NCBP2_HUMAN
ID NCBP2_HUMAN Reviewed; 156 AA.
AC P52298; B2RE91; B4DMK7; E9PAR5; Q14924; Q2TS50;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Nuclear cap-binding protein subunit 2;
DE AltName: Full=20 kDa nuclear cap-binding protein;
DE AltName: Full=Cell proliferation-inducing gene 55 protein;
DE AltName: Full=NCBP 20 kDa subunit;
DE Short=CBP20;
DE AltName: Full=NCBP-interacting protein 1;
DE Short=NIP1;
GN Name=NCBP2; Synonyms=CBP20; ORFNames=PIG55;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 9-25 AND
RP 113-145.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Cervix carcinoma;
RX PubMed=7478990; DOI=10.1093/nar/23.18.3638;
RA Kataoka N., Ohno M., Moda I., Shimura Y.;
RT "Identification of the factors that interact with NCBP, an 80 kDa nuclear
RT cap binding protein.";
RL Nucleic Acids Res. 23:3638-3641(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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] (ISOFORM 1).
RA Kim J.W.;
RT "Identification of a human cell proliferation gene.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix;
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 [9]
RP SUBCELLULAR LOCATION.
RX PubMed=8601613; DOI=10.1083/jcb.133.1.5;
RA Visa N., Izaurralde E., Ferreira J., Daneholt B., Mattaj I.W.;
RT "A nuclear cap-binding complex binds Balbiani ring pre-mRNA
RT cotranscriptionally and accompanies the ribonucleoprotein particle during
RT nuclear export.";
RL J. Cell Biol. 133:5-14(1996).
RN [10]
RP INTERACTION WITH HNRNPF AND HNRNPH1.
RX PubMed=9111328; DOI=10.1128/mcb.17.5.2587;
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 [11]
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 CBP20.";
RL Cell 106:607-617(2001).
RN [12]
RP FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION, AND INTERACTION WITH EIF4G1.
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 [13]
RP FUNCTION IN MRNA EXPORT.
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 [14]
RP FUNCTION IN MRNA EXPORT, AND INTERACTION WITH ALYREF/THOC4.
RX PubMed=17363367; DOI=10.1074/jbc.m700629200;
RA Nojima T., Hirose T., Kimura H., Hagiwara M.;
RT "The interaction between cap-binding complex and RNA export factor is
RT required for intronless mRNA export.";
RL J. Biol. Chem. 282:15645-15651(2007).
RN [15]
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 eIF4E-
RT bound mRNA.";
RL Nat. Struct. Mol. Biol. 14:974-979(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [17]
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 translation
RT initiation seems to be restricted to CBP80/20-bound mRNA.";
RL EMBO Rep. 9:446-451(2008).
RN [18]
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 cell
RT proliferation.";
RL Cell 138:328-339(2009).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [20]
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., Buerckstuemmer T.,
RA 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 [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [23]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-146, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [24]
RP FUNCTION, INTERACTION WITH NCBP1; SRRT; KPNA3 AND PHAX, RNA-BINDING, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=26382858; DOI=10.1038/ncomms9192;
RA Gebhardt A., Habjan M., Benda C., Meiler A., Haas D.A., Hein M.Y., Mann A.,
RA Mann M., Habermann B., Pichlmair A.;
RT "mRNA export through an additional cap-binding complex consisting of NCBP1
RT and NCBP3.";
RL Nat. Commun. 6:8192-8192(2015).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 20-790 IN COMPLEX WITH NCBP1,
RP RNA-BINDING, AND MUTAGENESIS OF PHE-25; TYR-43; ASN-46; PHE-83; ASP-114;
RP ASP-116 AND PHE-119.
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 [26]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 20-790 IN COMPLEX WITH NCBP1 AND
RP MRNA CAP, RNA-BINDING, AND MUTAGENESIS OF TYR-20; TYR-43; ARG-112 AND
RP TYR-138.
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 the
RT human nuclear cap-binding complex.";
RL EMBO J. 21:5548-5557(2002).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) IN COMPLEX WITH NCBP1 AND MRNA CAP,
RP AND RNA-BINDING.
