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Q13347 (EIF3I_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. 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:
Eukaryotic translation initiation factor 3 subunit I

Short name=eIF3i
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 2
TGF-beta receptor-interacting protein 1
Short name=TRIP-1
eIF-3-beta
eIF3 p36
Gene names
Name:EIF3I
Synonyms:EIF3S2, TRIP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length325 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. HAMAP-Rule MF_03008

Subunit structure

Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation leads to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. Ref.5 Ref.6 Ref.9 Ref.11 Ref.12

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03008.

Post-translational modification

Phosphorylated by TGF-beta type II receptor. HAMAP-Rule MF_03008

Sequence similarities

Belongs to the eIF-3 subunit I family.

Contains 5 WD repeats.

Mass spectrometry

Molecular mass is 36501.9 Da from positions 1 - 325. Ref.11

Molecular mass is 36503.2±0.4 Da from positions 1 - 325. Determined by MALDI. Ref.12

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   DomainRepeat
WD repeat
   Molecular functionInitiation factor
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular protein metabolic process

Traceable author statement. Source: Reactome

formation of translation preinitiation complex

Inferred from electronic annotation. Source: UniProtKB-HAMAP

gene expression

Traceable author statement. Source: Reactome

regulation of translational initiation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

translation

Traceable author statement. Source: Reactome

translational initiation

Inferred from direct assay Ref.10. Source: UniProtKB

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

eukaryotic 43S preinitiation complex

Inferred from electronic annotation. Source: UniProtKB-HAMAP

eukaryotic 48S preinitiation complex

Inferred from electronic annotation. Source: UniProtKB-HAMAP

eukaryotic translation initiation factor 3 complex

Inferred from direct assay Ref.11Ref.10Ref.12. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

   Molecular_functionprotein binding

Inferred from physical interaction Ref.6PubMed 18624398PubMed 18628297. Source: IntAct

translation initiation factor activity

Inferred from direct assay Ref.10. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CLEC4GQ6UXB43EBI-354047,EBI-2114729
EIF3BP558844EBI-354047,EBI-366696

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 325325Eukaryotic translation initiation factor 3 subunit I HAMAP-Rule MF_03008
PRO_0000051036

Regions

Repeat8 – 4740WD 1 HAMAP-Rule MF_03008
Repeat50 – 9142WD 2 HAMAP-Rule MF_03008
Repeat144 – 18340WD 3 HAMAP-Rule MF_03008
Repeat186 – 22540WD 4 HAMAP-Rule MF_03008
Repeat283 – 32442WD 5 HAMAP-Rule MF_03008

Amino acid modifications

Modified residue2641N6-acetyllysine Ref.13
Modified residue3081Phosphotyrosine Ref.7
Cross-link282Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) HAMAP-Rule MF_03008

Sequences

Sequence LengthMass (Da)Tools
Q13347 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 02797BB72A752A96

FASTA32536,502
        10         20         30         40         50         60 
MKPILLQGHE RSITQIKYNR EGDLLFTVAK DPIVNVWYSV NGERLGTYMG HTGAVWCVDA 

        70         80         90        100        110        120 
DWDTKHVLTG SADNSCRLWD CETGKQLALL KTNSAVRTCG FDFGGNIIMF STDKQMGYQC 

       130        140        150        160        170        180 
FVSFFDLRDP SQIDNNEPYM KIPCNDSKIT SAVWGPLGEC IIAGHESGEL NQYSAKSGEV 

       190        200        210        220        230        240 
LVNVKEHSRQ INDIQLSRDM TMFVTASKDN TAKLFDSTTL EHQKTFRTER PVNSAALSPN 

       250        260        270        280        290        300 
YDHVVLGGGQ EAMDVTTTST RIGKFEARFF HLAFEEEFGR VKGHFGPINS VAFHPDGKSY 

