Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P52298

- NCBP2_HUMAN

UniProt

P52298 - NCBP2_HUMAN

Protein

Nuclear cap-binding protein subunit 2

Gene

NCBP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    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.7 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei20 – 201mRNA cap2 Publications
    Binding sitei43 – 431mRNA cap2 Publications

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. RNA 7-methylguanosine cap binding Source: UniProtKB
    5. RNA cap binding Source: UniProtKB

    GO - Biological processi

    1. 7-methylguanosine mRNA capping Source: UniProtKB
    2. gene expression Source: Reactome
    3. gene silencing by RNA Source: UniProtKB-KW
    4. histone mRNA metabolic process Source: Reactome
    5. mRNA 3'-end processing Source: Reactome
    6. mRNA cis splicing, via spliceosome Source: UniProtKB
    7. mRNA export from nucleus Source: Reactome
    8. mRNA metabolic process Source: Reactome
    9. mRNA splicing, via spliceosome Source: Reactome
    10. ncRNA metabolic process Source: Reactome
    11. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
    12. positive regulation of RNA export from nucleus Source: UniProtKB
    13. positive regulation of viral transcription Source: Reactome
    14. regulation of translational initiation Source: UniProtKB
    15. RNA metabolic process Source: Reactome
    16. RNA splicing Source: UniProtKB
    17. snRNA export from nucleus Source: UniProtKB
    18. spliceosomal snRNP assembly Source: Reactome
    19. termination of RNA polymerase II transcription Source: Reactome
    20. transcription elongation from RNA polymerase II promoter Source: Reactome
    21. transcription from RNA polymerase II promoter Source: Reactome
    22. viral process Source: Reactome

    Keywords - Biological processi

    mRNA capping, mRNA processing, mRNA splicing, mRNA transport, Nonsense-mediated mRNA decay, RNA-mediated gene silencing, Translation regulation, Transport

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_1096. Processing of Intronless Pre-mRNAs.
    REACT_11066. snRNP Assembly.
    REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
    REACT_1364. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
    REACT_1470. mRNA Capping.
    REACT_1597. Transport of Mature mRNA derived from an Intron-Containing Transcript.
    REACT_1753. mRNA Splicing - Minor Pathway.
    REACT_1835. Transport of Mature mRNA Derived from an Intronless Transcript.
    REACT_1849. mRNA 3'-end processing.
    REACT_185. SLBP independent Processing of Histone Pre-mRNAs.
    REACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
    REACT_405. Transport of the SLBP Dependant Mature mRNA.
    REACT_424. Transport of the SLBP independent Mature mRNA.
    REACT_467. mRNA Splicing - Major Pathway.
    REACT_6261. Abortive elongation of HIV-1 transcript in the absence of Tat.
    REACT_6319. Formation of the HIV-1 Early Elongation Complex.
    REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
    REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
    REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
    REACT_846. Formation of the Early Elongation Complex.

    Protein family/group databases

    TCDBi9.A.60.1.1. the small nuclear rna exporter (snrna-e).

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:NCBP2
    Synonyms:CBP20
    ORF Names:PIG55
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:7659. NCBP2.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. mRNA cap binding complex Source: UniProtKB
    4. nuclear cap binding complex Source: InterPro
    5. nucleoplasm Source: UniProtKB
    6. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi20 – 201Y → A: Abolishes mRNA cap-binding. 1 Publication
    Mutagenesisi20 – 201Y → F: Strongly impairs mRNA cap-binding. 1 Publication
    Mutagenesisi25 – 251F → A: Does not affect mRNA cap-binding. 1 Publication
    Mutagenesisi43 – 431Y → A: Abolishes mRNA cap-binding. 2 Publications
    Mutagenesisi43 – 431Y → F: Does not affect mRNA cap-binding. 2 Publications
    Mutagenesisi46 – 461N → A: Does not affect mRNA cap-binding. 1 Publication
    Mutagenesisi83 – 831F → A: Abolishes mRNA cap-binding. 1 Publication
    Mutagenesisi85 – 851F → A: Impairs mRNA cap-binding.
    Mutagenesisi112 – 1121R → A or T: Does not affect mRNA cap-binding. 1 Publication
    Mutagenesisi114 – 1141D → A: Does not affect mRNA cap-binding. 1 Publication
    Mutagenesisi116 – 1161D → A: Abolishes mRNA cap-binding. 1 Publication
    Mutagenesisi119 – 1191F → A: Does not affect mRNA cap-binding. 1 Publication
    Mutagenesisi138 – 1381Y → A: Does not affect mRNA cap-binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA31462.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 156155Nuclear cap-binding protein subunit 2PRO_0000081499Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei18 – 181Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP52298.
    PaxDbiP52298.
    PRIDEiP52298.

    PTM databases

    PhosphoSiteiP52298.

    Expressioni

    Gene expression databases

    ArrayExpressiP52298.
    BgeeiP52298.
    CleanExiHS_NCBP2.
    GenevestigatoriP52298.

    Organism-specific databases

    HPAiHPA044850.

    Interactioni

    Subunit structurei

    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.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NCBP1Q091616EBI-464729,EBI-464743

    Protein-protein interaction databases

    BioGridi116578. 15 interactions.
    DIPiDIP-33246N.
    IntActiP52298. 8 interactions.
    MINTiMINT-248711.
    STRINGi9606.ENSP00000326806.

    Structurei

    Secondary structure

    1
    156
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 104
    Helixi13 – 153
    Beta strandi23 – 275
    Turni34 – 385
    Beta strandi41 – 466
    Helixi53 – 608
    Helixi61 – 633
    Beta strandi66 – 738
    Turni75 – 773
    Beta strandi80 – 9011
    Helixi91 – 10010
    Turni101 – 1033
    Beta strandi104 – 1063
    Beta strandi112 – 1176
    Turni121 – 1244
    Helixi134 – 1374
    Helixi144 – 1463

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    DisProtiDP00393.
    ProteinModelPortaliP52298.
    SMRiP52298. Positions 5-149.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP52298.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini40 – 11879RRMPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni112 – 1165mRNA cap-binding
    Regioni123 – 1275mRNA cap-binding
    Regioni133 – 1342mRNA cap-binding

    Sequence similaritiesi

    Belongs to the RRM NCBP2 family.Curated
    Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0724.
    HOGENOMiHOG000217589.
    HOVERGENiHBG052581.
    InParanoidiP52298.
    KOiK12883.
    OMAiGNRYEQE.
    PhylomeDBiP52298.
    TreeFamiTF313897.

    Family and domain databases

    Gene3Di3.30.70.330. 1 hit.
    InterProiIPR027157. NCBP2.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PANTHERiPTHR18847. PTHR18847. 1 hit.
    PfamiPF00076. RRM_1. 1 hit.
    [Graphical view]
    SMARTiSM00360. RRM. 1 hit.
    [Graphical view]
    PROSITEiPS50102. RRM. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P52298-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MSGGLLKALR SDSYVELSQY RDQHFRGDNE EQEKLLKKSC TLYVGNLSFY    50
    TTEEQIYELF SKSGDIKKII MGLDKMKKTA CGFCFVEYYS RADAENAMRY 100
    INGTRLDDRI IRTDWDAGFK EGRQYGRGRS GGQVRDEYRQ DYDAGRGGYG 150
    KLAQNQ 156
    Length:156
    Mass (Da):18,001
    Last modified:October 1, 1996 - v1
    Checksum:iB6C94F3182A2CC3D
    GO
    Isoform 2 (identifier: P52298-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-26: MSGGLLKALRSDSYVELSQYRDQHFR → MVLRKLYA

    Show »
    Length:138
    Mass (Da):15,937
    Checksum:iD2475AF0597FDC0F
    GO
    Isoform 3 (identifier: P52298-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         40-93: CTLYVGNLSFYTTEEQIYELFSKSGDIKKIIMGLDKMKKTACGFCFVEYYSRAD → Y

    Note: Gene prediction based on EST data.

    Show »
    Length:103
    Mass (Da):11,932
    Checksum:i0790F40FF3E16B61
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti97 – 971A → S in BAA09599. (PubMed:7478990)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2626MSGGL…DQHFR → MVLRKLYA in isoform 2. 1 PublicationVSP_038125Add
    BLAST
    Alternative sequencei40 – 9354CTLYV…YSRAD → Y in isoform 3. CuratedVSP_053823Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS3323.1. [P52298-1]
    CCDS46986.1. [P52298-3]
    PIRiI37222.
    S60109.
    RefSeqiNP_001036005.1. NM_001042540.1. [P52298-3]
    NP_031388.2. NM_007362.3. [P52298-1]
    XP_005269370.1. XM_005269313.1. [P52298-2]
    UniGeneiHs.591671.

    Genome annotation databases

    EnsembliENST00000321256; ENSP00000326806; ENSG00000114503. [P52298-1]
    ENST00000427641; ENSP00000397619; ENSG00000114503. [P52298-3]
    ENST00000452404; ENSP00000412785; ENSG00000114503. [P52298-2]
    GeneIDi22916.
    KEGGihsa:22916.
    UCSCiuc003fxb.1. human. [P52298-1]
    uc011btz.1. human. [P52298-2]

    Polymorphism databases

    DMDMi1705651.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS3323.1. [P52298-1 ]
    CCDS46986.1. [P52298-3 ]
    PIRi I37222.
    S60109.
    RefSeqi NP_001036005.1. NM_001042540.1. [P52298-3 ]
    NP_031388.2. NM_007362.3. [P52298-1 ]
    XP_005269370.1. XM_005269313.1. [P52298-2 ]
    UniGenei Hs.591671.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1H2T X-ray 2.15 Z 1-156 [» ]
    1H2U X-ray 2.40 X/Y 1-156 [» ]
    1H2V X-ray 2.00 Z 1-156 [» ]
    1H6K X-ray 2.00 X/Y/Z 22-120 [» ]
    1N52 X-ray 2.11 B 1-156 [» ]
    1N54 X-ray 2.72 B 1-156 [» ]
    3FEX X-ray 3.55 B 1-156 [» ]
    3FEY X-ray 2.20 B 1-156 [» ]
    DisProti DP00393.
    ProteinModelPortali P52298.
    SMRi P52298. Positions 5-149.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116578. 15 interactions.
    DIPi DIP-33246N.
    IntActi P52298. 8 interactions.
    MINTi MINT-248711.
    STRINGi 9606.ENSP00000326806.

    Protein family/group databases

    TCDBi 9.A.60.1.1. the small nuclear rna exporter (snrna-e).

    PTM databases

    PhosphoSitei P52298.

    Polymorphism databases

    DMDMi 1705651.

    Proteomic databases

    MaxQBi P52298.
    PaxDbi P52298.
    PRIDEi P52298.

    Protocols and materials databases

    DNASUi 22916.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000321256 ; ENSP00000326806 ; ENSG00000114503 . [P52298-1 ]
    ENST00000427641 ; ENSP00000397619 ; ENSG00000114503 . [P52298-3 ]
    ENST00000452404 ; ENSP00000412785 ; ENSG00000114503 . [P52298-2 ]
    GeneIDi 22916.
    KEGGi hsa:22916.
    UCSCi uc003fxb.1. human. [P52298-1 ]
    uc011btz.1. human. [P52298-2 ]

    Organism-specific databases

    CTDi 22916.
    GeneCardsi GC03M196662.
    HGNCi HGNC:7659. NCBP2.
    HPAi HPA044850.
    MIMi 605133. gene.
    neXtProti NX_P52298.
    PharmGKBi PA31462.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0724.
    HOGENOMi HOG000217589.
    HOVERGENi HBG052581.
    InParanoidi P52298.
    KOi K12883.
    OMAi GNRYEQE.
    PhylomeDBi P52298.
    TreeFami TF313897.

    Enzyme and pathway databases

    Reactomei REACT_1096. Processing of Intronless Pre-mRNAs.
    REACT_11066. snRNP Assembly.
    REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
    REACT_1364. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
    REACT_1470. mRNA Capping.
    REACT_1597. Transport of Mature mRNA derived from an Intron-Containing Transcript.
    REACT_1753. mRNA Splicing - Minor Pathway.
    REACT_1835. Transport of Mature mRNA Derived from an Intronless Transcript.
    REACT_1849. mRNA 3'-end processing.
    REACT_185. SLBP independent Processing of Histone Pre-mRNAs.
    REACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
    REACT_405. Transport of the SLBP Dependant Mature mRNA.
    REACT_424. Transport of the SLBP independent Mature mRNA.
    REACT_467. mRNA Splicing - Major Pathway.
    REACT_6261. Abortive elongation of HIV-1 transcript in the absence of Tat.
    REACT_6319. Formation of the HIV-1 Early Elongation Complex.
    REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
    REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
    REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
    REACT_846. Formation of the Early Elongation Complex.

    Miscellaneous databases

    ChiTaRSi NCBP2. human.
    EvolutionaryTracei P52298.
    GenomeRNAii 22916.
    NextBioi 43603.
    PROi P52298.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P52298.
    Bgeei P52298.
    CleanExi HS_NCBP2.
    Genevestigatori P52298.

    Family and domain databases

    Gene3Di 3.30.70.330. 1 hit.
    InterProi IPR027157. NCBP2.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    PANTHERi PTHR18847. PTHR18847. 1 hit.
    Pfami PF00076. RRM_1. 1 hit.
    [Graphical view ]
    SMARTi SM00360. RRM. 1 hit.
    [Graphical view ]
    PROSITEi PS50102. RRM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. 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.
      , 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.
      , 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. 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.

    Entry informationi

    Entry nameiNCBP2_HUMAN
    AccessioniPrimary (citable) accession number: P52298
    Secondary accession number(s): B2RE91
    , B4DMK7, E9PAR5, Q14924, Q2TS50
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 154 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3