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 protein
RT complex.";
RL Nat. Struct. Biol. 9:912-917(2002).
CC -!- FUNCTION: Component of the cap-binding complex (CBC), which binds co-
CC transcriptionally to the 5' cap of pre-mRNAs and is involved in various
CC processes such as pre-mRNA splicing, translation regulation, nonsense-
CC mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs
CC (miRNAs) and mRNA export. The CBC complex is involved in mRNA export
CC from the nucleus via its interaction with ALYREF/THOC4/ALY, leading to
CC the recruitment of the mRNA export machinery to the 5' end of mRNA and
CC to mRNA export in a 5' to 3' direction through the nuclear pore. The
CC CBC complex is also involved in mediating U snRNA and intronless mRNAs
CC export from the nucleus. The CBC complex is essential for a pioneer
CC round 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 plays a
CC central role in nonsense-mediated mRNA decay (NMD), NMD only taking
CC place in mRNAs bound to the CBC complex, but not on eIF4E-bound mRNAs.
CC The CBC complex enhances NMD in mRNAs containing at least one exon-
CC junction complex (EJC) via its interaction with UPF1, promoting the
CC interaction between UPF1 and UPF2. The CBC complex is also involved in
CC 'failsafe' NMD, which is independent of the EJC complex, while it does
CC not participate in Staufen-mediated mRNA decay (SMD). During cell
CC proliferation, the CBC complex is also involved in microRNAs (miRNAs)
CC biogenesis via its interaction with SRRT/ARS2, thereby being required
CC for miRNA-mediated RNA interference. The CBC complex also acts as a
CC negative regulator of PARN, thereby acting as an inhibitor of mRNA
CC deadenylation. In the CBC complex, NCBP2/CBP20 recognizes and binds
CC capped RNAs (m7GpppG-capped RNA) but requires NCBP1/CBP80 to stabilize
CC the movement of its N-terminal loop and lock the CBC into a high
CC affinity cap-binding state with the cap structure. The conventional
CC cap-binding complex with NCBP2 binds both small nuclear RNA (snRNA) and
CC messenger (mRNA) and is involved in their export from the nucleus
CC (PubMed:26382858). {ECO:0000269|PubMed:11551508,
CC ECO:0000269|PubMed:15361857, ECO:0000269|PubMed:17190602,
CC ECO:0000269|PubMed:17363367, ECO:0000269|PubMed:17873884,
CC ECO:0000269|PubMed:18369367, ECO:0000269|PubMed:19632182,
CC ECO:0000269|PubMed:26382858}.
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 (PubMed:26382858). Found in a U snRNA export complex
CC with PHAX/RNUXA, NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-capped
CC RNA. Interacts with PHAX/RNUXA, EIF4G1, HNRNPF, HNRNPH1 and
CC ALYREF/THOC4/ALY. Interacts with SRRT/ARS2 and KPNA3 (PubMed:26382858).
CC {ECO:0000269|PubMed:11545740, ECO:0000269|PubMed:12374755,
CC ECO:0000269|PubMed:12434151, ECO:0000269|PubMed:15361857,
CC ECO:0000269|PubMed:17363367, ECO:0000269|PubMed:26382858,
CC ECO:0000269|PubMed:9111328}.
CC -!- INTERACTION:
CC P52298; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-464729, EBI-741037;
CC P52298; Q09161: NCBP1; NbExp=50; IntAct=EBI-464729, EBI-464743;
CC P52298-1; Q14974-1: KPNB1; NbExp=2; IntAct=EBI-15798444, EBI-15488647;
CC P52298-1; Q09161: NCBP1; NbExp=8; IntAct=EBI-15798444, EBI-464743;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8601613}. Cytoplasm
CC {ECO:0000269|PubMed:8601613}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P52298-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P52298-2; Sequence=VSP_038125;
CC Name=3;
CC IsoId=P52298-3; Sequence=VSP_053823;
CC -!- SIMILARITY: Belongs to the RRM NCBP2 family. {ECO:0000305}.
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DR EMBL; X84157; CAA58962.1; -; mRNA.
DR EMBL; D59253; BAA09599.1; -; mRNA.
DR EMBL; AK297506; BAG59919.1; -; mRNA.
DR EMBL; AK315903; BAH14274.1; -; mRNA.
DR EMBL; AK316601; BAG38188.1; -; mRNA.
DR EMBL; AY644767; AAV85455.1; -; mRNA.
DR EMBL; BT006842; AAP35488.1; -; mRNA.
DR EMBL; AC011322; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471191; EAW53624.1; -; Genomic_DNA.
DR EMBL; BC001255; AAH01255.1; -; mRNA.
DR CCDS; CCDS3323.1; -. [P52298-1]
DR CCDS; CCDS46986.1; -. [P52298-3]
DR CCDS; CCDS77878.1; -. [P52298-2]
DR PIR; I37222; I37222.
DR PIR; S60109; S60109.
DR RefSeq; NP_001036005.1; NM_001042540.1. [P52298-3]
DR RefSeq; NP_001294965.1; NM_001308036.1. [P52298-2]
DR RefSeq; NP_031388.2; NM_007362.3. [P52298-1]
DR PDB; 1H2T; X-ray; 2.15 A; Z=1-156.
DR PDB; 1H2U; X-ray; 2.40 A; X/Y=1-156.
DR PDB; 1H2V; X-ray; 2.00 A; Z=1-156.
DR PDB; 1H6K; X-ray; 2.00 A; X/Y/Z=22-120.
DR PDB; 1N52; X-ray; 2.11 A; B=1-156.
DR PDB; 1N54; X-ray; 2.72 A; B=1-156.
DR PDB; 3FEX; X-ray; 3.55 A; B=1-156.
DR PDB; 3FEY; X-ray; 2.20 A; B=1-156.
DR PDB; 5OO6; X-ray; 2.80 A; B/E/H/K/N/Q/T/W=1-156.
DR PDB; 5OOB; X-ray; 2.79 A; B/D/G/J=1-156.
DR PDB; 6D0Y; X-ray; 2.68 A; A=1-156.
DR PDB; 7ABG; EM; 7.80 A; A1=1-156.
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 PDBsum; 5OO6; -.
DR PDBsum; 5OOB; -.
DR PDBsum; 6D0Y; -.
DR PDBsum; 7ABG; -.
DR AlphaFoldDB; P52298; -.
DR SMR; P52298; -.
DR BioGRID; 116578; 111.
DR ComplexPortal; CPX-1427; Nuclear cap-binding complex.
DR CORUM; P52298; -.
DR DIP; DIP-33246N; -.
DR IntAct; P52298; 257.
DR MINT; P52298; -.
DR STRING; 9606.ENSP00000326806; -.
DR ChEMBL; CHEMBL4665589; -.
DR TCDB; 9.A.60.1.1; the small nuclear rna exporter (snrna-e).
DR GlyGen; P52298; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P52298; -.
DR PhosphoSitePlus; P52298; -.
DR SwissPalm; P52298; -.
DR BioMuta; NCBP2; -.
DR DMDM; 1705651; -.
DR EPD; P52298; -.
DR jPOST; P52298; -.
DR MassIVE; P52298; -.
DR MaxQB; P52298; -.
DR PaxDb; P52298; -.
DR PeptideAtlas; P52298; -.
DR PRIDE; P52298; -.
DR ProteomicsDB; 19067; -.
DR ProteomicsDB; 56477; -. [P52298-1]
DR ProteomicsDB; 56478; -. [P52298-2]
DR TopDownProteomics; P52298-1; -. [P52298-1]
DR Antibodypedia; 33952; 194 antibodies from 28 providers.
DR DNASU; 22916; -.
DR Ensembl; ENST00000321256.10; ENSP00000326806.5; ENSG00000114503.11. [P52298-1]
DR Ensembl; ENST00000427641.2; ENSP00000397619.2; ENSG00000114503.11. [P52298-3]
DR Ensembl; ENST00000452404.6; ENSP00000412785.2; ENSG00000114503.11. [P52298-2]
DR GeneID; 22916; -.