       310        320 
SSGGEDGYVR IHYFDPQYFE FEFEA 

« Hide

References

« Hide 'large scale' references
[1]"Conservation and diversity of eukaryotic translation initiation factor eIF3."
Asano K., Kinzy T.G., Merrick W.C., Hershey J.W.B.
J. Biol. Chem. 272:1101-1109(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"A WD-domain protein that is associated with and phosphorylated by the type II TGF-beta receptor."
Chen R.H., Miettinen P.J., Maruka E.M., Choy L., Derynck R.
Nature 377:548-552(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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: Lung and Muscle.
[4]Lubec G., Afjehi-Sadat L.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 269-280 AND 283-298, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[5]"Characterization of eIF3k: a newly discovered subunit of mammalian translation initiation factor eIF3."
Mayeur G.L., Fraser C.S., Peiretti F., Block K.L., Hershey J.W.B.
Eur. J. Biochem. 270:4133-4139(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EIF3B.
[6]"The j-subunit of human translation initiation factor eIF3 is required for the stable binding of eIF3 and its subcomplexes to 40 S ribosomal subunits in vitro."
Fraser C.S., Lee J.Y., Mayeur G.L., Bushell M., Doudna J.A., Hershey J.W.B.
J. Biol. Chem. 279:8946-8956(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EIF3B.
[7]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-308, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and its role in ribosomal dissociation and anti-association."
Kolupaeva V.G., Unbehaun A., Lomakin I.B., Hellen C.U.T., Pestova T.V.
RNA 11:470-486(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX.
[9]"Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e subunit."
LeFebvre A.K., Korneeva N.L., Trutschl M., Cvek U., Duzan R.D., Bradley C.A., Hershey J.W.B., Rhoads R.E.
J. Biol. Chem. 281:22917-22932(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"Reconstitution reveals the functional core of mammalian eIF3."
Masutani M., Sonenberg N., Yokoyama S., Imataka H.
EMBO J. 26:3373-3383(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX.
[11]"Structural characterization of the human eukaryotic initiation factor 3 protein complex by mass spectrometry."
Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L., Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A.
Mol. Cell. Proteomics 6:1135-1146(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX, MASS SPECTROMETRY.
[12]"Mass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3."
Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E., Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B., Doudna J.A., Robinson C.V.
Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX, MASS SPECTROMETRY.
[13]"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-264, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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].
[15]"Structural roles for human translation factor eIF3 in initiation of protein synthesis."
Siridechadilok B., Fraser C.S., Hall R.J., Doudna J.A., Nogales E.
Science 310:1513-1515(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING, ELECTRON MICROSCOPY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U39067 mRNA. Translation: AAC97144.1.
U36764 mRNA. Translation: AAC50224.1.
BC000413 mRNA. Translation: AAH00413.1.
BC003140 mRNA. Translation: AAH03140.1.
CCDSCCDS357.1.
PIRS60335.
RefSeqNP_003748.1. NM_003757.2.
UniGeneHs.530096.

3D structure databases

ProteinModelPortalQ13347.
SMRQ13347. Positions 1-324.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114217. 78 interactions.
DIPDIP-31116N.
IntActQ13347. 22 interactions.
MINTMINT-5004513.
STRING9606.ENSP00000362688.

PTM databases

PhosphoSiteQ13347.

Polymorphism databases

DMDM2494895.

2D gel databases

DOSAC-COBS-2DPAGEQ13347.
OGPQ13347.

Proteomic databases

MaxQBQ13347.
PaxDbQ13347.
PeptideAtlasQ13347.
PRIDEQ13347.

Protocols and materials databases

DNASU8668.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373586; ENSP00000362688; ENSG00000084623.
GeneID8668.
KEGGhsa:8668.
UCSCuc001bur.4. human.

Organism-specific databases

CTD8668.
GeneCardsGC01P032687.
HGNCHGNC:3272. EIF3I.
HPAHPA029939.
HPA029940.
MIM603911. gene.
neXtProtNX_Q13347.
PharmGKBPA162384875.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOGENOMHOG000231322.
HOVERGENHBG000900.
InParanoidQ13347.
KOK03246.
OMAKATVCAF.
PhylomeDBQ13347.
TreeFamTF101515.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_71. Gene Expression.
SignaLinkQ13347.

Gene expression databases

ArrayExpressQ13347.
BgeeQ13347.
CleanExHS_EIF3I.
GenevestigatorQ13347.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
HAMAPMF_03008. eIF3i.
InterProIPR027525. eIF3i.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF00400. WD40. 4 hits.
[Graphical view]
SMARTSM00320. WD40. 5 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEIF3I. human.
GeneWikiEIF3I.
GenomeRNAi8668.
NextBio32515.
PROQ13347.
SOURCESearch...

Entry information

Entry nameEIF3I_HUMAN
AccessionPrimary (citable) accession number: Q13347
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 144 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

MIM cross-references

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

Translation initiation factors

List of translation initiation factor entries

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM