P60842 (IF4A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	406 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Host-virus interaction Protein biosynthesis
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Helicase Hydrolase Initiation factor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cytokine-mediated signaling pathway Traceable author statement. Source: Reactome nuclear-transcribed mRNA poly(A) tail shortening Traceable author statement. Source: Reactome translational initiation Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Traceable author statement. Source: Reactome eukaryotic translation initiation factor 4F complex Traceable author statement PubMed 9168945. Source: UniProtKB
Molecular_function	ATP 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 helicase activity Traceable author statement PubMed 3215517. Source: UniProtKB mRNA binding Traceable author statement PubMed 3215517. 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

With	Entry	#Exp.	IntAct	Notes
EIF4G1	Q04637	7	EBI-73449,EBI-73711
EIF4G2	P78344	2	EBI-73449,EBI-296519
EIF4H	Q15056	2	EBI-73449,EBI-748492

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.17

Chain

2 – 406

405

Eukaryotic initiation factor 4A-I

PRO_0000054933

Regions

Domain

63 – 234

172

Helicase ATP-binding

Domain

245 – 406

162

Helicase C-terminal

Nucleotide binding

76 – 83

8

ATP By similarity

Motif

32 – 60

29

Q motif

Motif

182 – 185

4

DEAD box

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.17

Modified residue

4

1

Phosphoserine Ref.17

Modified residue

118

1

N6-acetyllysine Ref.14

Modified residue

174

1

N6-acetyllysine Ref.14

Natural variations

Alternative sequence

333 – 406

74

ARGID…VADLI → GKLYPQNRSRWTVWP in isoform 2.

VSP_046032

Secondary structure

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406

Helix Strand Turn

Details...

Beta strand

23 – 25

3

Helix

34 – 36

3

Helix

41 – 50

10

Helix

57 – 68

12

Beta strand

72 – 75

4

Helix

82 – 93

12

Beta strand

103 – 106

4

Helix

110 – 124

15

Turn

125 – 128

4

Beta strand

131 – 134

4

Turn

143 – 145

3

Beta strand

146 – 149

4

Beta strand

153 – 157

5

Helix

159 – 167

9

Beta strand

178 – 183

6

Helix

184 – 189

6

Turn

190 – 192

3

Helix

193 – 202

10

Beta strand

208 – 214

7

Helix

218 – 227

10

Beta strand

232 – 235

4

Beta strand

241 – 243

3

Beta strand

246 – 251

6

Helix

256 – 269

14

Beta strand

273 – 278

6

Helix

282 – 290

9

Turn

291 – 296

6

Beta strand

300 – 302

3

Helix

312 – 316

5

Helix

318 – 320

3

Beta strand

321 – 323

3

Beta strand

325 – 328

4

Helix

330 – 333

4

Helix

338 – 340

3

Beta strand

342 – 348

7

Helix

355 – 360

6

Turn

364 – 366

3

Beta strand

370 – 375

6

Helix

378 – 391

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 13, 2004. Version 1. Checksum: 6EF89939F3045420	FASTA	406	46,154
	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
	Isoform 2 [UniParc]. Checksum: 4ACB22D62DCA8BD0	FASTA	347	39,548
	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 AMHGDMDQKE RDVIMREFRS GSSRVLITTD LLGKLYPQNR SRWTVWP

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE.
[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.

IPI

IPI00025491.

PIR

S33681.

RefSeq

NP_001191439.1. NM_001204510.1.
NP_001407.1. NM_001416.3.

UniGene

Hs.129673.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2G9N	X-ray	2.25	A/B	20-236	[»]
2ZU6	X-ray	2.80	A/C/D/F	20-406	[»]
3EIQ	X-ray	3.50	A/D	1-406	[»]

ProteinModelPortal

P60842.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29755N.

IntAct

P60842. 34 interactions.

MINT

MINT-5001111.

STRING

9606.ENSP00000293831.

PTM databases

PhosphoSite

P60842.

Polymorphism databases

DMDM

46397463.

Proteomic databases

PaxDb

P60842.

PRIDE

P60842.

Protocols and materials databases

DNASU

1973.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000293831; ENSP00000293831; ENSG00000161960.
ENST00000577269; ENSP00000463486; ENSG00000161960.

GeneID

1973.

KEGG

hsa:1973.

UCSC

uc002gho.2. human.

Organism-specific databases

CTD

1973.

GeneCards

GC17P007476.

HGNC

HGNC:3282. EIF4A1.

HPA

CAB011689.

MIM

602641. gene.

neXtProt

NX_P60842.

PharmGKB

PA27710.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0513.

HOGENOM

HOG000268797.

HOVERGEN

HBG107989.

KO

K03257.

OMA

IKMFILD.

OrthoDB

EOG4640C1.

PhylomeDB

P60842.

Enzyme and pathway databases

Pathway_Interaction_DB

mtor_4pathway. mTOR signaling pathway.

Reactome

REACT_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

ArrayExpress

P60842.

Bgee

P60842.

CleanEx

HS_EIF4A1.

Genevestigator

P60842.

GermOnline

ENSG00000161960. Homo sapiens.

Family and domain databases

InterPro

IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]

Pfam

PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]

SMART

SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]

PROSITE

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]

ProtoNet

Search...

Other

ChiTaRS

EIF4A1. human.

EvolutionaryTrace

P60842.

GenomeRNAi

1973.

NextBio

35536557.

SOURCE

Search...

Entry information

Entry name

IF4A1_HUMAN

Accession

Primary (citable) accession number: P60842
Secondary accession number(s): B2R6L8 , D3DTP9, J3QLC4, P04765, Q5U018, Q61516

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	April 13, 2004
Last modified:	May 1, 2013
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.