Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P13639

- EF2_HUMAN

UniProt

P13639 - EF2_HUMAN

Protein

Elongation factor 2

Gene

EEF2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi26 – 338GTPBy similarity
    Nucleotide bindingi104 – 1085GTPBy similarity
    Nucleotide bindingi158 – 1614GTPBy similarity

    GO - Molecular functioni

    1. GTPase activity Source: Ensembl
    2. GTP binding Source: UniProtKB-KW
    3. poly(A) RNA binding Source: UniProtKB
    4. protein kinase binding Source: UniProt
    5. translation activator activity Source: UniProt
    6. translation elongation factor activity Source: UniProtKB-KW

    GO - Biological processi

    1. cell death Source: UniProtKB-KW
    2. cellular protein metabolic process Source: Reactome
    3. gene expression Source: Reactome
    4. positive regulation of gene expression Source: UniProt
    5. positive regulation of translation Source: UniProt
    6. translation Source: Reactome
    7. translational elongation Source: Reactome

    Keywords - Molecular functioni

    Elongation factor

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_1404. Peptide chain elongation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Elongation factor 2
    Short name:
    EF-2
    Gene namesi
    Name:EEF2
    Synonyms:EF2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:3214. EEF2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. membrane Source: UniProtKB
    4. nucleus Source: UniProt
    5. polysome Source: Ensembl
    6. ribonucleoprotein complex Source: MGI

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Spinocerebellar ataxia 26 (SCA26) [MIM:609306]: A form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti596 – 5961P → H in SCA26; compromises the mechanics of translocation. 1 Publication
    VAR_070792

    Keywords - Diseasei

    Disease mutation, Neurodegeneration, Spinocerebellar ataxia

    Organism-specific databases

    MIMi609306. phenotype.
    Orphaneti101112. Spinocerebellar ataxia type 26.
    PharmGKBiPA27650.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 858857Elongation factor 2PRO_0000091000Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei54 – 541Phosphothreonine1 Publication
    Modified residuei57 – 571Phosphothreonine2 Publications
    Modified residuei59 – 591Phosphothreonine2 Publications
    Modified residuei152 – 1521N6-succinyllysineBy similarity
    Modified residuei235 – 2351N6-acetyllysine1 Publication
    Modified residuei239 – 2391N6-acetyllysine1 Publication
    Modified residuei272 – 2721N6-acetyllysine; alternate1 Publication
    Modified residuei272 – 2721N6-succinyllysine; alternateBy similarity
    Modified residuei275 – 2751N6-acetyllysine1 Publication
    Modified residuei435 – 4351Phosphothreonine2 Publications
    Modified residuei439 – 4391N6-acetyllysineBy similarity
    Modified residuei445 – 4451N6-acetyllysine1 Publication
    Modified residuei502 – 5021Phosphoserine1 Publication
    Modified residuei572 – 5721N6-succinyllysineBy similarity
    Modified residuei619 – 6191N6-acetyllysineBy similarity
    Modified residuei715 – 7151DiphthamideBy similarity

    Post-translational modificationi

    Phosphorylation by EF-2 kinase completely inactivates EF-2.3 Publications
    Diphthamide is 2-[3-carboxyamido-3-(trimethyl-ammonio)propyl]histidine. Diphthamide can be ADP-ribosylated by diphtheria toxin and by Pseudomonas exotoxin A, thus arresting protein synthesis By similarity.By similarity
    ISGylated.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP13639.
    PaxDbiP13639.
    PeptideAtlasiP13639.
    PRIDEiP13639.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00186290.

    PTM databases

    PhosphoSiteiP13639.

    Expressioni

    Gene expression databases

    ArrayExpressiP13639.
    BgeeiP13639.
    CleanExiHS_EEF2.
    GenevestigatoriP13639.

    Organism-specific databases

    HPAiCAB007795.

