Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Nuclear cap-binding protein subunit 2 (20 kDa nuclear cap-binding protein) (Cell proliferation-inducing gene 55 protein) (NCBP 20 kDa subunit) (CBP20) (NCBP-interacting protein 1) (NIP1)

 NCBP2_HUMAN             Reviewed;         156 AA.
P52298; B2RE91; B4DMK7; E9PAR5; Q14924; Q2TS50;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 182.
RecName: Full=Nuclear cap-binding protein subunit 2;
AltName: Full=20 kDa nuclear cap-binding protein;
AltName: Full=Cell proliferation-inducing gene 55 protein;
AltName: Full=NCBP 20 kDa subunit;
Short=CBP20;
AltName: Full=NCBP-interacting protein 1;
Short=NIP1;
Name=NCBP2; Synonyms=CBP20; ORFNames=PIG55;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 9-25
AND 113-145.
PubMed=7651522; DOI=10.1038/376709a0;
Izaurralde E., Lewis J., Gamberi C., Jarmolowski A., McGuigan C.,
Mattaj A.W.;
"A cap-binding protein complex mediating U snRNA export.";
Nature 376:709-712(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Cervix carcinoma;
PubMed=7478990; DOI=10.1093/nar/23.18.3638;
Kataoka N., Ohno M., Moda I., Shimura Y.;
"Identification of the factors that interact with NCBP, an 80 kDa
nuclear cap binding protein.";
Nucleic Acids Res. 23:3638-3641(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kim J.W.;
"Identification of a human cell proliferation gene.";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cervix;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
SUBCELLULAR LOCATION.
PubMed=8601613; DOI=10.1083/jcb.133.1.5;
Visa N., Izaurralde E., Ferreira J., Daneholt B., Mattaj I.W.;
"A nuclear cap-binding complex binds Balbiani ring pre-mRNA
cotranscriptionally and accompanies the ribonucleoprotein particle
during nuclear export.";
J. Cell Biol. 133:5-14(1996).
[10]
INTERACTION WITH HNRNPF AND HNRNPH1.
PubMed=9111328; DOI=10.1128/MCB.17.5.2587;
Gamberi C., Izaurralde E., Beisel C., Mattaj I.W.;
"Interaction between the human nuclear cap-binding protein complex and
hnRNP F.";
Mol. Cell. Biol. 17:2587-2597(1997).
[11]
FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION.
PubMed=11551508; DOI=10.1016/S0092-8674(01)00475-5;
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).
[12]
FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION, AND INTERACTION WITH
EIF4G1.
PubMed=15361857; DOI=10.1038/nsmb824;
Lejeune F., Ranganathan A.C., Maquat L.E.;
"eIF4G is required for the pioneer round of translation in mammalian
cells.";
Nat. Struct. Mol. Biol. 11:992-1000(2004).
[13]
FUNCTION IN MRNA EXPORT.
PubMed=17190602; DOI=10.1016/j.cell.2006.10.044;
Cheng H., Dufu K., Lee C.-S., Hsu J.L., Dias A., Reed R.;
"Human mRNA export machinery recruited to the 5' end of mRNA.";
Cell 127:1389-1400(2006).
[14]
FUNCTION IN MRNA EXPORT, AND INTERACTION WITH ALYREF/THOC4.
PubMed=17363367; DOI=10.1074/jbc.M700629200;
Nojima T., Hirose T., Kimura H., Hagiwara M.;
"The interaction between cap-binding complex and RNA export factor is
required for intronless mRNA export.";
J. Biol. Chem. 282:15645-15651(2007).
[15]
FUNCTION IN NONSENSE-MEDIATED MRNA DECAY.
PubMed=17873884; DOI=10.1038/nsmb1297;
Matsuda D., Hosoda N., Kim Y.K., Maquat L.E.;
"Failsafe nonsense-mediated mRNA decay does not detectably target
eIF4E-bound mRNA.";
Nat. Struct. Mol. Biol. 14:974-979(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[17]
FUNCTION IN NONSENSE-MEDIATED MRNA DECAY.
PubMed=18369367; DOI=10.1038/embor.2008.36;
Woeller C.F., Gaspari M., Isken O., Maquat L.E.;
"NMD resulting from encephalomyocarditis virus IRES-directed
translation initiation seems to be restricted to CBP80/20-bound
mRNA.";
EMBO Rep. 9:446-451(2008).
[18]
FUNCTION IN MIRNAS BIOGENESIS.
PubMed=19632182; DOI=10.1016/j.cell.2009.04.046;
Gruber J.J., Zatechka D.S., Sabin L.R., Yong J., Lum J.J., Kong M.,
Zong W.-X., Zhang Z., Lau C.-K., Rawlings J., Cherry S., Ihle J.N.,
Dreyfuss G., Thompson C.B.;
"Ars2 links the nuclear cap-binding complex to RNA interference and
cell proliferation.";
Cell 138:328-339(2009).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[23]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-146, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[24]
FUNCTION, INTERACTION WITH NCBP1; SRRT; KPNA3 AND PHAX, RNA-BINDING,
AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=26382858; DOI=10.1038/ncomms9192;
Gebhardt A., Habjan M., Benda C., Meiler A., Haas D.A., Hein M.Y.,
Mann A., Mann M., Habermann B., Pichlmair A.;
"mRNA export through an additional cap-binding complex consisting of
NCBP1 and NCBP3.";
Nat. Commun. 6:8192-8192(2015).
[25]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 20-790 IN COMPLEX WITH NCBP1,
RNA-BINDING, AND MUTAGENESIS OF PHE-25; TYR-43; ASN-46; PHE-83;
ASP-114; ASP-116 AND PHE-119.
PubMed=11545740; DOI=10.1016/S1097-2765(01)00299-4;
Mazza C., Ohno M., Segref A., Mattaj I.W., Cusack S.;
"Crystal structure of the human nuclear cap binding complex.";
Mol. Cell 8:383-396(2001).
[26]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 20-790 IN COMPLEX WITH NCBP1
AND MRNA CAP, RNA-BINDING, AND MUTAGENESIS OF TYR-20; TYR-43; ARG-112
AND TYR-138.
PubMed=12374755; DOI=10.1093/emboj/cdf538;
Mazza C., Segref A., Mattaj I.W., Cusack S.;
"Large-scale induced fit recognition of an m(7)GpppG cap analogue by
the human nuclear cap-binding complex.";
EMBO J. 21:5548-5557(2002).
[27]
X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) IN COMPLEX WITH NCBP1 AND MRNA
CAP, AND RNA-BINDING.
PubMed=12434151; DOI=10.1038/nsb874;
Calero G., Wilson K.F., Ly T., Rios-Steiner J.L., Clardy J.C.,
Cerione R.A.;
"Structural basis of m7GpppG binding to the nuclear cap-binding
protein complex.";
Nat. Struct. Biol. 9:912-917(2002).
-!- FUNCTION: Component of the cap-binding complex (CBC), which binds
co-transcriptionally to the 5' cap of pre-mRNAs and is involved in
various processes such as pre-mRNA splicing, translation
regulation, nonsense-mediated mRNA decay, RNA-mediated gene
silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC
complex is involved in mRNA export from the nucleus via its
interaction with ALYREF/THOC4/ALY, leading to the recruitment of
the mRNA export machinery to the 5' end of mRNA and to mRNA export
in a 5' to 3' direction through the nuclear pore. The CBC complex
is also involved in mediating U snRNA and intronless mRNAs export
from the nucleus. The CBC complex is essential for a pioneer round
of mRNA translation, before steady state translation when the CBC
complex is replaced by cytoplasmic cap-binding protein eIF4E. The
pioneer round of mRNA translation mediated by the CBC complex
plays a central role in nonsense-mediated mRNA decay (NMD), NMD
only taking place in mRNAs bound to the CBC complex, but not on
eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs
containing at least one exon-junction complex (EJC) via its
interaction with UPF1, promoting the interaction between UPF1 and
UPF2. The CBC complex is also involved in 'failsafe' NMD, which is
independent of the EJC complex, while it does not participate in
Staufen-mediated mRNA decay (SMD). During cell proliferation, the
CBC complex is also involved in microRNAs (miRNAs) biogenesis via
its interaction with SRRT/ARS2, thereby being required for miRNA-
mediated RNA interference. The CBC complex also acts as a negative
regulator of PARN, thereby acting as an inhibitor of mRNA
deadenylation. In the CBC complex, NCBP2/CBP20 recognizes and
binds capped RNAs (m7GpppG-capped RNA) but requires NCBP1/CBP80 to
stabilize the movement of its N-terminal loop and lock the CBC
into a high affinity cap-binding state with the cap structure. The
conventional cap-binding complex with NCBP2 binds both small
nuclear RNA (snRNA) and messenger (mRNA) and is involved in their
export from the nucleus (PubMed:26382858).
{ECO:0000269|PubMed:11551508, ECO:0000269|PubMed:15361857,
ECO:0000269|PubMed:17190602, ECO:0000269|PubMed:17363367,
ECO:0000269|PubMed:17873884, ECO:0000269|PubMed:18369367,
ECO:0000269|PubMed:19632182, ECO:0000269|PubMed:26382858}.
-!- SUBUNIT: Component of the nuclear cap-binding complex (CBC), a
heterodimer composed of NCBP1/CBP80 and NCBP2/CBP20 that interacts
with m7GpppG-capped RNA (PubMed:26382858). Found in a U snRNA
export complex with PHAX/RNUXA, NCBP1/CBP80, NCBP2/CBP20, RAN,
XPO1 and m7G-capped RNA. Interacts with PHAX/RNUXA, EIF4G1,
HNRNPF, HNRNPH1 and ALYREF/THOC4/ALY. Interacts with SRRT/ARS2 and
KPNA3 (PubMed:26382858). {ECO:0000269|PubMed:11545740,
ECO:0000269|PubMed:12374755, ECO:0000269|PubMed:12434151,
ECO:0000269|PubMed:15361857, ECO:0000269|PubMed:17363367,
ECO:0000269|PubMed:26382858, ECO:0000269|PubMed:9111328}.
-!- INTERACTION:
Q14974-1:KPNB1; NbExp=2; IntAct=EBI-15798444, EBI-15488647;
Q9BRK4:LZTS2; NbExp=3; IntAct=EBI-464729, EBI-741037;
Q09161:NCBP1; NbExp=8; IntAct=EBI-15798444, EBI-464743;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8601613}.
Cytoplasm {ECO:0000269|PubMed:8601613}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P52298-1; Sequence=Displayed;
Name=2;
IsoId=P52298-2; Sequence=VSP_038125;
Name=3;
IsoId=P52298-3; Sequence=VSP_053823;
Note=Gene prediction based on EST data.;
-!- SIMILARITY: Belongs to the RRM NCBP2 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X84157; CAA58962.1; -; mRNA.
EMBL; D59253; BAA09599.1; -; mRNA.
EMBL; AK297506; BAG59919.1; -; mRNA.
EMBL; AK315903; BAH14274.1; -; mRNA.
EMBL; AK316601; BAG38188.1; -; mRNA.
EMBL; AY644767; AAV85455.1; -; mRNA.
EMBL; BT006842; AAP35488.1; -; mRNA.
EMBL; AC011322; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471191; EAW53624.1; -; Genomic_DNA.
EMBL; BC001255; AAH01255.1; -; mRNA.
CCDS; CCDS3323.1; -. [P52298-1]
CCDS; CCDS46986.1; -. [P52298-3]
CCDS; CCDS77878.1; -. [P52298-2]
PIR; I37222; I37222.
PIR; S60109; S60109.
RefSeq; NP_001036005.1; NM_001042540.1. [P52298-3]
RefSeq; NP_001294965.1; NM_001308036.1. [P52298-2]
RefSeq; NP_031388.2; NM_007362.3. [P52298-1]
UniGene; Hs.591671; -.
PDB; 1H2T; X-ray; 2.15 A; Z=1-156.
PDB; 1H2U; X-ray; 2.40 A; X/Y=1-156.
PDB; 1H2V; X-ray; 2.00 A; Z=1-156.
PDB; 1H6K; X-ray; 2.00 A; X/Y/Z=22-120.
PDB; 1N52; X-ray; 2.11 A; B=1-156.
PDB; 1N54; X-ray; 2.72 A; B=1-156.
PDB; 3FEX; X-ray; 3.55 A; B=1-156.
PDB; 3FEY; X-ray; 2.20 A; B=1-156.
PDBsum; 1H2T; -.
PDBsum; 1H2U; -.
PDBsum; 1H2V; -.
PDBsum; 1H6K; -.
PDBsum; 1N52; -.
PDBsum; 1N54; -.
PDBsum; 3FEX; -.
PDBsum; 3FEY; -.
DisProt; DP00393; -.
ProteinModelPortal; P52298; -.
SMR; P52298; -.
BioGrid; 116578; 47.
CORUM; P52298; -.
DIP; DIP-33246N; -.
IntAct; P52298; 40.
MINT; MINT-248711; -.
STRING; 9606.ENSP00000326806; -.
TCDB; 9.A.60.1.1; the small nuclear rna exporter (snrna-e).
iPTMnet; P52298; -.
PhosphoSitePlus; P52298; -.
SwissPalm; P52298; -.
BioMuta; NCBP2; -.
DMDM; 1705651; -.
EPD; P52298; -.
MaxQB; P52298; -.
PaxDb; P52298; -.
PeptideAtlas; P52298; -.
PRIDE; P52298; -.
TopDownProteomics; P52298-1; -. [P52298-1]
DNASU; 22916; -.
Ensembl; ENST00000321256; ENSP00000326806; ENSG00000114503. [P52298-1]
Ensembl; ENST00000427641; ENSP00000397619; ENSG00000114503. [P52298-3]
Ensembl; ENST00000452404; ENSP00000412785; ENSG00000114503. [P52298-2]
GeneID; 22916; -.
KEGG; hsa:22916; -.
UCSC; uc003fxd.2; human. [P52298-1]
CTD; 22916; -.
DisGeNET; 22916; -.
EuPathDB; HostDB:ENSG00000114503.10; -.
GeneCards; NCBP2; -.
HGNC; HGNC:7659; NCBP2.
HPA; HPA044850; -.
HPA; HPA062483; -.
MIM; 605133; gene.
neXtProt; NX_P52298; -.
OpenTargets; ENSG00000114503; -.
PharmGKB; PA31462; -.
eggNOG; KOG0121; Eukaryota.
eggNOG; ENOG4111FJQ; LUCA.
GeneTree; ENSGT00390000003197; -.
HOGENOM; HOG000217589; -.
HOVERGEN; HBG052581; -.
InParanoid; P52298; -.
KO; K12883; -.
OMA; RQDYDPA; -.
OrthoDB; EOG091G0RKX; -.
PhylomeDB; P52298; -.
TreeFam; TF313897; -.
Reactome; R-HSA-109688; Cleavage of Growing Transcript in the Termination Region.
Reactome; R-HSA-111367; SLBP independent Processing of Histone Pre-mRNAs.
Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
Reactome; R-HSA-113418; Formation of the Early Elongation Complex.
Reactome; R-HSA-159227; Transport of the SLBP independent Mature mRNA.
Reactome; R-HSA-159230; Transport of the SLBP Dependant Mature mRNA.
Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
Reactome; R-HSA-167158; Formation of the HIV-1 Early Elongation Complex.
Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat.
Reactome; R-HSA-167242; Abortive elongation of HIV-1 transcript in the absence of Tat.
Reactome; R-HSA-191859; snRNP Assembly.
Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
Reactome; R-HSA-6803529; FGFR2 alternative splicing.
Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
Reactome; R-HSA-72086; mRNA Capping.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
Reactome; R-HSA-72187; mRNA 3'-end processing.
Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
Reactome; R-HSA-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
Reactome; R-HSA-77595; Processing of Intronless Pre-mRNAs.
Reactome; R-HSA-8851708; Signaling by FGFR2 IIIa TM.
Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
ChiTaRS; NCBP2; human.
EvolutionaryTrace; P52298; -.
GenomeRNAi; 22916; -.
PRO; PR:P52298; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000114503; -.
CleanEx; HS_NCBP2; -.
ExpressionAtlas; P52298; baseline and differential.
Genevisible; P52298; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005845; C:mRNA cap binding complex; IDA:UniProtKB.
