(data stored in SCRATCH zone)

SWISSPROT: 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   05-JUL-2017, entry version 180.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 9-25
RP   AND 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
RT   nuclear 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.,
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] (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
RT   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.,
RA   Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA   Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA   Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA   Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA   Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA   Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA   Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA   Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA   Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA   Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA   Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA   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.,
RA   Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA   Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA   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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: 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
RT   during 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
RT   CBP20.";
RL   Cell 106:607-617(2001).
RN   [12]
RP   FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION, AND INTERACTION WITH
RP   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
RT   eIF4E-bound mRNA.";
RL   Nat. Struct. Mol. Biol. 14:974-979(2007).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION
RP   BY 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,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., 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
RT   translation initiation seems to be restricted to CBP80/20-bound
RT   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
RT   cell 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.,
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   [21]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [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.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal 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
RP   BY 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
RP   MASS 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.,
RA   Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
RA   Vemulapalli V., 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,
RP   AND 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.,
RA   Mann A., Mann M., Habermann B., Pichlmair A.;
RT   "mRNA export through an additional cap-binding complex consisting of
RT   NCBP1 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;
RP   ASP-114; 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
RP   AND MRNA CAP, RNA-BINDING, AND MUTAGENESIS OF TYR-20; TYR-43; ARG-112
RP   AND 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
RT   the 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
RP   CAP, 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
RT   protein complex.";
RL   Nat. Struct. Biol. 9:912-917(2002).
CC   -!- FUNCTION: Component of the cap-binding complex (CBC), which binds
CC       co-transcriptionally to the 5' cap of pre-mRNAs and is involved in
CC       various processes such as pre-mRNA splicing, translation
CC       regulation, nonsense-mediated mRNA decay, RNA-mediated gene
CC       silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC
CC       complex is involved in mRNA export from the nucleus via its
CC       interaction with 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, thereby being required for miRNA-
CC       mediated 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, NCBP2/CBP20 recognizes and
CC       binds capped RNAs (m7GpppG-capped RNA) but requires NCBP1/CBP80 to
CC       stabilize the movement of its N-terminal loop and lock the CBC
CC       into a high affinity cap-binding state with the cap structure. The
CC       conventional cap-binding complex with NCBP2 binds both small
CC       nuclear RNA (snRNA) and messenger (mRNA) and is involved in their
CC       export from the nucleus (PubMed:26382858).
CC       {ECO:0000269|PubMed:11551508, ECO:0000269|PubMed:15361857,
CC       ECO:0000269|PubMed:17190602, ECO:0000269|PubMed:17363367,
CC       ECO:0000269|PubMed:17873884, ECO:0000269|PubMed:18369367,
CC       ECO:0000269|PubMed:19632182, 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
CC       with m7GpppG-capped RNA (PubMed:26382858). Found in a U snRNA
CC       export complex with PHAX/RNUXA, NCBP1/CBP80, NCBP2/CBP20, RAN,
CC       XPO1 and m7G-capped RNA. Interacts with PHAX/RNUXA, EIF4G1,
CC       HNRNPF, HNRNPH1 and ALYREF/THOC4/ALY. Interacts with SRRT/ARS2 and
CC       KPNA3 (PubMed:26382858). {ECO:0000269|PubMed:11545740,
CC       ECO:0000269|PubMed:12374755, ECO:0000269|PubMed:12434151,
CC       ECO:0000269|PubMed:15361857, ECO:0000269|PubMed:17363367,
CC       ECO:0000269|PubMed:26382858, ECO:0000269|PubMed:9111328}.
CC   -!- INTERACTION:
CC       Q9BRK4:LZTS2; NbExp=3; IntAct=EBI-464729, EBI-741037;
CC       Q09161:NCBP1; NbExp=8; IntAct=EBI-464729, EBI-464743;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8601613}.
CC       Cytoplasm {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         Note=Gene prediction based on EST data.;
CC   -!- SIMILARITY: Belongs to the RRM NCBP2 family. {ECO:0000305}.
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   UniGene; Hs.591671; -.
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   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; DP00393; -.
DR   ProteinModelPortal; P52298; -.
DR   SMR; P52298; -.
DR   BioGrid; 116578; 46.
DR   DIP; DIP-33246N; -.
DR   IntAct; P52298; 39.
DR   MINT; MINT-248711; -.
DR   STRING; 9606.ENSP00000326806; -.
DR   TCDB; 9.A.60.1.1; the small nuclear rna exporter (snrna-e).
DR   iPTMnet; P52298; -.
DR   PhosphoSitePlus; P52298; -.
DR   SwissPalm; P52298; -.
DR   BioMuta; NCBP2; -.
DR   DMDM; 1705651; -.
DR   EPD; P52298; -.
DR   MaxQB; P52298; -.
DR   PaxDb; P52298; -.
DR   PeptideAtlas; P52298; -.
DR   PRIDE; P52298; -.
DR   TopDownProteomics; P52298-1; -. [P52298-1]
DR   DNASU; 22916; -.
DR   Ensembl; ENST00000321256; ENSP00000326806; ENSG00000114503. [P52298-1]
DR   Ensembl; ENST00000427641; ENSP00000397619; ENSG00000114503. [P52298-3]
DR   Ensembl; ENST00000452404; ENSP00000412785; ENSG00000114503. [P52298-2]
DR   GeneID; 22916; -.
DR   KEGG; hsa:22916; -.
DR   UCSC; uc003fxd.2; human. [P52298-1]
DR   CTD; 22916; -.
DR   DisGeNET; 22916; -.
DR   GeneCards; NCBP2; -.
DR   HGNC; HGNC:7659; NCBP2.
DR   HPA; HPA044850; -.
DR   HPA; HPA062483; -.
DR   MIM; 605133; gene.
DR   neXtProt; NX_P52298; -.
DR   OpenTargets; ENSG00000114503; -.
DR   PharmGKB; PA31462; -.
DR   eggNOG; KOG0121; Eukaryota.
DR   eggNOG; ENOG4111FJQ; LUCA.
DR   GeneTree; ENSGT00390000003197; -.
DR   HOGENOM; HOG000217589; -.
DR   HOVERGEN; HBG052581; -.
DR   InParanoid; P52298; -.
DR   KO; K12883; -.
DR   OMA; RQDYDPA; -.
DR   OrthoDB; EOG091G0RKX; -.
DR   PhylomeDB; P52298; -.
DR   TreeFam; TF313897; -.
DR   Reactome; R-HSA-109688; Cleavage of Growing Transcript in the Termination Region.
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-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-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   ChiTaRS; NCBP2; human.
DR   EvolutionaryTrace; P52298; -.
DR   GenomeRNAi; 22916; -.
DR   PRO; PR:P52298; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   Bgee; ENSG00000114503; -.
DR   CleanEx; HS_NCBP2; -.
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; IBA:GO_Central.
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; IDA:UniProtKB.
DR   GO; GO:0000339; F:RNA cap binding; NAS:UniProtKB.
DR   GO; GO:0017069; F:snRNA binding; IDA:UniProtKB.
DR   GO; GO:0006370; P:7-methylguanosine mRNA capping; TAS:Reactome.
DR   GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
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; IDA:UniProtKB.
DR   GO; GO:0006406; P:mRNA export from nucleus; TAS:Reactome.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
DR   GO; GO:0051168; P:nuclear export; 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; IMP:UniProtKB.
DR   GO; GO:0046833; P:positive regulation of RNA export from nucleus; ISS:UniProtKB.
DR   GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IMP:UniProtKB.
DR   GO; GO:0006446; P:regulation of translational initiation; IDA:UniProtKB.
DR   GO; GO:0006405; P:RNA export from nucleus; TAS:Reactome.
DR   GO; GO:0016070; P:RNA metabolic process; TAS:Reactome.
DR   GO; GO:0008380; P:RNA splicing; ISS:UniProtKB.
DR   GO; GO:0006408; P:snRNA export from nucleus; ISS:UniProtKB.
DR   GO; GO:0042795; P:snRNA transcription from RNA polymerase II promoter; 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:0006366; P:transcription from RNA polymerase II promoter; TAS:Reactome.
DR   CDD; cd12240; RRM_NCBP2; 1.
DR   InterPro; IPR027157; NCBP2.
DR   InterPro; IPR034148; NCBP2_RRM.
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;
DR   PRODOM; P52298.
DR   SWISS-2DPAGE; P52298.
KW   3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW   Cytoplasm; Direct protein sequencing; Methylation; mRNA processing;
KW   mRNA splicing; mRNA transport; Nonsense-mediated mRNA decay; Nucleus;
KW   Phosphoprotein; Reference proteome; RNA-binding;
KW   RNA-mediated gene silencing; Translation regulation; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:22814378}.
FT   CHAIN         2    156       Nuclear cap-binding protein subunit 2.
FT                                /FTId=PRO_0000081499.
FT   DOMAIN       40    118       RRM. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00176}.
FT   REGION      112    116       mRNA cap-binding.
FT   REGION      123    127       mRNA cap-binding.
FT   REGION      133    134       mRNA cap-binding.
FT   BINDING      20     20       mRNA cap. {ECO:0000269|PubMed:12374755,
FT                                ECO:0000269|PubMed:12434151}.
FT   BINDING      43     43       mRNA cap. {ECO:0000269|PubMed:12374755,
FT                                ECO:0000269|PubMed:12434151}.
