P38919 (IF4A3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Eukaryotic initiation factor 4A-III
Short name=eIF-4A-III
Short name=eIF4A-III
EC=3.6.4.13

Alternative name(s):
ATP-dependent RNA helicase DDX48
ATP-dependent RNA helicase eIF4A-3
DEAD box protein 48
Eukaryotic initiation factor 4A-like NUK-34
Eukaryotic translation initiation factor 4A isoform 3
Nuclear matrix protein 265
Short name=NMP 265
Short name=hNMP 265

Gene names

Name:	EIF4A3
Synonyms:	DDX48, KIAA0111

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	411 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. Component of a splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of a few core proteins and several more peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Core components of the EJC, that remains bound to spliced mRNAs throughout all stages of mRNA metabolism, functions to mark the position of the exon-exon junction in the mature mRNA and thereby influences downstream processes of gene expression including mRNA splicing, nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Constitutes at least part of the platform anchoring other EJC proteins to spliced mRNAs. Its RNA-dependent ATPase and RNA-helicase activities are induced by CASC3, but abolished in presence of the MAGOH/RBM8A heterodimer, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The inhibition of ATPase activity by the MAGOH/RBM8A heterodimer increases the RNA-binding affinity of the EJC. Involved in translational enhancement of spliced mRNAs after formation of the 80S ribosome complex. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Shows higher affinity for single-stranded RNA in an ATP-bound core EJC complex than after the ATP is hydrolyzed. Ref.12 Ref.15 Ref.16 Ref.20 Ref.24
Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	Part of the EJC core complex that contains CASC3, EIF4A3, MAGOH and RBM8A. Found in a mRNA splicing-dependent exon junction complex (EJC), at least composed of ACIN1, CASC3, EIF4A3, MAGOH, PNN, RBM8A, RNPS1, SAP18 and ALYREF/THOC4. Interacts with CASC3, MAGOH, NXF1, RBM8A and ALYREF/THOC4. Identified in the spliceosome C complex. May interact with NOM1. Interacts with POLDIP3. Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.19 Ref.21
Subcellular location	Nucleus. Nucleus speckle. Cytoplasm. Note: Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Detected in dendritic layer as well as the nuclear and cytoplasmic (somatic) compartments of neurons. Colocalizes with STAU1 and FMR1 in dendrites By similarity. Ref.10 Ref.13
Tissue specificity	Ubiquitously expressed. Ref.10
Sequence similarities	Belongs to the DEAD box helicase family. eIF4A subfamily. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain.
Sequence caution	The sequence BAA04879.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Nonsense-mediated mRNA decay Translation regulation Transport mRNA processing mRNA splicing mRNA transport rRNA processing
Cellular component	Cytoplasm Nucleus Spliceosome
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Helicase Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cytokine-mediated signaling pathway Traceable author statement. Source: Reactome mRNA splicing, via spliceosome Inferred by curator Ref.11. Source: UniProtKB mRNA transport Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of translation Inferred from direct assay PubMed 10523622. Source: HGNC nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Inferred from mutant phenotype Ref.15. Source: UniProtKB nuclear-transcribed mRNA poly(A) tail shortening Traceable author statement. Source: Reactome positive regulation of mRNA splicing, via spliceosome Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara positive regulation of translation Inferred from mutant phenotype Ref.21. Source: UniProtKB rRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	catalytic step 2 spliceosome Inferred from direct assay Ref.11. Source: UniProtKB cytosol Traceable author statement. Source: Reactome exon-exon junction complex Inferred from direct assay PubMed 16601204. Source: UniProtKB nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from direct assay PubMed 10523622. Source: HGNC ATP-dependent RNA helicase activity Inferred from direct assay PubMed 10523622. Source: HGNC poly(A) RNA binding Inferred from direct assay PubMed 10523622. Source: HGNC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CASC3	O15234	7	EBI-299104,EBI-299118
MAGOH	P61326	20	EBI-299104,EBI-299134
RBM8A	Q9Y5S9	21	EBI-299104,EBI-447231
THRAP3	Q9Y2W1	2	EBI-299104,EBI-352039
UPF3B	Q9BZI7	7	EBI-299104,EBI-372780

