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Protein

Eukaryotic translation initiation factor 1A, X-chromosomal

Gene

Eif1ax

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript 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 (By similarity).By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

ReactomeiREACT_283953. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_292264. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_292503. Translation initiation complex formation.
REACT_305839. Ribosomal scanning and start codon recognition.
REACT_308559. Formation of a pool of free 40S subunits.
REACT_340387. L13a-mediated translational silencing of Ceruloplasmin expression.

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:Eif1ay
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1913485. Eif1ax.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 144143Eukaryotic translation initiation factor 1A, X-chromosomalPRO_0000145107Add
BLAST

Proteomic databases

MaxQBiQ8BMJ3.
PaxDbiQ8BMJ3.
PRIDEiQ8BMJ3.

2D gel databases

REPRODUCTION-2DPAGEQ8BMJ3.

PTM databases

PhosphoSiteiQ8BMJ3.

Expressioni

Gene expression databases

BgeeiQ8BMJ3.
GenevisibleiQ8BMJ3. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000084387.

Structurei

3D structure databases

ProteinModelPortaliQ8BMJ3.
SMRiQ8BMJ3. Positions 2-131.
ModBaseiSearch...
MobiDBiSearch...

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.
InParanoidiQ8BMJ3.
KOiK03236.
OMAiVICGIIR.
OrthoDBiEOG7VHT0G.
PhylomeDBiQ8BMJ3.
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.

Q8BMJ3-1 [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 - v3
Checksum:i1C4209855B21BFD4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 461R → G in BAC36971 (PubMed:16141072).Curated
Sequence conflicti63 – 631G → R in BAB23869 (PubMed:16141072).Curated
Sequence conflicti95 – 951Y → N in BAC27259 (PubMed:16141072).Curated
Sequence conflicti136 – 1361D → E in BAC27130 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005185 mRNA. Translation: BAB23869.1.
AK007301 mRNA. Translation: BAB24942.1.
AK012233 mRNA. Translation: BAB28110.1.
AK012464 mRNA. Translation: BAB28259.3.
AK012714 mRNA. Translation: BAB28428.1.
AK021283 mRNA. Translation: BAB32361.1.
AK030774 mRNA. Translation: BAC27130.1.
AK031113 mRNA. Translation: BAC27259.1.
AK077710 mRNA. Translation: BAC36971.1.
AK090053 mRNA. Translation: BAC41069.1.
AK134827 mRNA. Translation: BAE22301.1.
AK134969 mRNA. Translation: BAE22363.1.
AK165574 mRNA. Translation: BAE38266.1.
AK166629 mRNA. Translation: BAE38904.1.
AK166852 mRNA. Translation: BAE39071.1.
BC027284 mRNA. Translation: AAH27284.1.
CCDSiCCDS41192.1.
RefSeqiNP_079713.2. NM_025437.4.
UniGeneiMm.294623.

Genome annotation databases

EnsembliENSMUST00000087143; ENSMUSP00000084387; ENSMUSG00000067194.
GeneIDi66235.
KEGGimmu:66235.
UCSCiuc009usl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005185 mRNA. Translation: BAB23869.1.
AK007301 mRNA. Translation: BAB24942.1.
AK012233 mRNA. Translation: BAB28110.1.
AK012464 mRNA. Translation: BAB28259.3.
AK012714 mRNA. Translation: BAB28428.1.
AK021283 mRNA. Translation: BAB32361.1.
AK030774 mRNA. Translation: BAC27130.1.
AK031113 mRNA. Translation: BAC27259.1.
AK077710 mRNA. Translation: BAC36971.1.
AK090053 mRNA. Translation: BAC41069.1.
AK134827 mRNA. Translation: BAE22301.1.
AK134969 mRNA. Translation: BAE22363.1.
AK165574 mRNA. Translation: BAE38266.1.
AK166629 mRNA. Translation: BAE38904.1.
AK166852 mRNA. Translation: BAE39071.1.
BC027284 mRNA. Translation: AAH27284.1.
CCDSiCCDS41192.1.
RefSeqiNP_079713.2. NM_025437.4.
UniGeneiMm.294623.

3D structure databases

ProteinModelPortaliQ8BMJ3.
SMRiQ8BMJ3. Positions 2-131.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000084387.

PTM databases

PhosphoSiteiQ8BMJ3.

2D gel databases

REPRODUCTION-2DPAGEQ8BMJ3.

Proteomic databases

MaxQBiQ8BMJ3.
PaxDbiQ8BMJ3.
PRIDEiQ8BMJ3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000087143; ENSMUSP00000084387; ENSMUSG00000067194.
GeneIDi66235.
KEGGimmu:66235.
UCSCiuc009usl.1. mouse.

Organism-specific databases

CTDi1964.
MGIiMGI:1913485. Eif1ax.

Phylogenomic databases

eggNOGiCOG0361.
GeneTreeiENSGT00390000008256.
HOGENOMiHOG000223675.
HOVERGENiHBG001131.
InParanoidiQ8BMJ3.
KOiK03236.
OMAiVICGIIR.
OrthoDBiEOG7VHT0G.
PhylomeDBiQ8BMJ3.
TreeFamiTF350394.

Enzyme and pathway databases

ReactomeiREACT_283953. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_292264. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_292503. Translation initiation complex formation.
REACT_305839. Ribosomal scanning and start codon recognition.
REACT_308559. Formation of a pool of free 40S subunits.
REACT_340387. L13a-mediated translational silencing of Ceruloplasmin expression.

Miscellaneous databases

NextBioi321045.
PROiQ8BMJ3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BMJ3.
GenevisibleiQ8BMJ3. MM.

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

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Blastocyst, Cerebellum, Embryo, Embryonic eye, Embryonic stem cell, Forelimb, Medulla oblongata, Olfactory bulb and Testis.
  2. "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].
    Strain: FVB/N.
    Tissue: Mammary gland.

Entry informationi

Entry nameiIF1AX_MOUSE
AccessioniPrimary (citable) accession number: Q8BMJ3
Secondary accession number(s): Q3UY50
, Q6ZWL8, Q8BJZ2, Q8BMH8, Q9CSL9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 102 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Translation initiation factors
    List of translation initiation factor entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. 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.