL445531; CAI15431.1; -; Genomic_DNA.
DR EMBL; AL162385; CAI15431.1; JOINED; Genomic_DNA.
DR EMBL; AL162385; CAI12861.1; -; Genomic_DNA.
DR EMBL; AL445531; CAI12861.1; JOINED; Genomic_DNA.
DR EMBL; AL162385; CAI12863.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC001450; AAH01450.1; -; mRNA.
DR PIR; S50082; S50082.
DR RefSeq; NP_002477.1; NM_002486.4.
DR UniGene; Hs.595669; -.
DR UniGene; Hs.686479; -.
DR PDB; 1H2T; X-ray; 2.15 A; C=20-790.
DR PDB; 1H2U; X-ray; 2.40 A; A/B=20-790.
DR PDB; 1H2V; X-ray; 2.00 A; C=20-790.
DR PDB; 1H6K; X-ray; 2.00 A; A/B/C=20-790.
DR PDB; 1N52; X-ray; 2.11 A; A=1-790.
DR PDB; 1N54; X-ray; 2.72 A; A=1-790.
DR PDB; 3FEX; X-ray; 3.55 A; A=1-790.
DR PDB; 3FEY; X-ray; 2.20 A; A=1-790.
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; DP00392; -.
DR ProteinModelPortal; Q09161; -.
DR SMR; Q09161; 2-790.
DR DIP; DIP-33244N; -.
DR IntAct; Q09161; 28.
DR MINT; MINT-248693; -.
DR STRING; 9606.ENSP00000364289; -.
DR TCDB; 9.A.60.1.1; the small nuclear rna exporter (snrna-e).
DR PhosphoSite; Q09161; -.
DR DMDM; 1705654; -.
DR PaxDb; Q09161; -.
DR PeptideAtlas; Q09161; -.
DR PRIDE; Q09161; -.
DR DNASU; 4686; -.
DR Ensembl; ENST00000375147; ENSP00000364289; ENSG00000136937.
DR GeneID; 4686; -.
DR KEGG; hsa:4686; -.
DR UCSC; uc004axq.3; human.
DR CTD; 4686; -.
DR GeneCards; GC09P100395; -.
DR HGNC; HGNC:7658; NCBP1.
DR MIM; 600469; gene.
DR neXtProt; NX_Q09161; -.
DR PharmGKB; PA31461; -.
DR eggNOG; NOG303489; -.
DR HOGENOM; HOG000007990; -.
DR HOVERGEN; HBG080328; -.
DR InParanoid; Q09161; -.
DR KO; K12882; -.
DR OMA; LICRVGE; -.
DR OrthoDB; EOG7K9K28; -.
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; NCBP1; human.
DR EvolutionaryTrace; Q09161; -.
DR GenomeRNAi; 4686; -.
DR NextBio; 18072; -.
DR PRO; PR:Q09161; -.
DR ArrayExpress; Q09161; -.
DR Bgee; Q09161; -.
DR CleanEx; HS_NCBP1; -.
DR Genevestigator; Q09161; -.
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; TAS:Reactome.
DR GO; GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0000339; F:RNA cap binding; TAS:ProtInc.
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; IEA:InterPro.
DR GO; GO:0006379; P:mRNA cleavage; IDA:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:UniProtKB.
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:0031442; P:positive regulation of mRNA 3'-end processing; IDA: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: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; 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 Direct protein sequencing; mRNA capping; mRNA processing;
KW mRNA splicing; mRNA transport; Nonsense-mediated mRNA decay; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-mediated gene silencing;
KW Translation regulation; Transport.
FT CHAIN 1 790 Nuclear cap-binding protein subunit 1.
FT /FTId=PRO_0000089364.
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 RPS6KB1.
FT MOD_RES 21 21 Phosphothreonine; by RPS6KB1.
FT MOD_RES 22 22 Phosphoserine; by RPS6KB1.
FT MOD_RES 204 204 N6-acetyllysine.
FT MOD_RES 698 698 N6-acetyllysine.
FT MUTAGEN 7 7 S->A: Reduced phosphorylation by RPS6KB1.
FT Abolishes phosphorylation by RPS6KB1;
FT when associated with 21-A-A-22.
FT MUTAGEN 17 18 KR->AA: Abolishes nuclear localization
FT and phosphorylation by RPS6KB1.
FT MUTAGEN 21 22 TS->A: Reduced phosphorylation by
FT RPS6KB1. Abolishes phosphorylation by
FT RPS6KB1; when associated with A-7.
