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Protein

Eukaryotic translation initiation factor 3 subunit I

Gene

Eif3i

Organism
Mus musculus (Mouse)
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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

ReactomeiR-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-72649. Translation initiation complex formation.
R-MMU-72689. Formation of a pool of free 40S subunits.
R-MMU-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-MMU-72702. Ribosomal scanning and start codon recognition.
R-MMU-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

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:Eif3i
Synonyms:Eif3s2, Trip1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1860763. Eif3i.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 325325Eukaryotic translation initiation factor 3 subunit IPRO_0000051037Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Phosphorylated by TGF-beta type II receptor.UniRule annotation

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9QZD9.
MaxQBiQ9QZD9.
PaxDbiQ9QZD9.
PRIDEiQ9QZD9.

2D gel databases

REPRODUCTION-2DPAGEQ9QZD9.

PTM databases

iPTMnetiQ9QZD9.
PhosphoSiteiQ9QZD9.

Expressioni

Gene expression databases

BgeeiQ9QZD9.
ExpressionAtlasiQ9QZD9. baseline and differential.
GenevisibleiQ9QZD9. MM.

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 may interact with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation may lead 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 annotation2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Eif4g1Q6NZJ63EBI-7466616,EBI-8175606

Protein-protein interaction databases

BioGridi207720. 55 interactions.
IntActiQ9QZD9. 58 interactions.
MINTiMINT-1869798.
STRINGi10090.ENSMUSP00000099653.

Structurei

3D structure databases

ProteinModelPortaliQ9QZD9.
SMRiQ9QZD9. Positions 1-324.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati8 – 4740WD 1Add
BLAST
Repeati50 – 9142WD 2Add
BLAST
Repeati144 – 18340WD 3Add
BLAST
Repeati186 – 22540WD 4Add
BLAST
Repeati283 – 32442WD 5Add
BLAST

Sequence similaritiesi

Belongs to the eIF-3 subunit I family.UniRule annotation
Contains 5 WD repeats.UniRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0643. Eukaryota.
ENOG410XQ3E. LUCA.
GeneTreeiENSGT00630000089849.
HOGENOMiHOG000231322.
HOVERGENiHBG000900.
InParanoidiQ9QZD9.
KOiK03246.
OMAiKATVCAF.
OrthoDBiEOG7PVWPK.
PhylomeDBiQ9QZD9.
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. 3 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.

Q9QZD9-1 [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 SQIDSNEPYM KIPCNDSKIT
160 170 180 190 200
SAVWGPLGEC VIAGHESGEL 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):36,461
Last modified:May 1, 2000 - v1
Checksum:i2B29405772675CC0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF188297 mRNA. Translation: AAF01455.1.
AF271072 mRNA. Translation: AAF76199.1.
AK012375 mRNA. Translation: BAB28197.1.
AK002896 mRNA. Translation: BAB22440.1.
AK010781 mRNA. Translation: BAB27177.1.
BC029625 mRNA. Translation: AAH29625.1.
CCDSiCCDS18698.1.
RefSeqiNP_061269.1. NM_018799.2.
UniGeneiMm.250874.

Genome annotation databases

EnsembliENSMUST00000102593; ENSMUSP00000099653; ENSMUSG00000028798.
GeneIDi54709.
KEGGimmu:54709.
UCSCiuc008uxm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF188297 mRNA. Translation: AAF01455.1.
AF271072 mRNA. Translation: AAF76199.1.
AK012375 mRNA. Translation: BAB28197.1.
AK002896 mRNA. Translation: BAB22440.1.
AK010781 mRNA. Translation: BAB27177.1.
BC029625 mRNA. Translation: AAH29625.1.
CCDSiCCDS18698.1.
RefSeqiNP_061269.1. NM_018799.2.
UniGeneiMm.250874.

3D structure databases

ProteinModelPortaliQ9QZD9.
SMRiQ9QZD9. Positions 1-324.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207720. 55 interactions.
IntActiQ9QZD9. 58 interactions.
MINTiMINT-1869798.
STRINGi10090.ENSMUSP00000099653.

PTM databases

iPTMnetiQ9QZD9.
PhosphoSiteiQ9QZD9.

2D gel databases

REPRODUCTION-2DPAGEQ9QZD9.

Proteomic databases

EPDiQ9QZD9.
MaxQBiQ9QZD9.
PaxDbiQ9QZD9.
PRIDEiQ9QZD9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000102593; ENSMUSP00000099653; ENSMUSG00000028798.
GeneIDi54709.
KEGGimmu:54709.
UCSCiuc008uxm.2. mouse.

Organism-specific databases

CTDi8668.
MGIiMGI:1860763. Eif3i.

Phylogenomic databases

eggNOGiKOG0643. Eukaryota.
ENOG410XQ3E. LUCA.
GeneTreeiENSGT00630000089849.
HOGENOMiHOG000231322.
HOVERGENiHBG000900.
InParanoidiQ9QZD9.
KOiK03246.
OMAiKATVCAF.
OrthoDBiEOG7PVWPK.
PhylomeDBiQ9QZD9.
TreeFamiTF101515.

Enzyme and pathway databases

ReactomeiR-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-72649. Translation initiation complex formation.
R-MMU-72689. Formation of a pool of free 40S subunits.
R-MMU-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-MMU-72702. Ribosomal scanning and start codon recognition.
R-MMU-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Miscellaneous databases

ChiTaRSiEif3i. mouse.
NextBioi311544.
PROiQ9QZD9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QZD9.
ExpressionAtlasiQ9QZD9. baseline and differential.
GenevisibleiQ9QZD9. MM.

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. 3 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. "Mouse TRIP-1 gene isolated from murine L-929 cells."
    Zhou A., Silverman R.H.
    Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Mus musculus TGF-beta receptor interacting protein 1 (TRIP1)."
    Joseph P., Fan L., Whong W.-Z., Ong T.-M.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo, Embryonic stem cell and Kidney.
  4. "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].
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  5. Lubec G., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 269-280.
    Tissue: Brain.
  6. "mTOR-dependent stimulation of the association of eIF4G and eIF3 by insulin."
    Harris T.E., Chi A., Shabanowitz J., Hunt D.F., Rhoads R.E., Lawrence J.C. Jr.
    EMBO J. 25:1659-1668(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EIF3B AND EIF4G1.
  7. "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, IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiEIF3I_MOUSE
AccessioniPrimary (citable) accession number: Q9QZD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Translation initiation factors
    List of translation initiation factor entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

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.