DR KEGG; hsa:22916; -.
DR MANE-Select; ENST00000321256.10; ENSP00000326806.5; NM_007362.5; NP_031388.2.
DR UCSC; uc003fxd.2; human. [P52298-1]
DR CTD; 22916; -.
DR DisGeNET; 22916; -.
DR GeneCards; NCBP2; -.
DR HGNC; HGNC:7659; NCBP2.
DR HPA; ENSG00000114503; Low tissue specificity.
DR MIM; 605133; gene.
DR neXtProt; NX_P52298; -.
DR OpenTargets; ENSG00000114503; -.
DR PharmGKB; PA31462; -.
DR VEuPathDB; HostDB:ENSG00000114503; -.
DR eggNOG; KOG0121; Eukaryota.
DR GeneTree; ENSGT00390000003197; -.
DR HOGENOM; CLU_070952_2_0_1; -.
DR InParanoid; P52298; -.
DR OMA; AENCMRY; -.
DR OrthoDB; 1421503at2759; -.
DR PhylomeDB; P52298; -.
DR TreeFam; TF313897; -.
DR PathwayCommons; P52298; -.
DR Reactome; R-HSA-111367; SLBP independent Processing of Histone Pre-mRNAs.
DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-HSA-113418; Formation of the Early Elongation Complex.
DR Reactome; R-HSA-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-HSA-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
DR Reactome; R-HSA-167158; Formation of the HIV-1 Early Elongation Complex.
DR Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat.
DR Reactome; R-HSA-167242; Abortive elongation of HIV-1 transcript in the absence of Tat.
DR Reactome; R-HSA-191859; snRNP Assembly.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-6803529; FGFR2 alternative splicing.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-HSA-72086; mRNA Capping.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-HSA-72187; mRNA 3'-end processing.
DR Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-HSA-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
DR Reactome; R-HSA-77595; Processing of Intronless Pre-mRNAs.
DR Reactome; R-HSA-8851708; Signaling by FGFR2 IIIa TM.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P52298; -.
DR SIGNOR; P52298; -.
DR BioGRID-ORCS; 22916; 786 hits in 1084 CRISPR screens.
DR ChiTaRS; NCBP2; human.
DR EvolutionaryTrace; P52298; -.
DR GenomeRNAi; 22916; -.
DR Pharos; P52298; Tbio.
DR PRO; PR:P52298; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P52298; protein.
DR Bgee; ENSG00000114503; Expressed in ganglionic eminence and 207 other tissues.
DR ExpressionAtlas; P52298; baseline and differential.
DR Genevisible; P52298; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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; IPI:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0034518; C:RNA cap binding complex; IMP:CAFA.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000339; F:RNA cap binding; IBA:GO_Central.
DR GO; GO:0017069; F:snRNA binding; IDA: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: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:0045292; P:mRNA cis splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; IPI:ComplexPortal.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; EXP:ComplexPortal.
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; IMP:UniProtKB.
DR GO; GO:1901409; P:positive regulation of phosphorylation of RNA polymerase II C-terminal domain; IC:ComplexPortal.
DR GO; GO:0046833; P:positive regulation of RNA export from nucleus; ISS:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0031053; P:primary miRNA processing; IC:ComplexPortal.
DR GO; GO:0006446; P:regulation of translational initiation; IDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; ISS:UniProtKB.
DR GO; GO:0006408; P:snRNA export from nucleus; ISS:UniProtKB.
DR CDD; cd12240; RRM_NCBP2; 1.
DR DisProt; DP00393; -.
DR Gene3D; 3.30.70.330; -; 1.
DR IDEAL; IID00238; -.
DR InterPro; IPR027157; NCBP2.
DR InterPro; IPR034148; NCBP2_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR18847; PTHR18847; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Methylation; mRNA processing; mRNA splicing;
KW mRNA transport; Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; RNA-mediated gene silencing;
KW Translation regulation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..156
FT /note="Nuclear cap-binding protein subunit 2"
FT /id="PRO_0000081499"
FT DOMAIN 40..118
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 124..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 20
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000269|PubMed:12374755,
FT ECO:0000269|PubMed:12434151"
FT BINDING 43
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000269|PubMed:12374755,
FT ECO:0000269|PubMed:12434151"
FT BINDING 112..116
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT BINDING 123..127
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT BINDING 133..134
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 146
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 1..26
FT /note="MSGGLLKALRSDSYVELSQYRDQHFR -> MVLRKLYA (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038125"
FT VAR_SEQ 40..93
FT /note="CTLYVGNLSFYTTEEQIYELFSKSGDIKKIIMGLDKMKKTACGFCFVEYYSR
FT AD -> Y (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_053823"
FT MUTAGEN 20
FT /note="Y->A: Abolishes mRNA cap-binding."
FT /evidence="ECO:0000269|PubMed:12374755"
FT MUTAGEN 20
FT /note="Y->F: Strongly impairs mRNA cap-binding."
FT /evidence="ECO:0000269|PubMed:12374755"
FT MUTAGEN 25
FT /note="F->A: Does not affect mRNA cap-binding."
FT /evidence="ECO:0000269|PubMed:11545740"
FT MUTAGEN 43
FT /note="Y->A: Abolishes mRNA cap-binding."
FT /evidence="ECO:0000269|PubMed:11545740,
FT ECO:0000269|PubMed:12374755"
FT MUTAGEN 43
FT /note="Y->F: Does not affect mRNA cap-binding."
FT /evidence="ECO:0000269|PubMed:11545740,
FT ECO:0000269|PubMed:12374755"
FT MUTAGEN 46
FT /note="N->A: Does not affect mRNA cap-binding."
FT /evidence="ECO:0000269|PubMed:11545740"
FT MUTAGEN 83
FT /note="F->A: Abolishes mRNA cap-binding."
FT /evidence="ECO:0000269|PubMed:11545740"
FT MUTAGEN 85
FT /note="F->A: Impairs mRNA cap-binding."
FT MUTAGEN 112
FT /note="R->A,T: Does not affect mRNA cap-binding."
FT /evidence="ECO:0000269|PubMed:12374755"
FT MUTAGEN 114
FT /note="D->A: Does not affect mRNA cap-binding."
FT /evidence="ECO:0000269|PubMed:11545740"
FT MUTAGEN 116
FT /note="D->A: Abolishes mRNA cap-binding."
FT /evidence="ECO:0000269|PubMed:11545740"
FT MUTAGEN 119
FT /note="F->A: Does not affect mRNA cap-binding."
FT /evidence="ECO:0000269|PubMed:11545740"
FT MUTAGEN 138
FT /note="Y->A: Does not affect mRNA cap-binding."
FT /evidence="ECO:0000269|PubMed:12374755"
FT CONFLICT 97
FT /note="A -> S (in Ref. 2; BAA09599)"
FT /evidence="ECO:0000305"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:1H2T"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1H2T"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:6D0Y"
FT TURN 34..38
FT /evidence="ECO:0007829|PDB:1H2V"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 53..60
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:1H2V"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:1H2V"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:1H2V"
FT STRAND 80..90
FT /evidence="ECO:0007829|PDB:1H2V"
FT HELIX 91..100
FT /evidence="ECO:0007829|PDB:1H2V"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:1H2V"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:1H2V"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:1H2V"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:1H2T"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:1H2T"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1H2T"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:5OOB"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:5OOB"
SQ SEQUENCE 156 AA; 18001 MW; B6C94F3182A2CC3D CRC64;
MSGGLLKALR SDSYVELSQY RDQHFRGDNE EQEKLLKKSC TLYVGNLSFY TTEEQIYELF
SKSGDIKKII MGLDKMKKTA CGFCFVEYYS RADAENAMRY INGTRLDDRI IRTDWDAGFK
EGRQYGRGRS GGQVRDEYRQ DYDAGRGGYG KLAQNQ