FT CONFLICT 80 80 P -> S (in Ref. 3; BAG35665).
FT CONFLICT 159 159 E -> D (in Ref. 4; BAD92470).
FT CONFLICT 674 674 S -> G (in Ref. 3; BAG35665).
FT HELIX 30 36
FT TURN 37 39
FT HELIX 46 59
FT HELIX 61 78
FT HELIX 80 82
FT HELIX 83 94
FT HELIX 98 117
FT HELIX 121 136
FT STRAND 138 140
FT HELIX 142 154
FT HELIX 155 157
FT HELIX 163 174
FT HELIX 177 204
FT HELIX 211 214
FT STRAND 216 218
FT STRAND 221 223
FT HELIX 228 241
FT TURN 242 244
FT STRAND 247 249
FT HELIX 252 256
FT TURN 257 259
FT HELIX 262 264
FT HELIX 294 296
FT STRAND 298 301
FT HELIX 309 325
FT HELIX 329 337
FT HELIX 347 359
FT HELIX 369 382
FT TURN 384 386
FT HELIX 387 400
FT HELIX 402 404
FT HELIX 407 421
FT TURN 422 426
FT HELIX 430 436
FT HELIX 444 458
FT HELIX 462 468
FT HELIX 471 476
FT STRAND 488 490
FT STRAND 493 495
FT HELIX 498 509
FT HELIX 514 520
FT HELIX 521 523
FT HELIX 541 554
FT TURN 555 557
FT HELIX 559 568
FT HELIX 570 576
FT HELIX 580 594
FT HELIX 598 610
FT HELIX 616 623
FT HELIX 626 628
FT TURN 629 633
FT HELIX 635 661
FT HELIX 693 731
FT HELIX 738 753
FT HELIX 755 758
FT HELIX 759 761
FT HELIX 762 768
FT HELIX 776 787
SQ SEQUENCE 790 AA; 91839 MW; F10DE7B9D16FDA0B CRC64;
MSRRRHSDEN DGGQPHKRRK TSDANETEDH LESLICKVGE KSACSLESNL EGLAGVLEAD
LPNYKSKILR LLCTVARLLP EKLTIYTTLV GLLNARNYNF GGEFVEAMIR QLKESLKANN
YNEAVYLVRF LSDLVNCHVI AAPSMVAMFE NFVSVTQEED VPQVRRDWYV YAFLSSLPWV
GKELYEKKDA EMDRIFANTE SYLKRRQKTH VPMLQVWTAD KPHPQEEYLD CLWAQIQKLK
KDRWQERHIL RPYLAFDSIL CEALQHNLPP FTPPPHTEDS VYPMPRVIFR MFDYTDDPEG
PVMPGSHSVE RFVIEENLHC IIKSHWKERK TCAAQLVSYP GKNKIPLNYH IVEVIFAELF
QLPAPPHIDV MYTTLLIELC KLQPGSLPQV LAQATEMLYM RLDTMNTTCV DRFINWFSHH
LSNFQFRWSW EDWSDCLSQD PESPKPKFVR EVLEKCMRLS YHQRILDIVP PTFSALCPAN
PTCIYKYGDE SSNSLPGHSV ALCLAVAFKS KATNDEIFSI LKDVPNPNQD DDDDEGFSFN
PLKIEVFVQT LLHLAAKSFS HSFSALAKFH EVFKTLAESD EGKLHVLRVM FEVWRNHPQM
IAVLVDKMIR TQIVDCAAVA NWIFSSELSR DFTRLFVWEI LHSTIRKMNK HVLKIQKELE
EAKEKLARQH KRRSDDDDRS SDRKDGVLEE QIERLQEKVE SAQSEQKNLF LVIFQRFIMI
LTEHLVRCET DGTSVLTPWY KNCIERLQQI FLQHHQIIQQ YMVTLENLLF TAELDPHILA
VFQQFCALQA
//
MIM
600469
*RECORD*
*FIELD* NO
600469
*FIELD* TI
*600469 NUCLEAR CAP-BINDING PROTEIN 1; NCBP1
;;NUCLEAR CAP-BINDING PROTEIN, 80-KD;;
read moreNCBP;;
CBP80
*FIELD* TX
CLONING
Monomethylated cap structures are found on many eukaryotic mRNAs. The
cap can stimulate cytoplasmic translation by facilitating ribosome
binding to mRNA. There is also evidence that the cap can play a role in
nuclear events such as splicing, where in vitro assays indicate that it
is required for the formation of the spliceosome. Further, it has been
suggested that the cap facilitates export of RNAs transcribed by RNA
polymerase II from the nucleus to the cytoplasm. Proteins that bind to
the cap structure are likely to be involved in these processes. Kataoka
et al. (1994) described the cloning of a gene that encodes an 80-kD
nuclear cap-binding protein (NCBP) found in HeLa cell nuclear extracts
that may be involved in mRNA splicing and RNA export. Partially purified
protein was sequenced, from which PCR primers were designed and used to
isolate a cDNA from a HeLa cell library (Kataoka et al., 1994). The cDNA
encodes a predicted 790-amino acid protein. Recombinant epitope-tagged
NCBP was exclusively localized to the nucleus and the nuclear
localization activity was demonstrated to be restricted to the
N-terminal 70 amino acids (Kataoka et al., 1994). The same cDNA was also
cloned by Izaurralde et al. (1994), who noted sequence similarity to the
yeast GRC3/STO1 protein.
