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Protein

Eukaryotic translation initiation factor 3 subunit I

Gene

EIF3I

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • translation initiation factor activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.
SignaLinkiQ13347.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 3 subunit IUniRule annotation
Short name:
eIF3iUniRule annotation
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 2UniRule annotation
TGF-beta receptor-interacting protein 1
Short name:
TRIP-1
eIF-3-betaUniRule annotation
eIF3 p36UniRule annotation
Gene namesi
Name:EIF3IUniRule annotation
Synonyms:EIF3S2UniRule annotation, TRIP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:3272. EIF3I.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162384875.

Polymorphism and mutation databases

BioMutaiEIF3I.
DMDMi2494895.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 325325Eukaryotic translation initiation factor 3 subunit IPRO_0000051036Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei264 – 2641N6-acetyllysine1 Publication
Cross-linki282 – 282Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei308 – 3081Phosphotyrosine1 Publication

Post-translational modificationi

Phosphorylated by TGF-beta type II receptor.UniRule annotation

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ13347.
PaxDbiQ13347.
PeptideAtlasiQ13347.
PRIDEiQ13347.

2D gel databases

DOSAC-COBS-2DPAGEQ13347.
OGPiQ13347.

PTM databases

PhosphoSiteiQ13347.

Expressioni

Gene expression databases

BgeeiQ13347.
CleanExiHS_EIF3I.
ExpressionAtlasiQ13347. baseline and differential.
GenevisibleiQ13347. HS.

Organism-specific databases

HPAiHPA029939.
HPA029940.

Interactioni

Subunit structurei

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.UniRule annotation5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CLEC4GQ6UXB43EBI-354047,EBI-2114729
EIF3BP558844EBI-354047,EBI-366696

Protein-protein interaction databases

BioGridi114217. 80 interactions.
DIPiDIP-31116N.
IntActiQ13347. 22 interactions.
MINTiMINT-5004513.
STRINGi9606.ENSP00000362688.

Structurei

3D structure databases

ProteinModelPortaliQ13347.
SMRiQ13347. Positions 1-324.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati1 – 3939WD 1Add
BLAST
Repeati43 – 8139WD 2Add
BLAST
Repeati87 – 12741WD 3Add
BLAST
Repeati135 – 17541WD 4Add
BLAST
Repeati180 – 21738WD 5Add
BLAST
Repeati221 – 26747WD 6Add
BLAST
Repeati275 – 31642WD 7Add
BLAST

Sequence similaritiesi

Belongs to the eIF-3 subunit I family.UniRule annotation
Contains 7 WD repeats.UniRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00630000089849.
HOGENOMiHOG000231322.
HOVERGENiHBG000900.
InParanoidiQ13347.
KOiK03246.
OMAiKATVCAF.
PhylomeDBiQ13347.
TreeFamiTF101515.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
HAMAPiMF_03008. eIF3i.
InterProiIPR027525. eIF3i.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 4 hits.
[Graphical view]
SMARTiSM00320. WD40. 5 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q13347-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPILLQGHE RSITQIKYNR EGDLLFTVAK DPIVNVWYSV NGERLGTYMG
60 70 80 90 100
HTGAVWCVDA DWDTKHVLTG SADNSCRLWD CETGKQLALL KTNSAVRTCG
110 120 130 140 150
FDFGGNIIMF STDKQMGYQC FVSFFDLRDP SQIDNNEPYM KIPCNDSKIT
160 170 180 190 200
SAVWGPLGEC IIAGHESGEL NQYSAKSGEV LVNVKEHSRQ INDIQLSRDM
210 220 230 240 250
TMFVTASKDN TAKLFDSTTL EHQKTFRTER PVNSAALSPN YDHVVLGGGQ
260 270 280 290 300
EAMDVTTTST RIGKFEARFF HLAFEEEFGR VKGHFGPINS VAFHPDGKSY
310 320
SSGGEDGYVR IHYFDPQYFE FEFEA
Length:325
Mass (Da):36,502
Last modified:November 1, 1996 - v1
Checksum:i02797BB72A752A96
GO

Mass spectrometryi

Molecular mass is 36501.9 Da from positions 1 - 325. 1 Publication
Molecular mass is 36503.2±0.4 Da from positions 1 - 325. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39067 mRNA. Translation: AAC97144.1.
U36764 mRNA. Translation: AAC50224.1.
BC000413 mRNA. Translation: AAH00413.1.
BC003140 mRNA. Translation: AAH03140.1.
CCDSiCCDS357.1.
PIRiS60335.
RefSeqiNP_003748.1. NM_003757.2.
XP_011540656.1. XM_011542354.1.
UniGeneiHs.530096.

Genome annotation databases

EnsembliENST00000373586; ENSP00000362688; ENSG00000084623.
GeneIDi8668.
KEGGihsa:8668.
UCSCiuc001bur.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39067 mRNA. Translation: AAC97144.1.
U36764 mRNA. Translation: AAC50224.1.
BC000413 mRNA. Translation: AAH00413.1.
BC003140 mRNA. Translation: AAH03140.1.
CCDSiCCDS357.1.
PIRiS60335.
RefSeqiNP_003748.1. NM_003757.2.
XP_011540656.1. XM_011542354.1.
UniGeneiHs.530096.

3D structure databases

ProteinModelPortaliQ13347.
SMRiQ13347. Positions 1-324.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114217. 80 interactions.
DIPiDIP-31116N.
IntActiQ13347. 22 interactions.
MINTiMINT-5004513.
STRINGi9606.ENSP00000362688.

PTM databases

PhosphoSiteiQ13347.

Polymorphism and mutation databases

BioMutaiEIF3I.
DMDMi2494895.

2D gel databases

DOSAC-COBS-2DPAGEQ13347.
OGPiQ13347.

Proteomic databases

MaxQBiQ13347.
PaxDbiQ13347.
PeptideAtlasiQ13347.
PRIDEiQ13347.

Protocols and materials databases

DNASUi8668.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373586; ENSP00000362688; ENSG00000084623.
GeneIDi8668.
KEGGihsa:8668.
UCSCiuc001bur.4. human.

Organism-specific databases

CTDi8668.
GeneCardsiGC01P032687.
HGNCiHGNC:3272. EIF3I.
HPAiHPA029939.
HPA029940.
MIMi603911. gene.
neXtProtiNX_Q13347.
PharmGKBiPA162384875.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00630000089849.
HOGENOMiHOG000231322.
HOVERGENiHBG000900.
InParanoidiQ13347.
KOiK03246.
OMAiKATVCAF.
PhylomeDBiQ13347.
TreeFamiTF101515.

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.
SignaLinkiQ13347.

Miscellaneous databases

ChiTaRSiEIF3I. human.
GeneWikiiEIF3I.
GenomeRNAii8668.
NextBioi32515.
PROiQ13347.
SOURCEiSearch...

Gene expression databases

BgeeiQ13347.
CleanExiHS_EIF3I.
ExpressionAtlasiQ13347. baseline and differential.
GenevisibleiQ13347. HS.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
HAMAPiMF_03008. eIF3i.
InterProiIPR027525. eIF3i.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 4 hits.
[Graphical view]
SMARTiSM00320. WD40. 5 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiEIF3I_HUMAN
AccessioniPrimary (citable) accession number: Q13347
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Translation initiation factors
    List of translation initiation factor entries
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.