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8

Chain

2 – 411

410

Eukaryotic initiation factor 4A-III

PRO_0000054942

Regions

Domain

69 – 239

171

Helicase ATP-binding

Domain

250 – 411

162

Helicase C-terminal

Nucleotide binding

85 – 90

6

ATP

Nucleotide binding

367 – 371

5

ATP

Motif

38 – 66

29

Q motif

Motif

187 – 190

4

DEAD box

Sites

Binding site

60

1

ATP; via carbonyl oxygen

Binding site

65

1

ATP

Binding site

342

1

ATP

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.8 Ref.25 Ref.27 Ref.29

Modified residue

12

1

Phosphoserine Ref.27 Ref.29

Modified residue

163

1

Phosphothreonine Ref.23 Ref.27

Modified residue

296

1

N6-acetyllysine Ref.26

Modified residue

321

1

N6-acetyllysine Ref.26

Experimental info

Mutagenesis

88

1

K → A: ATPase activity is not induced in presence of CASC3. Does not prevent EJC formation. Prevents the EJC disassembly. Ref.16

Sequence conflict

210

1

P → S in CAA56074. Ref.1

Sequence conflict

370

1

R → Q in CAA56074. Ref.1

Secondary structure

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411

Helix Strand Turn

Details...

Beta strand

23 – 25

3

Helix

40 – 43

4

Helix

47 – 56

10

Helix

63 – 73

11

Beta strand

78 – 81

4

Beta strand

84 – 86

3

Helix

88 – 98

11

Beta strand

109 – 112

4

Helix

116 – 129

14

Turn

130 – 134

5

Beta strand

137 – 140

4

Beta strand

143 – 145

3

Helix

146 – 155

10

Beta strand

158 – 162

5

Helix

164 – 172

9

Beta strand

183 – 187

5

Helix

189 – 192

4

Turn

195 – 197

3

Helix

198 – 205

8

Beta strand

213 – 219

7

Helix

223 – 226

4

Helix

229 – 231

3

Beta strand

237 – 239

3

Helix

243 – 245

3

Beta strand

251 – 260

10

Helix

263 – 275

13

Beta strand

277 – 283

7

Helix

287 – 299

13

Beta strand

305 – 307

3

Helix

313 – 324

12

Beta strand

330 – 333

4

Helix

335 – 337

3

Beta strand

338 – 340

3

Beta strand

346 – 353

8

Helix

358 – 365

8

Helix

370 – 372

3

Beta strand

375 – 382

8

Helix

383 – 385

3

Helix

386 – 395

10

Beta strand

400 – 402

3

Helix

408 – 411

4

Sequences

	Sequence		Length	Mass (Da)
	P38919 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 3A21888CA96CA5EA	FASTA	411	46,871
	10 20 30 40 50 60 MATTATMATS GSARKRLLKE EDMTKVEFET SEEVDVTPTF DTMGLREDLL RGIYAYGFEK 70 80 90 100 110 120 PSAIQQRAIK QIIKGRDVIA QSQSGTGKTA TFSISVLQCL DIQVRETQAL ILAPTRELAV 130 140 150 160 170 180 QIQKGLLALG DYMNVQCHAC IGGTNVGEDI RKLDYGQHVV AGTPGRVFDM IRRRSLRTRA 190 200 210 220 230 240 IKMLVLDEAD EMLNKGFKEQ IYDVYRYLPP ATQVVLISAT LPHEILEMTN KFMTDPIRIL 250 260 270 280 290 300 VKRDELTLEG IKQFFVAVER EEWKFDTLCD LYDTLTITQA VIFCNTKRKV DWLTEKMREA 310 320 330 340 350 360 NFTVSSMHGD MPQKERESIM KEFRSGASRV LISTDVWARG LDVPQVSLII NYDLPNNREL 370 380 390 400 410 YIHRIGRSGR YGRKGVAINF VKNDDIRILR DIEQYYSTQI DEMPMNVADL I

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of a putative human translation initiation factor with similarity to initiation factor 4AII." Leffers H., Wiemann S., Ansorge W. Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Skin.
[2]	"Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1." Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N. DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Bone marrow.
[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]. Tissue: Heart.
[4]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"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].
[6]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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]. Tissue: Lymph, Placenta and Skin.
[8]	Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M. Submitted (MAY-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-14, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: T-cell.
[9]	Lubec G., Vishwanath V. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 340-358, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[10]	"A human common nuclear matrix protein homologous to eukaryotic translation initiation factor 4A." Holzmann K., Gerner C., Poeltl A., Schaefer R., Obrist P., Ensinger C., Grimm R., Sauermann G. Biochem. Biophys. Res. Commun. 267:339-344(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Leukocyte.
[11]	"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis." Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J. RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[12]	"eIF4AIII binds spliced mRNA in the exon junction complex and is essential for nonsense-mediated decay." Shibuya T., Tange T.O., Sonenberg N., Moore M.J. Nat. Struct. Mol. Biol. 11:346-351(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN MRNA SPLICING AND NONSENSE-MEDIATED MRNA DECAY, INTERACTION WITH MAGOH AND RBM8A, RNA-BINDING.
[13]	"eIF4A3 is a novel component of the exon junction complex." Chan C.C., Dostie J., Diem M.D., Feng W., Mann M., Rappsilber J., Dreyfuss G. RNA 10:200-209(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE EXON JUNCTION COMPLEX, INTERACTION WITH NXF1 AND ALYREF/THOC4, RNA-BINDING, SUBCELLULAR LOCATION.
[14]	"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.
[15]	"Exon-junction complex components specify distinct routes of nonsense-mediated mRNA decay with differential cofactor requirements." Gehring N.H., Kunz J.B., Neu-Yilik G., Breit S., Viegas M.H., Hentze M.W., Kulozik A.E. Mol. Cell 20:65-75(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[16]	"The exon junction core complex is locked onto RNA by inhibition of eIF4AIII ATPase activity." Ballut L., Marchadier B., Baguet A., Tomasetto C., Seraphin B., Le Hir H. Nat. Struct. Mol. Biol. 12:861-869(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE CORE EXON JUNCTION COMPLEX, INTERACTION WITH CASC3, MUTAGENESIS OF LYS-88, RNA-BINDING.
[17]	"Biochemical analysis of the EJC reveals two new factors and a stable tetrameric protein core." Tange T.O., Shibuya T., Jurica M.S., Moore M.J. RNA 11:1869-1883(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE CORE EXON JUNCTION COMPLEX, IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX, MASS SPECTROMETRY.
[18]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[19]	"Mutational analysis of human eIF4AIII identifies regions necessary for exon junction complex formation and nonsense-mediated mRNA decay." Shibuya T., Tange T.O., Stroupe M.E., Moore M.J. RNA 12:360-374(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CASC3 AND MAGOH, MUTAGENESIS.
[20]	"MLN51 stimulates the RNA-helicase activity of eIF4AIII." Noble C.G., Song H. PLoS ONE 2:E303-E303(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN ATPASE AND RNA-HELICASE ACTIVITY.
[21]	"SKAR links pre-mRNA splicing to mTOR/S6K1-mediated enhanced translation efficiency of spliced mRNAs." Ma X.M., Yoon S.O., Richardson C.J., Julich K., Blenis J. Cell 133:303-313(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH POLDIP3.
[22]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[23]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-163, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[24]	"Exon junction complex enhances translation of spliced mRNAs at multiple steps." Lee H.C., Choe J., Chi S.G., Kim Y.K. Biochem. Biophys. Res. Commun. 384:334-340(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN MRNA TRANSLATION.
[25]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY.
[26]	"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-296 AND LYS-321, MASS SPECTROMETRY.
[27]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND THR-163, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[28]	"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].
[29]	"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 ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, MASS SPECTROMETRY.
[30]	"The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA." Bono F., Ebert J., Lorentzen E., Conti E. Cell 126:713-725(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 2-411 IN THE EJC COMPLEX WITH CASC3; MAGOH; RBM8A; AMP-PNP AND POLY URACIL.
[31]	"Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA." Andersen C.B., Ballut L., Johansen J.S., Chamieh H., Nielsen K.H., Oliveira C.L., Pedersen J.S., Seraphin B., Le Hir H., Andersen G.R. Science 313:1968-1972(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN THE EJC COMPLEX WITH CASC3; MAGOH; RBM8A; ADP-NP AND POLY URACIL.
[32]	"Mechanism of ATP turnover inhibition in the EJC." Nielsen K.H., Chamieh H., Andersen C.B., Fredslund F., Hamborg K., Le Hir H., Andersen G.R. RNA 15:67-75(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN THE EJC COMPLEX WITH CASC3; MAGOH; RBM8A; TRANSITION STATE ANALOG ADP-ALF3 AND POLY URACIL.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X79538 mRNA. Translation: CAA56074.1.
D21853 mRNA. Translation: BAA04879.2. Different initiation.
AK290608 mRNA. Translation: BAF83297.1.
CR456750 mRNA. Translation: CAG33031.1.
AC087741 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89584.1.
BC003662 mRNA. Translation: AAH03662.1.
BC004386 mRNA. Translation: AAH04386.1.
BC011151 mRNA. Translation: AAH11151.1.

IPI

IPI00009328.

PIR

S45142.

RefSeq

NP_055555.1. NM_014740.3.

UniGene

Hs.389649.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HXY	X-ray	3.30	A/B/C/D	23-410	[»]
2HYI	X-ray	2.30	C/I	1-411	[»]
2J0Q	X-ray	3.20	A/B	2-411	[»]
2J0S	X-ray	2.21	A	2-411	[»]
2J0U	X-ray	3.00	A/B	38-411	[»]
2XB2	X-ray	3.40	A/X	1-411	[»]
3EX7	X-ray	2.30	C/H	1-411	[»]

ProteinModelPortal

P38919.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33218N.

IntAct

P38919. 128 interactions.

MINT

MINT-1460615.

STRING

9606.ENSP00000269349.

Protein family/group databases

TCDB

3.A.18.1.1. nuclear mRNA exporter (mRNA-E) family.

PTM databases

PhosphoSite

P38919.

Polymorphism databases

DMDM

20532400.

2D gel databases

REPRODUCTION-2DPAGE

IPI00009328.

Proteomic databases

PaxDb

P38919.

PeptideAtlas

P38919.

PRIDE

P38919.

Protocols and materials databases

DNASU

9775.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000269349; ENSP00000269349; ENSG00000141543.

GeneID

9775.

KEGG

hsa:9775.

UCSC

uc002jxs.3. human.

Organism-specific databases

CTD

9775.

GeneCards

GC17M078109.

HGNC

HGNC:18683. EIF4A3.

HPA

HPA021878.

MIM

608546. gene.

neXtProt

NX_P38919.

PharmGKB

PA162384945.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0513.

HOGENOM

HOG000268797.

HOVERGEN

HBG107989.

InParanoid

P38919.

KO

K13025.

OMA

EDWKFDT.

OrthoDB

EOG4229JV.

PhylomeDB

P38919.

Enzyme and pathway databases

Reactome

REACT_21257. Metabolism of RNA.
REACT_6900. Immune System.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P38919.

Bgee

P38919.

CleanEx

HS_EIF4A3.

Genevestigator

P38919.

GermOnline

ENSG00000141543. Homo sapiens.

Family and domain databases

InterPro

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]

Pfam

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

SMART

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

SUPFAM

SSF52540. SSF52540. 2 hits.

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

EIF4A3. human.

EvolutionaryTrace

P38919.

GenomeRNAi

9775.

NextBio

36802.

SOURCE

Search...

Entry information

Entry name

IF4A3_HUMAN

Accession

Primary (citable) accession number: P38919
Secondary accession number(s): Q15033, Q6IBQ2, Q96A18

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 157 of the entry and version 4 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.