GENE FUNCTION
Nonsense-mediated decay (NMD) eliminates mRNAs that prematurely
terminate translation. Ishigaki et al. (2001) used antibody to CBP80 or
its cytoplasmic counterpart eIF4E (133440) to immunopurify
ribonucleoprotein (RNP) containing nonsense-free or nonsense-containing
transcripts. Data indicated that NMD takes place in association with
CBP80. The authors defined other components of NMD-susceptible mRNP as
CBP20 (605133), PABP2 (602279), eIF4G (600495), and the NMD factors UPF2
(605529) and UPF3 (see 605530). Consistent with the dependence of NMD on
translation, the NMD of CBP80-bound mRNA was blocked by cycloheximide or
suppressor tRNA. These findings provided evidence that translation can
take place in association with CBP80. They also indicated that
CBP80-bound mRNA undergoes a 'pioneer' round of translation, before
CBP80-CBP20 are replaced by eIF4E and the UPF2 and UPF3 proteins
dissociate from upstream of exon-exon junctions.
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.
MAPPING
By hybridizing to genomic DNA from a somatic cell hybrid panel, Chadwick
et al. (1996) mapped the NCBP1 gene to 9q34.1. There was no evidence for
a second locus in the human genome. Furthermore, NCBP1 hybridized to the
same cosmid as the XPA gene (611153), indicating close physical
proximity of the 2 loci. The close proximity of the 2 loci was conserved
also in the mouse, where the genes are located on chromosome 4.
*FIELD* RF
1. Chadwick, B. P.; Obermayr, F.; Frischauf, A.-M.: Nuclear cap binding
protein maps close to the xeroderma pigmentosum complementation group
A (XPA) locus in human and mouse. Genomics 35: 632-633, 1996.
2. Ishigaki, Y.; Li, X.; Serin, G.; Maquat, L. E.: Evidence for a
pioneer round of mRNA translation: mRNAs subject to nonsense-mediated
decay in mammalian cells are bound by CBP80 and CBP20. Cell 106:
607-617, 2001.
3. Izaurralde, E.; Lewis, J.; McGulian, M.; Jankowska, E.; Darzynkewicz,
E.; Mattaj, I. W.: A nuclear cap binding protein complex involved
in pre-mRNA splicing. Cell 78: 657-668, 1994.
4. Kataoka, N.; Ohno, M.; Kangawa, K.; Tokoro, Y.; Shimura, Y.: Cloning
of a complementary DNA encoding an 80 kilodalton nuclear cap binding
protein. Nucleic Acids Res. 22: 3861-3865, 1994.
