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Q09161

- NCBP1_HUMAN

UniProt

Q09161 - NCBP1_HUMAN

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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

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. RNA binding Source: ProtInc
  3. 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
Complete GO annotation...

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
Complete GO annotation...

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. 1 Publication
Mutagenesisi21 – 222TS → A: Reduced phosphorylation by RPS6KB1. Abolishes phosphorylation by RPS6KB1; when associated with A-7. 1 Publication

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

BgeeiQ09161.
CleanExiHS_NCBP1.
ExpressionAtlasiQ09161. baseline and differential.
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. 59 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.
GeneTreeiENSGT00390000001733.
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

        10         20         30         40         50
MSRRRHSDEN DGGQPHKRRK TSDANETEDH LESLICKVGE KSACSLESNL
60 70 80 90 100
EGLAGVLEAD LPNYKSKILR LLCTVARLLP EKLTIYTTLV GLLNARNYNF
110 120 130 140 150
GGEFVEAMIR QLKESLKANN YNEAVYLVRF LSDLVNCHVI AAPSMVAMFE
160 170 180 190 200
NFVSVTQEED VPQVRRDWYV YAFLSSLPWV GKELYEKKDA EMDRIFANTE
210 220 230 240 250
SYLKRRQKTH VPMLQVWTAD KPHPQEEYLD CLWAQIQKLK KDRWQERHIL
260 270 280 290 300
RPYLAFDSIL CEALQHNLPP FTPPPHTEDS VYPMPRVIFR MFDYTDDPEG
310 320 330 340 350
PVMPGSHSVE RFVIEENLHC IIKSHWKERK TCAAQLVSYP GKNKIPLNYH
360 370 380 390 400
IVEVIFAELF QLPAPPHIDV MYTTLLIELC KLQPGSLPQV LAQATEMLYM
410 420 430 440 450
RLDTMNTTCV DRFINWFSHH LSNFQFRWSW EDWSDCLSQD PESPKPKFVR
460 470 480 490 500
EVLEKCMRLS YHQRILDIVP PTFSALCPAN PTCIYKYGDE SSNSLPGHSV
510 520 530 540 550
ALCLAVAFKS KATNDEIFSI LKDVPNPNQD DDDDEGFSFN PLKIEVFVQT
560 570 580 590 600
LLHLAAKSFS HSFSALAKFH EVFKTLAESD EGKLHVLRVM FEVWRNHPQM
610 620 630 640 650
IAVLVDKMIR TQIVDCAAVA NWIFSSELSR DFTRLFVWEI LHSTIRKMNK
660 670 680 690 700
HVLKIQKELE EAKEKLARQH KRRSDDDDRS SDRKDGVLEE QIERLQEKVE
710 720 730 740 750
SAQSEQKNLF LVIFQRFIMI LTEHLVRCET DGTSVLTPWY KNCIERLQQI
760 770 780 790
FLQHHQIIQQ YMVTLENLLF TAELDPHILA VFQQFCALQA
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. 59 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.
GeneTreei ENSGT00390000001733.
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

Bgeei Q09161.
CleanExi HS_NCBP1.
ExpressionAtlasi Q09161. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 150 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