FT   MOD_RES       2      2       N-acetylserine.
FT                                {ECO:0000244|PubMed:22814378}.
FT   MOD_RES      13     13       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES      18     18       Phosphoserine.
FT                                {ECO:0000244|PubMed:17525332}.
FT   MOD_RES     146    146       Omega-N-methylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   VAR_SEQ       1     26       MSGGLLKALRSDSYVELSQYRDQHFR -> MVLRKLYA
FT                                (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_038125.
FT   VAR_SEQ      40     93       CTLYVGNLSFYTTEEQIYELFSKSGDIKKIIMGLDKMKKTA
FT                                CGFCFVEYYSRAD -> Y (in isoform 3).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_053823.
FT   MUTAGEN      20     20       Y->A: Abolishes mRNA cap-binding.
FT                                {ECO:0000269|PubMed:12374755}.
FT   MUTAGEN      20     20       Y->F: Strongly impairs mRNA cap-binding.
FT                                {ECO:0000269|PubMed:12374755}.
FT   MUTAGEN      25     25       F->A: Does not affect mRNA cap-binding.
FT                                {ECO:0000269|PubMed:11545740}.
FT   MUTAGEN      43     43       Y->A: Abolishes mRNA cap-binding.
FT                                {ECO:0000269|PubMed:11545740,
FT                                ECO:0000269|PubMed:12374755}.
FT   MUTAGEN      43     43       Y->F: Does not affect mRNA cap-binding.
FT                                {ECO:0000269|PubMed:11545740,
FT                                ECO:0000269|PubMed:12374755}.
FT   MUTAGEN      46     46       N->A: Does not affect mRNA cap-binding.
FT                                {ECO:0000269|PubMed:11545740}.
FT   MUTAGEN      83     83       F->A: Abolishes mRNA cap-binding.
FT                                {ECO:0000269|PubMed:11545740}.
FT   MUTAGEN      85     85       F->A: Impairs mRNA cap-binding.
FT   MUTAGEN     112    112       R->A,T: Does not affect mRNA cap-binding.
FT                                {ECO:0000269|PubMed:12374755}.
FT   MUTAGEN     114    114       D->A: Does not affect mRNA cap-binding.
FT                                {ECO:0000269|PubMed:11545740}.
FT   MUTAGEN     116    116       D->A: Abolishes mRNA cap-binding.
FT                                {ECO:0000269|PubMed:11545740}.
FT   MUTAGEN     119    119       F->A: Does not affect mRNA cap-binding.
FT                                {ECO:0000269|PubMed:11545740}.
FT   MUTAGEN     138    138       Y->A: Does not affect mRNA cap-binding.
FT                                {ECO:0000269|PubMed:12374755}.
FT   CONFLICT     97     97       A -> S (in Ref. 2; BAA09599).
FT                                {ECO:0000305}.
FT   HELIX         7     10       {ECO:0000244|PDB:1H2T}.
FT   HELIX        13     15       {ECO:0000244|PDB:1H2T}.
FT   STRAND       23     27       {ECO:0000244|PDB:1N54}.
FT   TURN         34     38       {ECO:0000244|PDB:1H2V}.
FT   STRAND       41     46       {ECO:0000244|PDB:1H2V}.
FT   HELIX        53     60       {ECO:0000244|PDB:1H2V}.
FT   HELIX        61     63       {ECO:0000244|PDB:1H2V}.
FT   STRAND       66     73       {ECO:0000244|PDB:1H2V}.
FT   TURN         75     77       {ECO:0000244|PDB:1H2V}.
FT   STRAND       80     90       {ECO:0000244|PDB:1H2V}.
FT   HELIX        91    100       {ECO:0000244|PDB:1H2V}.
FT   TURN        101    103       {ECO:0000244|PDB:1H2V}.
FT   STRAND      104    106       {ECO:0000244|PDB:1H2V}.
FT   STRAND      112    117       {ECO:0000244|PDB:1H2V}.
FT   TURN        121    124       {ECO:0000244|PDB:1H2T}.
FT   HELIX       134    137       {ECO:0000244|PDB:1H2T}.
FT   HELIX       144    146       {ECO:0000244|PDB:1H2T}.
SQ   SEQUENCE   156 AA;  18001 MW;  B6C94F3182A2CC3D CRC64;
     MSGGLLKALR SDSYVELSQY RDQHFRGDNE EQEKLLKKSC TLYVGNLSFY TTEEQIYELF
     SKSGDIKKII MGLDKMKKTA CGFCFVEYYS RADAENAMRY INGTRLDDRI IRTDWDAGFK
     EGRQYGRGRS GGQVRDEYRQ DYDAGRGGYG KLAQNQ
//

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