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

P34160 (NCBP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. 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 complex subunit 1
Alternative name(s):
80 kDa nuclear cap-binding protein
Short name=CBP80
Short name=NCBP 80 kDa subunit
Glycolysis regulation protein 3
Protein SUT1
Suppressor of TOP1 protein
Gene names
Name:STO1
Synonyms:CBC1, CBP80, GCR3, SUT1
Ordered Locus Names:YMR125W
ORF Names:YM8564.07, YM9553.01
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length861 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the CBC complex, which binds co-transcriptionally to the 5'-cap of pre-mRNAs and is involved in maturation, export and degradation of nuclear mRNAs. The CBC complex is required for efficient pre-mRNA splicing through efficient commitment complex and spliceosome formation. Together with NPL3, the CBC complex is required for export of mRNAs out of the nucleus. The CBC complex is also involved in nuclear mRNA degradation, probably by directing the mRNAs to the sites of degradation. Affects replication of the positive-strand RNA virus BMV. Ref.1 Ref.2 Ref.3 Ref.6 Ref.7 Ref.8 Ref.10 Ref.13 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20

Subunit structure

Component of the nuclear cap-binding complex (CBC), a heterodimer composed of STO1/CBC1 and CBC2 that interacts with capped RNAs. The complex interacts strongly with the importin subunit alpha SRP1. The SRP1-CBC trimer also binds to capped RNAs, but formation of the importin alpha/beta heterodimer upon binding of KAP95 to SRP1 in the cytoplasm causes dissociation of CBC from the RNA. The CBC complex is part of the commitment complex 1 (CC1), binding to the cap of pre-mRNA and interacting with U1 snRNP subunits MUD2 and SNU56. The CBC complex is part of the NRD1 complex, composed of CBC2, NAB1, NRD1, SEN1 and STO1/CBC2. The CBC complex also interacts with NPL3 and eIF4G (TIF4631 and TIF4632). Ref.6 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.21 Ref.22

Subcellular location

Nucleus. Cytoplasmperinuclear region. Note: Predominantly nuclear, is able to exit the nucleus in an RNA-dependent manner. Ref.3 Ref.6 Ref.13

Miscellaneous

Present with 11300 molecules/cell in log phase SD medium.

In contrast to metazoans, where the CBC complex is involved in the nuclear export of capped U snRNAs, it is believed that in yeast, U snRNAs are not exported from the nucleus and U snRNPs are assembled in the nucleus from RNAs and imported proteins.

Sequence similarities

Belongs to the NCBP1 family.

Contains 1 MIF4G domain.

Sequence caution

The sequence BAA01076.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence L27744 differs from that shown. Reason: Frameshift at position 708.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CBC2Q089207EBI-745,EBI-33556

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 861861Nuclear cap-binding protein complex subunit 1
PRO_0000087447

Regions

Domain36 – 264229MIF4G
Motif22 – 309Nuclear localization signal Potential
Compositional bias774 – 80128Asp/Glu-rich (acidic)
Compositional bias802 – 82524Arg/Lys-rich (basic)

Experimental info

Sequence conflict1641D → V in L27744. Ref.3
Sequence conflict6331R → I in L27744. Ref.3
Sequence conflict7041A → R in L27744. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P34160 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: EDD04907BDC9207D

FASTA861100,018
        10         20         30         40         50         60 
MFNRKRRGDF DEDENYRDFR PRMPKRQRIP PVVQLCKEMM PDIRTIGESV KAFEDDIKFL 

        70         80         90        100        110        120 
SEAIMNEYGH EDYFNNALLS TLNAVVVEQP QKQAAIALLT MVVNSKNNVA GKSIINYFFE 

       130        140        150        160        170        180 
ELQKWCKQTY NDEFKSTSNE TGPWNKIKLI LRFLSILSPM FLVDELINIY KSLFELSIEL 

       190        200        210        220        230        240 
NNLDPGNRVP LSEAIYTNTL LNIPYLFFFN RNNDGLRTKV EELLAYVEQN YLVKTTDINL 

       250        260        270        280        290        300 
LREYNGEPPY EMVELVRVVL PNVKKALINN LEQLNELFPD WNHLLTPQTG DEGFNDALTL 

       310        320        330        340        350        360 
PSVDDLKSFV RLNKNFGSVD SMWKTPRYAF HVYLPNSAGN FETVVPISTY AGQLFNDIII 

       370        380        390        400        410        420 
DLVESLEFNR KEVARQVITL DLFFKAGIFT EPGESIAQLI ATYEENPLAP TFKIEDLAIE 

       430        440        450        460        470        480 
TILGLIFKLP SVSQPFAYFY TLLVDICQNS PKAIAPVFGR AFRFFYSHLD SLDFELKLRY 

       490        500        510        520        530        540 
LDWFSIQMSN FNFSWKWNEW EDDSIKFGKY FYNPKVNFAK NLIQKELRLT SNFSEVEDSL 

       550        560        570        580        590        600 
PQEFTKYLDT SYIPRDQLIN YYQSLFTGYT VEEDSVRKND LYFRQEGVPM ENTVRKILDY 

       610        620        630        640        650        660 
THKANNSREV TELESILGEL KNEYGSIISD FNRFVIILLV QAVTDSGSRS LSHANKYIND 

       670        680        690        700        710        720 
LKEDLKTIFA KIELDIETKE YIIIEAVLTF WNANPQTGFL VADAFKYAGL LTSRTIFTFI 

       730        740        750        760        770        780 
FNETGLKNNG LIEATAIEAV FRNLSQQISE ENESGNNFEF VFERLCTIAN STIDLLDVNA 

       790        800        810        820        830        840 
DEDIEIPKVN GEMDIDDIED DKLDLKWKYF TVIGFIKSIL RRYSHEYREL ADKFIANIDN 

       850        860 
AIPHESTRRT ISNWIQETKE V 

« Hide

References

« Hide 'large scale' references
[1]"GCR3 encodes an acidic protein that is required for expression of glycolytic genes in Saccharomyces cerevisiae."
Uemura H., Jigami Y.
J. Bacteriol. 174:5526-5532(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]"Mutations in GCR3, a gene involved in the expression of glycolytic genes in Saccharomyces cerevisiae, suppress the temperature-sensitive growth of hpr1 mutants."
Uemura H., Pandit S., Jigami Y., Sternglanz R.
Genetics 142:1095-1103(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[3]"The role of nuclear cap binding protein Cbc1p of yeast in mRNA termination and degradation."
Das B., Guo Z., Russo P., Chartrand P., Sherman F.
Mol. Cell. Biol. 20:2827-2838(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION OF INTRON, FUNCTION, SUBCELLULAR LOCATION.
[4]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"Importin provides a link between nuclear protein import and U snRNA export."
Goerlich D., Kraft R., Kostka S., Vogel F., Hartmann E., Laskey R.A., Mattaj I.W., Izaurraide E.
Cell 87:21-32(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION IN THE CBC AND SRP1-CBC COMPLEXES, U SNRNA-BINDING, SUBCELLULAR LOCATION, FUNCTION OF THE CBC AND SRP1-CBC COMPLEXES.
[7]"A yeast cap binding protein complex (yCBC) acts at an early step in pre-mRNA splicing."
Lewis J.D., Goerlich D., Mattaj I.W.
Nucleic Acids Res. 24:3332-3336(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE CBC COMPLEX.
[8]"Arginine methylation facilitates the nuclear export of hnRNP proteins."
Shen E.C., Henry M.F., Weiss V.H., Valentini S.R., Silver P.A., Lee M.S.
Genes Dev. 12:679-691(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Identification of eight proteins that cross-link to pre-mRNA in the yeast commitment complex."
Zhang D., Rosbash M.
Genes Dev. 13:581-592(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRE-MRNA IN THE COMMITMENT COMPLEX.
[10]"Genetic and physical interactions involving the yeast nuclear cap-binding complex."
Fortes P., Kufel J., Fornerod M., Polycarpou-Schwarz M., Lafontaine D., Tollervey D., Mattaj I.W.
Mol. Cell. Biol. 19:6543-6553(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MUD2 AND SNU56, FUNCTION OF THE CBC COMPLEX.
[11]"A generic protein purification method for protein complex characterization and proteome exploration."
Rigaut G., Shevchenko A., Rutz B., Wilm M., Mann M., Seraphin B.
Nat. Biotechnol. 17:1030-1032(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE CBC COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION OF THE COMPLEX WITH CAPPED RNA.
[12]"Eukaryote-specific domains in translation initiation factors: implications for translation regulation and evolution of the translation system."
Aravind L., Koonin E.V.
Genome Res. 10:1172-1184(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN.
[13]"7The yeast mRNA-binding protein Npl3p interacts with the cap-binding complex."
Shen E.C., Stage-Zimmermann T., Chui P., Silver P.A.
J. Biol. Chem. 275:23718-23724(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NPL3, SUBCELLULAR LOCATION, FUNCTION.
[14]"The yeast nuclear cap binding complex can interact with translation factor eIF4G and mediate translation initiation."
Fortes P., Inada T., Preiss T., Hentze M.W., Mattaj I.W., Sachs A.B.
Mol. Cell 6:191-196(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EIF4G.
[15]"Degradation of normal mRNA in the nucleus of Saccharomyces cerevisiae."
Das B., Butler J.S., Sherman F.
Mol. Cell. Biol. 23:5502-5515(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[17]"Systematic, genome-wide identification of host genes affecting replication of a positive-strand RNA virus."
Kushner D.B., Lindenbach B.D., Grdzelishvili V.Z., Noueiry A.O., Paul S.M., Ahlquist P.
Proc. Natl. Acad. Sci. U.S.A. 100:15764-15769(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"The interaction of the cap-binding complex (CBC) with eIF4G is dispensable for translation in yeast."
Baron-Benhamou J., Fortes P., Inada T., Preiss T., Hentze M.W.
RNA 9:654-662(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE CBC COMPLEX.
[19]"Cap-binding protein 1-mediated and eukaryotic translation initiation factor 4E-mediated pioneer rounds of translation in yeast."
Gao Q., Das B., Sherman F., Maquat L.E.
Proc. Natl. Acad. Sci. U.S.A. 102:4258-4263(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[20]"A nuclear degradation pathway controls the abundance of normal mRNAs in Saccharomyces cerevisiae."
Kuai L., Das B., Sherman F.
Proc. Natl. Acad. Sci. U.S.A. 102:13962-13967(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[21]"Subunit architecture of multimeric complexes isolated directly from cells."
Hernandez H., Dziembowski A., Taverner T., Seraphin B., Robinson C.V.
EMBO Rep. 7:605-610(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE CBC COMPLEX, INTERACTION WITH SRP1, IDENTIFICATION BY MASS SPECTROMETRY.
[22]"Nrd1 interacts with the nuclear exosome for 3' processing of RNA polymerase II transcripts."
Vasiljeva L., Buratowski S.
Mol. Cell 21:239-248(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN NRD1 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D10224 Genomic DNA. Translation: BAA01076.1. Sequence problems.
L07650 Genomic DNA. No translation available.
L27744 Genomic DNA. No translation available.
Z49273 Genomic DNA. Translation: CAA89274.1.
Z48622 Genomic DNA. Translation: CAA88550.1.
BK006946 Genomic DNA. Translation: DAA10022.1.
PIRA44919.
RefSeqNP_013844.2. NM_001182626.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3UKYX-ray2.35C1-30[»]
ProteinModelPortalP34160.
SMRP34160. Positions 397-722.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35302. 177 interactions.
DIPDIP-4434N.
IntActP34160. 53 interactions.
MINTMINT-552943.
STRING4932.YMR125W.

Proteomic databases

MaxQBP34160.
PaxDbP34160.
PeptideAtlasP34160.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYMR125W; YMR125W; YMR125W.
GeneID855155.
KEGGsce:YMR125W.

Organism-specific databases

CYGDYMR125w2.
SGDS000004732. STO1.

Phylogenomic databases

eggNOGNOG303489.
GeneTreeENSGT00390000001733.
HOGENOMHOG000066047.
KOK12882.
OMATWKWAEW.
OrthoDBEOG7MKWFF.

Enzyme and pathway databases

BioCycYEAST:G3O-32818-MONOMER.

Gene expression databases

GenevestigatorP34160.

Family and domain databases

Gene3D1.25.40.180. 3 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

NextBio978566.

Entry information

Entry nameNCBP1_YEAST
AccessionPrimary (citable) accession number: P34160
Secondary accession number(s): D6VZU8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references