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Protein

Eukaryotic initiation factor 4A-III

Gene

EIF4A3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ATP-dependent RNA helicase. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). 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. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the function is different from the established EJC assembly. Involved in craniofacial development.7 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Enzyme regulationi

The ATPase activity is increased some 4-fold in the presence of RNA.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei60ATP; via carbonyl oxygen1
Binding sitei65ATP1
Binding sitei342ATP1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi85 – 90ATP6
Nucleotide bindingi367 – 371ATP5

GO - Molecular functioni

  • ATP binding Source: HGNC
  • ATP-dependent RNA helicase activity Source: HGNC
  • mRNA binding Source: UniProtKB
  • poly(A) binding Source: HGNC
  • poly(A) RNA binding Source: UniProtKB
  • ribonucleoprotein complex binding Source: Ensembl
  • RNA stem-loop binding Source: Ensembl
  • selenocysteine insertion sequence binding Source: Ensembl

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

mRNA processing, mRNA splicing, mRNA transport, Nonsense-mediated mRNA decay, rRNA processing, Translation regulation, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000141543-MONOMER.
BRENDAi3.6.4.13. 2681.
ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-1169408. ISG15 antiviral mechanism.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-429947. Deadenylation of mRNA.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72187. mRNA 3'-end processing.
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Protein family/group databases

TCDBi3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic initiation factor 4A-III (EC:3.6.4.13)
Short name:
eIF-4A-III
Short name:
eIF4A-III
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
Cleaved into the following chain:
Gene namesi
Name:EIF4A3
Synonyms:DDX48, KIAA0111
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:18683. EIF4A3.

Subcellular locationi

  • 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).By similarity

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: UniProtKB
  • cytoplasm Source: HGNC
  • cytosol Source: Reactome
  • dendrite Source: Ensembl
  • exon-exon junction complex Source: UniProtKB
  • membrane Source: UniProtKB
  • neuronal cell body Source: Ensembl
  • nuclear speck Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

Pathology & Biotechi

Involvement in diseasei

Richieri-Costa-Pereira syndrome (RCPS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry. EIF4A3 mutations resulting in Richieri-Costa-Pereira syndrome include a repeat expansion of 18 or 20 nucleotides in the 5' untranslated region. Affected individuals have 14 to 16 repeats, while healthy individuals have 3 to 12 repeats (PubMed:24360810).1 Publication
Disease descriptionA syndrome characterized by a unique pattern of anomalies consisting of microstomia, micrognathia, abnormal fusion of mandible, cleft palate/Robin sequence, absence of central lower incisors, minor ears anomalies, hypoplastic first ray, abnormal tibiae, hypoplastic halluces, and clubfeet. Learning disability is also a common finding.
See also OMIM:268305
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_071090270D → G in RCPS. 1 PublicationCorresponds to variant rs587777204dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi88K → A: ATPase activity is not induced in presence of CASC3. Does not prevent EJC formation. Prevents the EJC disassembly. 1 Publication1
Mutagenesisi270D → K: Loss of CWC22-binding and loss of incorporation into EJCs; when associated with K-273. 1 Publication1
Mutagenesisi273D → K: Loss of CWC22-binding and loss of incorporation into EJCs; when associated with K-270. 1 Publication1
Mutagenesisi276 – 277TI → GD: Loss of CWC22-binding and loss of incorporation into EJCs. 1 Publication2
Mutagenesisi301 – 303NFT → LAG: Loss of CWC22-binding and loss of incorporation into EJCs. 1 Publication3
Mutagenesisi334T → V: Reduced incorporation into EJCs. 1 Publication1
Mutagenesisi401D → K: Loss of incorporation into EJCs; when associated with R-402. 1 Publication1
Mutagenesisi402E → R: Loss of incorporation into EJCs; when associated with K-401. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi9775.
MalaCardsiEIF4A3.
MIMi268305. phenotype.
OpenTargetsiENSG00000141543.
Orphaneti3102. Richieri Costa-Pereira syndrome.
PharmGKBiPA162384945.

Polymorphism and mutation databases

BioMutaiEIF4A3.
DMDMi20532400.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004232671 – 411Eukaryotic initiation factor 4A-IIIAdd BLAST411
Initiator methionineiRemoved; alternateCombined sources1 Publication
ChainiPRO_00000549422 – 411Eukaryotic initiation factor 4A-III, N-terminally processedAdd BLAST410

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei2N-acetylalanine; in Eukaryotic initiation factor 4A-III, N-terminally processedCombined sources1 Publication1
Modified residuei12PhosphoserineCombined sources1
Cross-linki19Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei163PhosphothreonineCombined sources1
Modified residuei296N6-acetyllysineCombined sources1
Modified residuei321N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP38919.
MaxQBiP38919.
PaxDbiP38919.
PeptideAtlasiP38919.
PRIDEiP38919.

2D gel databases

REPRODUCTION-2DPAGEIPI00009328.

PTM databases

iPTMnetiP38919.
PhosphoSitePlusiP38919.
SwissPalmiP38919.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiENSG00000141543.
CleanExiHS_EIF4A3.
ExpressionAtlasiP38919. baseline and differential.
GenevisibleiP38919. HS.

Organism-specific databases

HPAiHPA021878.

Interactioni

Subunit structurei

Part of the mRNA splicing-dependent exon junction complex (EJC) complex; the core complex contains CASC3, EIF4A3, MAGOH and RBM8A. Interacts with CASC3, MAGOH, NXF1, RBM8A and ALYREF/THOC4. Identified in the spliceosome C complex. May interact with NOM1. Interacts with POLDIP3. Interacts with CWC22 and PRPF19 in an RNA-independent manner. Direct interaction with CWC22 is mediated by the helicase C-terminal domain. Full interaction with CWC22 occurs only when EIF4A3 is not part of the EJC and prevents EIF4A3 binding to RNA. Interacts with NCBP3 (PubMed:26382858).11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CASC3O152349EBI-299104,EBI-299118
CDCA7LQ96GN53EBI-299104,EBI-5278764
CWC22Q9HCG83EBI-299104,EBI-373289
MAGOHP6132620EBI-299104,EBI-299134
NOM1Q5C9Z43EBI-299104,EBI-2685618
PDCD4Q53EL63EBI-299104,EBI-935824
RBM8AQ9Y5S921EBI-299104,EBI-447231
THRAP3Q9Y2W12EBI-299104,EBI-352039
UPF3BQ9BZI77EBI-299104,EBI-372780

Protein-protein interaction databases

BioGridi115119. 262 interactors.
DIPiDIP-33218N.
IntActiP38919. 155 interactors.
MINTiMINT-1460615.
STRINGi9606.ENSP00000269349.

Structurei

Secondary structure

1411
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi23 – 25Combined sources3
Beta strandi28 – 32Combined sources5
Helixi40 – 42Combined sources3
Helixi47 – 56Combined sources10
Helixi65 – 73Combined sources9
Beta strandi78 – 81Combined sources4
Beta strandi84 – 86Combined sources3
Helixi88 – 98Combined sources11
Beta strandi102 – 104Combined sources3
Beta strandi109 – 112Combined sources4
Helixi116 – 129Combined sources14
Turni130 – 134Combined sources5
Beta strandi137 – 139Combined sources3
Helixi143 – 145Combined sources3
Helixi146 – 155Combined sources10
Beta strandi158 – 162Combined sources5
Helixi164 – 172Combined sources9
Beta strandi183 – 186Combined sources4
Helixi189 – 195Combined sources7
Helixi198 – 206Combined sources9
Beta strandi213 – 219Combined sources7
Helixi223 – 232Combined sources10
Beta strandi237 – 241Combined sources5
Helixi243 – 245Combined sources3
Beta strandi251 – 260Combined sources10
Helixi261 – 263Combined sources3
Helixi264 – 274Combined sources11
Beta strandi278 – 283Combined sources6
Helixi287 – 299Combined sources13
Beta strandi304 – 307Combined sources4
Beta strandi309 – 311Combined sources3
Helixi313 – 324Combined sources12
Beta strandi329 – 333Combined sources5
Helixi335 – 337Combined sources3
Beta strandi338 – 340Combined sources3
Beta strandi346 – 353Combined sources8
Beta strandi356 – 358Combined sources3
Helixi360 – 365Combined sources6
Beta strandi367 – 369Combined sources3
Helixi370 – 372Combined sources3
Beta strandi375 – 382Combined sources8
Helixi383 – 385Combined sources3
Helixi386 – 396Combined sources11
Beta strandi400 – 402Combined sources3
Helixi405 – 410Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HXYX-ray3.30A/B/C/D23-411[»]
2HYIX-ray2.30C/I1-411[»]
2J0QX-ray3.20A/B2-411[»]
2J0SX-ray2.21A2-411[»]
2J0UX-ray3.00A/B38-411[»]
2XB2X-ray3.40A/X1-411[»]
3EX7X-ray2.30C/H1-411[»]
4C9BX-ray2.00A1-411[»]
ProteinModelPortaliP38919.
SMRiP38919.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38919.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini69 – 239Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST171
Domaini250 – 411Helicase C-terminalPROSITE-ProRule annotationAdd BLAST162

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi38 – 66Q motifAdd BLAST29
Motifi187 – 190DEAD box4

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.
GeneTreeiENSGT00530000062880.
HOGENOMiHOG000268797.
HOVERGENiHBG107989.
InParanoidiP38919.
KOiK13025.
OMAiTATFCIS.
OrthoDBiEOG091G07OI.
PhylomeDBiP38919.
TreeFamiTF300466.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
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]

Sequencei

Sequence statusi: Complete.

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

P38919-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATTATMATS GSARKRLLKE EDMTKVEFET SEEVDVTPTF DTMGLREDLL
60 70 80 90 100
RGIYAYGFEK PSAIQQRAIK QIIKGRDVIA QSQSGTGKTA TFSISVLQCL
110 120 130 140 150
DIQVRETQAL ILAPTRELAV QIQKGLLALG DYMNVQCHAC IGGTNVGEDI
160 170 180 190 200
RKLDYGQHVV AGTPGRVFDM IRRRSLRTRA IKMLVLDEAD EMLNKGFKEQ
210 220 230 240 250
IYDVYRYLPP ATQVVLISAT LPHEILEMTN KFMTDPIRIL VKRDELTLEG
260 270 280 290 300
IKQFFVAVER EEWKFDTLCD LYDTLTITQA VIFCNTKRKV DWLTEKMREA
310 320 330 340 350
NFTVSSMHGD MPQKERESIM KEFRSGASRV LISTDVWARG LDVPQVSLII
360 370 380 390 400
NYDLPNNREL YIHRIGRSGR YGRKGVAINF VKNDDIRILR DIEQYYSTQI
410
DEMPMNVADL I
Length:411
Mass (Da):46,871
Last modified:January 23, 2007 - v4
Checksum:i3A21888CA96CA5EA
GO

Sequence cautioni

The sequence BAA04879 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti210P → S in CAA56074 (Ref. 1) Curated1
Sequence conflicti370R → Q in CAA56074 (Ref. 1) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_071090270D → G in RCPS. 1 PublicationCorresponds to variant rs587777204dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11767.1.
PIRiS45142.
RefSeqiNP_055555.1. NM_014740.3.
UniGeneiHs.389649.

Genome annotation databases

EnsembliENST00000269349; ENSP00000269349; ENSG00000141543.
GeneIDi9775.
KEGGihsa:9775.
UCSCiuc002jxs.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11767.1.
PIRiS45142.
RefSeqiNP_055555.1. NM_014740.3.
UniGeneiHs.389649.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HXYX-ray3.30A/B/C/D23-411[»]
2HYIX-ray2.30C/I1-411[»]
2J0QX-ray3.20A/B2-411[»]
2J0SX-ray2.21A2-411[»]
2J0UX-ray3.00A/B38-411[»]
2XB2X-ray3.40A/X1-411[»]
3EX7X-ray2.30C/H1-411[»]
4C9BX-ray2.00A1-411[»]
ProteinModelPortaliP38919.
SMRiP38919.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115119. 262 interactors.
DIPiDIP-33218N.
IntActiP38919. 155 interactors.
MINTiMINT-1460615.
STRINGi9606.ENSP00000269349.

Protein family/group databases

TCDBi3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

PTM databases

iPTMnetiP38919.
PhosphoSitePlusiP38919.
SwissPalmiP38919.

Polymorphism and mutation databases

BioMutaiEIF4A3.
DMDMi20532400.

2D gel databases

REPRODUCTION-2DPAGEIPI00009328.

Proteomic databases

EPDiP38919.
MaxQBiP38919.
PaxDbiP38919.
PeptideAtlasiP38919.
PRIDEiP38919.

Protocols and materials databases

DNASUi9775.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000269349; ENSP00000269349; ENSG00000141543.
GeneIDi9775.
KEGGihsa:9775.
UCSCiuc002jxs.3. human.

Organism-specific databases

CTDi9775.
DisGeNETi9775.
GeneCardsiEIF4A3.
HGNCiHGNC:18683. EIF4A3.
HPAiHPA021878.
MalaCardsiEIF4A3.
MIMi268305. phenotype.
608546. gene.
neXtProtiNX_P38919.
OpenTargetsiENSG00000141543.
Orphaneti3102. Richieri Costa-Pereira syndrome.
PharmGKBiPA162384945.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0327. Eukaryota.
COG0513. LUCA.
GeneTreeiENSGT00530000062880.
HOGENOMiHOG000268797.
HOVERGENiHBG107989.
InParanoidiP38919.
KOiK13025.
OMAiTATFCIS.
OrthoDBiEOG091G07OI.
PhylomeDBiP38919.
TreeFamiTF300466.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000141543-MONOMER.
BRENDAi3.6.4.13. 2681.
ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-1169408. ISG15 antiviral mechanism.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-429947. Deadenylation of mRNA.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72187. mRNA 3'-end processing.
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

ChiTaRSiEIF4A3. human.
EvolutionaryTraceiP38919.
GeneWikiiEIF4A3.
GenomeRNAii9775.
PROiP38919.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000141543.
CleanExiHS_EIF4A3.
ExpressionAtlasiP38919. baseline and differential.
GenevisibleiP38919. HS.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiIF4A3_HUMAN
AccessioniPrimary (citable) accession number: P38919
Secondary accession number(s): Q15033, Q6IBQ2, Q96A18
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 195 of the entry and version 4 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. Translation initiation factors
    List of translation initiation factor entries
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.