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O60573

- IF4E2_HUMAN

UniProt

O60573 - IF4E2_HUMAN

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Protein

Eukaryotic translation initiation factor 4E type 2

Gene
EIF4E2, EIF4EL3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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.

Sites

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

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. RNA cap binding Source: ProtInc
  4. translation factor activity, nucleic acid binding Source: ProtInc
  5. translation initiation factor activity Source: UniProtKB-KW
  6. ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  1. cytokine-mediated signaling pathway Source: Reactome
  2. in utero embryonic development Source: Ensembl
  3. 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

ReactomeiREACT_115831. 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
Alternative name(s):
Eukaryotic translation initiation factor 4E homologous protein
Eukaryotic translation initiation factor 4E-like 3
eIF4E-like protein 4E-LP
mRNA cap-binding protein 4EHP
mRNA cap-binding protein type 3
Gene namesi
Name:EIF4E2
Synonyms:EIF4EL3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:3293. EIF4E2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. mRNA cap binding complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi63 – 631W → A: Unable to bind capped mRNA.
Mutagenesisi95 – 951W → A: Ability to bind capped mRNA reduced to 40% of wild-type.
Mutagenesisi124 – 1263WED → FAA: Unable to bind capped mRNA.
Mutagenesisi124 – 1241W → A: Ability to bind capped mRNA reduced to less than 10% of wild-type.
Mutagenesisi124 – 1241W → F: Ability to bind capped mRNA reduced to 13% of wild-type.
Mutagenesisi125 – 1251E → A: Ability to bind capped mRNA reduced to less than 10% of wild-type.
Mutagenesisi126 – 1261D → A: Slight reduction in ability to bind capped mRNA.
Mutagenesisi135 – 1351W → A: Unable to bind capped mRNA.
Mutagenesisi148 – 1481W → A: Unable to bind capped mRNA.
Mutagenesisi183 – 1831W → A: Ability to bind capped mRNA reduced to less than 10% of wild-type.
Mutagenesisi183 – 1831W → F: Unable to bind capped mRNA.

Organism-specific databases

PharmGKBiPA27720.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 245245Eukaryotic translation initiation factor 4E type 2PRO_0000193664Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei134 – 1341N6-acetyllysine; alternate1 Publication
Cross-linki134 – 134Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15); alternate1 Publication
Cross-linki222 – 222Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)1 Publication

Post-translational modificationi

Ubiquitinated by ARIH1, leading to its degradation by the proteasome.1 Publication
ISGylation enhances its cap structure-binding activity and translation-inhibition activity.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiO60573.
PaxDbiO60573.
PRIDEiO60573.

PTM databases

PhosphoSiteiO60573.

Expressioni

Gene expression databases

ArrayExpressiO60573.
BgeeiO60573.
CleanExiHS_EIF4E2.
GenevestigatoriO60573.

Organism-specific databases

HPAiHPA019253.

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
EIF4ENIF1Q9NRA83EBI-398610,EBI-301024

Protein-protein interaction databases

BioGridi114856. 21 interactions.
DIPiDIP-32578N.
IntActiO60573. 15 interactions.
MINTiMINT-1440115.
STRINGi9606.ENSP00000258416.

Structurei

Secondary structure

1
245
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi55 – 6713
Helixi75 – 817
Beta strandi82 – 909
Helixi91 – 988
Helixi104 – 1063
Beta strandi109 – 1179
Turni127 – 1315
Beta strandi133 – 1397
Helixi144 – 15613
Beta strandi166 – 1738
Beta strandi178 – 1858
Helixi190 – 20314
Beta strandi212 – 2165
Helixi217 – 2226

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JGBX-ray1.70A45-234[»]
2JGCX-ray2.40A45-234[»]
ProteinModelPortaliO60573.
SMRiO60573. Positions 45-234.

Miscellaneous databases

EvolutionaryTraceiO60573.

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5053.
HOGENOMiHOG000186751.
HOVERGENiHBG107087.
InParanoidiO60573.
KOiK03259.
OMAiDSIKAWE.
OrthoDBiEOG7GQXWN.
PhylomeDBiO60573.
TreeFamiTF101529.

Family and domain databases

Gene3Di3.30.760.10. 1 hit.
InterProiIPR023398. TIF_eIF4e-like_dom.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O60573-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MNNKFDALKD DDSGDHDQNE ENSTQKDGEK EKTERDKNQS SSKRKAVVPG    50
PAEHPLQYNY TFWYSRRTPG RPTSSQSYEQ NIKQIGTFAS VEQFWRFYSH 100
MVRPGDLTGH SDFHLFKEGI KPMWEDDANK NGGKWIIRLR KGLASRCWEN 150
LILAMLGEQF MVGEEICGAV VSVRFQEDII SIWNKTASDQ ATTARIRDTL 200
RRVLNLPPNT IMEYKTHTDS IKMPGRLGPQ RLLFQNLWKP RLNVP 245
Length:245
Mass (Da):28,362
Last modified:August 1, 1998 - v1
Checksum:i3D3075BFA48B3C12
GO
Isoform 2 (identifier: O60573-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     223-234: MPGRLGPQRLLF → DNSSFRNTKITL
     235-245: Missing.

Note: No experimental confirmation available.

Show »
Length:234
Mass (Da):27,026
Checksum:iC63065135BA86C68
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei223 – 23412MPGRL…QRLLF → DNSSFRNTKITL in isoform 2. VSP_054783Add
BLAST
Alternative sequencei235 – 24511Missing in isoform 2. VSP_054784Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 2727MNNKF…STQKD → MMTVGTMIRMKKTAHRKI in AAC39871. 1 PublicationAdd
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF047695 mRNA. Translation: AAC18565.1.
AF068117 mRNA. Translation: AAC19374.1.
AF038957 mRNA. Translation: AAC39871.1.
AC073254 Genomic DNA. No translation available.
AC092165 Genomic DNA. No translation available.
AC093383 Genomic DNA. No translation available.
CH471063 Genomic DNA. Translation: EAW71008.1.
BC005392 mRNA. Translation: AAH05392.1.
BC005874 mRNA. Translation: AAH05874.1.
BC021226 mRNA. Translation: AAH21226.1.
BC021690 mRNA. Translation: AAH21690.1.
CCDSiCCDS2496.1. [O60573-1]
CCDS63159.1. [O60573-2]
RefSeqiNP_001263265.1. NM_001276336.1. [O60573-2]
NP_004837.1. NM_004846.3. [O60573-1]
UniGeneiHs.292026.

Genome annotation databases

EnsembliENST00000258416; ENSP00000258416; ENSG00000135930.
ENST00000409098; ENSP00000386996; ENSG00000135930.
GeneIDi9470.
KEGGihsa:9470.
UCSCiuc002vta.3. human. [O60573-1]
uc002vtb.1. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF047695 mRNA. Translation: AAC18565.1 .
AF068117 mRNA. Translation: AAC19374.1 .
AF038957 mRNA. Translation: AAC39871.1 .
AC073254 Genomic DNA. No translation available.
AC092165 Genomic DNA. No translation available.
AC093383 Genomic DNA. No translation available.
CH471063 Genomic DNA. Translation: EAW71008.1 .
BC005392 mRNA. Translation: AAH05392.1 .
BC005874 mRNA. Translation: AAH05874.1 .
BC021226 mRNA. Translation: AAH21226.1 .
BC021690 mRNA. Translation: AAH21690.1 .
CCDSi CCDS2496.1. [O60573-1 ]
CCDS63159.1. [O60573-2 ]
RefSeqi NP_001263265.1. NM_001276336.1. [O60573-2 ]
NP_004837.1. NM_004846.3. [O60573-1 ]
UniGenei Hs.292026.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2JGB X-ray 1.70 A 45-234 [» ]
2JGC X-ray 2.40 A 45-234 [» ]
ProteinModelPortali O60573.
SMRi O60573. Positions 45-234.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114856. 21 interactions.
DIPi DIP-32578N.
IntActi O60573. 15 interactions.
MINTi MINT-1440115.
STRINGi 9606.ENSP00000258416.

PTM databases

PhosphoSitei O60573.

Proteomic databases

MaxQBi O60573.
PaxDbi O60573.
PRIDEi O60573.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000258416 ; ENSP00000258416 ; ENSG00000135930 .
ENST00000409098 ; ENSP00000386996 ; ENSG00000135930 .
GeneIDi 9470.
KEGGi hsa:9470.
UCSCi uc002vta.3. human. [O60573-1 ]
uc002vtb.1. human.

Organism-specific databases

CTDi 9470.
GeneCardsi GC02P233414.
HGNCi HGNC:3293. EIF4E2.
HPAi HPA019253.
MIMi 605895. gene.
neXtProti NX_O60573.
PharmGKBi PA27720.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5053.
HOGENOMi HOG000186751.
HOVERGENi HBG107087.
InParanoidi O60573.
KOi K03259.
OMAi DSIKAWE.
OrthoDBi EOG7GQXWN.
PhylomeDBi O60573.
TreeFami TF101529.

Enzyme and pathway databases

Reactomei REACT_115831. ISG15 antiviral mechanism.

Miscellaneous databases

ChiTaRSi EIF4E2. human.
EvolutionaryTracei O60573.
GeneWikii EIF4E2.
GenomeRNAii 9470.
NextBioi 35481795.
PROi O60573.
SOURCEi Search...

Gene expression databases

ArrayExpressi O60573.
Bgeei O60573.
CleanExi HS_EIF4E2.
Genevestigatori O60573.

Family and domain databases

Gene3Di 3.30.760.10. 1 hit.
InterProi IPR023398. TIF_eIF4e-like_dom.
IPR001040. TIF_eIF_4E.
IPR019770. TIF_eIF_4E_CS.
[Graphical view ]
PANTHERi PTHR11960. PTHR11960. 1 hit.
Pfami PF01652. IF4E. 1 hit.
[Graphical view ]
SUPFAMi SSF55418. SSF55418. 1 hit.
PROSITEi PS00813. IF4E. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of 4EHP, a novel mammalian eIF4E-related cap-binding protein."
    Rom E., Kim H.C., Gingras A.-C., Marcotrigiano J., Favre D., Olsen H., Burley S.K., Sonenberg N.
    J. Biol. Chem. 273:13104-13109(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, 3D-STRUCTURE MODELING, MUTAGENESIS.
    Tissue: Follicular cell.
  2. "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] (ISOFORM 1), INTERACTION WITH EIF4EBP1; EIF4EBP2 AND EIF4EBP3.
    Tissue: Mammary gland.
  3. "Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning."
    Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., Wang Y.-X., Chen S.-J., Chen Z.
    Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Umbilical cord blood.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 1).
    Tissue: Muscle, Urinary bladder and Uterus.
  7. "Human homologue of ariadne promotes the ubiquitylation of translation initiation factor 4E homologous protein, 4EHP."
    Tan N.G., Ardley H.C., Scott G.B., Rose S.A., Markham A.F., Robinson P.A.
    FEBS Lett. 554:501-504(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY ARIH1.
  8. "ISG15 modification of the eIF4E cognate 4EHP enhances cap structure-binding activity of 4EHP."
    Okumura F., Zou W., Zhang D.E.
    Genes Dev. 21:255-260(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISGYLATION AT LYS-134 AND LYS-222.
  9. "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-134, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Structures of the human eIF4E homologous protein, h4EHP, in its m7GTP-bound and unliganded forms."
    Rosettani P., Knapp S., Vismara M.-G., Rusconi L., Cameron A.D.
    J. Mol. Biol. 368:691-705(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 45-234 IN COMPLEX WITH MRNA CAP ANALOGS AND EIF4EBP1.

Entry informationi

Entry nameiIF4E2_HUMAN
AccessioniPrimary (citable) accession number: O60573
Secondary accession number(s): B8ZZJ9, O75349
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: August 1, 1998
Last modified: September 3, 2014
This is version 128 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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