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Q13144 (EI2BE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Translation initiation factor eIF-2B subunit epsilon
Alternative name(s):
eIF-2B GDP-GTP exchange factor subunit epsilon
Gene names
Name:EIF2B5
Synonyms:EIF2BE
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length721 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Complex of five different subunits; alpha, beta, gamma, delta and epsilon. Interacts with RGS2. Ref.11

Post-translational modification

Phosphorylated at Ser-544 by DYRK2; this is required for subsequent phosphorylation by GSK3B By similarity. Phosphorylated on serine and threonine residues by GSK3B; phosphorylation inhibits its function. Ref.6

Polyubiquitinated, probably by NEDD4 By similarity.

Involvement in disease

Leukodystrophy with vanishing white matter (VWM) [MIM:603896]: A leukodystrophy that occurs mainly in children. Neurological signs include progressive cerebellar ataxia, spasticity, inconstant optic atrophy and relatively preserved mental abilities. The disease is chronic-progressive with, in most individuals, additional episodes of rapid deterioration following febrile infections or minor head trauma. While childhood onset is the most common form of the disorder, some severe forms are apparent at birth. A severe, early-onset form seen among the Cree and Chippewayan populations of Quebec and Manitoba is called Cree leukoencephalopathy. Milder forms may not become evident until adolescence or adulthood. Some females with milder forms of the disease who survive to adolescence exhibit ovarian dysfunction. This variant of the disorder is called ovarioleukodystrophy.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23

Sequence similarities

Belongs to the eIF-2B gamma/epsilon subunits family.

Contains 1 W2 domain.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Leukodystrophy
   Molecular functionInitiation factor
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processastrocyte development

Inferred from mutant phenotype PubMed 15723074. Source: UniProtKB

astrocyte differentiation

Inferred from mutant phenotype PubMed 15723074. Source: UniProtKB

cellular protein metabolic process

Traceable author statement. Source: Reactome

cellular response to drug

Inferred from direct assay PubMed 8626696. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

myelination

Inferred from mutant phenotype PubMed 14566705PubMed 15723074. Source: UniProtKB

negative regulation of translational initiation in response to stress

Inferred from sequence or structural similarity. Source: UniProtKB

oligodendrocyte development

Inferred from mutant phenotype PubMed 15217090. Source: UniProtKB

ovarian follicle development

Inferred from mutant phenotype PubMed 15507143. Source: UniProtKB

positive regulation of translational initiation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of GTPase activity

Inferred from direct assay PubMed 11323413. Source: GOC

response to endoplasmic reticulum stress

Inferred from mutant phenotype PubMed 16041584. Source: UniProtKB

response to glucose

Inferred from sequence or structural similarity. Source: UniProtKB

response to heat

Inferred from mutant phenotype PubMed 15723074. Source: UniProtKB

response to peptide hormone

Inferred from sequence or structural similarity. Source: UniProtKB

translation

Traceable author statement. Source: Reactome

translational initiation

Inferred from direct assay PubMed 16289705. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 11323413. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

eukaryotic translation initiation factor 2B complex

Inferred from direct assay PubMed 11323413PubMed 15060152. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionguanyl-nucleotide exchange factor activity

Inferred from mutant phenotype PubMed 15054402. Source: UniProtKB

translation initiation factor activity

Non-traceable author statement Ref.5. Source: UniProtKB

translation initiation factor binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 721720Translation initiation factor eIF-2B subunit epsilon
PRO_0000156073

Regions

Domain543 – 720178W2
Compositional bias505 – 5095Poly-Glu

Amino acid modifications

Modified residue21N-acetylalanine Ref.10 Ref.16 Ref.17
Modified residue271Phosphoserine By similarity
Modified residue1301Phosphoserine By similarity
Modified residue3221Phosphothreonine By similarity
Modified residue5441Phosphoserine; by DYRK2 Ref.7 Ref.8 Ref.9 Ref.13 Ref.15
Modified residue7171Phosphoserine Ref.12
Modified residue7181Phosphoserine Ref.12
Cross-link61Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link103Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link141Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link217Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Natural variant621D → V in VWM. Ref.22
VAR_068457
Natural variant681L → S in VWM. Ref.21
VAR_068458
Natural variant731V → G in VWM. Ref.18
VAR_012323
Natural variant741A → T in VWM. Ref.21
VAR_068459
Natural variant911T → A in VWM. Ref.18
Corresponds to variant rs28939717 [ dbSNP | Ensembl ].
VAR_012291
Natural variant1061L → F in VWM. Ref.18
VAR_012324
Natural variant1131R → C in VWM. Ref.22
VAR_068460
Natural variant1131R → H in VWM; with ovarian failure. Ref.18 Ref.20 Ref.21
Corresponds to variant rs113994049 [ dbSNP | Ensembl ].
VAR_012292
Natural variant1951R → C in VWM; with ovarian failure. Ref.20
VAR_016845
Natural variant1951R → H in VWM; Cree leukoencephalopathy type. Ref.19
VAR_016846
Natural variant2001N → T.
Corresponds to variant rs2971409 [ dbSNP | Ensembl ].
VAR_048919
Natural variant2691R → G in VWM. Ref.21
VAR_068461
Natural variant2691R → Q in VWM. Ref.22
VAR_068462
Natural variant2701D → H in VWM. Ref.23
VAR_068463
Natural variant2991R → H in VWM. Ref.18
VAR_012325
Natural variant3101C → F in VWM. Ref.21
VAR_068464
Natural variant3151R → C in VWM. Ref.22
VAR_068465
Natural variant3151R → G in VWM. Ref.18
VAR_012326
Natural variant3151R → H in VWM. Ref.18
VAR_012327
Natural variant3351C → R in VWM. Ref.21
VAR_068466
Natural variant3351C → S in VWM. Ref.22
VAR_068467
Natural variant3391R → P in VWM. Ref.18 Ref.22
VAR_012328
Natural variant3391R → Q in VWM. Ref.18
VAR_012329
Natural variant3391R → W in VWM. Ref.18
VAR_012330
Natural variant3761N → D in VWM. Ref.22
VAR_068468
Natural variant3861G → V in VWM. Ref.18 Ref.22
VAR_012293
Natural variant4301V → A in VWM. Ref.18
VAR_012331
Natural variant4471S → L in VWM. Ref.22
VAR_068469
Natural variant5871I → V. Ref.1 Ref.3 Ref.4 Ref.5 Ref.18
Corresponds to variant rs843358 [ dbSNP | Ensembl ].
VAR_012332
Natural variant6281W → R in VWM. Ref.18
Corresponds to variant rs28937596 [ dbSNP | Ensembl ].
VAR_012294
Natural variant6501E → K in VWM. Ref.18
VAR_012333

Secondary structure

..................... 721
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q13144 [UniParc].

Last modified October 23, 2007. Version 3.
Checksum: 08B39D3A5EE7D905

FASTA72180,380
        10         20         30         40         50         60 
MAAPVVAPPG VVVSRANKRS GAGPGGSGGG GARGAEEEPP PPLQAVLVAD SFDRRFFPIS 

        70         80         90        100        110        120 
KDQPRVLLPL ANVALIDYTL EFLTATGVQE TFVFCCWKAA QIKEHLLKSK WCRPTSLNVV 

       130        140        150        160        170        180 
RIITSELYRS LGDVLRDVDA KALVRSDFLL VYGDVISNIN ITRALEEHRL RRKLEKNVSV 

       190        200        210        220        230        240 
MTMIFKESSP SHPTRCHEDN VVVAVDSTTN RVLHFQKTQG LRRFAFPLSL FQGSSDGVEV 

       250        260        270        280        290        300 
RYDLLDCHIS ICSPQVAQLF TDNFDYQTRD DFVRGLLVNE EILGNQIHMH VTAKEYGARV 

