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P60842 (IF4A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic initiation factor 4A-I

Short name=eIF-4A-I
Short name=eIF4A-I
EC=3.6.4.13
Alternative name(s):
ATP-dependent RNA helicase eIF4A-1
Gene names
Name:EIF4A1
Synonyms:DDX2A, EIF4A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.18 Ref.19

Catalytic activity

ATP + H2O = ADP + phosphate.

Enzyme regulation

Helicase activity and function in translation are inhibited by interaction with PDCD4. Ref.18 Ref.19

Subunit structure

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. Interacts with human cytomegalovirus/HHV-5 protein UL69. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.15 Ref.18 Ref.19

Sequence similarities

Belongs to the DEAD box helicase family. eIF4A subfamily.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Ontologies

Keywords
   Biological processHost-virus interaction
Protein biosynthesis
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
RNA-binding
   Molecular functionHelicase
Hydrolase
Initiation factor
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA poly(A) tail shortening

Traceable author statement. Source: Reactome

organ regeneration

Inferred from electronic annotation. Source: Ensembl

translation

Traceable author statement. Source: Reactome

translational initiation

Traceable author statement. Source: Reactome

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

eukaryotic translation initiation factor 4F complex

Traceable author statement PubMed 9168945. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337PubMed 23376485. Source: UniProt

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent helicase activity

Inferred from electronic annotation. Source: InterPro

RNA cap binding

Traceable author statement PubMed 3215517. Source: UniProtKB

double-stranded RNA binding

Inferred from direct assay PubMed 21266579. Source: MGI

helicase activity

Traceable author statement PubMed 3215517. Source: UniProtKB

mRNA binding

Traceable author statement PubMed 3215517. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.12Ref.7. Source: UniProtKB

translation factor activity, nucleic acid binding

Traceable author statement PubMed 10880459PubMed 3215517. Source: UniProtKB

translation initiation factor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P60842-1)

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.
Isoform 2 (identifier: P60842-2)

The sequence of this isoform differs from the canonical sequence as follows:
     333-406: ARGIDVQQVS...EMPLNVADLI → GKLYPQNRSRWTVWP
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.17
Chain2 – 406405Eukaryotic initiation factor 4A-I
PRO_0000054933

Regions

Domain63 – 234172Helicase ATP-binding
Domain245 – 406162Helicase C-terminal
Nucleotide binding76 – 838ATP By similarity
Motif32 – 6029Q motif
Motif182 – 1854DEAD box

Amino acid modifications

Modified residue21N-acetylserine Ref.17
Modified residue41Phosphoserine Ref.17
Modified residue1181N6-acetyllysine Ref.14
Modified residue1741N6-acetyllysine Ref.14
Modified residue1931N6-acetyllysine By similarity
Modified residue2381N6-acetyllysine By similarity

Natural variations

Alternative sequence333 – 40674ARGID…VADLI → GKLYPQNRSRWTVWP in isoform 2.
VSP_046032

Secondary structure

........................................................................ 406
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 13, 2004. Version 1.
Checksum: 6EF89939F3045420

FASTA40646,154
        10         20         30         40         50         60 
MSASQDSRSR DNGPDGMEPE GVIESNWNEI VDSFDDMNLS ESLLRGIYAY GFEKPSAIQQ 

        70         80         90        100        110        120 
RAILPCIKGY DVIAQAQSGT GKTATFAISI LQQIELDLKA TQALVLAPTR ELAQQIQKVV 

       130        140        150        160        170        180 
MALGDYMGAS CHACIGGTNV RAEVQKLQME APHIIVGTPG RVFDMLNRRY LSPKYIKMFV 

       190        200        210        220        230        240 
LDEADEMLSR GFKDQIYDIF QKLNSNTQVV LLSATMPSDV LEVTKKFMRD PIRILVKKEE 

       250        260        270        280        290        300 
LTLEGIRQFY INVEREEWKL DTLCDLYETL TITQAVIFIN TRRKVDWLTE KMHARDFTVS 

       310        320        330        340        350        360 
AMHGDMDQKE RDVIMREFRS GSSRVLITTD LLARGIDVQQ VSLVINYDLP TNRENYIHRI 

       370        380        390        400 
GRGGRFGRKG VAINMVTEED KRTLRDIETF YNTSIEEMPL NVADLI 

« Hide

Isoform 2 [UniParc].

Checksum: 4ACB22D62DCA8BD0
Show »

FASTA34739,548

References

« Hide 'large scale' references
[1]"Nucleotide sequence of human cDNA encoding eukaryotic initiation factor 4AI."
Kim N.-S., Kato T., Abe N., Kato S.
Nucleic Acids Res. 21:2012-2012(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Heart.
[4]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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] (ISOFORMS 1 AND 2).
Tissue: Bone marrow and Lung.
[7]"Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation."
Craig A.W.B., Haghighat A., Yu A.T.K., Sonenberg N.
Nature 392:520-523(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PAIP1.
[8]"Novel Upf2p orthologues suggest a functional link between translation initiation and nonsense surveillance complexes."
Mendell J.T., Medghalchi S.M., Lake R.G., Noensie E.N., Dietz H.C.
Mol. Cell. Biol. 20:8944-8957(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UPF2.
[9]"Eukaryotic initiation factors 4A (eIF4A) and 4G (eIF4G) mutually interact in a 1:1 ratio in vivo."
Li W., Belsham G.J., Proud C.G.
J. Biol. Chem. 276:29111-29115(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EIF4E.
[10]"Exportin 7 defines a novel general nuclear export pathway."
Mingot J.-M., Bohnsack M.T., Jaekle U., Goerlich D.
EMBO J. 23:3227-3236(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH XPO7; ARHGAP1; VPS26A; VPS29; VPS35 AND SFN.
[11]"Identification of NOM1, a nucleolar, eIF4A binding protein encoded within the chromosome 7q36 breakpoint region targeted in cases of pediatric acute myeloid leukemia."
Simmons H.M., Ruis B.L., Kapoor M., Hudacek A.W., Conklin K.F.
Gene 347:137-145(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE INTERACTION WITH NOM1.
[12]"Cell stress modulates the function of splicing regulatory protein RBM4 in translation control."
Lin J.C., Hsu M., Tarn W.Y.
Proc. Natl. Acad. Sci. U.S.A. 104:2235-2240(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RBM4.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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-118 AND LYS-174, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Human cytomegalovirus UL69 protein facilitates translation by associating with the mRNA cap-binding complex and excluding 4EBP1."
Aoyagi M., Gaspar M., Shenk T.E.
Proc. Natl. Acad. Sci. U.S.A. 107:2640-2645(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HHV-5 PROTEIN UL69.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[18]"Structural basis for translational inhibition by the tumour suppressor Pdcd4."
Loh P.G., Yang H.S., Walsh M.A., Wang Q., Wang X., Cheng Z., Liu D., Song H.
EMBO J. 28:274-285(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) IN COMPLEX WITH PDCD4, FUNCTION, SUBUNIT, ENZYME REGULATION.
[19]"Crystal structure of the eIF4A-PDCD4 complex."
Chang J.H., Cho Y.H., Sohn S.Y., Choi J.M., Kim A., Kim Y.C., Jang S.K., Cho Y.
Proc. Natl. Acad. Sci. U.S.A. 106:3148-3153(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 20-406 IN COMPLEX WITH PDCD4, FUNCTION, ENZYME REGULATION, SUBUNIT.
[20]"Comparative structural analysis of human DEAD-box RNA helicases."
Schutz P., Karlberg T., van den Berg S., Collins R., Lehtio L., Hogbom M., Holmberg-Schiavone L., Tempel W., Park H.W., Hammarstrom M., Moche M., Thorsell A.G., Schuler H.
PLoS ONE 5:E12791-E12791(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 20-236.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D13748 mRNA. Translation: BAA02897.1.
BT019880 mRNA. Translation: AAV38683.1.
BT019881 mRNA. Translation: AAV38684.1.
AK312630 mRNA. Translation: BAG35515.1.
AC016876 Genomic DNA. No translation available.
CH471108 Genomic DNA. Translation: EAW90167.1.
CH471108 Genomic DNA. Translation: EAW90168.1.
CH471108 Genomic DNA. Translation: EAW90169.1.
BC006210 mRNA. No translation available.
BC009585 mRNA. Translation: AAH09585.1.
BC073752 mRNA. Translation: AAH73752.1.
CCDSCCDS11113.1. [P60842-1]
CCDS58511.1. [P60842-2]
PIRS33681.
RefSeqNP_001191439.1. NM_001204510.1. [P60842-2]
NP_001407.1. NM_001416.3. [P60842-1]
UniGeneHs.129673.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2G9NX-ray2.25A/B20-238[»]
2ZU6X-ray2.80A/C/D/F20-406[»]
3EIQX-ray3.50A/D1-406[»]
ProteinModelPortalP60842.
SMRP60842. Positions 22-400.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108289. 74 interactions.
DIPDIP-29755N.
IntActP60842. 41 interactions.
MINTMINT-5001111.
STRING9606.ENSP00000293831.

Chemistry

ChEMBLCHEMBL2052028.

PTM databases

PhosphoSiteP60842.

Polymorphism databases

DMDM46397463.

Proteomic databases

MaxQBP60842.
PaxDbP60842.
PRIDEP60842.

Protocols and materials databases

DNASU1973.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000293831; ENSP00000293831; ENSG00000161960. [P60842-1]
ENST00000577269; ENSP00000463486; ENSG00000161960. [P60842-2]
GeneID1973.
KEGGhsa:1973.
UCSCuc002gho.2. human. [P60842-1]

Organism-specific databases

CTD1973.
GeneCardsGC17P007476.
HGNCHGNC:3282. EIF4A1.
HPACAB011689.
MIM602641. gene.
neXtProtNX_P60842.
PharmGKBPA27710.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0513.
HOGENOMHOG000268797.
HOVERGENHBG107989.
KOK03257.
OMAWIADESG.
PhylomeDBP60842.
TreeFamTF101524.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_21257. Metabolism of RNA.
REACT_6900. Immune System.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP60842.
BgeeP60842.
CleanExHS_EIF4A1.
GenevestigatorP60842.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
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]
PfamPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEIF4A1. human.
EvolutionaryTraceP60842.
GeneWikiEIF4A1.
GenomeRNAi1973.
NextBio35536557.
PROP60842.
SOURCESearch...

Entry information

Entry nameIF4A1_HUMAN
AccessionPrimary (citable) accession number: P60842
Secondary accession number(s): B2R6L8 expand/collapse secondary AC list , D3DTP9, J3QLC4, P04765, Q5U018, Q61516
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: April 13, 2004
Last modified: July 9, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Translation initiation factors

List of translation initiation factor entries

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM