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Protein

Eukaryotic translation initiation factor 4E type 3

Gene

Eif4e3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis. May act as an inhibitor of EIF4E1 activity.1 Publication

GO - Molecular functioni

  1. translation initiation factor activity Source: UniProtKB-KW

GO - Biological processi

  1. regulation of translation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis, Translation regulation

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_198533. ISG15 antiviral mechanism.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 4E type 3
Short name:
eIF-4E type 3
Short name:
eIF-4E3
Short name:
eIF4E type 3
Short name:
eIF4E-3
Gene namesi
Name:Eif4e3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:1914142. Eif4e3.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: InterPro
  2. mRNA cap binding complex Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 207207Eukaryotic translation initiation factor 4E type 3PRO_0000287698Add
BLAST

Proteomic databases

MaxQBiQ9DBB5.
PaxDbiQ9DBB5.
PRIDEiQ9DBB5.

2D gel databases

REPRODUCTION-2DPAGEQ9DBB5.

PTM databases

PhosphoSiteiQ9DBB5.

Expressioni

Tissue specificityi

Only expressed in heart, skeletal muscle, lung and spleen.1 Publication

Gene expression databases

BgeeiQ9DBB5.
GenevestigatoriQ9DBB5.

Interactioni

Subunit structurei

eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least eIF4A, eIF4E and eIF4G (By similarity). EIF4E3 interacts with EIF4G1, but not with EIF4EBP1, EIF4EBP2 and EIF4EBP3.By similarity1 Publication

Protein-protein interaction databases

IntActiQ9DBB5. 1 interaction.
MINTiMINT-4127798.

Structurei

Secondary structure

1
207
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 154Combined sources
Turni17 – 204Combined sources
Beta strandi24 – 274Combined sources
Beta strandi31 – 4111Combined sources
Helixi49 – 557Combined sources
Beta strandi57 – 648Combined sources
Helixi65 – 7410Combined sources
Helixi78 – 803Combined sources
Beta strandi83 – 9311Combined sources
Helixi97 – 993Combined sources
Turni101 – 1055Combined sources
Beta strandi107 – 1137Combined sources
Turni115 – 1173Combined sources
Helixi118 – 12912Combined sources
Turni130 – 1323Combined sources
Helixi134 – 1374Combined sources
Beta strandi144 – 1518Combined sources
Beta strandi156 – 1638Combined sources
Helixi165 – 1673Combined sources
Turni168 – 1703Combined sources
Helixi173 – 1808Combined sources
Beta strandi187 – 1937Combined sources
Turni194 – 1963Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4B6UNMR-A1-207[»]
4B6VNMR-A1-207[»]
ProteinModelPortaliQ9DBB5.
SMRiQ9DBB5. Positions 16-207.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni98 – 9927-methylguanosine-containing mRNA cap bindingBy similarity
Regioni152 – 15767-methylguanosine-containing mRNA cap bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5053.
GeneTreeiENSGT00520000055549.
HOGENOMiHOG000059588.
HOVERGENiHBG107990.
InParanoidiQ9DBB5.
OMAiIYTVHTV.
OrthoDBiEOG7X6M1B.
PhylomeDBiQ9DBB5.

Family and domain databases

Gene3Di3.30.760.10. 1 hit.
InterProiIPR023398. TIF_eIF4e-like_dom.
IPR001040. TIF_eIF_4E.
[Graphical view]
PANTHERiPTHR11960. PTHR11960. 1 hit.
PfamiPF01652. IF4E. 1 hit.
[Graphical view]
SUPFAMiSSF55418. SSF55418. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9DBB5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALPPAAAPP GANEPLDKAL SALPPEPGGV PLHSPWTFWL DRSLPGATAA
60 70 80 90 100
ECASNLKKIY TVQTVQIFWS VYNNIPPVTS LPLRCSYHLM RGERRPLWEE
110 120 130 140 150
ESNAKGGVWK MKVPKDSTST VWKELLLATI GEQFTDCAAA DDEIIGVSVS
160 170 180 190 200
VRDREDVVQV WNVNASLVGE ATVLEKIHQL LPHIAFKAVF YKPHEEHHAF

EGGRGKH
Length:207
Mass (Da):22,836
Last modified:June 1, 2001 - v1
Checksum:i0263A317BFD0A4C1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti122 – 1221W → G in BAB24928 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY628329 mRNA. Translation: AAT45741.1.
AK005054 mRNA. Translation: BAB23780.1.
AK007268 mRNA. Translation: BAB24928.1.
BC027014 mRNA. Translation: AAH27014.1.
CCDSiCCDS20386.1.
RefSeqiNP_080105.1. NM_025829.4.
UniGeneiMm.32889.

Genome annotation databases

EnsembliENSMUST00000032151; ENSMUSP00000032151; ENSMUSG00000093661.
GeneIDi66892.
KEGGimmu:66892.
UCSCiuc009dbr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY628329 mRNA. Translation: AAT45741.1.
AK005054 mRNA. Translation: BAB23780.1.
AK007268 mRNA. Translation: BAB24928.1.
BC027014 mRNA. Translation: AAH27014.1.
CCDSiCCDS20386.1.
RefSeqiNP_080105.1. NM_025829.4.
UniGeneiMm.32889.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4B6UNMR-A1-207[»]
4B6VNMR-A1-207[»]
ProteinModelPortaliQ9DBB5.
SMRiQ9DBB5. Positions 16-207.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9DBB5. 1 interaction.
MINTiMINT-4127798.

PTM databases

PhosphoSiteiQ9DBB5.

2D gel databases

REPRODUCTION-2DPAGEQ9DBB5.

Proteomic databases

MaxQBiQ9DBB5.
PaxDbiQ9DBB5.
PRIDEiQ9DBB5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032151; ENSMUSP00000032151; ENSMUSG00000093661.
GeneIDi66892.
KEGGimmu:66892.
UCSCiuc009dbr.1. mouse.

Organism-specific databases

CTDi317649.
MGIiMGI:1914142. Eif4e3.

Phylogenomic databases

eggNOGiCOG5053.
GeneTreeiENSGT00520000055549.
HOGENOMiHOG000059588.
HOVERGENiHBG107990.
InParanoidiQ9DBB5.
OMAiIYTVHTV.
OrthoDBiEOG7X6M1B.
PhylomeDBiQ9DBB5.

Enzyme and pathway databases

ReactomeiREACT_198533. ISG15 antiviral mechanism.

Miscellaneous databases

NextBioi322945.
PROiQ9DBB5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DBB5.
GenevestigatoriQ9DBB5.

Family and domain databases

Gene3Di3.30.760.10. 1 hit.
InterProiIPR023398. TIF_eIF4e-like_dom.
IPR001040. TIF_eIF_4E.
[Graphical view]
PANTHERiPTHR11960. PTHR11960. 1 hit.
PfamiPF01652. IF4E. 1 hit.
[Graphical view]
SUPFAMiSSF55418. SSF55418. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of mammalian eIF4E-family members."
    Joshi B., Cameron A., Jagus R.
    Eur. J. Biochem. 271:2189-2203(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH EIF4G1.
    Strain: Czech II.
    Tissue: Lung tumor.
  2. "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: Liver and Testis.
  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].
    Strain: FVB/N-3.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiIF4E3_MOUSE
AccessioniPrimary (citable) accession number: Q9DBB5
Secondary accession number(s): Q9D983
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: June 1, 2001
Last modified: January 7, 2015
This is version 92 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.