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P60842

- IF4A1_HUMAN

UniProt

P60842 - IF4A1_HUMAN

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Protein
Eukaryotic initiation factor 4A-I
Gene
EIF4A1, DDX2A, EIF4A
Organism
Homo sapiens (Human)
Status
Reviewed - 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.2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Enzyme regulationi

Helicase activity and function in translation are inhibited by interaction with PDCD4.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi76 – 838ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATP-dependent helicase activity Source: InterPro
  3. RNA cap binding Source: UniProtKB
  4. double-stranded RNA binding Source: MGI
  5. helicase activity Source: UniProtKB
  6. mRNA binding Source: UniProtKB
  7. poly(A) RNA binding Source: UniProtKB
  8. protein binding Source: UniProtKB
  9. translation factor activity, nucleic acid binding Source: UniProtKB
  10. translation initiation factor activity Source: UniProtKB-KW

GO - Biological processi

  1. RNA metabolic process Source: Reactome
  2. cellular protein metabolic process Source: Reactome
  3. cytokine-mediated signaling pathway Source: Reactome
  4. gene expression Source: Reactome
  5. mRNA metabolic process Source: Reactome
  6. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
  7. nuclear-transcribed mRNA poly(A) tail shortening Source: Reactome
  8. organ regeneration Source: Ensembl
  9. translation Source: Reactome
  10. translational initiation Source: Reactome
  11. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Initiation factor

Keywords - Biological processi

Host-virus interaction, Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

ReactomeiREACT_115831. ISG15 antiviral mechanism.
REACT_1258. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
REACT_1979. Translation initiation complex formation.
REACT_20514. Deadenylation of mRNA.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:3282. EIF4A1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. eukaryotic translation initiation factor 4F complex Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27710.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 406405Eukaryotic initiation factor 4A-I
PRO_0000054933Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei4 – 41Phosphoserine1 Publication
Modified residuei118 – 1181N6-acetyllysine1 Publication
Modified residuei174 – 1741N6-acetyllysine1 Publication
Modified residuei193 – 1931N6-acetyllysine By similarity
Modified residuei238 – 2381N6-acetyllysine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP60842.
PaxDbiP60842.
PRIDEiP60842.

PTM databases

PhosphoSiteiP60842.

Expressioni

Gene expression databases

ArrayExpressiP60842.
BgeeiP60842.
CleanExiHS_EIF4A1.
GenevestigatoriP60842.

Organism-specific databases

HPAiCAB011689.

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. Interacts with human cytomegalovirus/HHV-5 protein UL69.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EIF4G1Q046377EBI-73449,EBI-73711
EIF4G2P783443EBI-73449,EBI-296519
EIF4HQ150562EBI-73449,EBI-748492

Protein-protein interaction databases

BioGridi108289. 75 interactions.
DIPiDIP-29755N.
IntActiP60842. 41 interactions.
MINTiMINT-5001111.
STRINGi9606.ENSP00000293831.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 253
Helixi34 – 363
Helixi41 – 5010
Helixi57 – 6812
Beta strandi72 – 754
Helixi82 – 9312
Beta strandi103 – 1064
Helixi110 – 12415
Turni125 – 1284
Beta strandi131 – 1344
Turni143 – 1453
Beta strandi146 – 1494
Beta strandi153 – 1575
Helixi159 – 1679
Beta strandi178 – 1836
Helixi184 – 1896
Turni190 – 1923
Helixi193 – 20210
Beta strandi208 – 2147
Helixi218 – 22710
Beta strandi232 – 2354
Beta strandi241 – 2433
Beta strandi246 – 2516
Helixi256 – 26914
Beta strandi273 – 2786
Helixi282 – 2909
Turni291 – 2966
Beta strandi300 – 3023
Helixi312 – 3165
Helixi318 – 3203
Beta strandi321 – 3233
Beta strandi325 – 3284
Helixi330 – 3334
Helixi338 – 3403
Beta strandi342 – 3487
Helixi355 – 3606
Turni364 – 3663
Beta strandi370 – 3756
Helixi378 – 39114

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2G9NX-ray2.25A/B20-238[»]
2ZU6X-ray2.80A/C/D/F20-406[»]
3EIQX-ray3.50A/D1-406[»]
ProteinModelPortaliP60842.
SMRiP60842. Positions 22-400.

Miscellaneous databases

EvolutionaryTraceiP60842.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini63 – 234172Helicase ATP-binding
Add
BLAST
Domaini245 – 406162Helicase C-terminal
Add
BLAST

Motif

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0513.
HOGENOMiHOG000268797.
HOVERGENiHBG107989.
KOiK03257.
OMAiWIADESG.
PhylomeDBiP60842.
TreeFamiTF101524.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. 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]
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P60842-1) [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

MSASQDSRSR DNGPDGMEPE GVIESNWNEI VDSFDDMNLS ESLLRGIYAY    50
GFEKPSAIQQ RAILPCIKGY DVIAQAQSGT GKTATFAISI LQQIELDLKA 100
TQALVLAPTR ELAQQIQKVV MALGDYMGAS CHACIGGTNV RAEVQKLQME 150
APHIIVGTPG RVFDMLNRRY LSPKYIKMFV LDEADEMLSR GFKDQIYDIF 200
QKLNSNTQVV LLSATMPSDV LEVTKKFMRD PIRILVKKEE LTLEGIRQFY 250
INVEREEWKL DTLCDLYETL TITQAVIFIN TRRKVDWLTE KMHARDFTVS 300
AMHGDMDQKE RDVIMREFRS GSSRVLITTD LLARGIDVQQ VSLVINYDLP 350
TNRENYIHRI GRGGRFGRKG VAINMVTEED KRTLRDIETF YNTSIEEMPL 400
NVADLI 406
Length:406
Mass (Da):46,154
Last modified:April 13, 2004 - v1
Checksum:i6EF89939F3045420
GO
Isoform 2 (identifier: P60842-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     333-406: ARGIDVQQVS...EMPLNVADLI → GKLYPQNRSRWTVWP

Note: No experimental confirmation available.

Show »
Length:347
Mass (Da):39,548
Checksum:i4ACB22D62DCA8BD0
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei333 – 40674ARGID…VADLI → GKLYPQNRSRWTVWP in isoform 2.
VSP_046032Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS11113.1. [P60842-1]
CCDS58511.1. [P60842-2]
PIRiS33681.
RefSeqiNP_001191439.1. NM_001204510.1. [P60842-2]
NP_001407.1. NM_001416.3. [P60842-1]
UniGeneiHs.129673.

Genome annotation databases

EnsembliENST00000293831; ENSP00000293831; ENSG00000161960. [P60842-1]
ENST00000577269; ENSP00000463486; ENSG00000161960. [P60842-2]
GeneIDi1973.
KEGGihsa:1973.
UCSCiuc002gho.2. human. [P60842-1]
uc002ghr.1. human.

Polymorphism databases

DMDMi46397463.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS11113.1. [P60842-1 ]
CCDS58511.1. [P60842-2 ]
PIRi S33681.
RefSeqi NP_001191439.1. NM_001204510.1. [P60842-2 ]
NP_001407.1. NM_001416.3. [P60842-1 ]
UniGenei Hs.129673.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2G9N X-ray 2.25 A/B 20-238 [» ]
2ZU6 X-ray 2.80 A/C/D/F 20-406 [» ]
3EIQ X-ray 3.50 A/D 1-406 [» ]
ProteinModelPortali P60842.
SMRi P60842. Positions 22-400.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108289. 75 interactions.
DIPi DIP-29755N.
IntActi P60842. 41 interactions.
MINTi MINT-5001111.
STRINGi 9606.ENSP00000293831.

Chemistry

ChEMBLi CHEMBL2052028.

PTM databases

PhosphoSitei P60842.

Polymorphism databases

DMDMi 46397463.

Proteomic databases

MaxQBi P60842.
PaxDbi P60842.
PRIDEi P60842.

Protocols and materials databases

DNASUi 1973.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000293831 ; ENSP00000293831 ; ENSG00000161960 . [P60842-1 ]
ENST00000577269 ; ENSP00000463486 ; ENSG00000161960 . [P60842-2 ]
GeneIDi 1973.
KEGGi hsa:1973.
UCSCi uc002gho.2. human. [P60842-1 ]
uc002ghr.1. human.

Organism-specific databases

CTDi 1973.
GeneCardsi GC17P007476.
HGNCi HGNC:3282. EIF4A1.
HPAi CAB011689.
MIMi 602641. gene.
neXtProti NX_P60842.
PharmGKBi PA27710.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0513.
HOGENOMi HOG000268797.
HOVERGENi HBG107989.
KOi K03257.
OMAi WIADESG.
PhylomeDBi P60842.
TreeFami TF101524.

Enzyme and pathway databases

Reactomei REACT_115831. ISG15 antiviral mechanism.
REACT_1258. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
REACT_1979. Translation initiation complex formation.
REACT_20514. Deadenylation of mRNA.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.

Miscellaneous databases

ChiTaRSi EIF4A1. human.
EvolutionaryTracei P60842.
GeneWikii EIF4A1.
GenomeRNAii 1973.
NextBioi 35536557.
PROi P60842.
SOURCEi Search...

Gene expression databases

ArrayExpressi P60842.
Bgeei P60842.
CleanExi HS_EIF4A1.
Genevestigatori P60842.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR011545. 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 ]
Pfami PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view ]
SMARTi SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
PROSITEi PS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 20-406 IN COMPLEX WITH PDCD4, FUNCTION, ENZYME REGULATION, SUBUNIT.
  20. Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 20-236.

Entry informationi

Entry nameiIF4A1_HUMAN
AccessioniPrimary (citable) accession number: P60842
Secondary accession number(s): B2R6L8
, D3DTP9, J3QLC4, P04765, Q5U018, Q61516
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: April 13, 2004
Last modified: September 3, 2014
This is version 129 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 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Translation initiation factors
    List of translation initiation factor entries
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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