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Protein

Translation initiation factor eIF-2B subunit epsilon

Gene

Eif2b5

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP.

GO - Molecular functioni

  • guanyl-nucleotide exchange factor activity Source: MGI
  • translation initiation factor activity Source: RGD
  • translation initiation factor binding Source: RGD

GO - Biological processi

  • aging Source: RGD
  • astrocyte development Source: UniProtKB
  • astrocyte differentiation Source: UniProtKB
  • cellular response to drug Source: UniProtKB
  • myelination Source: UniProtKB
  • negative regulation of translational initiation in response to stress Source: RGD
  • oligodendrocyte development Source: UniProtKB
  • ovarian follicle development Source: UniProtKB
  • positive regulation of translational initiation Source: UniProtKB
  • regulation of translation Source: RGD
  • response to endoplasmic reticulum stress Source: UniProtKB
  • response to glucose Source: UniProtKB
  • response to heat Source: UniProtKB
  • response to peptide hormone Source: UniProtKB
  • translational initiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

ReactomeiR-RNO-72731. Recycling of eIF2:GDP.

Names & Taxonomyi

Protein namesi
Recommended name:
Translation initiation factor eIF-2B subunit epsilon
Alternative name(s):
eIF-2B GDP-GTP exchange factor subunit epsilon
Gene namesi
Name:Eif2b5
Synonyms:Eif2be
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 11

Organism-specific databases

RGDi708380. Eif2b5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 716716Translation initiation factor eIF-2B subunit epsilonPRO_0000156075Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei22 – 221Phosphoserine1 Publication
Cross-linki56 – 56Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki98 – 98Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei125 – 1251Phosphoserine1 Publication
Cross-linki136 – 136Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki212 – 212Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei317 – 3171Phosphothreonine1 Publication
Modified residuei445 – 4451PhosphoserineBy similarity
Modified residuei461 – 4611PhosphoserineBy similarity
Modified residuei464 – 4641PhosphoserineBy similarity
Cross-linki500 – 500Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei527 – 5271PhosphoserineCombined sources
Modified residuei535 – 5351PhosphoserineCombined sources
Modified residuei539 – 5391Phosphoserine; by DYRK2Combined sources1 Publication
Modified residuei712 – 7121PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated on serine and threonine residues by GSK3B; phosphorylation inhibits its function (By similarity). Phosphorylated at Ser-539 by DYRK2; this is required for subsequent phosphorylation by GSK3B.By similarity2 Publications
Polyubiquitinated, probably by NEDD4.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ64350.
PRIDEiQ64350.

PTM databases

iPTMnetiQ64350.
PhosphoSiteiQ64350.

Expressioni

Gene expression databases

GenevisibleiQ64350. RN.

Interactioni

Subunit structurei

Complex of five different subunits; alpha, beta, gamma, delta and epsilon. Interacts with RGS2 (By similarity).By similarity

GO - Molecular functioni

  • translation initiation factor binding Source: RGD

Protein-protein interaction databases

BioGridi251366. 4 interactions.
STRINGi10116.ENSRNOP00000002321.

Structurei

3D structure databases

ProteinModelPortaliQ64350.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini538 – 715178W2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi19 – 268Poly-Gly
Compositional biasi34 – 374Poly-Pro

Sequence similaritiesi

Contains 1 W2 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1461. Eukaryota.
COG1208. LUCA.
GeneTreeiENSGT00510000047568.
HOGENOMiHOG000216610.
HOVERGENiHBG051460.
InParanoidiQ64350.
KOiK03240.
OMAiESEQSMD.
OrthoDBiEOG7PGDQ9.
PhylomeDBiQ64350.
TreeFamiTF101509.

Family and domain databases

Gene3Di1.25.40.180. 1 hit.
3.90.550.10. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR001451. Hexapep.
IPR016021. MIF4-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
IPR003307. W2_domain.
[Graphical view]
PfamiPF00132. Hexapep. 1 hit.
PF02020. W2. 1 hit.
[Graphical view]
SMARTiSM00515. eIF5C. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 2 hits.
PROSITEiPS51363. W2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q64350-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATAAVPSA VGGRANKRGG GSGGGGTQGA EEEPPPPLQA VLVADSFDRR
60 70 80 90 100
FFPISKDQPR VLLPLANVAL IDYTLEFLTA TGVQETFVFC CWKAAQIKEH
110 120 130 140 150
LQKSKWCHPT SLNVVRIITS DLYRSLGDVL RDVDAKALVR SDFLLIYGDV
160 170 180 190 200
VSNINISKAL EEHRLRRKLE KNVSVMTMVF KESSPSHPTR CHEDNVVLAV
210 220 230 240 250
DSTTNRILHF QKTQGLRHFS FPLGLFQGSL DGVEIRYDLL DCHISICSPQ
260 270 280 290 300
VAQLFTDNFD YQTRDDFVRG LLVNEEILGN QIHLHVTSRE YGARVSNLHM
310 320 330 340 350
YSAVCADVIR RWVYPLTPEV NFTDSSTQSY THSRHNIYRG PEVSLGHGSV
360 370 380 390 400
LEENVLLGAG TVVGSNCSIT NSVIGPNCHI GDNVVLDQAY LWQGVRVAAG
410 420 430 440 450
AQIHQSLLCD RAEVKERVIL KPHCVLTSQV VVGPDIILPE GSVISLHPPD
460 470 480 490 500
AEEDEDDGQF SDDSGADQEK EKVKLKGYNP AEVGPEGQGY LWKAEDVDEK
510 520 530 540 550
EDEELRQSLW GLMINMEEES ETESERSVDP EELDSRAGSP QLDDIRVFQN
560 570 580 590 600
EVLGTLQRGR EENISCDNLV LEINSLKYAY NISLKEVMQV LSHVVLEFPL
610 620 630 640 650
QQVDGVLDPN RYCALLLPLL KAWSPVFRNY IKRAADHLEA LAAIEDFFLE
660 670 680 690 700
HETLVPSLAK VLMAFYQLEI LAEETILSWF SQRDITDKGQ QLRKNQQLQR
710
FIQWLREAEE ESSDDD
Length:716
Mass (Da):80,206
Last modified:April 4, 2006 - v2
Checksum:i4C6E4C570C196CC0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti118 – 1181I → T in AAB17690 (PubMed:8688467).Curated
Sequence conflicti118 – 1181I → T in AAB17691 (PubMed:8688467).Curated
Sequence conflicti293 – 2931A → S in AAB17690 (PubMed:8688467).Curated
Sequence conflicti293 – 2931A → S in AAB17691 (PubMed:8688467).Curated
Sequence conflicti306 – 3061A → T in AAB17690 (PubMed:8688467).Curated
Sequence conflicti306 – 3061A → T in AAB17691 (PubMed:8688467).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19516 mRNA. Translation: AAB17690.1.
U19511 Genomic DNA. Translation: AAB17691.1.
BC085698 mRNA. Translation: AAH85698.1.
RefSeqiNP_620221.2. NM_138866.2.
UniGeneiRn.10607.

Genome annotation databases

EnsembliENSRNOT00000002321; ENSRNOP00000002321; ENSRNOG00000038160.
GeneIDi192234.
KEGGirno:192234.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19516 mRNA. Translation: AAB17690.1.
U19511 Genomic DNA. Translation: AAB17691.1.
BC085698 mRNA. Translation: AAH85698.1.
RefSeqiNP_620221.2. NM_138866.2.
UniGeneiRn.10607.

3D structure databases

ProteinModelPortaliQ64350.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi251366. 4 interactions.
STRINGi10116.ENSRNOP00000002321.

PTM databases

iPTMnetiQ64350.
PhosphoSiteiQ64350.

Proteomic databases

PaxDbiQ64350.
PRIDEiQ64350.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000002321; ENSRNOP00000002321; ENSRNOG00000038160.
GeneIDi192234.
KEGGirno:192234.

Organism-specific databases

CTDi8893.
RGDi708380. Eif2b5.

Phylogenomic databases

eggNOGiKOG1461. Eukaryota.
COG1208. LUCA.
GeneTreeiENSGT00510000047568.
HOGENOMiHOG000216610.
HOVERGENiHBG051460.
InParanoidiQ64350.
KOiK03240.
OMAiESEQSMD.
OrthoDBiEOG7PGDQ9.
PhylomeDBiQ64350.
TreeFamiTF101509.

Enzyme and pathway databases

ReactomeiR-RNO-72731. Recycling of eIF2:GDP.

Miscellaneous databases

NextBioi622848.
PROiQ64350.

Gene expression databases

GenevisibleiQ64350. RN.

Family and domain databases

Gene3Di1.25.40.180. 1 hit.
3.90.550.10. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR001451. Hexapep.
IPR016021. MIF4-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
IPR003307. W2_domain.
[Graphical view]
PfamiPF00132. Hexapep. 1 hit.
PF02020. W2. 1 hit.
[Graphical view]
SMARTiSM00515. eIF5C. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 2 hits.
PROSITEiPS51363. W2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of complementary and genomic DNAs encoding the epsilon-subunit of rat translation initiation factor-2B."
    Flowers K.M., Mellor H., Matts R.L., Kimball S.R., Jefferson L.S.
    Biochim. Biophys. Acta 1307:318-324(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: Sprague-Dawley.
  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].
    Tissue: Heart.
  3. "The kinase DYRK phosphorylates protein-synthesis initiation factor eIF2Bepsilon at Ser539 and the microtubule-associated protein tau at Thr212: potential role for DYRK as a glycogen synthase kinase 3-priming kinase."
    Woods Y.L., Cohen P., Becker W., Jakes R., Goedert M., Wang X., Proud C.G.
    Biochem. J. 355:609-615(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, PHOSPHORYLATION AT SER-539.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527; SER-535 AND SER-539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "Identification of ubiquitin-modified lysine residues and novel phosphorylation sites on eukaryotic initiation factor 2B epsilon."
    Tuckow A.P., Kazi A.A., Kimball S.R., Jefferson L.S.
    Biochem. Biophys. Res. Commun. 436:41-46(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-22; SER-125 AND THR-317, UBIQUITINATION AT LYS-56; LYS-98; LYS-136; LYS-212 AND LYS-500 BY NEDD4.

Entry informationi

Entry nameiEI2BE_RAT
AccessioniPrimary (citable) accession number: Q64350
Secondary accession number(s): Q5RKL3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 4, 2006
Last modified: May 11, 2016
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.