    Interactioni

    Subunit structurei

    Component of the mRNA surveillance SURF complex, at least composed of ERF1, ERF3 (ERF3A or ERF3B), EEF2, UPF1/RENT1, SMG1, SMG8 and SMG9.1 Publication

    Protein-protein interaction databases

    BioGridi108258. 122 interactions.
    IntActiP13639. 47 interactions.
    MINTiMINT-4999025.
    STRINGi9606.ENSP00000307940.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Aelectron microscopy5.00z1-858[»]
    ProteinModelPortaliP13639.
    SMRiP13639. Positions 3-858.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini17 – 362346tr-type GPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.PROSITE-ProRule annotation
    Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0480.
    HOGENOMiHOG000231589.
    HOVERGENiHBG001838.
    InParanoidiP13639.
    KOiK03234.
    OMAiRWAPVPE.
    OrthoDBiEOG7WDN1S.
    PhylomeDBiP13639.
    TreeFamiTF300575.

    Family and domain databases

    Gene3Di3.30.230.10. 1 hit.
    3.30.70.240. 1 hit.
    3.40.50.300. 1 hit.
    InterProiIPR000795. EF_GTP-bd_dom.
    IPR009022. EFG_III-V.
    IPR000640. EFG_V.
    IPR027417. P-loop_NTPase.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    IPR005225. Small_GTP-bd_dom.
    IPR009000. Transl_B-barrel.
    IPR005517. Transl_elong_EFG/EF2_IV.
    IPR004161. Transl_elong_EFTu/EF1A_2.
    [Graphical view]
    PfamiPF00679. EFG_C. 1 hit.
    PF14492. EFG_II. 1 hit.
    PF03764. EFG_IV. 1 hit.
    PF00009. GTP_EFTU. 1 hit.
    PF03144. GTP_EFTU_D2. 1 hit.
    [Graphical view]
    PRINTSiPR00315. ELONGATNFCT.
    SMARTiSM00838. EFG_C. 1 hit.
    SM00889. EFG_IV. 1 hit.
    [Graphical view]
    SUPFAMiSSF50447. SSF50447. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF54211. SSF54211. 1 hit.
    SSF54980. SSF54980. 2 hits.
    TIGRFAMsiTIGR00231. small_GTP. 1 hit.
    PROSITEiPS00301. G_TR_1. 1 hit.
    PS51722. G_TR_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P13639-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVNFTVDQIR AIMDKKANIR NMSVIAHVDH GKSTLTDSLV CKAGIIASAR    50
    AGETRFTDTR KDEQERCITI KSTAISLFYE LSENDLNFIK QSKDGAGFLI 100
    NLIDSPGHVD FSSEVTAALR VTDGALVVVD CVSGVCVQTE TVLRQAIAER 150
    IKPVLMMNKM DRALLELQLE PEELYQTFQR IVENVNVIIS TYGEGESGPM 200
    GNIMIDPVLG TVGFGSGLHG WAFTLKQFAE MYVAKFAAKG EGQLGPAERA 250
    KKVEDMMKKL WGDRYFDPAN GKFSKSATSP EGKKLPRTFC QLILDPIFKV 300
    FDAIMNFKKE ETAKLIEKLD IKLDSEDKDK EGKPLLKAVM RRWLPAGDAL 350
    LQMITIHLPS PVTAQKYRCE LLYEGPPDDE AAMGIKSCDP KGPLMMYISK 400
    MVPTSDKGRF YAFGRVFSGL VSTGLKVRIM GPNYTPGKKE DLYLKPIQRT 450
    ILMMGRYVEP IEDVPCGNIV GLVGVDQFLV KTGTITTFEH AHNMRVMKFS 500
    VSPVVRVAVE AKNPADLPKL VEGLKRLAKS DPMVQCIIEE SGEHIIAGAG 550
    ELHLEICLKD LEEDHACIPI KKSDPVVSYR ETVSEESNVL CLSKSPNKHN 600
    RLYMKARPFP DGLAEDIDKG EVSARQELKQ RARYLAEKYE WDVAEARKIW 650
    CFGPDGTGPN ILTDITKGVQ YLNEIKDSVV AGFQWATKEG ALCEENMRGV 700
    RFDVHDVTLH ADAIHRGGGQ IIPTARRCLY ASVLTAQPRL MEPIYLVEIQ 750
    CPEQVVGGIY GVLNRKRGHV FEESQVAGTP MFVVKAYLPV NESFGFTADL 800
    RSNTGGQAFP QCVFDHWQIL PGDPFDNSSR PSQVVAETRK RKGLKEGIPA 850
    LDNFLDKL 858
    Length:858
    Mass (Da):95,338
    Last modified:January 23, 2007 - v4
    Checksum:i78BD1710236C0D9C
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti596 – 5961P → H in SCA26; compromises the mechanics of translocation. 1 Publication
    VAR_070792

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51466 mRNA. Translation: CAA35829.1.
    Z11692 mRNA. Translation: CAA77750.1.
    AY942181 mRNA. Translation: AAX34409.1.
    CH471139 Genomic DNA. Translation: EAW69274.1.
    CH471139 Genomic DNA. Translation: EAW69275.1.
    BC126259 mRNA. Translation: AAI26260.1.
    BC136313 mRNA. Translation: AAI36314.1.
    M19997 mRNA. Translation: AAA50388.1.
    CCDSiCCDS12117.1.
    PIRiS18294. EFHU2.
    RefSeqiNP_001952.1. NM_001961.3.
    UniGeneiHs.515070.

    Genome annotation databases

    EnsembliENST00000309311; ENSP00000307940; ENSG00000167658.
    GeneIDi1938.
    KEGGihsa:1938.
    UCSCiuc002lze.3. human.

    Polymorphism databases

    DMDMi119172.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51466 mRNA. Translation: CAA35829.1 .
    Z11692 mRNA. Translation: CAA77750.1 .
    AY942181 mRNA. Translation: AAX34409.1 .
    CH471139 Genomic DNA. Translation: EAW69274.1 .
    CH471139 Genomic DNA. Translation: EAW69275.1 .
    BC126259 mRNA. Translation: AAI26260.1 .
    BC136313 mRNA. Translation: AAI36314.1 .
    M19997 mRNA. Translation: AAA50388.1 .
    CCDSi CCDS12117.1.
    PIRi S18294. EFHU2.
    RefSeqi NP_001952.1. NM_001961.3.
    UniGenei Hs.515070.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3J3A electron microscopy 5.00 z 1-858 [» ]
    ProteinModelPortali P13639.
    SMRi P13639. Positions 3-858.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108258. 122 interactions.
    IntActi P13639. 47 interactions.
    MINTi MINT-4999025.
    STRINGi 9606.ENSP00000307940.

    Chemistry

    ChEMBLi CHEMBL1795108.

    PTM databases

    PhosphoSitei P13639.

    Polymorphism databases

    DMDMi 119172.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00186290.

    Proteomic databases

    MaxQBi P13639.
    PaxDbi P13639.
    PeptideAtlasi P13639.
    PRIDEi P13639.

    Protocols and materials databases

    DNASUi 1938.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000309311 ; ENSP00000307940 ; ENSG00000167658 .
    GeneIDi 1938.
    KEGGi hsa:1938.
    UCSCi uc002lze.3. human.

    Organism-specific databases

    CTDi 1938.
    GeneCardsi GC19M003976.
    HGNCi HGNC:3214. EEF2.
    HPAi CAB007795.
    MIMi 130610. gene.
    609306. phenotype.
    neXtProti NX_P13639.
    Orphaneti 101112. Spinocerebellar ataxia type 26.
    PharmGKBi PA27650.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0480.
    HOGENOMi HOG000231589.
    HOVERGENi HBG001838.
    InParanoidi P13639.
    KOi K03234.
    OMAi RWAPVPE.
    OrthoDBi EOG7WDN1S.
    PhylomeDBi P13639.
    TreeFami TF300575.

    Enzyme and pathway databases

    Reactomei REACT_1404. Peptide chain elongation.

    Miscellaneous databases

    ChiTaRSi EEF2. human.
    GeneWikii EEF2.
    GenomeRNAii 1938.
    NextBioi 7853.
    PROi P13639.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P13639.
    Bgeei P13639.
    CleanExi HS_EEF2.
    Genevestigatori P13639.

    Family and domain databases

    Gene3Di 3.30.230.10. 1 hit.
    3.30.70.240. 1 hit.
    3.40.50.300. 1 hit.
    InterProi IPR000795. EF_GTP-bd_dom.
    IPR009022. EFG_III-V.
    IPR000640. EFG_V.
    IPR027417. P-loop_NTPase.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    IPR005225. Small_GTP-bd_dom.
    IPR009000. Transl_B-barrel.
    IPR005517. Transl_elong_EFG/EF2_IV.
    IPR004161. Transl_elong_EFTu/EF1A_2.
    [Graphical view ]
    Pfami PF00679. EFG_C. 1 hit.
    PF14492. EFG_II. 1 hit.
    PF03764. EFG_IV. 1 hit.
    PF00009. GTP_EFTU. 1 hit.
    PF03144. GTP_EFTU_D2. 1 hit.
    [Graphical view ]
    PRINTSi PR00315. ELONGATNFCT.
    SMARTi SM00838. EFG_C. 1 hit.
    SM00889. EFG_IV. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50447. SSF50447. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF54211. SSF54211. 1 hit.
    SSF54980. SSF54980. 2 hits.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS00301. G_TR_1. 1 hit.
    PS51722. G_TR_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequence of the coding region of human elongation factor 2 (EF-2) by enzymatic amplification of cDNA from human ovarian granulosa cells."
      Rapp G., Klaudiny J., Hagendorff G., Luck M.R., Heinz K.
      Biol. Chem. Hoppe-Seyler 370:1071-1075(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Ovary.
    2. "Construction of a plasmid containing the complete coding region of human elongation factor 2."
      Hanes J., Freudenstein J., Rapp G., Scheit K.H.
      Biol. Chem. Hoppe-Seyler 373:201-204(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. Ustek D., Bektas M., Cakiris A., Oku B., Bermek E.
      Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Peripheral blood.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Brain.
    6. "Cloning and sequence analysis of a cDNA from human ovarian granulosa cells encoding the C-terminal part of human elongation factor 2."
      Rapp G., Mucha J., Einspanier R., Luck M., Scheit K.H.
      Biol. Chem. Hoppe-Seyler 369:247-250(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 501-858.
    7. Lubec G., Vishwanath V.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 796-801, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    8. Bienvenut W.V.
      Submitted (AUG-2001) to UniProtKB
      Cited for: CLEAVAGE OF INITIATOR METHIONINE.
    9. Cited for: ISGYLATION.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-435 AND SER-502, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "SMG-8 and SMG-9, two novel subunits of the SMG-1 complex, regulate remodeling of the mRNA surveillance complex during nonsense-mediated mRNA decay."
      Yamashita A., Izumi N., Kashima I., Ohnishi T., Saari B., Katsuhata Y., Muramatsu R., Morita T., Iwamatsu A., Hachiya T., Kurata R., Hirano H., Anderson P., Ohno S.
      Genes Dev. 23:1091-1105(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE SURF COMPLEX.
    14. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-235; LYS-239; LYS-272; LYS-275 AND LYS-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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 THR-57; THR-59 AND THR-435, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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 THR-54; THR-57 AND THR-59, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "A conserved eEF2 coding variant in SCA26 leads to loss of translational fidelity and increased susceptibility to proteostatic insult."
      Hekman K.E., Yu G.Y., Brown C.D., Zhu H., Du X., Gervin K., Undlien D.E., Peterson A., Stevanin G., Clark H.B., Pulst S.M., Bird T.D., White K.P., Gomez C.M.
      Hum. Mol. Genet. 21:5472-5483(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SCA26 HIS-596, CHARACTERIZATION OF VARIANT SCA26 HIS-596.

    Entry informationi

    Entry nameiEF2_HUMAN
    AccessioniPrimary (citable) accession number: P13639
    Secondary accession number(s): B2RMP5, D6W618, Q58J86
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 163 of the entry and version 4 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: 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