5. 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
Stylianos E. Antonarakis - updated: 9/24/2001
*FIELD* CD
Victor A. McKusick: 3/27/1995
*FIELD* ED
carol: 07/12/2007
mgross: 10/30/2001
mgross: 9/24/2001
mgross: 7/12/2000
mgross: 1/18/2000
alopez: 7/31/1998
dkim: 7/30/1998
jamie: 6/3/1997
mark: 9/9/1996
terry: 8/23/1996
mark: 5/8/1995
mark: 4/4/1995
mark: 3/27/1995
*RECORD*
*FIELD* NO
600469
*FIELD* TI
*600469 NUCLEAR CAP-BINDING PROTEIN 1; NCBP1
;;NUCLEAR CAP-BINDING PROTEIN, 80-KD;;
read moreNCBP;;
CBP80
*FIELD* TX
CLONING
Monomethylated cap structures are found on many eukaryotic mRNAs. The
cap can stimulate cytoplasmic translation by facilitating ribosome
binding to mRNA. There is also evidence that the cap can play a role in
nuclear events such as splicing, where in vitro assays indicate that it
is required for the formation of the spliceosome. Further, it has been
suggested that the cap facilitates export of RNAs transcribed by RNA
polymerase II from the nucleus to the cytoplasm. Proteins that bind to
the cap structure are likely to be involved in these processes. Kataoka
et al. (1994) described the cloning of a gene that encodes an 80-kD
nuclear cap-binding protein (NCBP) found in HeLa cell nuclear extracts
that may be involved in mRNA splicing and RNA export. Partially purified
protein was sequenced, from which PCR primers were designed and used to
isolate a cDNA from a HeLa cell library (Kataoka et al., 1994). The cDNA
encodes a predicted 790-amino acid protein. Recombinant epitope-tagged
NCBP was exclusively localized to the nucleus and the nuclear
localization activity was demonstrated to be restricted to the
N-terminal 70 amino acids (Kataoka et al., 1994). The same cDNA was also
cloned by Izaurralde et al. (1994), who noted sequence similarity to the
yeast GRC3/STO1 protein.
GENE FUNCTION
Nonsense-mediated decay (NMD) eliminates mRNAs that prematurely
terminate translation. Ishigaki et al. (2001) used antibody to CBP80 or
its cytoplasmic counterpart eIF4E (133440) to immunopurify
ribonucleoprotein (RNP) containing nonsense-free or nonsense-containing
transcripts. Data indicated that NMD takes place in association with
CBP80. The authors defined other components of NMD-susceptible mRNP as
CBP20 (605133), PABP2 (602279), eIF4G (600495), and the NMD factors UPF2
(605529) and UPF3 (see 605530). Consistent with the dependence of NMD on
translation, the NMD of CBP80-bound mRNA was blocked by cycloheximide or
suppressor tRNA. These findings provided evidence that translation can
take place in association with CBP80. They also indicated that
CBP80-bound mRNA undergoes a 'pioneer' round of translation, before
CBP80-CBP20 are replaced by eIF4E and the UPF2 and UPF3 proteins
dissociate from upstream of exon-exon junctions.
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.
MAPPING
By hybridizing to genomic DNA from a somatic cell hybrid panel, Chadwick
et al. (1996) mapped the NCBP1 gene to 9q34.1. There was no evidence for
a second locus in the human genome. Furthermore, NCBP1 hybridized to the
same cosmid as the XPA gene (611153), indicating close physical
proximity of the 2 loci. The close proximity of the 2 loci was conserved
also in the mouse, where the genes are located on chromosome 4.
*FIELD* RF
1. Chadwick, B. P.; Obermayr, F.; Frischauf, A.-M.: Nuclear cap binding
protein maps close to the xeroderma pigmentosum complementation group
A (XPA) locus in human and mouse. Genomics 35: 632-633, 1996.
2. Ishigaki, Y.; Li, X.; Serin, G.; Maquat, L. E.: Evidence for a
pioneer round of mRNA translation: mRNAs subject to nonsense-mediated
decay in mammalian cells are bound by CBP80 and CBP20. Cell 106:
607-617, 2001.
3. Izaurralde, E.; Lewis, J.; McGulian, M.; Jankowska, E.; Darzynkewicz,
E.; Mattaj, I. W.: A nuclear cap binding protein complex involved
in pre-mRNA splicing. Cell 78: 657-668, 1994.
4. Kataoka, N.; Ohno, M.; Kangawa, K.; Tokoro, Y.; Shimura, Y.: Cloning
of a complementary DNA encoding an 80 kilodalton nuclear cap binding
protein. Nucleic Acids Res. 22: 3861-3865, 1994.
5. 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
Stylianos E. Antonarakis - updated: 9/24/2001
*FIELD* CD
Victor A. McKusick: 3/27/1995
*FIELD* ED
carol: 07/12/2007
mgross: 10/30/2001
mgross: 9/24/2001
mgross: 7/12/2000
mgross: 1/18/2000
alopez: 7/31/1998
dkim: 7/30/1998
jamie: 6/3/1997
mark: 9/9/1996
terry: 8/23/1996
mark: 5/8/1995
mark: 4/4/1995
mark: 3/27/1995