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Protein

Eukaryotic translation initiation factor 2 subunit 2

Gene

Eif2s2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

eIF-2 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).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri279 – 30325C4-typeSequence analysisAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • in utero embryonic development Source: MGI
  • male germ cell proliferation Source: MGI
  • male gonad development Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-382556. ABC-family proteins mediated transport.
R-MMU-72649. Translation initiation complex formation.
R-MMU-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-MMU-72702. Ribosomal scanning and start codon recognition.
R-MMU-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-MMU-72731. Recycling of eIF2:GDP.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 2 subunit 2
Alternative name(s):
Eukaryotic translation initiation factor 2 subunit beta
Short name:
eIF-2-beta
Gene namesi
Name:Eif2s2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1914454. Eif2s2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 331330Eukaryotic translation initiation factor 2 subunit 2PRO_0000137407Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei13 – 131PhosphoserineBy similarity
Modified residuei36 – 361PhosphothreonineBy similarity
Modified residuei67 – 671PhosphoserineCombined sources
Modified residuei105 – 1051PhosphoserineCombined sources
Modified residuei158 – 1581PhosphoserineBy similarity
Modified residuei216 – 2161PhosphoserineBy similarity
Modified residuei263 – 2631N6-acetyllysineBy similarity
Modified residuei291 – 2911N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ99L45.
MaxQBiQ99L45.
PaxDbiQ99L45.
PRIDEiQ99L45.

PTM databases

iPTMnetiQ99L45.
PhosphoSiteiQ99L45.
SwissPalmiQ99L45.

Expressioni

Gene expression databases

BgeeiQ99L45.
ExpressionAtlasiQ99L45. baseline and differential.
GenevisibleiQ99L45. MM.

Interactioni

Subunit structurei

Heterotrimer composed of an alpha, a beta and a gamma chain (By similarity). Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5.By similarity1 Publication

Protein-protein interaction databases

BioGridi212014. 3 interactions.
IntActiQ99L45. 1 interaction.
MINTiMINT-1857216.
STRINGi10090.ENSMUSP00000096777.

Structurei

3D structure databases

ProteinModelPortaliQ99L45.
SMRiQ99L45. Positions 172-303.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi14 – 218Poly-Lys
Compositional biasi79 – 879Poly-Lys
Compositional biasi124 – 1296Poly-Lys

Sequence similaritiesi

Belongs to the eIF-2-beta/eIF-5 family.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri279 – 30325C4-typeSequence analysisAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG2768. Eukaryota.
COG1601. LUCA.
GeneTreeiENSGT00390000001804.
HOGENOMiHOG000107198.
HOVERGENiHBG000927.
InParanoidiQ99L45.
KOiK03238.
OMAiPEVMEED.
OrthoDBiEOG71ZP2X.
PhylomeDBiQ99L45.
TreeFamiTF101503.

Family and domain databases

Gene3Di3.30.30.50. 1 hit.
InterProiIPR002735. Transl_init_fac_IF2/IF5.
IPR016189. Transl_init_fac_IF2/IF5_N.
IPR016190. Transl_init_fac_IF2/IF5_Zn-bd.
[Graphical view]
PfamiPF01873. eIF-5_eIF-2B. 1 hit.
[Graphical view]
SMARTiSM00653. eIF2B_5. 1 hit.
[Graphical view]
SUPFAMiSSF100966. SSF100966. 1 hit.
SSF75689. SSF75689. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q99L45-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGDEMIFDP TMSKKKKKKK KPFMLDEEGD AQTEETQPSE TKEVEPEPTE
60 70 80 90 100
EKDVDADEED SRKKDASDDL DDLNFFNQKK KKKKTKKIFD IDEAEEAIKD
110 120 130 140 150
VKIESDAQEP AEPEDDLDIM LGNKKKKKKN VKFPEEDEIL EKDEALEDED
160 170 180 190 200
SKKDDGISFS SQTAWAGSER DYTYEELLNR VFNIMREKNP DMVAGEKRKF
210 220 230 240 250
VMKPPQVVRV GTKKTSFVNF TDICKLLHRQ PKHLLAFLLA ELGTSGSIDG
260 270 280 290 300
NNQLVIKGRF QQKQIENVLR RYIKEYVTCH TCRSPDTILQ KDTRLYFLQC
310 320 330
ETCHSRCSVA SIKTGFQAVT GKRAQLRAKA N
Length:331
Mass (Da):38,092
Last modified:June 1, 2001 - v1
Checksum:iE91BEBBF330B7A5C
GO

Sequence cautioni

The sequence BAB28490.2 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011503 mRNA. Translation: BAB27663.1.
AK012817 mRNA. Translation: BAB28490.2. Different initiation.
BC003848 mRNA. Translation: AAH03848.1.
CCDSiCCDS38292.1.
RefSeqiNP_080306.1. NM_026030.2.
UniGeneiMm.377134.
Mm.470088.

Genome annotation databases

EnsembliENSMUST00000099173; ENSMUSP00000096777; ENSMUSG00000074656.
ENSMUST00000166171; ENSMUSP00000128257; ENSMUSG00000074656.
GeneIDi67204.
KEGGimmu:67204.
UCSCiuc008njw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011503 mRNA. Translation: BAB27663.1.
AK012817 mRNA. Translation: BAB28490.2. Different initiation.
BC003848 mRNA. Translation: AAH03848.1.
CCDSiCCDS38292.1.
RefSeqiNP_080306.1. NM_026030.2.
UniGeneiMm.377134.
Mm.470088.

3D structure databases

ProteinModelPortaliQ99L45.
SMRiQ99L45. Positions 172-303.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212014. 3 interactions.
IntActiQ99L45. 1 interaction.
MINTiMINT-1857216.
STRINGi10090.ENSMUSP00000096777.

PTM databases

iPTMnetiQ99L45.
PhosphoSiteiQ99L45.
SwissPalmiQ99L45.

Proteomic databases

EPDiQ99L45.
MaxQBiQ99L45.
PaxDbiQ99L45.
PRIDEiQ99L45.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000099173; ENSMUSP00000096777; ENSMUSG00000074656.
ENSMUST00000166171; ENSMUSP00000128257; ENSMUSG00000074656.
GeneIDi67204.
KEGGimmu:67204.
UCSCiuc008njw.1. mouse.

Organism-specific databases

CTDi8894.
MGIiMGI:1914454. Eif2s2.

Phylogenomic databases

eggNOGiKOG2768. Eukaryota.
COG1601. LUCA.
GeneTreeiENSGT00390000001804.
HOGENOMiHOG000107198.
HOVERGENiHBG000927.
InParanoidiQ99L45.
KOiK03238.
OMAiPEVMEED.
OrthoDBiEOG71ZP2X.
PhylomeDBiQ99L45.
TreeFamiTF101503.

Enzyme and pathway databases

ReactomeiR-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-382556. ABC-family proteins mediated transport.
R-MMU-72649. Translation initiation complex formation.
R-MMU-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-MMU-72702. Ribosomal scanning and start codon recognition.
R-MMU-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-MMU-72731. Recycling of eIF2:GDP.

Miscellaneous databases

PROiQ99L45.
SOURCEiSearch...

Gene expression databases

BgeeiQ99L45.
ExpressionAtlasiQ99L45. baseline and differential.
GenevisibleiQ99L45. MM.

Family and domain databases

Gene3Di3.30.30.50. 1 hit.
InterProiIPR002735. Transl_init_fac_IF2/IF5.
IPR016189. Transl_init_fac_IF2/IF5_N.
IPR016190. Transl_init_fac_IF2/IF5_Zn-bd.
[Graphical view]
PfamiPF01873. eIF-5_eIF-2B. 1 hit.
[Graphical view]
SMARTiSM00653. eIF2B_5. 1 hit.
[Graphical view]
SUPFAMiSSF100966. SSF100966. 1 hit.
SSF75689. SSF75689. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: Embryo.
  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.
  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 EIF2S1; CELF1; CALR; CALR3; HSPA5 AND HSP90B1.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiIF2B_MOUSE
AccessioniPrimary (citable) accession number: Q99L45
Secondary accession number(s): Q9CSH6, Q9CT12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 130 of the entry and version 1 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

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 one 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.