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Q8BMJ3

- IF1AX_MOUSE

UniProt

Q8BMJ3 - IF1AX_MOUSE

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Protein

Eukaryotic translation initiation factor 1A, X-chromosomal

Gene

Eif1ax

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

  1. poly(A) RNA binding Source: Ensembl
  2. translation initiation factor activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

ReactomeiREACT_236458. Ribosomal scanning and start codon recognition.
REACT_249044. Formation of a pool of free 40S subunits.
REACT_249316. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_256488. Translation initiation complex formation.
REACT_259469. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_262078. GTP hydrolysis and joining of the 60S ribosomal subunit.

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: Chromosome X

Organism-specific databases

MGIiMGI:1913485. Eif1ax.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 144144Eukaryotic 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.
GenevestigatoriQ8BMJ3.

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.
OMAiWNEYATI.
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.

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 .
CCDSi CCDS41192.1.
RefSeqi NP_079713.2. NM_025437.4.
UniGenei Mm.294623.

3D structure databases

ProteinModelPortali Q8BMJ3.
SMRi Q8BMJ3. Positions 2-131.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q8BMJ3.

2D gel databases

REPRODUCTION-2DPAGE Q8BMJ3.

Proteomic databases

MaxQBi Q8BMJ3.
PaxDbi Q8BMJ3.
PRIDEi Q8BMJ3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000087143 ; ENSMUSP00000084387 ; ENSMUSG00000067194 .
GeneIDi 66235.
KEGGi mmu:66235.
UCSCi uc009usl.1. mouse.

Organism-specific databases

CTDi 1964.
MGIi MGI:1913485. Eif1ax.

Phylogenomic databases

eggNOGi COG0361.
GeneTreei ENSGT00390000008256.
HOGENOMi HOG000223675.
HOVERGENi HBG001131.
InParanoidi Q8BMJ3.
KOi K03236.
OMAi WNEYATI.
OrthoDBi EOG7VHT0G.
PhylomeDBi Q8BMJ3.
TreeFami TF350394.

Enzyme and pathway databases

Reactomei REACT_236458. Ribosomal scanning and start codon recognition.
REACT_249044. Formation of a pool of free 40S subunits.
REACT_249316. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_256488. Translation initiation complex formation.
REACT_259469. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_262078. GTP hydrolysis and joining of the 60S ribosomal subunit.

Miscellaneous databases

NextBioi 321045.
PROi Q8BMJ3.
SOURCEi Search...

Gene expression databases

Bgeei Q8BMJ3.
Genevestigatori Q8BMJ3.

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

  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: November 26, 2014
This is version 97 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