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Q09161

- NCBP1_HUMAN

UniProt

Q09161 - NCBP1_HUMAN

Protein

Nuclear cap-binding protein subunit 1

Gene

NCBP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Component of the cap-binding complex (CBC), which binds cotranscriptionally 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 and is 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, NCBP1/CBP80 does not bind directly capped RNAs (m7GpppG-capped RNA) but is required to stabilize the movement of the N-terminal loop of NCBP2/CBP20 and lock the CBC into a high affinity cap-binding state with the cap structure.13 Publications

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. RNA binding Source: ProtInc
    4. RNA cap binding Source: ProtInc

    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: InterPro
    7. mRNA cleavage Source: UniProtKB
    8. mRNA export from nucleus Source: UniProtKB
    9. mRNA metabolic process Source: Reactome
    10. mRNA splicing, via spliceosome Source: Reactome
    11. ncRNA metabolic process Source: Reactome
    12. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
    13. positive regulation of mRNA 3'-end processing Source: UniProtKB
    14. positive regulation of viral transcription Source: Reactome
    15. regulation of translational initiation Source: UniProtKB
    16. RNA metabolic process Source: Reactome
    17. RNA splicing Source: Reactome
    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

    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 1
    Alternative name(s):
    80 kDa nuclear cap-binding protein
    Short name:
    CBP80
    Short name:
    NCBP 80 kDa subunit
    Gene namesi
    Name:NCBP1
    Synonyms:CBP80, NCBP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:7658. NCBP1.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. mitochondrion Source: HPA
    4. mRNA cap binding complex Source: UniProtKB
    5. nuclear cap binding complex Source: InterPro
    6. nucleoplasm Source: Reactome
    7. nucleus Source: UniProtKB
    8. plasma membrane Source: HPA
    9. ribonucleoprotein complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi7 – 71S → A: Reduced phosphorylation by RPS6KB1. Abolishes phosphorylation by RPS6KB1; when associated with 21-A-A-22. 1 Publication
    Mutagenesisi17 – 182KR → AA: Abolishes nuclear localization and phosphorylation by RPS6KB1.
    Mutagenesisi21 – 222TS → A: Reduced phosphorylation by RPS6KB1. Abolishes phosphorylation by RPS6KB1; when associated with A-7.

    Organism-specific databases

    PharmGKBiPA31461.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 790790Nuclear cap-binding protein subunit 1PRO_0000089364Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei7 – 71Phosphoserine; by RPS6KB11 Publication
    Modified residuei21 – 211Phosphothreonine; by RPS6KB12 Publications
    Modified residuei22 – 221Phosphoserine; by RPS6KB13 Publications
    Modified residuei204 – 2041N6-acetyllysine1 Publication
    Modified residuei698 – 6981N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ09161.
    PaxDbiQ09161.
    PeptideAtlasiQ09161.
    PRIDEiQ09161.

    PTM databases

    PhosphoSiteiQ09161.

    Expressioni

    Gene expression databases

    ArrayExpressiQ09161.
    BgeeiQ09161.
    CleanExiHS_NCBP1.
    GenevestigatoriQ09161.

    Organism-specific databases

    HPAiHPA042411.
    HPA049031.

    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 containing RNUXA/PHAX, NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-capped RNA. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with RNUXA/PHAX, SRRT/ARS2, EIF4G2, IGF2BP1, HNRNPF, HNRNPH1, KIAA0427/CTIF, PARN, DROSHA, UPF1 and ALYREF/THOC4. May interact with EIF4G1; the interaction is however controversial since it is reported by PubMed:11340157, PubMed:15059963 and PubMed:15361857, but is not observed by PubMed:19648179. The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A.13 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NCBP2P522986EBI-464743,EBI-464729
    PARNO954532EBI-464743,EBI-372832
    POLDIP3Q9BY773EBI-464743,EBI-1776152
    RPS6P627533EBI-464743,EBI-356625

    Protein-protein interaction databases

    BioGridi110766. 57 interactions.
    DIPiDIP-33244N.
    IntActiQ09161. 29 interactions.
    MINTiMINT-248693.
    STRINGi9606.ENSP00000364289.

    Structurei

    Secondary structure

    1
    790
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi30 – 367
    Turni37 – 393
    Helixi46 – 5914
    Helixi61 – 7818
    Helixi80 – 823
    Helixi83 – 9412
    Helixi98 – 11720
    Helixi121 – 13616
    Beta strandi138 – 1403
    Helixi142 – 15413
    Helixi155 – 1573
    Helixi163 – 17412
    Helixi177 – 20428
    Helixi211 – 2144
    Beta strandi216 – 2183
    Beta strandi221 – 2233
    Helixi228 – 24114
    Turni242 – 2443
    Beta strandi247 – 2493
    Helixi252 – 2565
    Turni257 – 2593
    Helixi262 – 2643
    Helixi294 – 2963
    Beta strandi298 – 3014
    Helixi309 – 32517
    Helixi329 – 3379
    Helixi347 – 35913
    Helixi369 – 38214
    Turni384 – 3863
    Helixi387 – 40014
    Helixi402 – 4043
    Helixi407 – 42115
    Turni422 – 4265
    Helixi430 – 4367
    Helixi444 – 45815
    Helixi462 – 4687
    Helixi471 – 4766
    Beta strandi488 – 4903
    Beta strandi493 – 4953
    Helixi498 – 50912
    Helixi514 – 5207
    Helixi521 – 5233
    Helixi541 – 55414
    Turni555 – 5573
    Helixi559 – 56810
    Helixi570 – 5767
    Helixi580 – 59415
    Helixi598 – 61013
    Helixi616 – 6238
    Helixi626 – 6283
    Turni629 – 6335
    Helixi635 – 66127
    Helixi693 – 73139
    Helixi738 – 75316
    Helixi755 – 7584
    Helixi759 – 7613
    Helixi762 – 7687
    Helixi776 – 78712

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1H2TX-ray2.10C20-652[»]
    C702-790[»]
    1H2UX-ray2.40A/B20-652[»]
    A/B702-790[»]
    1H2VX-ray2.00C20-790[»]
    1H6KX-ray2.00A/B/C20-790[»]
    1N52X-ray2.11A1-790[»]
    1N54X-ray2.72A1-790[»]
    3FEXX-ray3.55A1-790[»]
    3FEYX-ray2.20A1-790[»]
    DisProtiDP00392.
    ProteinModelPortaliQ09161.
    SMRiQ09161. Positions 2-790.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ09161.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini28 – 240213MIF4GAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili643 – 71371Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi3 – 2018Nuclear localization signalSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the NCBP1 family.Curated
    Contains 1 MIF4G domain.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG303489.
    HOGENOMiHOG000007990.
    HOVERGENiHBG080328.
    InParanoidiQ09161.
    KOiK12882.
    OMAiLICRVGE.
    OrthoDBiEOG7K9K28.
    PhylomeDBiQ09161.
    TreeFamiTF313400.

    Family and domain databases

    Gene3Di1.25.40.180. 4 hits.
    InterProiIPR016024. ARM-type_fold.
    IPR027159. CBP80.
    IPR016021. MIF4-like_typ_1/2/3.
    IPR015172. MIF4G-like_typ-1.
    IPR015174. MIF4G-like_typ-2.
    IPR003890. MIF4G-like_typ-3.
    [Graphical view]
    PANTHERiPTHR12412. PTHR12412. 1 hit.
    PfamiPF02854. MIF4G. 1 hit.
    PF09088. MIF4G_like. 1 hit.
    PF09090. MIF4G_like_2. 1 hit.
    [Graphical view]
    SMARTiSM00543. MIF4G. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 3 hits.

    Sequencei

    Sequence statusi: Complete.

    Q09161-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRRRHSDEN DGGQPHKRRK TSDANETEDH LESLICKVGE KSACSLESNL    50
    EGLAGVLEAD LPNYKSKILR LLCTVARLLP EKLTIYTTLV GLLNARNYNF 100
    GGEFVEAMIR QLKESLKANN YNEAVYLVRF LSDLVNCHVI AAPSMVAMFE 150
    NFVSVTQEED VPQVRRDWYV YAFLSSLPWV GKELYEKKDA EMDRIFANTE 200
    SYLKRRQKTH VPMLQVWTAD KPHPQEEYLD CLWAQIQKLK KDRWQERHIL 250
    RPYLAFDSIL CEALQHNLPP FTPPPHTEDS VYPMPRVIFR MFDYTDDPEG 300
    PVMPGSHSVE RFVIEENLHC IIKSHWKERK TCAAQLVSYP GKNKIPLNYH 350
    IVEVIFAELF QLPAPPHIDV MYTTLLIELC KLQPGSLPQV LAQATEMLYM 400
    RLDTMNTTCV DRFINWFSHH LSNFQFRWSW EDWSDCLSQD PESPKPKFVR 450
    EVLEKCMRLS YHQRILDIVP PTFSALCPAN PTCIYKYGDE SSNSLPGHSV 500
    ALCLAVAFKS KATNDEIFSI LKDVPNPNQD DDDDEGFSFN PLKIEVFVQT 550
    LLHLAAKSFS HSFSALAKFH EVFKTLAESD EGKLHVLRVM FEVWRNHPQM 600
    IAVLVDKMIR TQIVDCAAVA NWIFSSELSR DFTRLFVWEI LHSTIRKMNK 650
    HVLKIQKELE EAKEKLARQH KRRSDDDDRS SDRKDGVLEE QIERLQEKVE 700
    SAQSEQKNLF LVIFQRFIMI LTEHLVRCET DGTSVLTPWY KNCIERLQQI 750
    FLQHHQIIQQ YMVTLENLLF TAELDPHILA VFQQFCALQA 790
    Length:790
    Mass (Da):91,839
    Last modified:October 1, 1996 - v1
    Checksum:iF10DE7B9D16FDA0B
    GO

