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Protein

Eukaryotic translation initiation factor 6

Gene

TIF6

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

Binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit to form the 80S initiation complex in the cytoplasm. Is also involved in ribosome biogenesis. Associates with pre-60S subunits in the nucleus and is involved in its nuclear export. Cytoplasmic release of TIF6 from 60S subunits and nuclear relocalization is promoted by the GTPase RIA1/EFL1 and by SDO1. Also required for pre-rRNA processing.UniRule annotation6 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • ribosomal large subunit binding Source: SGD
  • ribosome binding Source: InterPro
  • translation initiation factor activity Source: UniProtKB-HAMAP

GO - Biological processi

  • assembly of large subunit precursor of preribosome Source: SGD
  • maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
  • maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
  • mature ribosome assembly Source: UniProtKB-HAMAP
  • ribosomal large subunit biogenesis Source: SGD
  • ribosomal subunit export from nucleus Source: SGD
  • rRNA processing Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis, Ribosome biogenesis

Enzyme and pathway databases

BioCyciYEAST:G3O-34176-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 6UniRule annotation
Short name:
eIF-6UniRule annotation
Gene namesi
Name:TIF6UniRule annotation
Synonyms:CDC95
Ordered Locus Names:YPR016C
ORF Names:LPZ15C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPR016C.
SGDiS000006220. TIF6.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • cytosol Source: GO_Central
  • nucleolus Source: SGD
  • nucleus Source: SGD
  • preribosome, large subunit precursor Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 245245Eukaryotic translation initiation factor 6PRO_0000153742Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei174 – 1741Phosphoserine; by CK1UniRule annotation
Modified residuei175 – 1751Phosphoserine; by CK1UniRule annotation
Modified residuei231 – 2311PhosphoserineCombined sources

Post-translational modificationi

Phosphorylation at Ser-174 and Ser-175 promotes nuclear export.UniRule annotation2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12522.

PTM databases

iPTMnetiQ12522.

Interactioni

Subunit structurei

Monomer. Associates with the 60S ribosomal subunit.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-9046,EBI-9046
LSG1P531455EBI-9046,EBI-23885
NOG2P537424EBI-9046,EBI-28532

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi36193. 132 interactions.
DIPiDIP-5395N.
IntActiQ12522. 77 interactions.
MINTiMINT-527536.

Structurei

Secondary structure

1
245
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54Combined sources
Helixi13 – 164Combined sources
Beta strandi17 – 193Combined sources
Beta strandi24 – 274Combined sources
Helixi32 – 4211Combined sources
Turni43 – 453Combined sources
Beta strandi48 – 514Combined sources
Helixi59 – 624Combined sources
Beta strandi67 – 737Combined sources
Helixi78 – 8710Combined sources
Beta strandi92 – 976Combined sources
Helixi104 – 1074Combined sources
Beta strandi108 – 1103Combined sources
Beta strandi112 – 1176Combined sources
Helixi123 – 13311Combined sources
Beta strandi135 – 1395Combined sources
Helixi148 – 1503Combined sources
Beta strandi151 – 1544Combined sources
Beta strandi159 – 1613Combined sources
Helixi167 – 17711Combined sources
Beta strandi181 – 1833Combined sources
Turni187 – 1893Combined sources
Helixi193 – 1964Combined sources
Beta strandi197 – 1993Combined sources
Beta strandi204 – 2074Combined sources
Helixi212 – 22110Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G62X-ray2.50A1-224[»]
2X7Nelectron microscopy11.80B1-224[»]
3J2Ielectron microscopy11.90B1-245[»]
4V7Felectron microscopy8.70m1-245[»]
5FL8electron microscopy9.50m1-245[»]
ProteinModelPortaliQ12522.
SMRiQ12522. Positions 1-224.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12522.

Family & Domainsi

Sequence similaritiesi

Belongs to the eIF-6 family.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000015972.
HOGENOMiHOG000230605.
InParanoidiQ12522.
KOiK03264.
OMAiNDWCAFT.
OrthoDBiEOG7TTQKB.

Family and domain databases

HAMAPiMF_00032. eIF_6.
InterProiIPR002769. eIF6.
[Graphical view]
PANTHERiPTHR10784. PTHR10784. 1 hit.
PfamiPF01912. eIF-6. 1 hit.
[Graphical view]
PIRSFiPIRSF006413. IF-6. 1 hit.
SMARTiSM00654. eIF6. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00323. eIF-6. 1 hit.

Sequencei

Sequence statusi: Complete.

Q12522-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATRTQFENS NEIGVFSKLT NTYCLVAVGG SENFYSAFEA ELGDAIPIVH
60 70 80 90 100
TTIAGTRIIG RMTAGNRRGL LVPTQTTDQE LQHLRNSLPD SVKIQRVEER
110 120 130 140 150
LSALGNVICC NDYVALVHPD IDRETEELIS DVLGVEVFRQ TISGNILVGS
160 170 180 190 200
YCSLSNQGGL VHPQTSVQDQ EELSSLLQVP LVAGTVNRGS SVVGAGMVVN
210 220 230 240
DYLAVTGLDT TAPELSVIES IFRLQDAQPE SISGNLRDTL IETYS
Length:245
Mass (Da):26,458
Last modified:November 1, 1996 - v1
Checksum:i1BCE041C61DFD2A8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71255 Genomic DNA. Translation: CAA95012.1.
Z49919 Genomic DNA. Translation: CAA90161.1.
U31900 Genomic DNA. Translation: AAA97594.1.
AY692916 Genomic DNA. Translation: AAT92935.1.
BK006949 Genomic DNA. Translation: DAA11442.1.
PIRiS57550.
RefSeqiNP_015341.1. NM_001184113.1.

Genome annotation databases

EnsemblFungiiYPR016C; YPR016C; YPR016C.
GeneIDi856126.
KEGGisce:YPR016C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71255 Genomic DNA. Translation: CAA95012.1.
Z49919 Genomic DNA. Translation: CAA90161.1.
U31900 Genomic DNA. Translation: AAA97594.1.
AY692916 Genomic DNA. Translation: AAT92935.1.
BK006949 Genomic DNA. Translation: DAA11442.1.
PIRiS57550.
RefSeqiNP_015341.1. NM_001184113.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G62X-ray2.50A1-224[»]
2X7Nelectron microscopy11.80B1-224[»]
3J2Ielectron microscopy11.90B1-245[»]
4V7Felectron microscopy8.70m1-245[»]
5FL8electron microscopy9.50m1-245[»]
ProteinModelPortaliQ12522.
SMRiQ12522. Positions 1-224.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36193. 132 interactions.
DIPiDIP-5395N.
IntActiQ12522. 77 interactions.
MINTiMINT-527536.

PTM databases

iPTMnetiQ12522.

Proteomic databases

MaxQBiQ12522.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPR016C; YPR016C; YPR016C.
GeneIDi856126.
KEGGisce:YPR016C.

Organism-specific databases

EuPathDBiFungiDB:YPR016C.
SGDiS000006220. TIF6.

Phylogenomic databases

GeneTreeiENSGT00390000015972.
HOGENOMiHOG000230605.
InParanoidiQ12522.
KOiK03264.
OMAiNDWCAFT.
OrthoDBiEOG7TTQKB.

Enzyme and pathway databases

BioCyciYEAST:G3O-34176-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ12522.
PROiQ12522.

Family and domain databases

HAMAPiMF_00032. eIF_6.
InterProiIPR002769. eIF6.
[Graphical view]
PANTHERiPTHR10784. PTHR10784. 1 hit.
PfamiPF01912. eIF-6. 1 hit.
[Graphical view]
PIRSFiPIRSF006413. IF-6. 1 hit.
SMARTiSM00654. eIF6. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00323. eIF-6. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Cloning of murine translation initiation factor 6 and functional analysis of the homologous sequence YPR016c in Saccharomyces cerevisiae."
    Wood L.C., Ashby M.N., Grunfeld C., Feingold K.R.
    J. Biol. Chem. 274:11653-11659(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, SUBCELLULAR LOCATION.
  5. "The beta4 integrin interactor p27(BBP/eIF6) is an essential nuclear matrix protein involved in 60S ribosomal subunit assembly."
    Sanvito F., Piatti S., Villa A., Bossi M., Lucchini G., Marchisio P.C., Biffo S.
    J. Cell Biol. 144:823-837(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "The Saccharomyces cerevisiae homologue of mammalian translation initiation factor 6 does not function as a translation initiation factor."
    Si K., Maitra U.
    Mol. Cell. Biol. 19:1416-1426(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. "The nucle(ol)ar Tif6p and Efl1p are required for a late cytoplasmic step of ribosome synthesis."
    Senger B., Lafontaine D.L.J., Graindorge J.-S., Gadal O., Camasses A., Sanni A., Garnier J.-M., Breitenbach M., Hurt E., Fasiolo F.
    Mol. Cell 8:1363-1373(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "The Saccharomyces cerevisiae TIF6 gene encoding translation initiation factor 6 is required for 60S ribosomal subunit biogenesis."
    Basu U., Si K., Warner J.R., Maitra U.
    Mol. Cell. Biol. 21:1453-1462(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. "Phosphorylation of mammalian eukaryotic translation initiation factor 6 and its Saccharomyces cerevisiae homologue Tif6p: evidence that phosphorylation of Tif6p regulates its nucleocytoplasmic distribution and is required for yeast cell growth."
    Basu U., Si K., Deng H., Maitra U.
    Mol. Cell. Biol. 23:6187-6199(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, NUCLEOCYTOPLASMIC SHUTTLING.
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  11. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  12. "The Shwachman-Bodian-Diamond syndrome protein mediates translational activation of ribosomes in yeast."
    Menne T.F., Goyenechea B., Sanchez-Puig N., Wong C.C., Tonkin L.M., Ancliff P.J., Brost R.L., Costanzo M., Boone C., Warren A.J.
    Nat. Genet. 39:486-495(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  13. "The Saccharomyces cerevisiae 60 S ribosome biogenesis factor Tif6p is regulated by Hrr25p-mediated phosphorylation."
    Ray P., Basu U., Ray A., Majumdar R., Deng H., Maitra U.
    J. Biol. Chem. 283:9681-9691(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-174.
  14. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Crystal structures of ribosome anti-association factor IF6."
    Groft C.M., Beckmann R., Sali A., Burley S.K.
    Nat. Struct. Biol. 7:1156-1164(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS), FUNCTION.
  17. "Mechanism of eIF6-mediated inhibition of ribosomal subunit joining."
    Gartmann M., Blau M., Armache J.P., Mielke T., Topf M., Beckmann R.
    J. Biol. Chem. 285:14848-14851(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.8 ANGSTROMS) OF 1-224.

Entry informationi

Entry nameiIF6_YEAST
AccessioniPrimary (citable) accession number: Q12522
Secondary accession number(s): D6W426
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 18600 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Translation initiation factors
    List of translation initiation factor entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: 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.