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Protein

Nuclear cap-binding protein complex subunit 1

Gene

STO1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.13 Publications

GO - Molecular functioni

  • mRNA binding Source: SGD
  • RNA cap binding Source: InterPro

GO - Biological processi

  • 7-methylguanosine mRNA capping Source: UniProtKB-KW
  • mRNA cis splicing, via spliceosome Source: InterPro
  • mRNA splicing, via spliceosome Source: SGD
  • mRNA transport Source: UniProtKB-KW
  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: SGD
  • response to osmotic stress Source: SGD
Complete GO annotation...

Keywords - Biological processi

mRNA capping, mRNA processing, mRNA splicing, mRNA transport, Nonsense-mediated mRNA decay, Transport

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32818-MONOMER.
ReactomeiR-SCE-113418. Formation of the Early Elongation Complex.
R-SCE-72086. mRNA Capping.
R-SCE-72165. mRNA Splicing - Minor Pathway.
R-SCE-77595. Processing of Intronless Pre-mRNAs.
R-SCE-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-SCE-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:STO1
Synonyms:CBC1, CBP80, GCR3, SUT1
Ordered Locus Names:YMR125W
ORF Names:YM8564.07, YM9553.01
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR125W.
SGDiS000004732. STO1.

Subcellular locationi

GO - Cellular componenti

  • commitment complex Source: SGD
  • nuclear cap binding complex Source: SGD
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • polysome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000874471 – 861Nuclear cap-binding protein complex subunit 1Add BLAST861

Proteomic databases

MaxQBiP34160.
PRIDEiP34160.

Interactioni

Subunit structurei

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).8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CBC2Q089207EBI-745,EBI-33556

Protein-protein interaction databases

BioGridi35302. 176 interactors.
DIPiDIP-4434N.
IntActiP34160. 53 interactors.
MINTiMINT-552943.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UKYX-ray2.35C1-30[»]
ProteinModelPortaliP34160.
SMRiP34160.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini36 – 264MIF4GAdd BLAST229

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi22 – 30Nuclear localization signalSequence analysis9

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi774 – 801Asp/Glu-rich (acidic)Add BLAST28
Compositional biasi802 – 825Arg/Lys-rich (basic)Add BLAST24

Sequence similaritiesi

Belongs to the NCBP1 family.Curated
Contains 1 MIF4G domain.Curated

Phylogenomic databases

GeneTreeiENSGT00390000001733.
HOGENOMiHOG000066047.
InParanoidiP34160.
KOiK12882.
OMAiGRSTWKP.
OrthoDBiEOG092C0PVP.

Family and domain databases

Gene3Di1.25.40.180. 3 hits.
InterProiIPR016024. ARM-type_fold.
IPR027159. CBP80.
IPR016021. MIF4-like.
IPR015172. MIF4G-like_typ-1.
IPR015174. MIF4G-like_typ-2.
IPR003890. MIF4G-like_typ-3.
[Graphical view]
PANTHERiPTHR12412. PTHR12412. 2 hits.
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.

P34160-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFNRKRRGDF DEDENYRDFR PRMPKRQRIP PVVQLCKEMM PDIRTIGESV
60 70 80 90 100
KAFEDDIKFL SEAIMNEYGH EDYFNNALLS TLNAVVVEQP QKQAAIALLT
110 120 130 140 150
MVVNSKNNVA GKSIINYFFE ELQKWCKQTY NDEFKSTSNE TGPWNKIKLI
160 170 180 190 200
LRFLSILSPM FLVDELINIY KSLFELSIEL NNLDPGNRVP LSEAIYTNTL
210 220 230 240 250
LNIPYLFFFN RNNDGLRTKV EELLAYVEQN YLVKTTDINL LREYNGEPPY
260 270 280 290 300
EMVELVRVVL PNVKKALINN LEQLNELFPD WNHLLTPQTG DEGFNDALTL
310 320 330 340 350
PSVDDLKSFV RLNKNFGSVD SMWKTPRYAF HVYLPNSAGN FETVVPISTY
360 370 380 390 400
AGQLFNDIII DLVESLEFNR KEVARQVITL DLFFKAGIFT EPGESIAQLI
410 420 430 440 450
ATYEENPLAP TFKIEDLAIE TILGLIFKLP SVSQPFAYFY TLLVDICQNS
460 470 480 490 500
PKAIAPVFGR AFRFFYSHLD SLDFELKLRY LDWFSIQMSN FNFSWKWNEW
510 520 530 540 550
EDDSIKFGKY FYNPKVNFAK NLIQKELRLT SNFSEVEDSL PQEFTKYLDT
560 570 580 590 600
SYIPRDQLIN YYQSLFTGYT VEEDSVRKND LYFRQEGVPM ENTVRKILDY
610 620 630 640 650
THKANNSREV TELESILGEL KNEYGSIISD FNRFVIILLV QAVTDSGSRS
660 670 680 690 700
LSHANKYIND LKEDLKTIFA KIELDIETKE YIIIEAVLTF WNANPQTGFL
710 720 730 740 750
VADAFKYAGL LTSRTIFTFI FNETGLKNNG LIEATAIEAV FRNLSQQISE
760 770 780 790 800
ENESGNNFEF VFERLCTIAN STIDLLDVNA DEDIEIPKVN GEMDIDDIED
810 820 830 840 850
DKLDLKWKYF TVIGFIKSIL RRYSHEYREL ADKFIANIDN AIPHESTRRT
860
ISNWIQETKE V
Length:861
Mass (Da):100,018
Last modified:October 1, 1996 - v2
Checksum:iEDD04907BDC9207D
GO

Sequence cautioni

The sequence BAA01076 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence L27744 differs from that shown. Reason: Frameshift at position 708.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti164D → V in L27744 (PubMed:10733586).Curated1
Sequence conflicti633R → I in L27744 (PubMed:10733586).Curated1
Sequence conflicti704A → R in L27744 (PubMed:10733586).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA44919.
RefSeqiNP_013844.2. NM_001182626.1.

Genome annotation databases

EnsemblFungiiYMR125W; YMR125W; YMR125W.
GeneIDi855155.
KEGGisce:YMR125W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA44919.
RefSeqiNP_013844.2. NM_001182626.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UKYX-ray2.35C1-30[»]
ProteinModelPortaliP34160.
SMRiP34160.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35302. 176 interactors.
DIPiDIP-4434N.
IntActiP34160. 53 interactors.
MINTiMINT-552943.

Proteomic databases

MaxQBiP34160.
PRIDEiP34160.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR125W; YMR125W; YMR125W.
GeneIDi855155.
KEGGisce:YMR125W.

Organism-specific databases

EuPathDBiFungiDB:YMR125W.
SGDiS000004732. STO1.

Phylogenomic databases

GeneTreeiENSGT00390000001733.
HOGENOMiHOG000066047.
InParanoidiP34160.
KOiK12882.
OMAiGRSTWKP.
OrthoDBiEOG092C0PVP.

Enzyme and pathway databases

BioCyciYEAST:G3O-32818-MONOMER.
ReactomeiR-SCE-113418. Formation of the Early Elongation Complex.
R-SCE-72086. mRNA Capping.
R-SCE-72165. mRNA Splicing - Minor Pathway.
R-SCE-77595. Processing of Intronless Pre-mRNAs.
R-SCE-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-SCE-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

PROiP34160.

Family and domain databases

Gene3Di1.25.40.180. 3 hits.
InterProiIPR016024. ARM-type_fold.
IPR027159. CBP80.
IPR016021. MIF4-like.
IPR015172. MIF4G-like_typ-1.
IPR015174. MIF4G-like_typ-2.
IPR003890. MIF4G-like_typ-3.
[Graphical view]
PANTHERiPTHR12412. PTHR12412. 2 hits.
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.
ProtoNetiSearch...

Entry informationi

Entry nameiNCBP1_YEAST
AccessioniPrimary (citable) accession number: P34160
Secondary accession number(s): D6VZU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 11300 molecules/cell in log phase SD medium.1 Publication
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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.