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P52298 (NCBP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclear cap-binding protein subunit 2
Alternative name(s):
20 kDa nuclear cap-binding protein
Cell proliferation-inducing gene 55 protein
NCBP 20 kDa subunit
Short name=CBP20
NCBP-interacting protein 1
Short name=NIP1
Gene names
Name:NCBP2
Synonyms:CBP20
ORF Names:PIG55
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length156 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18

Subunit structure

Component of the nuclear cap-binding complex (CBC), a heterodimer composed of NCBP1/CBP80 and NCBP2/CBP20 that interacts with m7GpppG-capped RNA. Found in a U snRNA export complex with RNUXA/PHAX, NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-capped RNA. Interacts with RNUXA/PHAX, EIF4G1, HNRNPF, HNRNPH1 and ALYREF/THOC4/ALY. Ref.10 Ref.12 Ref.14

Subcellular location

Nucleus. Cytoplasm Ref.9.

Sequence similarities

Belongs to the RRM NCBP2 family.

Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
   Biological processmRNA capping
mRNA processing
mRNA splicing
mRNA transport
Nonsense-mediated mRNA decay
RNA-mediated gene silencing
Translation regulation
Transport
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandRNA-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process7-methylguanosine mRNA capping

Inferred from direct assay Ref.24. Source: UniProtKB

RNA metabolic process

Traceable author statement. Source: Reactome

RNA splicing

Inferred from sequence or structural similarity. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

gene silencing by RNA

Inferred from electronic annotation. Source: UniProtKB-KW

histone mRNA metabolic process

Traceable author statement. Source: Reactome

mRNA 3'-end processing

Traceable author statement. Source: Reactome

mRNA cis splicing, via spliceosome

Inferred from direct assay PubMed 18426921. Source: UniProtKB

mRNA export from nucleus

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

mRNA splicing, via spliceosome

Traceable author statement. Source: Reactome

ncRNA metabolic process

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Inferred from direct assay Ref.11. Source: UniProtKB

positive regulation of RNA export from nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of viral transcription

Traceable author statement. Source: Reactome

regulation of translational initiation

Inferred from direct assay Ref.11. Source: UniProtKB

snRNA export from nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

spliceosomal snRNP assembly

Traceable author statement. Source: Reactome

termination of RNA polymerase II transcription

Traceable author statement. Source: Reactome

transcription elongation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay Ref.9. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

mRNA cap binding complex

Inferred from direct assay Ref.24Ref.1PubMed 9342333. Source: UniProtKB

nuclear cap binding complex

Inferred from electronic annotation. Source: InterPro

nucleoplasm

Inferred from direct assay Ref.9. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 9342333. Source: UniProtKB

   Molecular_functionRNA 7-methylguanosine cap binding

Inferred from direct assay Ref.24PubMed 18426921. Source: UniProtKB

RNA cap binding

Non-traceable author statement Ref.1. Source: UniProtKB

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.2Ref.10. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NCBP1Q091616EBI-464729,EBI-464743

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P52298-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P52298-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MSGGLLKALRSDSYVELSQYRDQHFR → MVLRKLYA
Isoform 3 (identifier: P52298-3)

The sequence of this isoform differs from the canonical sequence as follows:
     40-93: CTLYVGNLSFYTTEEQIYELFSKSGDIKKIIMGLDKMKKTACGFCFVEYYSRAD → Y
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.21
Chain2 – 156155Nuclear cap-binding protein subunit 2
PRO_0000081499

Regions

Domain40 – 11879RRM
Region112 – 1165mRNA cap-binding
Region123 – 1275mRNA cap-binding
Region133 – 1342mRNA cap-binding

Sites

Binding site201mRNA cap
Binding site431mRNA cap

Amino acid modifications

Modified residue21N-acetylserine Ref.21
Modified residue181Phosphoserine Ref.16

Natural variations

Alternative sequence1 – 2626MSGGL…DQHFR → MVLRKLYA in isoform 2.
VSP_038125
Alternative sequence40 – 9354CTLYV…YSRAD → Y in isoform 3.
VSP_053823

Experimental info

Mutagenesis201Y → A: Abolishes mRNA cap-binding. Ref.23
Mutagenesis201Y → F: Strongly impairs mRNA cap-binding. Ref.23
Mutagenesis251F → A: Does not affect mRNA cap-binding. Ref.22
Mutagenesis431Y → A: Abolishes mRNA cap-binding. Ref.22 Ref.23
Mutagenesis431Y → F: Does not affect mRNA cap-binding. Ref.22 Ref.23
Mutagenesis461N → A: Does not affect mRNA cap-binding. Ref.22
Mutagenesis831F → A: Abolishes mRNA cap-binding. Ref.22
Mutagenesis851F → A: Impairs mRNA cap-binding.
Mutagenesis1121R → A or T: Does not affect mRNA cap-binding. Ref.23
Mutagenesis1141D → A: Does not affect mRNA cap-binding. Ref.22
Mutagenesis1161D → A: Abolishes mRNA cap-binding. Ref.22
Mutagenesis1191F → A: Does not affect mRNA cap-binding. Ref.22
Mutagenesis1381Y → A: Does not affect mRNA cap-binding. Ref.23
Sequence conflict971A → S in BAA09599. Ref.2

Secondary structure

............................... 156
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: B6C94F3182A2CC3D

FASTA15618,001
        10         20         30         40         50         60 
MSGGLLKALR SDSYVELSQY RDQHFRGDNE EQEKLLKKSC TLYVGNLSFY TTEEQIYELF 

        70         80         90        100        110        120 
SKSGDIKKII MGLDKMKKTA CGFCFVEYYS RADAENAMRY INGTRLDDRI IRTDWDAGFK 

       130        140        150 
EGRQYGRGRS GGQVRDEYRQ DYDAGRGGYG KLAQNQ 

« Hide

Isoform 2 [UniParc].

Checksum: D2475AF0597FDC0F
Show »

FASTA13815,937
Isoform 3 [UniParc].

Checksum: 0790F40FF3E16B61
Show »

FASTA10311,932

References

« Hide 'large scale' references
[1]"A cap-binding protein complex mediating U snRNA export."
Izaurralde E., Lewis J., Gamberi C., Jarmolowski A., McGuigan C., Mattaj A.W.
Nature 376:709-712(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 9-25 AND 113-145.
[2]"Identification of the factors that interact with NCBP, an 80 kDa nuclear cap binding protein."
Kataoka N., Ohno M., Moda I., Shimura Y.
Nucleic Acids Res. 23:3638-3641(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Cervix carcinoma.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain.
[4]"Identification of a human cell proliferation gene."
Kim J.W.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"The DNA sequence, annotation and analysis of human chromosome 3."
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. expand/collapse author list , 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.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Cervix.
[9]"A nuclear cap-binding complex binds Balbiani ring pre-mRNA cotranscriptionally and accompanies the ribonucleoprotein particle during nuclear export."
Visa N., Izaurralde E., Ferreira J., Daneholt B., Mattaj I.W.
J. Cell Biol. 133:5-14(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[10]"Interaction between the human nuclear cap-binding protein complex and hnRNP F."
Gamberi C., Izaurralde E., Beisel C., Mattaj I.W.
Mol. Cell. Biol. 17:2587-2597(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HNRNPF AND HNRNPH1.
[11]"Evidence for a pioneer round of mRNA translation: mRNAs subject to nonsense-mediated decay in mammalian cells are bound by CBP80 and CBP20."
Ishigaki Y., Li X., Serin G., Maquat L.E.
Cell 106:607-617(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION.
[12]"eIF4G is required for the pioneer round of translation in mammalian cells."
Lejeune F., Ranganathan A.C., Maquat L.E.
Nat. Struct. Mol. Biol. 11:992-1000(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION, INTERACTION WITH EIF4G1.
[13]"Human mRNA export machinery recruited to the 5' end of mRNA."
Cheng H., Dufu K., Lee C.-S., Hsu J.L., Dias A., Reed R.
Cell 127:1389-1400(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MRNA EXPORT.
[14]"The interaction between cap-binding complex and RNA export factor is required for intronless mRNA export."
Nojima T., Hirose T., Kimura H., Hagiwara M.
J. Biol. Chem. 282:15645-15651(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MRNA EXPORT, INTERACTION WITH ALYREF/THOC4.
[15]"Failsafe nonsense-mediated mRNA decay does not detectably target eIF4E-bound mRNA."
Matsuda D., Hosoda N., Kim Y.K., Maquat L.E.
Nat. Struct. Mol. Biol. 14:974-979(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY.
[16]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
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.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[17]"NMD resulting from encephalomyocarditis virus IRES-directed translation initiation seems to be restricted to CBP80/20-bound mRNA."
Woeller C.F., Gaspari M., Isken O., Maquat L.E.
EMBO Rep. 9:446-451(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY.
[18]"Ars2 links the nuclear cap-binding complex to RNA interference and cell proliferation."
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.
Cell 138:328-339(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MIRNAS BIOGENESIS.
[19]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[20]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[22]"Crystal structure of the human nuclear cap binding complex."
Mazza C., Ohno M., Segref A., Mattaj I.W., Cusack S.
Mol. Cell 8:383-396(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 20-790 IN COMPLEX WITH NCBP1, RNA-BINDING, MUTAGENESIS OF PHE-25; TYR-43; ASN-46; PHE-83; ASP-114; ASP-116 AND PHE-119.
[23]"Large-scale induced fit recognition of an m(7)GpppG cap analogue by the human nuclear cap-binding complex."
Mazza C., Segref A., Mattaj I.W., Cusack S.
EMBO J. 21:5548-5557(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 20-790 IN COMPLEX WITH NCBP1 AND MRNA CAP, RNA-BINDING, MUTAGENESIS OF TYR-20; TYR-43; ARG-112 AND TYR-138.
[24]"Structural basis of m7GpppG binding to the nuclear cap-binding protein complex."
Calero G., Wilson K.F., Ly T., Rios-Steiner J.L., Clardy J.C., Cerione R.A.
Nat. Struct. Biol. 9:912-917(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) IN COMPLEX WITH NCBP1 AND MRNA CAP, RNA-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X84157 mRNA. Translation: CAA58962.1.
D59253 mRNA. Translation: BAA09599.1.
AK297506 mRNA. Translation: BAG59919.1.
AK315903 mRNA. Translation: BAH14274.1.
AK316601 mRNA. Translation: BAG38188.1.
AY644767 mRNA. Translation: AAV85455.1.
BT006842 mRNA. Translation: AAP35488.1.
AC011322 Genomic DNA. No translation available.
CH471191 Genomic DNA. Translation: EAW53624.1.
BC001255 mRNA. Translation: AAH01255.1.
CCDSCCDS3323.1. [P52298-1]
PIRI37222.
S60109.
RefSeqNP_001036005.1. NM_001042540.1. [P52298-3]
NP_031388.2. NM_007362.3. [P52298-1]
XP_005269370.1. XM_005269313.1. [P52298-2]
UniGeneHs.591671.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H2TX-ray2.15Z1-156[»]
1H2UX-ray2.40X/Y1-156[»]
1H2VX-ray2.00Z1-156[»]
1H6KX-ray2.00X/Y/Z22-120[»]
1N52X-ray2.11B1-156[»]
1N54X-ray2.72B1-156[»]
3FEXX-ray3.55B1-156[»]
3FEYX-ray2.20B1-156[»]
DisProtDP00393.
ProteinModelPortalP52298.
SMRP52298. Positions 5-149.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116578. 13 interactions.
DIPDIP-33246N.
IntActP52298. 8 interactions.
MINTMINT-248711.
STRING9606.ENSP00000326806.

Protein family/group databases

TCDB9.A.60.1.1. the small nuclear rna exporter (snrna-e).

PTM databases

PhosphoSiteP52298.

Polymorphism databases

DMDM1705651.

Proteomic databases

MaxQBP52298.
PaxDbP52298.
PRIDEP52298.

Protocols and materials databases

DNASU22916.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000321256; ENSP00000326806; ENSG00000114503. [P52298-1]
ENST00000427641; ENSP00000397619; ENSG00000114503.
ENST00000452404; ENSP00000412785; ENSG00000114503. [P52298-2]
GeneID22916.
KEGGhsa:22916.
UCSCuc003fxb.1. human. [P52298-1]
uc011btz.1. human. [P52298-2]

Organism-specific databases

CTD22916.
GeneCardsGC03M196662.
HGNCHGNC:7659. NCBP2.
HPAHPA044850.
MIM605133. gene.
neXtProtNX_P52298.
PharmGKBPA31462.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0724.
HOGENOMHOG000217589.
HOVERGENHBG052581.
InParanoidP52298.
KOK12883.
OMAGNRYEQE.
PhylomeDBP52298.
TreeFamTF313897.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_1788. Transcription.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

ArrayExpressP52298.
BgeeP52298.
CleanExHS_NCBP2.
GenevestigatorP52298.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR027157. NCBP2.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PANTHERPTHR18847. PTHR18847. 1 hit.
PfamPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNCBP2. human.
EvolutionaryTraceP52298.
GenomeRNAi22916.
NextBio43603.
PROP52298.
SOURCESearch...

Entry information

Entry nameNCBP2_HUMAN
AccessionPrimary (citable) accession number: P52298
Secondary accession number(s): B2RE91 expand/collapse secondary AC list , B4DMK7, E9PAR5, Q14924, Q2TS50
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM