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Q09161 (NCBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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, NCBP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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.1 Ref.7 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.20 Ref.22 Ref.25 Ref.26

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 since it is reported by Ref.11, Ref.13 and Ref.14, but is not observed by Ref.26. The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A. Ref.8 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.21 Ref.26

Subcellular location

Nucleus. Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.19 Ref.26

Sequence similarities

Belongs to the NCBP1 family.

Contains 1 MIF4G domain.

Sequence caution

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.

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
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process7-methylguanosine mRNA capping

Inferred from direct assay Ref.34. Source: UniProtKB

RNA metabolic process

Traceable author statement. Source: Reactome

RNA splicing

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

gene silencing by RNA

Inferred from electronic annotation. Source: UniProtKB-KW

histone mRNA metabolic process

Traceable author statement. Source: Reactome

mRNA 3'-end processing

Traceable author statement. Source: Reactome

mRNA cis splicing, via spliceosome

Inferred from electronic annotation. Source: InterPro

mRNA cleavage

Inferred from direct assay PubMed 9342333. Source: UniProtKB

mRNA export from nucleus

Inferred from mutant phenotype Ref.16. Source: UniProtKB

mRNA metabolic process

Traceable author statement. Source: Reactome

mRNA splicing, via spliceosome

Traceable author statement. Source: Reactome

ncRNA metabolic process

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Inferred from direct assay Ref.10Ref.20. Source: UniProtKB

positive regulation of mRNA 3'-end processing

Inferred from direct assay PubMed 9342333. Source: UniProtKB

positive regulation of viral transcription

Traceable author statement. Source: Reactome

regulation of translational initiation

Inferred from direct assay Ref.10. Source: UniProtKB

spliceosomal snRNP assembly

Traceable author statement. Source: Reactome

termination of RNA polymerase II transcription

Traceable author statement. Source: Reactome

transcription elongation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

mRNA cap binding complex

Inferred from direct assay Ref.34Ref.7PubMed 9342333. Source: UniProtKB

mitochondrion

Inferred from direct assay. Source: HPA

nuclear cap binding complex

Inferred from electronic annotation. Source: InterPro

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.26PubMed 9342333. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: HPA

ribonucleoprotein complex

Inferred from direct assay Ref.19. Source: UniProtKB

   Molecular_functionRNA binding

Traceable author statement Ref.1. Source: ProtInc

RNA cap binding

Traceable author statement Ref.1. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.16Ref.19PubMed 17468741Ref.26PubMed 7478990Ref.8. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 790790Nuclear cap-binding protein subunit 1
PRO_0000089364

Regions

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

Amino acid modifications

Modified residue71Phosphoserine; by RPS6KB1 Ref.9
Modified residue211Phosphothreonine; by RPS6KB1 Ref.9 Ref.24
Modified residue221Phosphoserine; by RPS6KB1 Ref.9 Ref.24 Ref.27
Modified residue2041N6-acetyllysine Ref.28
Modified residue6981N6-acetyllysine Ref.28

Experimental info

Mutagenesis71S → A: Reduced phosphorylation by RPS6KB1. Abolishes phosphorylation by RPS6KB1; when associated with 21-A-A-22. Ref.9
Mutagenesis17 – 182KR → AA: Abolishes nuclear localization and phosphorylation by RPS6KB1.
Mutagenesis21 – 222TS → A: Reduced phosphorylation by RPS6KB1. Abolishes phosphorylation by RPS6KB1; when associated with A-7.
Sequence conflict801P → S in BAG35665. Ref.3
Sequence conflict1591E → D in BAD92470. Ref.4
Sequence conflict6741S → G in BAG35665. Ref.3

Secondary structure

......................................................................................................... 790
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q09161 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: F10DE7B9D16FDA0B

FASTA79091,839
        10         20         30         40         50         60 
MSRRRHSDEN 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 EMDRIFANTE SYLKRRQKTH VPMLQVWTAD KPHPQEEYLD CLWAQIQKLK 

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

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

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

       430        440        450        460        470        480 
LSNFQFRWSW EDWSDCLSQD PESPKPKFVR EVLEKCMRLS YHQRILDIVP PTFSALCPAN 

       490        500        510        520        530        540 
PTCIYKYGDE SSNSLPGHSV ALCLAVAFKS KATNDEIFSI LKDVPNPNQD DDDDEGFSFN 

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

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

       670        680        690        700        710        720 
EAKEKLARQH KRRSDDDDRS SDRKDGVLEE QIERLQEKVE SAQSEQKNLF LVIFQRFIMI 

       730        740        750        760        770        780 
LTEHLVRCET DGTSVLTPWY KNCIERLQQI FLQHHQIIQQ YMVTLENLLF TAELDPHILA 

       790 
VFQQFCALQA 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"A cap-binding protein complex mediating U snRNA export."
Izaurralde E., Lewis J., Gamberi C., Jarmolowski A., McGuigan C., Mattaj A.W.
Nature 376:709-712(1995) [PubMed] [Europe PMC] [Abstract]
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]"Molecular composition of IMP1 ribonucleoprotein granules."
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C.
Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS6728.1.
PIRS50082.
RefSeqNP_002477.1. NM_002486.4.
UniGeneHs.595669.
Hs.686479.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
DisProtDP00392.
ProteinModelPortalQ09161.
SMRQ09161. Positions 2-790.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110766. 53 interactions.
DIPDIP-33244N.
IntActQ09161. 29 interactions.
MINTMINT-248693.
STRING9606.ENSP00000364289.

Protein family/group databases

TCDB9.A.60.1.1. the small nuclear rna exporter (snrna-e).

PTM databases

PhosphoSiteQ09161.

Polymorphism databases

DMDM1705654.

Proteomic databases

MaxQBQ09161.
PaxDbQ09161.
PeptideAtlasQ09161.
PRIDEQ09161.

Protocols and materials databases

DNASU4686.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375147; ENSP00000364289; ENSG00000136937.
GeneID4686.
KEGGhsa:4686.
UCSCuc004axq.3. human.

Organism-specific databases

CTD4686.
GeneCardsGC09P100395.
HGNCHGNC:7658. NCBP1.
HPAHPA042411.
HPA049031.
MIM600469. gene.
neXtProtNX_Q09161.
PharmGKBPA31461.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG303489.
HOGENOMHOG000007990.
HOVERGENHBG080328.
InParanoidQ09161.
KOK12882.
OMALICRVGE.
OrthoDBEOG7K9K28.
PhylomeDBQ09161.
TreeFamTF313400.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_1788. Transcription.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

ArrayExpressQ09161.
BgeeQ09161.
CleanExHS_NCBP1.
GenevestigatorQ09161.

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. human.
EvolutionaryTraceQ09161.
GenomeRNAi4686.
NextBio18072.
PROQ09161.
SOURCESearch...

Entry information

Entry nameNCBP1_HUMAN
AccessionPrimary (citable) accession number: Q09161
Secondary accession number(s): B2R718 expand/collapse secondary AC list , Q59G76, Q5T1V0, Q5T7X2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM