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Q6ZWX6 (IF2A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic translation initiation factor 2 subunit 1
Alternative name(s):
Eukaryotic translation initiation factor 2 subunit alpha
Short name=eIF-2-alpha
Short name=eIF-2A
Short name=eIF-2alpha
Gene names
Name:Eif2s1
Synonyms:Eif2a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length315 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B By similarity.

Subunit structure

Heterotrimer composed of an alpha, a beta and a gamma chain. Interacts with ABCF1. Associates with ribosomes. Interaction with METAP2 protects EIF2S1 from inhibitory phosphorylation By similarity. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Ref.3

Subcellular location

Cytoplasmic granule. Note: The cytoplasmic granules are stress granules which are a dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress. Co-localizes with NANOS3 in the stress granules. Ref.4

Post-translational modification

Substrate for at least 4 kinases: EIF2AK3/PERK, GCN2, HRI and PKR. Phosphorylation stabilizes the eIF-2/GDP/eIF-2B complex and prevents GDP/GTP exchange reaction, thus impairing the recycling of eIF-2 between successive rounds of initiation and leading to global inhibition of translation By similarity.

Sequence similarities

Belongs to the eIF-2-alpha family.

Contains 1 S1 motif domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 315315Eukaryotic translation initiation factor 2 subunit 1
PRO_0000137383

Regions

Domain17 – 8872S1 motif

Amino acid modifications

Modified residue491Phosphoserine; by HRI By similarity
Modified residue521Phosphoserine; by EIF2AK3, GCN2, HRI and PKR By similarity
Modified residue1411N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6ZWX6 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 018480B89175D118

FASTA31536,108
        10         20         30         40         50         60 
MPGLSCRFYQ HKFPEVEDVV MVNVRSIAEM GAYVSLLEYN NIEGMILLSE LSRRRIRSIN 

        70         80         90        100        110        120 
KLIRIGRNEC VVVIRVDKEK GYIDLSKRRV SPEEAIKCED KFTKSKTVYS ILRHVAEVLE 

       130        140        150        160        170        180 
YTKDEQLESL FQRTAWVFDD KYKRPGYGAY DAFKHAVSDP SILDSLDLNE DEREVLINNI 

       190        200        210        220        230        240 
NRRLTPQAVK IRADIEVACY GYEGIDAVKE ALRAGLNCST ETMPIKINLI APPRYVMTTT 

       250        260        270        280        290        300 
TLERTEGLSV LNQAMAVIKE KIEEKRGVFN VQMEPKVVTD TDETELARQL ERLERENAEV 

       310 
DGDDDAEEME AKAED 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
[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: Czech II and FVB/N.
Tissue: Eye, Kidney and Mammary tumor.
[3]"Age-specific CUGBP1-eIF2 complex increases translation of CCAAT/enhancer-binding protein beta in old liver."
Timchenko L.T., Salisbury E., Wang G.-L., Nguyen H., Albrecht J.H., Hershey J.W., Timchenko N.A.
J. Biol. Chem. 281:32806-32819(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN AN EIF2 COMPLEX WITH CELF1; EIF2S2; CALR; CALR3; HSPA5 AND HSP90B1.
[4]"Functional reconstruction of NANOS3 expression in the germ cell lineage by a novel transgenic reporter reveals distinct subcellular localizations of NANOS3."
Yamaji M., Tanaka T., Shigeta M., Chuma S., Saga Y., Saitou M.
Reproduction 139:381-393(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK010592 mRNA. Translation: BAB27049.1.
AK143499 mRNA. Translation: BAE25400.1.
AK167763 mRNA. Translation: BAE39796.1.
BC005463 mRNA. Translation: AAH05463.1.
BC016448 mRNA. Translation: AAH16448.1.
BC016497 mRNA. Translation: AAH16497.1.
IPIIPI00474446.
RefSeqNP_080390.1. NM_026114.3.
UniGeneMm.196220.

3D structure databases

ProteinModelPortalQ6ZWX6.
SMRQ6ZWX6. Positions 4-303.
ModBaseSearch...

Protein-protein interaction databases

IntActQ6ZWX6. 5 interactions.
STRING10090.ENSMUSP00000071214.

PTM databases

PhosphoSiteQ6ZWX6.

Proteomic databases

PaxDbQ6ZWX6.
PRIDEQ6ZWX6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000071230; ENSMUSP00000071214; ENSMUSG00000021116.
GeneID13665.
KEGGmmu:13665.
UCSCuc007nzk.1. mouse.

Organism-specific databases

CTD1965.
MGIMGI:95299. Eif2s1.

Phylogenomic databases

eggNOGCOG1093.
GeneTreeENSGT00390000007015.
HOGENOMHOG000199476.
HOVERGENHBG001910.
InParanoidQ6ZWX6.
KOK03237.
OMAEKCTERF.
OrthoDBEOG4BZN35.

Gene expression databases

ArrayExpressQ6ZWX6.
BgeeQ6ZWX6.
CleanExMM_EIF2A.
GenevestigatorQ6ZWX6.
GermOnlineENSMUSG00000021116. Mus musculus.

Family and domain databases

Gene3D1.10.150.190. 1 hit.
2.40.50.140. 1 hit.
3.30.70.1130. 1 hit.
InterProIPR012340. NA-bd_OB-fold.
IPR003029. Rbsml_prot_S1_RNA-bd_dom.
IPR022967. RNA-binding_domain_S1.
IPR024055. TIF2_asu_C.
IPR024054. TIF2_asu_middle.
IPR011488. TIF_2_asu.
[Graphical view]
PfamPF07541. EIF_2_alpha. 1 hit.
PF00575. S1. 1 hit.
[Graphical view]
SMARTSM00316. S1. 1 hit.
[Graphical view]
SUPFAMSSF50249. Nucleic_acid_OB. 1 hit.
SSF110993. SSF110993. 1 hit.
SSF116742. SSF116742. 1 hit.
PROSITEPS50126. S1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChEMBLCHEMBL1770036.
NextBio284416.
SOURCESearch...

Entry information

Entry nameIF2A_MOUSE
AccessionPrimary (citable) accession number: Q6ZWX6
Secondary accession number(s): Q3TIQ0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2004
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 83 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Translation initiation factors

List of translation initiation factor entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families