GO; GO:0005846; C:nuclear cap binding complex; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0034518; C:RNA cap binding complex; IMP:CAFA.
GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0000339; F:RNA cap binding; NAS:UniProtKB.
GO; GO:0017069; F:snRNA binding; IDA:UniProtKB.
GO; GO:0006370; P:7-methylguanosine mRNA capping; TAS:Reactome.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
GO; GO:0008334; P:histone mRNA metabolic process; TAS:Reactome.
GO; GO:0031124; P:mRNA 3'-end processing; TAS:Reactome.
GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IDA:UniProtKB.
GO; GO:0006406; P:mRNA export from nucleus; TAS:Reactome.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:0051168; P:nuclear export; TAS:Reactome.
GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:UniProtKB.
GO; GO:0031442; P:positive regulation of mRNA 3'-end processing; IMP:UniProtKB.
GO; GO:0046833; P:positive regulation of RNA export from nucleus; ISS:UniProtKB.
GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IMP:UniProtKB.
GO; GO:0006446; P:regulation of translational initiation; IDA:UniProtKB.
GO; GO:0006405; P:RNA export from nucleus; TAS:Reactome.
GO; GO:0016070; P:RNA metabolic process; TAS:Reactome.
GO; GO:0008380; P:RNA splicing; ISS:UniProtKB.
GO; GO:0006408; P:snRNA export from nucleus; ISS:UniProtKB.
GO; GO:0042795; P:snRNA transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:Reactome.
CDD; cd12240; RRM_NCBP2; 1.
InterPro; IPR027157; NCBP2.
InterPro; IPR034148; NCBP2_RRM.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
PANTHER; PTHR18847; PTHR18847; 1.
Pfam; PF00076; RRM_1; 1.
SMART; SM00360; RRM; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Methylation; mRNA processing;
mRNA splicing; mRNA transport; Nonsense-mediated mRNA decay; Nucleus;
Phosphoprotein; Reference proteome; RNA-binding;
RNA-mediated gene silencing; Translation regulation; Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 156 Nuclear cap-binding protein subunit 2.
/FTId=PRO_0000081499.
DOMAIN 40 118 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REGION 112 116 mRNA cap-binding.
REGION 123 127 mRNA cap-binding.
REGION 133 134 mRNA cap-binding.
BINDING 20 20 mRNA cap. {ECO:0000269|PubMed:12374755,
ECO:0000269|PubMed:12434151}.
BINDING 43 43 mRNA cap. {ECO:0000269|PubMed:12374755,
ECO:0000269|PubMed:12434151}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 18 18 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 146 146 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
VAR_SEQ 1 26 MSGGLLKALRSDSYVELSQYRDQHFR -> MVLRKLYA
(in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038125.
VAR_SEQ 40 93 CTLYVGNLSFYTTEEQIYELFSKSGDIKKIIMGLDKMKKTA
CGFCFVEYYSRAD -> Y (in isoform 3).
{ECO:0000305}.
/FTId=VSP_053823.
MUTAGEN 20 20 Y->A: Abolishes mRNA cap-binding.
{ECO:0000269|PubMed:12374755}.
MUTAGEN 20 20 Y->F: Strongly impairs mRNA cap-binding.
{ECO:0000269|PubMed:12374755}.
MUTAGEN 25 25 F->A: Does not affect mRNA cap-binding.
{ECO:0000269|PubMed:11545740}.
MUTAGEN 43 43 Y->A: Abolishes mRNA cap-binding.
{ECO:0000269|PubMed:11545740,
ECO:0000269|PubMed:12374755}.
MUTAGEN 43 43 Y->F: Does not affect mRNA cap-binding.
{ECO:0000269|PubMed:11545740,
ECO:0000269|PubMed:12374755}.
MUTAGEN 46 46 N->A: Does not affect mRNA cap-binding.
{ECO:0000269|PubMed:11545740}.
MUTAGEN 83 83 F->A: Abolishes mRNA cap-binding.
{ECO:0000269|PubMed:11545740}.
MUTAGEN 85 85 F->A: Impairs mRNA cap-binding.
MUTAGEN 112 112 R->A,T: Does not affect mRNA cap-binding.
{ECO:0000269|PubMed:12374755}.
MUTAGEN 114 114 D->A: Does not affect mRNA cap-binding.
{ECO:0000269|PubMed:11545740}.
MUTAGEN 116 116 D->A: Abolishes mRNA cap-binding.
{ECO:0000269|PubMed:11545740}.
MUTAGEN 119 119 F->A: Does not affect mRNA cap-binding.
{ECO:0000269|PubMed:11545740}.
MUTAGEN 138 138 Y->A: Does not affect mRNA cap-binding.
{ECO:0000269|PubMed:12374755}.
CONFLICT 97 97 A -> S (in Ref. 2; BAA09599).
{ECO:0000305}.
HELIX 7 10 {ECO:0000244|PDB:1H2T}.
HELIX 13 15 {ECO:0000244|PDB:1H2T}.
STRAND 23 27 {ECO:0000244|PDB:1N54}.
TURN 34 38 {ECO:0000244|PDB:1H2V}.
STRAND 41 46 {ECO:0000244|PDB:1H2V}.
HELIX 53 60 {ECO:0000244|PDB:1H2V}.
HELIX 61 63 {ECO:0000244|PDB:1H2V}.
STRAND 66 73 {ECO:0000244|PDB:1H2V}.
TURN 75 77 {ECO:0000244|PDB:1H2V}.
STRAND 80 90 {ECO:0000244|PDB:1H2V}.
HELIX 91 100 {ECO:0000244|PDB:1H2V}.
TURN 101 103 {ECO:0000244|PDB:1H2V}.
STRAND 104 106 {ECO:0000244|PDB:1H2V}.
STRAND 112 117 {ECO:0000244|PDB:1H2V}.
TURN 121 124 {ECO:0000244|PDB:1H2T}.
HELIX 134 137 {ECO:0000244|PDB:1H2T}.
HELIX 144 146 {ECO:0000244|PDB:1H2T}.
SEQUENCE 156 AA; 18001 MW; B6C94F3182A2CC3D CRC64;
MSGGLLKALR SDSYVELSQY RDQHFRGDNE EQEKLLKKSC TLYVGNLSFY TTEEQIYELF
SKSGDIKKII MGLDKMKKTA CGFCFVEYYS RADAENAMRY INGTRLDDRI IRTDWDAGFK
EGRQYGRGRS GGQVRDEYRQ DYDAGRGGYG KLAQNQ


Related products :

Catalog number Product name Quantity
EIAAB26507 20 kDa nuclear cap-binding protein,CBP20,CBP20,Cell proliferation-inducing gene 55 protein,Homo sapiens,Human,NCBP 20 kDa subunit,NCBP2,NCBP-interacting protein 1,NIP1,Nuclear cap-binding protein subu
EIAAB26505 20 kDa nuclear cap-binding protein,CBP20,Cbp20,Mouse,Mus musculus,NCBP 20 kDa subunit,Ncbp2,Nuclear cap-binding protein subunit 2
EIAAB26506 20 kDa nuclear cap-binding protein,Bos taurus,Bovine,CBP20,CBP20,NCBP 20 kDa subunit,NCBP2,Nuclear cap-binding protein subunit 2
EIAAB26504 20 kDa nuclear cap-binding protein,CBP20,Cbp20,NCBP 20 kDa subunit,Ncbp2,Nuclear cap-binding protein subunit 2,Rat,Rattus norvegicus
EIAAB26503 20 kDa nuclear cap-binding protein,CBP20,CBP20,Chicken,Gallus gallus,NCBP 20 kDa subunit,NCBP2,Nuclear cap-binding protein subunit 2,RCJMB04_9i16
EIAAB26499 80 kDa nuclear cap-binding protein,CBP80,CBP80,Homo sapiens,Human,NCBP,NCBP 80 kDa subunit,NCBP1,Nuclear cap-binding protein subunit 1
EIAAB26500 80 kDa nuclear cap-binding protein,CBP80,Cbp80,Mouse,Mus musculus,NCBP 80 kDa subunit,Ncbp1,Nuclear cap-binding protein subunit 1
EIAAB26502 80 kDa nuclear cap-binding protein,CBP80,Cbp80,NCBP 80 kDa subunit,Ncbp1,Nuclear cap-binding protein subunit 1,Rat,Rattus norvegicus
Y050612 Anti_NCBP1(80 kDa nuclear cap binding protein) (NCBP 80 kDa subunit) 100ug
EIAAB26501 80 kDa nuclear cap-binding protein,CBP80,CBP80,Chicken,Gallus gallus,NCBP 80 kDa subunit,NCBP1,Nuclear cap-binding protein subunit 1,RCJMB04_14d7
Y050612 Anti-NCBP180 kDa nuclear cap binding protein NCBP 80 kDa subunit antibody 250ug
