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Protein

Eukaryotic translation initiation factor 1A, X-chromosomal

Gene

EIF1AX

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits.

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. translation factor activity, nucleic acid binding Source: ProtInc
  3. translation initiation factor activity Source: UniProtKB-KW

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. gene expression Source: Reactome
  3. translation Source: Reactome
  4. translational initiation Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
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 translation initiation factor 1A, X-chromosomal
Short name:
eIF-1A X isoform
Alternative name(s):
Eukaryotic translation initiation factor 4C
Short name:
eIF-4C
Gene namesi
Name:EIF1AX
Synonyms:EIF1A, EIF4C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:3250. EIF1AX.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27684.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 144143Eukaryotic translation initiation factor 1A, X-chromosomalPRO_0000145101Add
BLAST

Proteomic databases

MaxQBiP47813.
PaxDbiP47813.
PRIDEiP47813.

Expressioni

Gene expression databases

BgeeiP47813.
CleanExiHS_EIF1AX.
ExpressionAtlasiP47813. baseline and differential.
GenevestigatoriP47813.

Organism-specific databases

HPAiHPA002561.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
IPO13O9482914EBI-1045377,EBI-747310

Protein-protein interaction databases

BioGridi108284. 27 interactions.
DIPiDIP-40995N.
IntActiP47813. 4 interactions.
MINTiMINT-144981.
STRINGi9606.ENSP00000368927.

Structurei

Secondary structure

1
144
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 126Combined sources
Beta strandi33 – 419Combined sources
Beta strandi43 – 519Combined sources
Turni52 – 543Combined sources
Beta strandi55 – 606Combined sources
Helixi64 – 674Combined sources
Beta strandi76 – 805Combined sources
Beta strandi82 – 876Combined sources
Beta strandi90 – 956Combined sources
Turni97 – 993Combined sources
Helixi100 – 1067Combined sources
Beta strandi120 – 1223Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D7QNMR-A2-144[»]
3ZJYX-ray3.60C1-112[»]
4KZYX-ray7.01n1-144[»]
4KZZX-ray7.03n1-144[»]
ProteinModelPortaliP47813.
SMRiP47813. Positions 2-131.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP47813.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 9675S1-likeAdd
BLAST

Sequence similaritiesi

Belongs to the eIF-1A family.Curated
Contains 1 S1-like domain.Curated

Phylogenomic databases

eggNOGiCOG0361.
GeneTreeiENSGT00390000008256.
HOGENOMiHOG000223675.
HOVERGENiHBG001131.
InParanoidiP47813.
KOiK03236.
OMAiWNEYATI.
OrthoDBiEOG7VHT0G.
PhylomeDBiP47813.
TreeFamiTF350394.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_00216. aIF_1A.
InterProiIPR012340. NA-bd_OB-fold.
IPR006196. RNA-binding_domain_S1_IF1.
IPR001253. TIF_eIF-1A.
IPR018104. TIF_eIF-1A_CS.
[Graphical view]
PANTHERiPTHR21668. PTHR21668. 1 hit.
PfamiPF01176. eIF-1a. 1 hit.
[Graphical view]
ProDomiPD005579. TIF_eIF-1A. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00652. eIF1a. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00523. eIF-1A. 1 hit.
PROSITEiPS01262. IF1A. 1 hit.
PS50832. S1_IF1_TYPE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P47813-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKNKGKGGK NRRRGKNENE SEKRELVFKE DGQEYAQVIK MLGNGRLEAM
60 70 80 90 100
CFDGVKRLCH IRGKLRKKVW INTSDIILVG LRDYQDNKAD VILKYNADEA
110 120 130 140
RSLKAYGELP EHAKINETDT FGPGDDDEIQ FDDIGDDDED IDDI
Length:144
Mass (Da):16,460
Last modified:January 23, 2007 - v2
Checksum:i1C4209855B21BFD4
GO

Sequence cautioni

The sequence CAI40551.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L18960 mRNA. Translation: AAA19812.1.
AK312320 mRNA. Translation: BAG35242.1.
BT007064 mRNA. Translation: AAP35727.1.
AL732366 Genomic DNA. Translation: CAI40550.1.
AL732366 Genomic DNA. Translation: CAI40551.1. Sequence problems.
BC000793 mRNA. Translation: AAH00793.1.
BC067851 mRNA. Translation: AAH67851.1.
CCDSiCCDS14196.1.
PIRiC53045.
RefSeqiNP_001403.1. NM_001412.3.
UniGeneiHs.522590.

Genome annotation databases

EnsembliENST00000379607; ENSP00000368927; ENSG00000173674.
GeneIDi1964.
KEGGihsa:1964.
UCSCiuc004czt.3. human.

Polymorphism databases

DMDMi1352425.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L18960 mRNA. Translation: AAA19812.1.
AK312320 mRNA. Translation: BAG35242.1.
BT007064 mRNA. Translation: AAP35727.1.
AL732366 Genomic DNA. Translation: CAI40550.1.
AL732366 Genomic DNA. Translation: CAI40551.1. Sequence problems.
BC000793 mRNA. Translation: AAH00793.1.
BC067851 mRNA. Translation: AAH67851.1.
CCDSiCCDS14196.1.
PIRiC53045.
RefSeqiNP_001403.1. NM_001412.3.
UniGeneiHs.522590.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D7QNMR-A2-144[»]
3ZJYX-ray3.60C1-112[»]
4KZYX-ray7.01n1-144[»]
4KZZX-ray7.03n1-144[»]
ProteinModelPortaliP47813.
SMRiP47813. Positions 2-131.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108284. 27 interactions.
DIPiDIP-40995N.
IntActiP47813. 4 interactions.
MINTiMINT-144981.
STRINGi9606.ENSP00000368927.

Polymorphism databases

DMDMi1352425.

Proteomic databases

MaxQBiP47813.
PaxDbiP47813.
PRIDEiP47813.

Protocols and materials databases

DNASUi1964.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379607; ENSP00000368927; ENSG00000173674.
GeneIDi1964.
KEGGihsa:1964.
UCSCiuc004czt.3. human.

Organism-specific databases

CTDi1964.
GeneCardsiGC0XM020052.
H-InvDBHIX0028844.
HGNCiHGNC:3250. EIF1AX.
HPAiHPA002561.
MIMi300186. gene.
neXtProtiNX_P47813.
PharmGKBiPA27684.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0361.
GeneTreeiENSGT00390000008256.
HOGENOMiHOG000223675.
HOVERGENiHBG001131.
InParanoidiP47813.
KOiK03236.
OMAiWNEYATI.
OrthoDBiEOG7VHT0G.
PhylomeDBiP47813.
TreeFamiTF350394.

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
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

ChiTaRSiEIF1AX. human.
EvolutionaryTraceiP47813.
GeneWikiiEIF1AX.
GenomeRNAii1964.
NextBioi7965.
PROiP47813.
SOURCEiSearch...

Gene expression databases

BgeeiP47813.
CleanExiHS_EIF1AX.
ExpressionAtlasiP47813. baseline and differential.
GenevestigatoriP47813.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_00216. aIF_1A.
InterProiIPR012340. NA-bd_OB-fold.
IPR006196. RNA-binding_domain_S1_IF1.
IPR001253. TIF_eIF-1A.
IPR018104. TIF_eIF-1A_CS.
[Graphical view]
PANTHERiPTHR21668. PTHR21668. 1 hit.
PfamiPF01176. eIF-1a. 1 hit.
[Graphical view]
ProDomiPD005579. TIF_eIF-1A. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00652. eIF1a. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00523. eIF-1A. 1 hit.
PROSITEiPS01262. IF1A. 1 hit.
PS50832. S1_IF1_TYPE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Determination of the amino acid sequence of rabbit, human, and wheat germ protein synthesis factor eIF-4C by cloning and chemical sequencing."
    Dever T.E., Wei C.-L., Benkowski L.A., Browning K., Merrick W.C., Hershey J.W.B.
    J. Biol. Chem. 269:3212-3218(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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: Cerebellum.
  3. "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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Hypothalamus and Placenta.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "The eIF1A solution structure reveals a large RNA-binding surface important for scanning function."
    Battiste J.L., Pestova T.V., Hellen C.U., Wagner G.
    Mol. Cell 5:109-119(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiIF1AX_HUMAN
AccessioniPrimary (citable) accession number: P47813
Secondary accession number(s): B2R5U5
, Q0VGC2, Q5JPS5, Q5JPS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 146 of the entry and version 2 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 X
    Human chromosome X: 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

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 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.