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Protein

Eukaryotic initiation factor 4A-I

Gene

Eif4a1

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

Functioni

ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon.

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi76 – 838ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-1169408. ISG15 antiviral mechanism.
R-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-429947. Deadenylation of mRNA.
R-MMU-72649. Translation initiation complex formation.
R-MMU-72662. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
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 initiation factor 4A-I (EC:3.6.4.13)
Short name:
eIF-4A-I
Short name:
eIF4A-I
Alternative name(s):
ATP-dependent RNA helicase eIF4A-1
Gene namesi
Name:Eif4a1
Synonyms:Ddx2a, Eif4a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:95303. Eif4a1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 406405Eukaryotic initiation factor 4A-IPRO_0000054935Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei4 – 41PhosphoserineBy similarity
Modified residuei118 – 1181N6-acetyllysineBy similarity
Modified residuei174 – 1741N6-acetyllysineBy similarity
Modified residuei193 – 1931N6-acetyllysineCombined sources
Modified residuei238 – 2381N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP60843.
PaxDbiP60843.
PRIDEiP60843.

2D gel databases

REPRODUCTION-2DPAGEP60843.

PTM databases

iPTMnetiP60843.
PhosphoSiteiP60843.
SwissPalmiP60843.

Expressioni

Gene expression databases

BgeeiP60843.
CleanExiMM_EIF4A1.
ExpressionAtlasiP60843. baseline and differential.
GenevisibleiP60843. 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 EIF4G1/EIF4G3. Interacts with PAIP1, EIF4E and UPF2. Found in a complex with XPO7, EIF4A1, ARHGAP1, VPS26A, VPS29, VPS35 and SFN. May interact with NOM1. Interacts with PDCD4; this interferes with the interaction between EIF4A and EIF4G. Interacts with RBM4 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Eif4g1Q6NZJ62EBI-6665935,EBI-8175606
Pdcd4Q618234EBI-6665935,EBI-296473

Protein-protein interaction databases

BioGridi199418. 5 interactions.
IntActiP60843. 8 interactions.
MINTiMINT-202155.
STRINGi10090.ENSMUSP00000127034.

Chemistry

BindingDBiP60843.

Structurei

3D structure databases

ProteinModelPortaliP60843.
SMRiP60843. Positions 22-400.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini63 – 234172Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini245 – 406162Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi32 – 6029Q motifAdd
BLAST
Motifi182 – 1854DEAD box

Sequence similaritiesi

Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0327. Eukaryota.
COG0513. LUCA.
HOGENOMiHOG000268797.
HOVERGENiHBG107989.
InParanoidiP60843.
KOiK03257.
OMAiQQIDVEM.
OrthoDBiEOG7XPZ5M.
PhylomeDBiP60843.
TreeFamiTF101524.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR031258. EIF4A1/2.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PANTHERiPTHR24031:SF226. PTHR24031:SF226. 1 hit.
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P60843-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSASQDSRSR DNGPDGMEPE GVIESNWNEI VDSFDDMNLS ESLLRGIYAY
60 70 80 90 100
GFEKPSAIQQ RAILPCIKGY DVIAQAQSGT GKTATFAISI LQQIELDLKA
110 120 130 140 150
TQALVLAPTR ELAQQIQKVV MALGDYMGAS CHACIGGTNV RAEVQKLQME
160 170 180 190 200
APHIIVGTPG RVFDMLNRRY LSPKYIKMFV LDEADEMLSR GFKDQIYDIF
210 220 230 240 250
QKLNSNTQVV LLSATMPSDV LEVTKKFMRD PIRILVKKEE LTLEGIRQFY
260 270 280 290 300
INVEREEWKL DTLCDLYETL TITQAVIFIN TRRKVDWLTE KMHARDFTVS
310 320 330 340 350
AMHGDMDQKE RDVIMREFRS GSSRVLITTD LLARGIDVQQ VSLVINYDLP
360 370 380 390 400
TNRENYIHRI GRGGRFGRKG VAINMVTEED KRTLRDIETF YNTSIEEMPL

NVADLI
Length:406
Mass (Da):46,154
Last modified:April 13, 2004 - v1
Checksum:i6EF89939F3045420
GO

Sequence cautioni

The sequence CAA26842.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA26843.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA26845.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA26846.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti300 – 3001S → C in AAA50407 (PubMed:3215517).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03039 mRNA. Translation: CAA26842.1. Different initiation.
X03039 mRNA. Translation: CAA26843.1. Different initiation.
X03040 mRNA. Translation: CAA26845.1. Different initiation.
X03040 mRNA. Translation: CAA26846.1. Different initiation.
L36611
, M22873, L36608, L36609, L36610 Genomic DNA. Translation: AAA50407.1.
AB011595 Genomic DNA. Translation: BAA25075.1.
AK077429 mRNA. Translation: BAC36796.1.
BC049915 mRNA. Translation: AAH49915.1.
CCDSiCCDS24904.1.
PIRiJS0039. FIMS4A.
RefSeqiNP_659207.1. NM_144958.4.
UniGeneiMm.26680.
Mm.279821.
Mm.371557.
Mm.473799.

Genome annotation databases

EnsembliENSMUST00000163666; ENSMUSP00000127034; ENSMUSG00000059796.
GeneIDi13681.
KEGGimmu:13681.
UCSCiuc007jra.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03039 mRNA. Translation: CAA26842.1. Different initiation.
X03039 mRNA. Translation: CAA26843.1. Different initiation.
X03040 mRNA. Translation: CAA26845.1. Different initiation.
X03040 mRNA. Translation: CAA26846.1. Different initiation.
L36611
, M22873, L36608, L36609, L36610 Genomic DNA. Translation: AAA50407.1.
AB011595 Genomic DNA. Translation: BAA25075.1.
AK077429 mRNA. Translation: BAC36796.1.
BC049915 mRNA. Translation: AAH49915.1.
CCDSiCCDS24904.1.
PIRiJS0039. FIMS4A.
RefSeqiNP_659207.1. NM_144958.4.
UniGeneiMm.26680.
Mm.279821.
Mm.371557.
Mm.473799.

3D structure databases

ProteinModelPortaliP60843.
SMRiP60843. Positions 22-400.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199418. 5 interactions.
IntActiP60843. 8 interactions.
MINTiMINT-202155.
STRINGi10090.ENSMUSP00000127034.

Chemistry

BindingDBiP60843.

PTM databases

iPTMnetiP60843.
PhosphoSiteiP60843.
SwissPalmiP60843.

2D gel databases

REPRODUCTION-2DPAGEP60843.

Proteomic databases

EPDiP60843.
PaxDbiP60843.
PRIDEiP60843.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000163666; ENSMUSP00000127034; ENSMUSG00000059796.
GeneIDi13681.
KEGGimmu:13681.
UCSCiuc007jra.2. mouse.

Organism-specific databases

CTDi1973.
MGIiMGI:95303. Eif4a1.

Phylogenomic databases

eggNOGiKOG0327. Eukaryota.
COG0513. LUCA.
HOGENOMiHOG000268797.
HOVERGENiHBG107989.
InParanoidiP60843.
KOiK03257.
OMAiQQIDVEM.
OrthoDBiEOG7XPZ5M.
PhylomeDBiP60843.
TreeFamiTF101524.

Enzyme and pathway databases

ReactomeiR-MMU-1169408. ISG15 antiviral mechanism.
R-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-429947. Deadenylation of mRNA.
R-MMU-72649. Translation initiation complex formation.
R-MMU-72662. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
R-MMU-72702. Ribosomal scanning and start codon recognition.
R-MMU-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Miscellaneous databases

NextBioi284438.
PROiP60843.
SOURCEiSearch...

Gene expression databases

BgeeiP60843.
CleanExiMM_EIF4A1.
ExpressionAtlasiP60843. baseline and differential.
GenevisibleiP60843. MM.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR031258. EIF4A1/2.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PANTHERiPTHR24031:SF226. PTHR24031:SF226. 1 hit.
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of eukaryotic protein synthesis initiation factor genes: isolation and characterization of cDNA clones encoding factor eIF-4A."
    Nielsen P.J., McMaster G.K., Trachsel H.
    Nucleic Acids Res. 13:6867-6880(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Isolation and mapping of a gene for protein synthesis initiation factor 4A and its expression during differentiation of murine erythroleukemia cells."
    Reddy N.S., Roth W.W., Bragg P.W., Wahba A.J.
    Gene 70:231-243(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Miyashita A., Shimizu N., Nakajima T., Odani S., Kuwano R.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129.
  4. "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.
  5. "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: Czech II.
    Tissue: Mammary gland.
  6. "Mutational analysis of a DEAD box RNA helicase: the mammalian translation initiation factor eIF-4A."
    Pause A., Somenberg N.
    EMBO J. 11:2643-2654(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-193 AND LYS-238, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiIF4A1_MOUSE
AccessioniPrimary (citable) accession number: P60843
Secondary accession number(s): P04765, Q61516
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: April 13, 2004
Last modified: May 11, 2016
This is version 127 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. 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.