    Sequence cautioni

    The sequence BAD92470.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAI12863.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti80 – 801P → S in BAG35665. (PubMed:14702039)Curated
    Sequence conflicti159 – 1591E → D in BAD92470. 1 PublicationCurated
    Sequence conflicti674 – 6741S → G in BAG35665. (PubMed:14702039)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X80030 mRNA. Translation: CAA56334.1.
    D32002 mRNA. Translation: BAA06769.1.
    AK312807 mRNA. Translation: BAG35665.1.
    AB209233 mRNA. Translation: BAD92470.1. Different initiation.
    AL445531, AL162385 Genomic DNA. Translation: CAI15431.1.
    AL162385, AL445531 Genomic DNA. Translation: CAI12861.1.
    AL162385 Genomic DNA. Translation: CAI12863.1. Sequence problems.
    BC001450 mRNA. Translation: AAH01450.1.
    CCDSiCCDS6728.1.
    PIRiS50082.
    RefSeqiNP_002477.1. NM_002486.4.
    UniGeneiHs.595669.
    Hs.686479.

    Genome annotation databases

    EnsembliENST00000375147; ENSP00000364289; ENSG00000136937.
    GeneIDi4686.
    KEGGihsa:4686.
    UCSCiuc004axq.3. human.

    Polymorphism databases

    DMDMi1705654.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X80030 mRNA. Translation: CAA56334.1 .
    D32002 mRNA. Translation: BAA06769.1 .
    AK312807 mRNA. Translation: BAG35665.1 .
    AB209233 mRNA. Translation: BAD92470.1 . Different initiation.
    AL445531 , AL162385 Genomic DNA. Translation: CAI15431.1 .
    AL162385 , AL445531 Genomic DNA. Translation: CAI12861.1 .
    AL162385 Genomic DNA. Translation: CAI12863.1 . Sequence problems.
    BC001450 mRNA. Translation: AAH01450.1 .
    CCDSi CCDS6728.1.
    PIRi S50082.
    RefSeqi NP_002477.1. NM_002486.4.
    UniGenei Hs.595669.
    Hs.686479.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1H2T X-ray 2.10 C 20-652 [» ]
    C 702-790 [» ]
    1H2U X-ray 2.40 A/B 20-652 [» ]
    A/B 702-790 [» ]
    1H2V X-ray 2.00 C 20-790 [» ]
    1H6K X-ray 2.00 A/B/C 20-790 [» ]
    1N52 X-ray 2.11 A 1-790 [» ]
    1N54 X-ray 2.72 A 1-790 [» ]
    3FEX X-ray 3.55 A 1-790 [» ]
    3FEY X-ray 2.20 A 1-790 [» ]
    DisProti DP00392.
    ProteinModelPortali Q09161.
    SMRi Q09161. Positions 2-790.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110766. 57 interactions.
    DIPi DIP-33244N.
    IntActi Q09161. 29 interactions.
    MINTi MINT-248693.
    STRINGi 9606.ENSP00000364289.

    Protein family/group databases

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

    PTM databases

    PhosphoSitei Q09161.

    Polymorphism databases

    DMDMi 1705654.

    Proteomic databases

    MaxQBi Q09161.
    PaxDbi Q09161.
    PeptideAtlasi Q09161.
    PRIDEi Q09161.

    Protocols and materials databases

    DNASUi 4686.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375147 ; ENSP00000364289 ; ENSG00000136937 .
    GeneIDi 4686.
    KEGGi hsa:4686.
    UCSCi uc004axq.3. human.

    Organism-specific databases

    CTDi 4686.
    GeneCardsi GC09P100395.
    HGNCi HGNC:7658. NCBP1.
    HPAi HPA042411.
    HPA049031.
    MIMi 600469. gene.
    neXtProti NX_Q09161.
    PharmGKBi PA31461.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG303489.
    HOGENOMi HOG000007990.
    HOVERGENi HBG080328.
    InParanoidi Q09161.
    KOi K12882.
    OMAi LICRVGE.
    OrthoDBi EOG7K9K28.
    PhylomeDBi Q09161.
    TreeFami TF313400.

    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 NCBP1. human.
    EvolutionaryTracei Q09161.
    GenomeRNAii 4686.
    NextBioi 18072.
    PROi Q09161.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q09161.
    Bgeei Q09161.
    CleanExi HS_NCBP1.
    Genevestigatori Q09161.

    Family and domain databases

    Gene3Di 1.25.40.180. 4 hits.
    InterProi IPR016024. ARM-type_fold.
    IPR027159. CBP80.
    IPR016021. MIF4-like_typ_1/2/3.
    IPR015172. MIF4G-like_typ-1.
    IPR015174. MIF4G-like_typ-2.
    IPR003890. MIF4G-like_typ-3.
    [Graphical view ]
    PANTHERi PTHR12412. PTHR12412. 1 hit.
    Pfami PF02854. MIF4G. 1 hit.
    PF09088. MIF4G_like. 1 hit.
    PF09090. MIF4G_like_2. 1 hit.
    [Graphical view ]
    SMARTi SM00543. MIF4G. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 3 hits.
    ProtoNeti Search...

    Publicationsi

    1. "A nuclear cap binding protein complex involved in pre-mRNA splicing."
      Izaurralde E., Lewis J., McGuigan C., Jankowska E., Darzynkiewicz E., Mattaj I.W.
      Cell 78:657-668(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 119-128; 513-522 AND 687-693, FUNCTION IN MRNA SPLICING.
    2. "Cloning of a complementary DNA encoding an 80 kilodalton nuclear cap binding protein."
      Kataoka N., Ohno M., Kangawa K., Tokoro Y., Shimura Y.
      Nucleic Acids Res. 22:3861-3865(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    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].
      Tissue: Testis.
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    5. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
      Tissue: Placenta.
    7. Cited for: FUNCTION.
    8. "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.
    9. "Cdc42 stimulates RNA splicing via the S6 kinase and a novel S6 kinase target, the nuclear cap-binding complex."
      Wilson K.F., Wu W.J., Cerione R.A.
      J. Biol. Chem. 275:37307-37310(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-7; THR-21 AND SER-22, MUTAGENESIS OF SER-7; 17-LYS-ARG-18 AND 21-THR-SER-22.
    10. "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.
    11. "Interaction of eukaryotic translation initiation factor 4G with the nuclear cap-binding complex provides a link between nuclear and cytoplasmic functions of the m(7) guanosine cap."
      McKendrick L., Thompson E., Ferreira J., Morley S.J., Lewis J.D.
      Mol. Cell. Biol. 21:3632-3641(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF4G1.
    12. "The exon junction complex is detected on CBP80-bound but not eIF4E-bound mRNA in mammalian cells: dynamics of mRNP remodeling."
      Lejeune F., Ishigaki Y., Li X., Maquat L.E.
      EMBO J. 21:3536-3545(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "The pioneer translation initiation complex is functionally distinct from but structurally overlaps with the steady-state translation initiation complex."
      Chiu S.-Y., Lejeune F., Ranganathan A.C., Maquat L.E.
      Genes Dev. 18:745-754(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION, INTERACTION WITH EIF4G1.
    14. "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 AND EIF4G2.
    15. "CBP80 promotes interaction of Upf1 with Upf2 during nonsense-mediated mRNA decay in mammalian cells."
      Hosoda N., Kim Y.K., Lejeune F., Maquat L.E.
      Nat. Struct. Mol. Biol. 12:893-901(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, INTERACTION WITH UPF1.
    16. "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, INTERACTION WITH ALYREF/THOC4.
    17. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "Inhibition of mRNA deadenylation by the nuclear cap binding complex (CBC)."
      Balatsos N.A.A., Nilsson P., Mazza C., Cusack S., Virtanen A.
      J. Biol. Chem. 281:4517-4522(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MRNA DEADENYLATION, INTERACTION WITH PARN.
    19. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    20. "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.
    21. "SKAR links pre-mRNA splicing to mTOR/S6K1-mediated enhanced translation efficiency of spliced mRNAs."
      Ma X.M., Yoon S.O., Richardson C.J., Julich K., Blenis J.
      Cell 133:303-313(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH POLDIP3.
    22. "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.
    23. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21 AND SER-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. "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.
    26. "A new MIF4G domain-containing protein, CTIF, directs nuclear cap-binding protein CBP80/20-dependent translation."
      Kim K.M., Cho H., Choi K., Kim J., Kim B.-W., Ko Y.-G., Jang S.K., Kim Y.K.
      Genes Dev. 23:2033-2045(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION, INTERACTION WITH KIAA0427, SUBCELLULAR LOCATION.
    27. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    28. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-204 AND LYS-698, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    30. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. "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 NCBP2.
    33. "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 NCBP2.
    34. "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 NCBP2.

    Entry informationi

    Entry nameiNCBP1_HUMAN
    AccessioniPrimary (citable) accession number: Q09161
    Secondary accession number(s): B2R718
    , Q59G76, Q5T1V0, Q5T7X2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 149 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 9
      Human chromosome 9: 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