Y050612 Anti-NCBP1(80 kDa nuclear cap binding protein) (NCBP 80 kDa subunit) Antibody 100ug
EIAAB28268 82 kDa FMRP-interacting protein,82-FIP,Cell proliferation-inducing gene 1 protein,FMRP-interacting protein 2,Homo sapiens,Human,KIAA1321,Nuclear fragile X mental retardation-interacting protein 2,NUFI
AS09 530 rabbit polyclonal CBP20 | nuclear cap-binding protein subunit 2 200
EIAAB36467 49 kDa TATA box-binding protein-interacting protein,49 kDa TBP-interacting protein,54 kDa erythrocyte cytosolic protein,ECP-54,Homo sapiens,Human,INO80 complex subunit H,INO80H,NMP 238,NMP238,Nuclear
EIAAB27518 54 kDa nuclear RNA- and DNA-binding protein,55 kDa nuclear protein,DNA-binding p52_p100 complex, 52 kDa subunit,Homo sapiens,Human,NMT55,NONO,NonO protein,Non-POU domain-containing octamer-binding pro
AS09 530 Antibody: CBP20 | nuclear cap-binding protein subunit 2, Immunogen: http:__www.uniprot.org_uniprot_Q9XFD1, Host: rabbit, polyclonal, Confirmed reactivity: Arabidopsis thaliana 200
18-003-43630 Non-POU domain-containing octamer-binding protein - NonO protein; 54 kDa nuclear RNA- and DNA-binding protein; p54(nrb); p54nrb; 55 kDa nuclear protein; NMT55; DNA-binding p52_p100 complex. 52 kDa sub 0.1 mg Protein A
18-003-44214 Non-POU domain-containing octamer-binding protein - NonO protein; 54 kDa nuclear RNA- and DNA-binding protein; p54(nrb); p54nrb; 55 kDa nuclear protein; NMT55; DNA-binding p52_p100 complex. 52 kDa sub 0.1 mg Protein A
EIAAB27106 CAAT box DNA-binding protein subunit A,CBF-B,CCAAT-binding transcription factor subunit B,Nfya,NF-YA,Nuclear transcription factor Y subunit A,Nuclear transcription factor Y subunit alpha,Rat,Rattus no
EIAAB27109 CAAT box DNA-binding protein subunit B,CBF-A,CCAAT-binding transcription factor subunit A,Nfyb,NF-YB,Nuclear transcription factor Y subunit B,Nuclear transcription factor Y subunit beta,Rat,Rattus nor
EIAAB27113 CAAT box DNA-binding protein subunit C,CBF-C,CCAAT-binding transcription factor subunit C,Nfyc,NF-YC,Nuclear transcription factor Y subunit C,Nuclear transcription factor Y subunit gamma,Rat,Rattus no
EIAAB26847 Amyloid beta A4 protein-binding family A member 2-binding protein,APBA2BP,Homo sapiens,Human,NECAB3,Nek2-interacting protein 1,Neuronal calcium-binding protein 3,NIP1,N-terminal EF-hand calcium-bindin
E0266h ELISA 47 kDa heat shock protein,Arsenic-transactivated protein 3,AsTP3,CBP1,CBP2,Cell proliferation-inducing gene 14 protein,Collagen-binding protein,Colligin,Homo sapiens,HSP47,Human,PIG14,Rheumatoid 96T
U0266h CLIA 47 kDa heat shock protein,Arsenic-transactivated protein 3,AsTP3,CBP1,CBP2,Cell proliferation-inducing gene 14 protein,Collagen-binding protein,Colligin,Homo sapiens,HSP47,Human,PIG14,Rheumatoid 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur