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P47813

- IF1AX_HUMAN

UniProt

P47813 - IF1AX_HUMAN

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Protein

Eukaryotic translation initiation factor 1A, X-chromosomal

Gene

EIF1AX

Organism
Homo sapiens (Human)
Status
Reviewed - 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
Chaini1 – 144144Eukaryotic 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. 28 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.

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 .
CCDSi CCDS14196.1.
PIRi C53045.
RefSeqi NP_001403.1. NM_001412.3.
UniGenei Hs.522590.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1D7Q NMR - A 2-144 [» ]
3ZJY X-ray 3.60 C 1-112 [» ]
4KZY X-ray 7.01 n 1-144 [» ]
4KZZ X-ray 7.03 n 1-144 [» ]
ProteinModelPortali P47813.
SMRi P47813. Positions 2-131.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108284. 28 interactions.
DIPi DIP-40995N.
IntActi P47813. 4 interactions.
MINTi MINT-144981.
STRINGi 9606.ENSP00000368927.

Polymorphism databases

DMDMi 1352425.

Proteomic databases

MaxQBi P47813.
PaxDbi P47813.
PRIDEi P47813.

Protocols and materials databases

DNASUi 1964.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000379607 ; ENSP00000368927 ; ENSG00000173674 .
GeneIDi 1964.
KEGGi hsa:1964.
UCSCi uc004czt.3. human.

Organism-specific databases

CTDi 1964.
GeneCardsi GC0XM020052.
H-InvDB HIX0028844.
HGNCi HGNC:3250. EIF1AX.
HPAi HPA002561.
MIMi 300186. gene.
neXtProti NX_P47813.
PharmGKBi PA27684.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0361.
GeneTreei ENSGT00390000008256.
HOGENOMi HOG000223675.
HOVERGENi HBG001131.
InParanoidi P47813.
KOi K03236.
OMAi WNEYATI.
OrthoDBi EOG7VHT0G.
PhylomeDBi P47813.
TreeFami TF350394.

Enzyme and pathway databases

Reactomei REACT_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

ChiTaRSi EIF1AX. human.
EvolutionaryTracei P47813.
GeneWikii EIF1AX.
GenomeRNAii 1964.
NextBioi 7965.
PROi P47813.
SOURCEi Search...

Gene expression databases

Bgeei P47813.
CleanExi HS_EIF1AX.
ExpressionAtlasi P47813. baseline and differential.
Genevestigatori P47813.

Family and domain databases

Gene3Di 2.40.50.140. 1 hit.
HAMAPi MF_00216. aIF_1A.
InterProi IPR012340. NA-bd_OB-fold.
IPR006196. RNA-binding_domain_S1_IF1.
IPR001253. TIF_eIF-1A.
IPR018104. TIF_eIF-1A_CS.
[Graphical view ]
PANTHERi PTHR21668. PTHR21668. 1 hit.
Pfami PF01176. eIF-1a. 1 hit.
[Graphical view ]
ProDomi PD005579. TIF_eIF-1A. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00652. eIF1a. 1 hit.
[Graphical view ]
SUPFAMi SSF50249. SSF50249. 1 hit.
TIGRFAMsi TIGR00523. eIF-1A. 1 hit.
PROSITEi PS01262. IF1A. 1 hit.
PS50832. S1_IF1_TYPE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: November 26, 2014
This is version 144 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