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Protein

Translation initiation factor eIF-2B subunit epsilon

Gene

Eif2b5

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

Functioni

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

ReactomeiR-MMU-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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:2446176. Eif2b5.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • eukaryotic translation initiation factor 2B complex Source: UniProtKB
  • nucleus Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 717717Translation initiation factor eIF-2B subunit epsilonPRO_0000239429Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei23 – 231PhosphoserineBy similarity
Cross-linki57 – 57Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki99 – 99Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei126 – 1261PhosphoserineBy similarity
Cross-linki137 – 137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki213 – 213Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei318 – 3181PhosphothreonineBy similarity
Modified residuei446 – 4461PhosphoserineBy similarity
Modified residuei462 – 4621PhosphoserineBy similarity
Modified residuei465 – 4651PhosphoserineBy similarity
Cross-linki501 – 501Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei528 – 5281PhosphoserineBy similarity
Modified residuei536 – 5361PhosphoserineBy similarity
Modified residuei540 – 5401Phosphoserine; by DYRK2Combined sources
Modified residuei713 – 7131PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated at Ser-540 by DYRK2; this is required for subsequent phosphorylation by GSK3B. Phosphorylated on serine and threonine residues by GSK3B; phosphorylation inhibits its function (By similarity).By similarity
Polyubiquitinated, probably by NEDD4.By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8CHW4.
MaxQBiQ8CHW4.
PaxDbiQ8CHW4.
PRIDEiQ8CHW4.

PTM databases

iPTMnetiQ8CHW4.
PhosphoSiteiQ8CHW4.

Expressioni

Gene expression databases

BgeeiQ8CHW4.
ExpressionAtlasiQ8CHW4. baseline and differential.
GenevisibleiQ8CHW4. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000003320.

Structurei

3D structure databases

ProteinModelPortaliQ8CHW4.
SMRiQ8CHW4. Positions 343-368, 543-711.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini539 – 716178W2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 W2 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1461. Eukaryota.
COG1208. LUCA.
GeneTreeiENSGT00510000047568.
HOGENOMiHOG000216610.
HOVERGENiHBG051460.
InParanoidiQ8CHW4.
KOiK03240.
OMAiINALRCK.
OrthoDBiEOG7PGDQ9.
PhylomeDBiQ8CHW4.
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.

Q8CHW4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATAAVPGA AAGRASKRGG GGSGGGGTQG AEEEPPPPLQ AVLVADSFNR
60 70 80 90 100
RFFPISKDQP RVLLPLANVA LIDYTLEFLT ATGVQETFVF CCWKAAQIKE
110 120 130 140 150
HLQKSKWCHP TSPNVVRIIT SELYRSLGDV LRDVDAKALV RSDFLLIYGD
160 170 180 190 200
VISNINICRA LEEHRLRRKL EKNVSVMTMV FKESSPSHPT RCHEDNVVMA
210 220 230 240 250
VDSATNRVLH FQKTQGLRRF SFPLSLFQGS GDGVEIRYDL LDCHISICSP
260 270 280 290 300
QVAQLFTDNF DYQTRDDFVR GILMNEEVLG NQIHLHVTTR EYGARVSNLH
310 320 330 340 350
MYSAVCADVI RRWVYPLTPE VNFTDSTTQS YTHSRHNIYR GPEVSLGHGS
360 370 380 390 400
VLEENVLLGA GTVIGSNCSI TNSVIGPNCH IGDNVVLDQA YLWQGVRVAA
410 420 430 440 450
GAQIHQSLLC DRAEVKERVK LKPYCVLTSQ VVVGPDITLP EGSVISLHPP
460 470 480 490 500
DAEEDEDDGQ FSDDSGADQE KEKVKLKGYN PAEVGLEGQG YLWKAEGVNS
510 520 530 540 550
KEDEELRQSL WGLMIKTEEE SETESEGSVD PEELDSRAGS PQLDDIRVFQ
560 570 580 590 600
NEVLGTLQRG REENISCENL VLEINSLKHA YNISLKEVMQ VLTLVVLEFP
610 620 630 640 650
LQQVDGLLDP NRYCALLLPL LKAWSPVLRN YIKRAADHLE ALAAIEDFFL
660 670 680 690 700
EHETLVTSMA KVLMAFYQLE ILAEETILSW FSQRDTTDEG QQLRKNQQLQ
710
RFIQWLREAE EESSEDD
Length:717
Mass (Da):80,086
Last modified:March 1, 2003 - v1
Checksum:i61455A437B7D513B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti54 – 541P → H in BAE36132 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK160985 mRNA. Translation: BAE36132.1.
BC038620 mRNA. Translation: AAH38620.1.
BC085255 mRNA. Translation: AAH85255.1.
CCDSiCCDS28047.1.
RefSeqiNP_758469.1. NM_172265.2.
UniGeneiMm.233855.

Genome annotation databases

EnsembliENSMUST00000003320; ENSMUSP00000003320; ENSMUSG00000003235.
GeneIDi224045.
KEGGimmu:224045.
UCSCiuc007ypu.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK160985 mRNA. Translation: BAE36132.1.
BC038620 mRNA. Translation: AAH38620.1.
BC085255 mRNA. Translation: AAH85255.1.
CCDSiCCDS28047.1.
RefSeqiNP_758469.1. NM_172265.2.
UniGeneiMm.233855.

3D structure databases

ProteinModelPortaliQ8CHW4.
SMRiQ8CHW4. Positions 343-368, 543-711.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000003320.

PTM databases

iPTMnetiQ8CHW4.
PhosphoSiteiQ8CHW4.

Proteomic databases

EPDiQ8CHW4.
MaxQBiQ8CHW4.
PaxDbiQ8CHW4.
PRIDEiQ8CHW4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000003320; ENSMUSP00000003320; ENSMUSG00000003235.
GeneIDi224045.
KEGGimmu:224045.
UCSCiuc007ypu.2. mouse.

Organism-specific databases

CTDi8893.
MGIiMGI:2446176. Eif2b5.

Phylogenomic databases

eggNOGiKOG1461. Eukaryota.
COG1208. LUCA.
GeneTreeiENSGT00510000047568.
HOGENOMiHOG000216610.
HOVERGENiHBG051460.
InParanoidiQ8CHW4.
KOiK03240.
OMAiINALRCK.
OrthoDBiEOG7PGDQ9.
PhylomeDBiQ8CHW4.
TreeFamiTF101509.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ8CHW4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CHW4.
ExpressionAtlasiQ8CHW4. baseline and differential.
GenevisibleiQ8CHW4. MM.

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

  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: Head.
  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: Liver and Mammary tumor.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiEI2BE_MOUSE
AccessioniPrimary (citable) accession number: Q8CHW4
Secondary accession number(s): Q3TU39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 105 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.