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Protein

Eukaryotic translation initiation factor 4E type 2

Gene

Eif4e2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei110 – 11017-methylguanosine-containing mRNA capBy similarity

GO - Molecular functioni

GO - Biological processi

  • in utero embryonic development Source: MGI
  • negative regulation of translation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis, Translation regulation

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-1169408. ISG15 antiviral mechanism.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 4E type 2
Short name:
eIF-4E type 2
Short name:
eIF4E type 2
Short name:
eIF4E-2
Short name:
mRNA cap-binding protein type 2
Alternative name(s):
Eukaryotic translation initiation factor 4E-like 3
eIF4E-like protein 4E-LP
Gene namesi
Name:Eif4e2
Synonyms:Eif4el3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1914440. Eif4e2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 245245Eukaryotic translation initiation factor 4E type 2PRO_0000193665Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei134 – 1341N6-acetyllysine; alternateBy similarity
Cross-linki134 – 134Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15); alternateBy similarity
Cross-linki222 – 222Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)By similarity

Post-translational modificationi

Ubiquitinated by ARIH1, leading to its degradation by the proteasome.By similarity
ISGylation enhances its cap structure-binding activity and translation-inhibition activity.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiQ8BMB3.
MaxQBiQ8BMB3.
PaxDbiQ8BMB3.
PRIDEiQ8BMB3.

PTM databases

iPTMnetiQ8BMB3.
PhosphoSiteiQ8BMB3.

Expressioni

Tissue specificityi

Widely expressed with highest levels in testis, kidney and liver.1 Publication

Gene expression databases

BgeeiQ8BMB3.
ExpressionAtlasiQ8BMB3. baseline and differential.
GenevisibleiQ8BMB3. MM.

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. eIF4E is also known to interact with other partners (By similarity). EIF4E2 interacts with EIF4EBP1, EIF4EBP2 and EIF4EBP3 but not with eIF4G.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ8BMB3. 3 interactions.
MINTiMINT-4098469.
STRINGi10090.ENSMUSP00000108859.

Structurei

3D structure databases

ProteinModelPortaliQ8BMB3.
SMRiQ8BMB3. Positions 45-234.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni54 – 574EIF4EBP1/2/3 bindingBy similarity
Regioni78 – 7927-methylguanosine-containing mRNA cap bindingBy similarity
Regioni95 – 995EIF4EBP1/2/3 bindingBy similarity
Regioni124 – 12527-methylguanosine-containing mRNA cap bindingBy similarity
Regioni150 – 1578EIF4EBP1/2/3 bindingBy similarity
Regioni174 – 17967-methylguanosine-containing mRNA cap bindingBy similarity
Regioni222 – 22437-methylguanosine-containing mRNA cap bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1669. Eukaryota.
COG5053. LUCA.
GeneTreeiENSGT00520000055549.
HOGENOMiHOG000186751.
HOVERGENiHBG107087.
InParanoidiQ8BMB3.
KOiK03259.
TreeFamiTF101529.

Family and domain databases

Gene3Di3.30.760.10. 1 hit.
InterProiIPR023398. TIF_eIF4e-like.
IPR001040. TIF_eIF_4E.
IPR019770. TIF_eIF_4E_CS.
[Graphical view]
PANTHERiPTHR11960. PTHR11960. 1 hit.
PfamiPF01652. IF4E. 1 hit.
[Graphical view]
SUPFAMiSSF55418. SSF55418. 1 hit.
PROSITEiPS00813. IF4E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BMB3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNKFDALKD DDSGDHDQNE ENSTQKDGEK EKTDRDKSQS SGKRKAVVPG
60 70 80 90 100
PAEHPLQYNY TFWYSRRTPG RPTSSQSYEQ NIKQIGTFAS VEQFWKFYSH
110 120 130 140 150
MVRPGDLTGH SDFHLFKEGI KPMWEDDANK NGGKWIIRLR KGLASRCWEN
160 170 180 190 200
LILAMLGEQF MVGEEICGAV VSVRFQEDII SIWNKTASDQ ATTARIRDTL
210 220 230 240
RRVLNLPPNT IMEYKTHTDS IKMPGRLGPQ RLLFQNLWKP RLNVP
Length:245
Mass (Da):28,263
Last modified:March 1, 2003 - v1
Checksum:iAA722843721A01CC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti200 – 2001L → F in AAC19373 (PubMed:15153109).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF068116 mRNA. Translation: AAC19373.1.
AK032965 mRNA. Translation: BAC28102.1.
AK150495 mRNA. Translation: BAE29610.1.
BC045153 mRNA. Translation: AAH45153.1.
CCDSiCCDS35652.1.
RefSeqiNP_001034259.1. NM_001039170.1.
NP_075803.2. NM_023314.3.
UniGeneiMm.227183.

Genome annotation databases

EnsembliENSMUST00000113233; ENSMUSP00000108859; ENSMUSG00000026254.
GeneIDi26987.
KEGGimmu:26987.
UCSCiuc007bwk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF068116 mRNA. Translation: AAC19373.1.
AK032965 mRNA. Translation: BAC28102.1.
AK150495 mRNA. Translation: BAE29610.1.
BC045153 mRNA. Translation: AAH45153.1.
CCDSiCCDS35652.1.
RefSeqiNP_001034259.1. NM_001039170.1.
NP_075803.2. NM_023314.3.
UniGeneiMm.227183.

3D structure databases

ProteinModelPortaliQ8BMB3.
SMRiQ8BMB3. Positions 45-234.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8BMB3. 3 interactions.
MINTiMINT-4098469.
STRINGi10090.ENSMUSP00000108859.

PTM databases

iPTMnetiQ8BMB3.
PhosphoSiteiQ8BMB3.

Proteomic databases

EPDiQ8BMB3.
MaxQBiQ8BMB3.
PaxDbiQ8BMB3.
PRIDEiQ8BMB3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000113233; ENSMUSP00000108859; ENSMUSG00000026254.
GeneIDi26987.
KEGGimmu:26987.
UCSCiuc007bwk.1. mouse.

Organism-specific databases

CTDi9470.
MGIiMGI:1914440. Eif4e2.

Phylogenomic databases

eggNOGiKOG1669. Eukaryota.
COG5053. LUCA.
GeneTreeiENSGT00520000055549.
HOGENOMiHOG000186751.
HOVERGENiHBG107087.
InParanoidiQ8BMB3.
KOiK03259.
TreeFamiTF101529.

Enzyme and pathway databases

ReactomeiR-MMU-1169408. ISG15 antiviral mechanism.

Miscellaneous databases

ChiTaRSiEif4e2. mouse.
NextBioi304927.
PROiQ8BMB3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BMB3.
ExpressionAtlasiQ8BMB3. baseline and differential.
GenevisibleiQ8BMB3. MM.

Family and domain databases

Gene3Di3.30.760.10. 1 hit.
InterProiIPR023398. TIF_eIF4e-like.
IPR001040. TIF_eIF_4E.
IPR019770. TIF_eIF_4E_CS.
[Graphical view]
PANTHERiPTHR11960. PTHR11960. 1 hit.
PfamiPF01652. IF4E. 1 hit.
[Graphical view]
SUPFAMiSSF55418. SSF55418. 1 hit.
PROSITEiPS00813. IF4E. 1 hit.
[Graphical view]
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, INTERACTION WITH EIF4EBP1; EIF4EBP2 AND EIF4EBP3, TISSUE SPECIFICITY.
    Strain: NIH Swiss.
  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: Bone marrow and Mesonephros.
  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 gland.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Liver, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiIF4E2_MOUSE
AccessioniPrimary (citable) accession number: Q8BMB3
Secondary accession number(s): O88503, Q3UCK2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: March 1, 2003
Last modified: May 11, 2016
This is version 103 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, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.