       310        320        330        340        350        360 
SNLHMYSAVC ADVIRRWVYP LTPEANFTDS TTQSCTHSRH NIYRGPEVSL GHGSILEENV 

       370        380        390        400        410        420 
LLGSGTVIGS NCFITNSVIG PGCHIGDNVV LDQTYLWQGV RVAAGAQIHQ SLLCDNAEVK 

       430        440        450        460        470        480 
ERVTLKPRSV LTSQVVVGPN ITLPEGSVIS LHPPDAEEDE DDGEFSDDSG ADQEKDKVKM 

       490        500        510        520        530        540 
KGYNPAEVGA AGKGYLWKAA GMNMEEEEEL QQNLWGLKIN MEEESESESE QSMDSEEPDS 

       550        560        570        580        590        600 
RGGSPQMDDI KVFQNEVLGT LQRGKEENIS CDNLVLEINS LKYAYNISLK EVMQVLSHVV 

       610        620        630        640        650        660 
LEFPLQQMDS PLDSSRYCAL LLPLLKAWSP VFRNYIKRAA DHLEALAAIE DFFLEHEALG 

       670        680        690        700        710        720 
ISMAKVLMAF YQLEILAEET ILSWFSQRDT TDKGQQLRKN QQLQRFIQWL KEAEEESSED 


D 

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References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-587.
Tissue: Brain.
[2]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-587.
[4]"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], VARIANT VAL-587.
Tissue: Lung.
[5]"Cloning and characterization of cDNAs encoding the epsilon-subunit of eukaryotic initiation factor-2B from rabbit and human."
Asuru A.I., Mellor H., Thomas N.S.B., Yu L., Chen J.-J., Crosby J.S., Hartson S.D., Kimball S.R., Jefferson L.S., Matts R.L.
Biochim. Biophys. Acta 1307:309-317(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 81-721, VARIANT VAL-587.
[6]"Glycogen synthase kinase-3 is rapidly inactivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B."
Welsh G.I., Proud C.G.
Biochem. J. 294:625-629(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY GSK3B.
[7]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[8]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[11]"Translational control by RGS2."
Nguyen C.H., Ming H., Zhao P., Hugendubler L., Gros R., Kimball S.R., Chidiac P.
J. Cell Biol. 186:755-765(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RGS2.
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-717 AND SER-718, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Subunits of the translation initiation factor eIF2B are mutant in leukoencephalopathy with vanishing white matter."
Leegwater P.A.J., Vermeulen G., Koenst A.A.M., Naidu S., Mulders J., Visser A., Kersbergen P., Mobach D., Fonds D., van Berkel C.G.M., Lemmers R.J.L.F., Frants R.R., Oudejans C.B.M., Schutgens R.B.H., Pronk J.C., van der Knaap M.S.
Nat. Genet. 29:383-388(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VWM GLY-73; ALA-91; PHE-106; HIS-113; HIS-299; GLY-315; HIS-315; PRO-339; GLN-339; TRP-339; VAL-386; ALA-430; ARG-628 AND LYS-650, VARIANT VAL-587.
[19]"Cree leukoencephalopathy and CACH/VWM disease are allelic at the EIF2B5 locus."
Fogli A., Wong K., Eymard-Pierre E., Wenger J., Bouffard J.-P., Goldin E., Black D.N., Boespflug-Tanguy O., Schiffmann R.
Ann. Neurol. 52:506-510(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VWM HIS-195.
[20]"Ovarian failure related to eukaryotic initiation factor 2B mutations."
Fogli A., Rodriguez D., Eymard-Pierre E., Bouhour F., Labauge P., Meaney B.F., Zeesman S., Kaneski C.R., Schiffmann R., Boespflug-Tanguy O.
Am. J. Hum. Genet. 72:1544-1550(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VWM HIS-113 AND CYS-195.
[21]"Identification of ten novel mutations in patients with eIF2B-related disorders."
Ohlenbusch A., Henneke M., Brockmann K., Goerg M., Hanefeld F., Kohlschutter A., Gartner J.
Hum. Mutat. 25:411-411(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VWM SER-68; THR-74; HIS-113; GLY-269; PHE-310 AND ARG-335.
[22]"Identification of novel EIF2B mutations in Chinese patients with vanishing white matter disease."
Wu Y., Pan Y., Du L., Wang J., Gu Q., Gao Z., Li J., Leng X., Qin J., Wu X., Jiang Y.
J. Hum. Genet. 54:74-77(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VWM VAL-62; CYS-113; GLN-269; CYS-315; SER-335; PRO-339; ASP-376; VAL-386 AND LEU-447.
[23]"Adult-onset leukoencephalopathies with vanishing white matter with novel missense mutations in EIF2B2, EIF2B3, and EIF2B5."
Matsukawa T., Wang X., Liu R., Wortham N.C., Onuki Y., Kubota A., Hida A., Kowa H., Fukuda Y., Ishiura H., Mitsui J., Takahashi Y., Aoki S., Takizawa S., Shimizu J., Goto J., Proud C.G., Tsuji S.
Neurogenetics 12:259-261(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VWM HIS-270.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK091646 mRNA. Translation: BAC03712.1.
AC131235 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78299.1.
BC013590 mRNA. Translation: AAH13590.1.
U23028 mRNA. Translation: AAC50646.1.
RefSeqNP_003898.2. NM_003907.2.
UniGeneHs.283551.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3JUIX-ray2.00A547-721[»]
ProteinModelPortalQ13144.
SMRQ13144. Positions 335-454, 547-715.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114410. 8 interactions.
IntActQ13144. 1 interaction.
MINTMINT-3027192.
STRING9606.ENSP00000273783.

PTM databases

PhosphoSiteQ13144.

Polymorphism databases

DMDM160359049.

Proteomic databases

PaxDbQ13144.
PRIDEQ13144.

Protocols and materials databases

DNASU8893.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000273783; ENSP00000273783; ENSG00000145191.
GeneID8893.
KEGGhsa:8893.
UCSCuc003fmp.3. human.

Organism-specific databases

CTD8893.
GeneCardsGC03P183852.
H-InvDBHIX0003921.
HGNCHGNC:3261. EIF2B5.
HPACAB015412.
MIM603896. phenotype.
603945. gene.
neXtProtNX_Q13144.
Orphanet99854. Cree leukoencephalopathy.
157716. Late infantile CACH syndrome.
99853. Ovarioleukodystrophy.
PharmGKBPA27692.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1208.
HOGENOMHOG000216610.
HOVERGENHBG051460.
InParanoidQ13144.
KOK03240.
OMAESEQSMD.
OrthoDBEOG7PGDQ9.
PhylomeDBQ13144.
TreeFamTF101509.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ13144.
BgeeQ13144.
CleanExHS_EIF2B5.
GenevestigatorQ13144.

Family and domain databases

Gene3D1.25.40.180. 1 hit.
InterProIPR016024. ARM-type_fold.
IPR001451. Hexapep_transf.
IPR016021. MIF4-like_typ_1/2/3.
IPR011004. Trimer_LpxA-like.
IPR003307. W2_domain.
[Graphical view]
PfamPF00132. Hexapep. 1 hit.
PF02020. W2. 1 hit.
[Graphical view]
SMARTSM00515. eIF5C. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
SSF51161. SSF51161. 1 hit.
PROSITEPS51363. W2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ13144.
GeneWikiEIF2B5.
GenomeRNAi8893.
NextBio33399.
PROQ13144.
SOURCESearch...

Entry information

Entry nameEI2BE_HUMAN
AccessionPrimary (citable) accession number: Q13144
Secondary accession number(s): Q541Z1, Q96D04
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 23, 2007
Last modified: April 16, 2014
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM