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Q13144

- EI2BE_HUMAN

UniProt

Q13144 - EI2BE_HUMAN

Protein

Translation initiation factor eIF-2B subunit epsilon

Gene

EIF2B5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 3 (23 Oct 2007)
      Previous versions | rss
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    Functioni

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

    GO - Molecular functioni

    1. guanyl-nucleotide exchange factor activity Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. translation initiation factor activity Source: UniProtKB
    4. translation initiation factor binding Source: UniProtKB

    GO - Biological processi

    1. astrocyte development Source: UniProtKB
    2. astrocyte differentiation Source: UniProtKB
    3. cellular protein metabolic process Source: Reactome
    4. cellular response to drug Source: UniProtKB
    5. gene expression Source: Reactome
    6. myelination Source: UniProtKB
    7. negative regulation of translational initiation in response to stress Source: UniProtKB
    8. oligodendrocyte development Source: UniProtKB
    9. ovarian follicle development Source: UniProtKB
    10. positive regulation of GTPase activity Source: GOC
    11. positive regulation of translational initiation Source: UniProtKB
    12. response to endoplasmic reticulum stress Source: UniProtKB
    13. response to glucose Source: UniProtKB
    14. response to heat Source: UniProtKB
    15. response to peptide hormone Source: UniProtKB
    16. translation Source: Reactome
    17. translational initiation Source: UniProtKB

    Keywords - Molecular functioni

    Initiation factor

    Keywords - Biological processi

    Protein biosynthesis

    Enzyme and pathway databases

    ReactomeiREACT_1815. 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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:3261. EIF2B5.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. eukaryotic translation initiation factor 2B complex Source: UniProtKB
    4. nucleus Source: UniProtKB

    Pathology & Biotechi

    Involvement in diseasei

    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.6 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti62 – 621D → V in VWM. 1 Publication
    VAR_068457
    Natural varianti68 – 681L → S in VWM. 1 Publication
    VAR_068458
    Natural varianti73 – 731V → G in VWM. 1 Publication
    VAR_012323
    Natural varianti74 – 741A → T in VWM. 1 Publication
    VAR_068459
    Natural varianti91 – 911T → A in VWM. 1 Publication
    Corresponds to variant rs28939717 [ dbSNP | Ensembl ].
    VAR_012291
    Natural varianti106 – 1061L → F in VWM. 1 Publication
    VAR_012324
    Natural varianti113 – 1131R → C in VWM. 1 Publication
    VAR_068460
    Natural varianti113 – 1131R → H in VWM; with ovarian failure. 3 Publications
    Corresponds to variant rs113994049 [ dbSNP | Ensembl ].
    VAR_012292
    Natural varianti195 – 1951R → C in VWM; with ovarian failure. 1 Publication
    VAR_016845
    Natural varianti195 – 1951R → H in VWM; Cree leukoencephalopathy type. 1 Publication
    VAR_016846
    Natural varianti269 – 2691R → G in VWM. 1 Publication
    VAR_068461
    Natural varianti269 – 2691R → Q in VWM. 1 Publication
    VAR_068462
    Natural varianti270 – 2701D → H in VWM. 1 Publication
    VAR_068463
    Natural varianti299 – 2991R → H in VWM. 1 Publication
    VAR_012325
    Natural varianti310 – 3101C → F in VWM. 1 Publication
    VAR_068464
    Natural varianti315 – 3151R → C in VWM. 1 Publication
    VAR_068465
    Natural varianti315 – 3151R → G in VWM. 1 Publication
    VAR_012326
    Natural varianti315 – 3151R → H in VWM. 1 Publication
    VAR_012327
    Natural varianti335 – 3351C → R in VWM. 1 Publication
    VAR_068466
    Natural varianti335 – 3351C → S in VWM. 1 Publication
    VAR_068467
    Natural varianti339 – 3391R → P in VWM. 2 Publications
    VAR_012328
    Natural varianti339 – 3391R → Q in VWM. 1 Publication
    VAR_012329
    Natural varianti339 – 3391R → W in VWM. 1 Publication
    VAR_012330
    Natural varianti376 – 3761N → D in VWM. 1 Publication
    VAR_068468
    Natural varianti386 – 3861G → V in VWM. 2 Publications
    VAR_012293
    Natural varianti430 – 4301V → A in VWM. 1 Publication
    VAR_012331
    Natural varianti447 – 4471S → L in VWM. 1 Publication
    VAR_068469
    Natural varianti628 – 6281W → R in VWM. 1 Publication
    Corresponds to variant rs28937596 [ dbSNP | Ensembl ].
    VAR_012294
    Natural varianti650 – 6501E → K in VWM. 1 Publication
    VAR_012333

    Keywords - Diseasei

    Disease mutation, Leukodystrophy

    Organism-specific databases

    MIMi603896. phenotype.
    Orphaneti99854. Cree leukoencephalopathy.
    157716. Late infantile CACH syndrome.
    99853. Ovarioleukodystrophy.
    PharmGKBiPA27692.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 721720Translation initiation factor eIF-2B subunit epsilonPRO_0000156073Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei27 – 271PhosphoserineBy similarity
    Cross-linki61 – 61Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki103 – 103Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei130 – 1301PhosphoserineBy similarity
    Cross-linki141 – 141Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki217 – 217Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei322 – 3221PhosphothreonineBy similarity
    Modified residuei544 – 5441Phosphoserine; by DYRK26 Publications
    Modified residuei717 – 7171Phosphoserine2 Publications
    Modified residuei718 – 7181Phosphoserine2 Publications

    Post-translational modificationi

    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.By similarity7 Publications
    Polyubiquitinated, probably by NEDD4.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ13144.
    PaxDbiQ13144.
    PRIDEiQ13144.

    PTM databases

    PhosphoSiteiQ13144.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13144.
    BgeeiQ13144.
    CleanExiHS_EIF2B5.
    GenevestigatoriQ13144.

    Organism-specific databases

    HPAiCAB015412.

    Interactioni

    Subunit structurei

    Complex of five different subunits; alpha, beta, gamma, delta and epsilon. Interacts with RGS2.1 Publication

    Protein-protein interaction databases

    BioGridi114410. 8 interactions.
    IntActiQ13144. 1 interaction.
    MINTiMINT-3027192.
    STRINGi9606.ENSP00000273783.

    Structurei

    Secondary structure

    1
    721
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi548 – 56720
    Helixi571 – 58414
    Helixi589 – 60214
    Helixi603 – 6075
    Helixi614 – 63522
    Helixi639 – 65517
    Helixi657 – 6626
    Helixi663 – 67210
    Helixi678 – 6858
    Helixi693 – 6975
    Helixi701 – 71414

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3JUIX-ray2.00A548-721[»]
    ProteinModelPortaliQ13144.
    SMRiQ13144. Positions 342-451, 547-715.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13144.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini543 – 720178W2PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi505 – 5095Poly-Glu

    Sequence similaritiesi

    Contains 1 W2 domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1208.
    HOGENOMiHOG000216610.
    HOVERGENiHBG051460.
    InParanoidiQ13144.
    KOiK03240.
    OMAiESEQSMD.
    OrthoDBiEOG7PGDQ9.
    PhylomeDBiQ13144.
    TreeFamiTF101509.

    Family and domain databases

    Gene3Di1.25.40.180. 1 hit.
    3.90.550.10. 1 hit.
    InterProiIPR016024. ARM-type_fold.
    IPR001451. Hexapep_transf.
    IPR016021. MIF4-like_typ_1/2/3.
    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.

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

    Q13144-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAPVVAPPG VVVSRANKRS GAGPGGSGGG GARGAEEEPP PPLQAVLVAD    50
    SFDRRFFPIS KDQPRVLLPL ANVALIDYTL EFLTATGVQE TFVFCCWKAA 100
    QIKEHLLKSK WCRPTSLNVV RIITSELYRS LGDVLRDVDA KALVRSDFLL 150
    VYGDVISNIN ITRALEEHRL RRKLEKNVSV MTMIFKESSP SHPTRCHEDN 200
    VVVAVDSTTN RVLHFQKTQG LRRFAFPLSL FQGSSDGVEV RYDLLDCHIS 250
    ICSPQVAQLF TDNFDYQTRD DFVRGLLVNE EILGNQIHMH VTAKEYGARV 300
    SNLHMYSAVC ADVIRRWVYP LTPEANFTDS TTQSCTHSRH NIYRGPEVSL 350
    GHGSILEENV LLGSGTVIGS NCFITNSVIG PGCHIGDNVV LDQTYLWQGV 400
    RVAAGAQIHQ SLLCDNAEVK ERVTLKPRSV LTSQVVVGPN ITLPEGSVIS 450
    LHPPDAEEDE DDGEFSDDSG ADQEKDKVKM KGYNPAEVGA AGKGYLWKAA 500
    GMNMEEEEEL QQNLWGLKIN MEEESESESE QSMDSEEPDS RGGSPQMDDI 550
    KVFQNEVLGT LQRGKEENIS CDNLVLEINS LKYAYNISLK EVMQVLSHVV 600
    LEFPLQQMDS PLDSSRYCAL LLPLLKAWSP VFRNYIKRAA DHLEALAAIE 650
    DFFLEHEALG ISMAKVLMAF YQLEILAEET ILSWFSQRDT TDKGQQLRKN 700
    QQLQRFIQWL KEAEEESSED D 721
    Length:721
    Mass (Da):80,380
    Last modified:October 23, 2007 - v3
    Checksum:i08B39D3A5EE7D905
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti62 – 621D → V in VWM. 1 Publication
    VAR_068457
    Natural varianti68 – 681L → S in VWM. 1 Publication
    VAR_068458
    Natural varianti73 – 731V → G in VWM. 1 Publication
    VAR_012323
    Natural varianti74 – 741A → T in VWM. 1 Publication
    VAR_068459
    Natural varianti91 – 911T → A in VWM. 1 Publication
    Corresponds to variant rs28939717 [ dbSNP | Ensembl ].
    VAR_012291
    Natural varianti106 – 1061L → F in VWM. 1 Publication
    VAR_012324
    Natural varianti113 – 1131R → C in VWM. 1 Publication
    VAR_068460
    Natural varianti113 – 1131R → H in VWM; with ovarian failure. 3 Publications
    Corresponds to variant rs113994049 [ dbSNP | Ensembl ].
    VAR_012292
    Natural varianti195 – 1951R → C in VWM; with ovarian failure. 1 Publication
    VAR_016845
    Natural varianti195 – 1951R → H in VWM; Cree leukoencephalopathy type. 1 Publication
    VAR_016846
    Natural varianti200 – 2001N → T.
    Corresponds to variant rs2971409 [ dbSNP | Ensembl ].
    VAR_048919
    Natural varianti269 – 2691R → G in VWM. 1 Publication
    VAR_068461
    Natural varianti269 – 2691R → Q in VWM. 1 Publication
    VAR_068462
    Natural varianti270 – 2701D → H in VWM. 1 Publication
    VAR_068463
    Natural varianti299 – 2991R → H in VWM. 1 Publication
    VAR_012325
    Natural varianti310 – 3101C → F in VWM. 1 Publication
    VAR_068464
    Natural varianti315 – 3151R → C in VWM. 1 Publication
    VAR_068465
    Natural varianti315 – 3151R → G in VWM. 1 Publication
    VAR_012326
    Natural varianti315 – 3151R → H in VWM. 1 Publication
    VAR_012327
    Natural varianti335 – 3351C → R in VWM. 1 Publication
    VAR_068466
    Natural varianti335 – 3351C → S in VWM. 1 Publication
    VAR_068467
    Natural varianti339 – 3391R → P in VWM. 2 Publications
    VAR_012328
    Natural varianti339 – 3391R → Q in VWM. 1 Publication
    VAR_012329
    Natural varianti339 – 3391R → W in VWM. 1 Publication
    VAR_012330
    Natural varianti376 – 3761N → D in VWM. 1 Publication
    VAR_068468
    Natural varianti386 – 3861G → V in VWM. 2 Publications
    VAR_012293
    Natural varianti430 – 4301V → A in VWM. 1 Publication
    VAR_012331
    Natural varianti447 – 4471S → L in VWM. 1 Publication
    VAR_068469
    Natural varianti587 – 5871I → V.5 Publications
    Corresponds to variant rs843358 [ dbSNP | Ensembl ].
    VAR_012332
    Natural varianti628 – 6281W → R in VWM. 1 Publication
    Corresponds to variant rs28937596 [ dbSNP | Ensembl ].
    VAR_012294
    Natural varianti650 – 6501E → K in VWM. 1 Publication
    VAR_012333

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS3252.1.
    RefSeqiNP_003898.2. NM_003907.2.
    UniGeneiHs.283551.

    Genome annotation databases

    EnsembliENST00000273783; ENSP00000273783; ENSG00000145191.
    GeneIDi8893.
    KEGGihsa:8893.
    UCSCiuc003fmp.3. human.

    Polymorphism databases

    DMDMi160359049.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Mendelian genes eukaryotic translation initiation factor 2B, subunit 5 epsilon, 82kDa (EIF2B5)

    Leiden Open Variation Database (LOVD)

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS3252.1.
    RefSeqi NP_003898.2. NM_003907.2.
    UniGenei Hs.283551.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3JUI X-ray 2.00 A 548-721 [» ]
    ProteinModelPortali Q13144.
    SMRi Q13144. Positions 342-451, 547-715.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114410. 8 interactions.
    IntActi Q13144. 1 interaction.
    MINTi MINT-3027192.
    STRINGi 9606.ENSP00000273783.

    PTM databases

    PhosphoSitei Q13144.

    Polymorphism databases

    DMDMi 160359049.

    Proteomic databases

    MaxQBi Q13144.
    PaxDbi Q13144.
    PRIDEi Q13144.

    Protocols and materials databases

    DNASUi 8893.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000273783 ; ENSP00000273783 ; ENSG00000145191 .
    GeneIDi 8893.
    KEGGi hsa:8893.
    UCSCi uc003fmp.3. human.

    Organism-specific databases

    CTDi 8893.
    GeneCardsi GC03P183852.
    GeneReviewsi EIF2B5.
    H-InvDB HIX0003921.
    HGNCi HGNC:3261. EIF2B5.
    HPAi CAB015412.
    MIMi 603896. phenotype.
    603945. gene.
    neXtProti NX_Q13144.
    Orphaneti 99854. Cree leukoencephalopathy.
    157716. Late infantile CACH syndrome.
    99853. Ovarioleukodystrophy.
    PharmGKBi PA27692.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1208.
    HOGENOMi HOG000216610.
    HOVERGENi HBG051460.
    InParanoidi Q13144.
    KOi K03240.
    OMAi ESEQSMD.
    OrthoDBi EOG7PGDQ9.
    PhylomeDBi Q13144.
    TreeFami TF101509.

    Enzyme and pathway databases

    Reactomei REACT_1815. Recycling of eIF2:GDP.

    Miscellaneous databases

    EvolutionaryTracei Q13144.
    GeneWikii EIF2B5.
    GenomeRNAii 8893.
    NextBioi 33399.
    PROi Q13144.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13144.
    Bgeei Q13144.
    CleanExi HS_EIF2B5.
    Genevestigatori Q13144.

    Family and domain databases

    Gene3Di 1.25.40.180. 1 hit.
    3.90.550.10. 1 hit.
    InterProi IPR016024. ARM-type_fold.
    IPR001451. Hexapep_transf.
    IPR016021. MIF4-like_typ_1/2/3.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR011004. Trimer_LpxA-like.
    IPR003307. W2_domain.
    [Graphical view ]
    Pfami PF00132. Hexapep. 1 hit.
    PF02020. W2. 1 hit.
    [Graphical view ]
    SMARTi SM00515. eIF5C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    SSF51161. SSF51161. 1 hit.
    SSF53448. SSF53448. 2 hits.
    PROSITEi PS51363. W2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. 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. 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. 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. 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. Cited for: VARIANT VWM HIS-195.
    20. 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.

    Entry informationi

    Entry nameiEI2BE_HUMAN
    AccessioniPrimary (citable) accession number: Q13144
    Secondary accession number(s): Q541Z1, Q96D04
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: October 23, 2007
    Last modified: October 1, 2014
    This is version 144 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3