Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q3UYV9 (NCBP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Ncbp1
Synonyms:Cbp80
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length790 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8

Subunit structure

Component of the nuclear cap-binding complex (CBC), a heterodimer composed of NCBP1/CBP80 and NCBP2/CBP20 that interacts with m7GpppG-capped RNA. Found in a U snRNA export complex 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. Ref.5 Ref.6 Ref.8

Subcellular location

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

Sequence similarities

Belongs to the NCBP1 family.

Contains 1 MIF4G domain.

Ontologies

Keywords
   Biological processmRNA capping
mRNA processing
mRNA splicing
mRNA transport
Nonsense-mediated mRNA decay
RNA-mediated gene silencing
Translation regulation
Transport
   Cellular componentCytoplasm
Nucleus
   DomainCoiled coil
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process7-methylguanosine mRNA capping

Inferred from sequence or structural similarity. Source: UniProtKB

gene silencing by RNA

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA cis splicing, via spliceosome

Inferred from electronic annotation. Source: InterPro

mRNA cleavage

Inferred from sequence or structural similarity. Source: UniProtKB

mRNA export from nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of mRNA 3'-end processing

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of translational initiation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

mRNA cap binding complex

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear cap binding complex

Inferred from electronic annotation. Source: InterPro

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

ribonucleoprotein complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionRNA cap binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 790790Nuclear cap-binding protein subunit 1
PRO_0000239779

Regions

Domain28 – 240213MIF4G
Coiled coil643 – 71371 Potential
Motif3 – 2018Nuclear localization signal Potential

Amino acid modifications

Modified residue71Phosphoserine By similarity
Modified residue211Phosphothreonine By similarity
Modified residue221Phosphoserine Ref.7
Modified residue2041N6-acetyllysine By similarity
Modified residue6981N6-acetyllysine By similarity

Experimental info

Sequence conflict3191H → R in BAE22102. Ref.1
Sequence conflict4431S → R in BAE22102. Ref.1
Sequence conflict4531L → I in BAE22102. Ref.1
Sequence conflict5741K → Q in BAE22102. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q3UYV9 [UniParc].

Last modified June 13, 2006. Version 2.
Checksum: BE27F89BDBC19CF2

FASTA79091,927
        10         20         30         40         50         60 
MSRRRHSYEN DGGQPHKRRK TSDANETEDH LESLICKVGE KSACSLESNL EGLAGVLEAD 

        70         80         90        100        110        120 
LPNYKSKILR LLCTVARLLP EKLTIYTTLV GLLNARNYNF GGEFVEAMIR QLKESLKANN 

       130        140        150        160        170        180 
YNEAVYLVRF LSDLVNCHVI AAPSMVAMFE NFVSVTQEED VPQVRRDWYV YAFLSSLPWV 

       190        200        210        220        230        240 
GKELYEKKDA EMDRIFSTTE SYLKRRQKTH VPMLQVWTAD KPHPQEEYLD CLWAQIQKLK 

       250        260        270        280        290        300 
KDRWQERHIL RPYLAFDSIL CEALQHNLPP FTPPPHTEDS VYPMPRVIFR MFDYTDDPEG 

       310        320        330        340        350        360 
PVMPGSHSVE RFVIEENLHC IIKSYWKERK TCAAQLVSYP GKNKIPLNYH IVEVIFAELF 

       370        380        390        400        410        420 
QLPAPPHIDV MYTTLLIELC KLQPGSLPQV LAQATEMLYM RLDTMSTTCV DRFINWFSHH 

       430        440        450        460        470        480 
LSNFQFRWSW EDWSDCLTQD LESPKPKFVR EVLEKCMRLS YHQHILDIVP PTFSALCPAN 

       490        500        510        520        530        540 
PTCIYKYGDE SSNSLPGHSV ALCLSVAFKS KATNDEIFSI LKDVPNPNQV DDDDEGFRFN 

       550        560        570        580        590        600 
PLKIEVFVQT LLHLAAKSFS HSFSALAKFH EVFKTLAESD KGKLHVLRVM FEVWRNHPQM 

       610        620        630        640        650        660 
IAVLVDKMIR TQIVDCAAVA NWIFSSELSR DFTRLFVWEI LHSTIRKMNK HVLKIQKELE 

       670        680        690        700        710        720 
EAKEKLARQH KRRSDDDDRS SDRKDGALEE QIERLQEKVE AAQSEQKNLF LVIFQRFIMI 

       730        740        750        760        770        780 
LTEHLVRCET DGTSILTPWY KNCIERLQQI FLQHHQTIQQ YMVTLENLLF TAELDPHILA 

       790 
VFQQFCALQA 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001028373.2. NM_001033201.3.
UniGeneMm.389536.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3UKZX-ray2.30C1-23[»]
3UL0X-ray2.00C1-23[»]
ProteinModelPortalQ3UYV9.
SMRQ3UYV9. Positions 2-790.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ3UYV9.

Proteomic databases

PaxDbQ3UYV9.
PRIDEQ3UYV9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030014; ENSMUSP00000030014; ENSMUSG00000028330.
GeneID433702.
KEGGmmu:433702.
UCSCuc008stk.1. mouse.

Organism-specific databases

CTD4686.
MGIMGI:1891840. Ncbp1.

Phylogenomic databases

eggNOGNOG303489.
GeneTreeENSGT00390000001733.
HOGENOMHOG000007990.
HOVERGENHBG080328.
InParanoidB1AWH4.
KOK12882.
OMALICRVGE.
OrthoDBEOG7K9K28.
PhylomeDBQ3UYV9.
TreeFamTF313400.

Gene expression databases

BgeeQ3UYV9.
GenevestigatorQ3UYV9.

Family and domain databases

Gene3D1.25.40.180. 4 hits.
InterProIPR016024. 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]
PANTHERPTHR12412. PTHR12412. 1 hit.
PfamPF02854. MIF4G. 1 hit.
PF09088. MIF4G_like. 1 hit.
PF09090. MIF4G_like_2. 1 hit.
[Graphical view]
SMARTSM00543. MIF4G. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 3 hits.
ProtoNetSearch...

Other

ChiTaRSNCBP1. mouse.
NextBio408905.
PROQ3UYV9.
SOURCESearch...

Entry information

Entry nameNCBP1_MOUSE
AccessionPrimary (citable) accession number: Q3UYV9
Secondary accession number(s): B1AWH4, Q3TEM1, Q7TNE8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: June 13, 2006
Last modified: April 16, 2014
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot