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Q3UYV9

- NCBP1_MOUSE

UniProt

Q3UYV9 - NCBP1_MOUSE

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Protein

Nuclear cap-binding protein subunit 1

Gene
Ncbp1, Cbp80
Organism
Mus musculus (Mouse)
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.1 Publication

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. RNA cap binding Source: InterPro

GO - Biological processi

  1. 7-methylguanosine mRNA capping Source: UniProtKB
  2. gene silencing by RNA Source: UniProtKB-KW
  3. mRNA cis splicing, via spliceosome Source: InterPro
  4. mRNA cleavage Source: UniProtKB
  5. mRNA export from nucleus Source: UniProtKB
  6. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
  7. positive regulation of mRNA 3'-end processing Source: UniProtKB
  8. regulation of translational initiation Source: UniProtKB
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_198524. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_198528. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_203462. Formation of the Early Elongation Complex.
REACT_206812. snRNP Assembly.
REACT_212343. Transport of the SLBP independent Mature mRNA.
REACT_215668. SLBP independent Processing of Histone Pre-mRNAs.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:1891840. Ncbp1.

Subcellular locationi

Nucleus. Cytoplasm By similarity
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs By similarity.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. mRNA cap binding complex Source: UniProtKB
  3. nuclear cap binding complex Source: InterPro
  4. nucleus Source: UniProtKB
  5. ribonucleoprotein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 790790Nuclear cap-binding protein subunit 1PRO_0000239779Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei7 – 71Phosphoserine By similarity
Modified residuei21 – 211Phosphothreonine By similarity
Modified residuei22 – 221Phosphoserine1 Publication
Modified residuei204 – 2041N6-acetyllysine By similarity
Modified residuei698 – 6981N6-acetyllysine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ3UYV9.
PaxDbiQ3UYV9.
PRIDEiQ3UYV9.

PTM databases

PhosphoSiteiQ3UYV9.

Expressioni

Gene expression databases

BgeeiQ3UYV9.
GenevestigatoriQ3UYV9.

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. The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active).4 Publications

Protein-protein interaction databases

BioGridi241386. 1 interaction.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UKZX-ray2.30C1-23[»]
3UL0X-ray2.00C1-23[»]
ProteinModelPortaliQ3UYV9.
SMRiQ3UYV9. Positions 2-790.

Family & Domainsi

Domains and Repeats

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili643 – 71371 Reviewed predictionAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi3 – 2018Nuclear localization signal Reviewed predictionAdd
BLAST

Sequence similaritiesi

Belongs to the NCBP1 family.
Contains 1 MIF4G domain.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG303489.
GeneTreeiENSGT00390000001733.
HOGENOMiHOG000007990.
HOVERGENiHBG080328.
InParanoidiB1AWH4.
KOiK12882.
OMAiLICRVGE.
OrthoDBiEOG7K9K28.
PhylomeDBiQ3UYV9.
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.

Q3UYV9-1 [UniParc]FASTAAdd to Basket

« Hide

MSRRRHSYEN DGGQPHKRRK TSDANETEDH LESLICKVGE KSACSLESNL    50
EGLAGVLEAD LPNYKSKILR LLCTVARLLP EKLTIYTTLV GLLNARNYNF 100
GGEFVEAMIR QLKESLKANN YNEAVYLVRF LSDLVNCHVI AAPSMVAMFE 150
NFVSVTQEED VPQVRRDWYV YAFLSSLPWV GKELYEKKDA EMDRIFSTTE 200
SYLKRRQKTH VPMLQVWTAD KPHPQEEYLD CLWAQIQKLK KDRWQERHIL 250
RPYLAFDSIL CEALQHNLPP FTPPPHTEDS VYPMPRVIFR MFDYTDDPEG 300
PVMPGSHSVE RFVIEENLHC IIKSYWKERK TCAAQLVSYP GKNKIPLNYH 350
IVEVIFAELF QLPAPPHIDV MYTTLLIELC KLQPGSLPQV LAQATEMLYM 400
RLDTMSTTCV DRFINWFSHH LSNFQFRWSW EDWSDCLTQD LESPKPKFVR 450
EVLEKCMRLS YHQHILDIVP PTFSALCPAN PTCIYKYGDE SSNSLPGHSV 500
ALCLSVAFKS KATNDEIFSI LKDVPNPNQV DDDDEGFRFN PLKIEVFVQT 550
LLHLAAKSFS HSFSALAKFH EVFKTLAESD KGKLHVLRVM FEVWRNHPQM 600
IAVLVDKMIR TQIVDCAAVA NWIFSSELSR DFTRLFVWEI LHSTIRKMNK 650
HVLKIQKELE EAKEKLARQH KRRSDDDDRS SDRKDGALEE QIERLQEKVE 700
AAQSEQKNLF LVIFQRFIMI LTEHLVRCET DGTSILTPWY KNCIERLQQI 750
FLQHHQTIQQ YMVTLENLLF TAELDPHILA VFQQFCALQA 790
Length:790
Mass (Da):91,927
Last modified:June 13, 2006 - v2
Checksum:iBE27F89BDBC19CF2
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti319 – 3191H → R in BAE22102. 1 Publication
Sequence conflicti443 – 4431S → R in BAE22102. 1 Publication
Sequence conflicti453 – 4531L → I in BAE22102. 1 Publication
Sequence conflicti574 – 5741K → Q in BAE22102. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK134334 mRNA. Translation: BAE22102.1.
AK169557 mRNA. Translation: BAE41227.1.
AL929438, AL732615 Genomic DNA. Translation: CAM14995.1.
AL732615, AL929438 Genomic DNA. Translation: CAM17033.1.
CH466565 Genomic DNA. Translation: EDL02380.1.
BC055777 mRNA. Translation: AAH55777.1.
BC138898 mRNA. Translation: AAI38899.1.
CCDSiCCDS18145.1.
RefSeqiNP_001028373.2. NM_001033201.3.
UniGeneiMm.389536.

Genome annotation databases

EnsembliENSMUST00000030014; ENSMUSP00000030014; ENSMUSG00000028330.
GeneIDi433702.
KEGGimmu:433702.
UCSCiuc008stk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK134334 mRNA. Translation: BAE22102.1 .
AK169557 mRNA. Translation: BAE41227.1 .
AL929438 , AL732615 Genomic DNA. Translation: CAM14995.1 .
AL732615 , AL929438 Genomic DNA. Translation: CAM17033.1 .
CH466565 Genomic DNA. Translation: EDL02380.1 .
BC055777 mRNA. Translation: AAH55777.1 .
BC138898 mRNA. Translation: AAI38899.1 .
CCDSi CCDS18145.1.
RefSeqi NP_001028373.2. NM_001033201.3.
UniGenei Mm.389536.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3UKZ X-ray 2.30 C 1-23 [» ]
3UL0 X-ray 2.00 C 1-23 [» ]
ProteinModelPortali Q3UYV9.
SMRi Q3UYV9. Positions 2-790.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 241386. 1 interaction.

PTM databases

PhosphoSitei Q3UYV9.

Proteomic databases

MaxQBi Q3UYV9.
PaxDbi Q3UYV9.
PRIDEi Q3UYV9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000030014 ; ENSMUSP00000030014 ; ENSMUSG00000028330 .
GeneIDi 433702.
KEGGi mmu:433702.
UCSCi uc008stk.1. mouse.

Organism-specific databases

CTDi 4686.
MGIi MGI:1891840. Ncbp1.

Phylogenomic databases

eggNOGi NOG303489.
GeneTreei ENSGT00390000001733.
HOGENOMi HOG000007990.
HOVERGENi HBG080328.
InParanoidi B1AWH4.
KOi K12882.
OMAi LICRVGE.
OrthoDBi EOG7K9K28.
PhylomeDBi Q3UYV9.
TreeFami TF313400.

Enzyme and pathway databases

Reactomei REACT_198524. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_198528. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_203462. Formation of the Early Elongation Complex.
REACT_206812. snRNP Assembly.
REACT_212343. Transport of the SLBP independent Mature mRNA.
REACT_215668. SLBP independent Processing of Histone Pre-mRNAs.

Miscellaneous databases

ChiTaRSi NCBP1. mouse.
NextBioi 408905.
PROi Q3UYV9.
SOURCEi Search...

Gene expression databases

Bgeei Q3UYV9.
Genevestigatori Q3UYV9.

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. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Testis and Thymus.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Strain: C57BL/6.
    Tissue: Brain.
  5. "PHAX, a mediator of U snRNA nuclear export whose activity is regulated by phosphorylation."
    Ohno M., Segref A., Bachi A., Wilm M., Mattaj I.W.
    Cell 101:187-198(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A U SNRNA EXPORT COMPLEX WITH RNUXA/PHAX; NCBP2; RAN; XPO1 AND M7G-CAPPED RNA.
  6. "The evolutionarily conserved region of the U snRNA export mediator PHAX is a novel RNA-binding domain that is essential for U snRNA export."
    Segref A., Mattaj I.W., Ohno M.
    RNA 7:351-360(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNUXA/PHAX.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "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, INTERACTION WITH SRRT AND DROSHA.
  9. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Feedback regulation of transcriptional termination by the mammalian circadian clock PERIOD complex."
    Padmanabhan K., Robles M.S., Westerling T., Weitz C.J.
    Science 337:599-602(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A LARGE PER COMPLEX, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiNCBP1_MOUSE
AccessioniPrimary (citable) accession number: Q3UYV9
Secondary accession number(s): B1AWH4, Q3TEM1, Q7TNE8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: June 13, 2006
Last modified: September 3, 2014
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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