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P26641

- EF1G_HUMAN

UniProt

P26641 - EF1G_HUMAN

Protein

Elongation factor 1-gamma

Gene

EEF1G

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Probably plays a role in anchoring the complex to other cellular components.

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. translation elongation factor activity Source: UniProtKB-KW

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. gene expression Source: Reactome
    3. response to virus Source: UniProtKB
    4. translation Source: Reactome
    5. translational elongation Source: Reactome

    Keywords - Molecular functioni

    Elongation factor

    Keywords - Biological processi

    Protein biosynthesis

    Enzyme and pathway databases

    ReactomeiREACT_1477. Eukaryotic Translation Elongation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Elongation factor 1-gamma
    Short name:
    EF-1-gamma
    Alternative name(s):
    eEF-1B gamma
    Gene namesi
    Name:EEF1G
    Synonyms:EF1G
    ORF Names:PRO1608
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:3213. EEF1G.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. membrane Source: UniProtKB
    4. nucleus Source: UniProt

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27649.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed5 Publications
    Chaini2 – 437436Elongation factor 1-gammaPRO_0000208813Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications
    Modified residuei147 – 1471N6-acetyllysine1 Publication
    Modified residuei212 – 2121N6-acetyllysineBy similarity
    Modified residuei401 – 4011N6-acetyllysineBy similarity
    Modified residuei434 – 4341N6-acetyllysine; alternate1 Publication
    Modified residuei434 – 4341N6-malonyllysine; alternate1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP26641.
    PaxDbiP26641.
    PRIDEiP26641.

    2D gel databases

    OGPiP26641.

    PTM databases

    PhosphoSiteiP26641.

    Expressioni

    Tissue specificityi

    Highly expressed in pancreatic tumor tissue and to a lesser extent in normal kidney, intestine, pancreas, stomach, lung, brain, spleen and liver.

    Inductioni

    Down-regulated in response to enterovirus 71 (EV71) infection.1 Publication

    Gene expression databases

    CleanExiHS_EEF1G.
    GenevestigatoriP26641.

    Organism-specific databases

    HPAiHPA040688.

    Interactioni

    Subunit structurei

    EF-1 is composed of four subunits: alpha, beta, delta, and gamma.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EEF1B2P245343EBI-351467,EBI-354334
    EEF1DP296923EBI-351467,EBI-358607
    TRIM63Q969Q12EBI-351467,EBI-5661333

    Protein-protein interaction databases

    BioGridi108257. 123 interactions.
    DIPiDIP-32516N.
    IntActiP26641. 113 interactions.
    MINTiMINT-1191315.

    Structurei

    Secondary structure

    1
    437
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi279 – 2813
    Helixi290 – 29910
    Helixi302 – 3043
    Helixi306 – 3116
    Turni316 – 3183
    Beta strandi320 – 3245
    Helixi329 – 3313
    Helixi338 – 34811
    Helixi349 – 3513
    Helixi353 – 3553
    Beta strandi356 – 3583
    Beta strandi361 – 3644
    Beta strandi370 – 38112
    Helixi384 – 3863
    Helixi388 – 3903
    Helixi394 – 3963
    Helixi408 – 41811
    Turni424 – 4263

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PBUNMR-A276-437[»]
    ProteinModelPortaliP26641.
    SMRiP26641. Positions 1-202, 276-437.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP26641.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 8786GST N-terminalAdd
    BLAST
    Domaini88 – 216129GST C-terminalAdd
    BLAST
    Domaini276 – 437162EF-1-gamma C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 EF-1-gamma C-terminal domain.PROSITE-ProRule annotation
    Contains 1 GST C-terminal domain.Curated
    Contains 1 GST N-terminal domain.Curated

    Phylogenomic databases

    eggNOGiCOG0625.
    HOGENOMiHOG000235245.
    HOVERGENiHBG051444.
    InParanoidiP26641.
    KOiK03233.
    OrthoDBiEOG72G177.
    PhylomeDBiP26641.
    TreeFamiTF314343.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.30.70.1010. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    IPR001662. Transl_elong_EF1_G_con.
    [Graphical view]
    PfamiPF00647. EF1G. 1 hit.
    PF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    SSF89942. SSF89942. 1 hit.
    PROSITEiPS50040. EF1G_C. 1 hit.
    PS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P26641-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAAGTLYTYP ENWRAFKALI AAQYSGAQVR VLSAPPHFHF GQTNRTPEFL    50
    RKFPAGKVPA FEGDDGFCVF ESNAIAYYVS NEELRGSTPE AAAQVVQWVS 100
    FADSDIVPPA STWVFPTLGI MHHNKQATEN AKEEVRRILG LLDAYLKTRT 150
    FLVGERVTLA DITVVCTLLW LYKQVLEPSF RQAFPNTNRW FLTCINQPQF 200
    RAVLGEVKLC EKMAQFDAKK FAETQPKKDT PRKEKGSREE KQKPQAERKE 250
    EKKAAAPAPE EEMDECEQAL AAEPKAKDPF AHLPKSTFVL DEFKRKYSNE 300
    DTLSVALPYF WEHFDKDGWS LWYSEYRFPE ELTQTFMSCN LITGMFQRLD 350
    KLRKNAFASV ILFGTNNSSS ISGVWVFRGQ ELAFPLSPDW QVDYESYTWR 400
    KLDPGSEETQ TLVREYFSWE GAFQHVGKAF NQGKIFK 437
    Length:437
    Mass (Da):50,119
    Last modified:January 23, 2007 - v3
    Checksum:iA6110663110CF3FC
    GO
    Isoform 2 (identifier: P26641-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-4: MAAG → MAERWVAPAVLRRARFASTFFLSPQIYAHKDGDLRSAFFILSFKRGEFIPFLNW

    Note: No experimental confirmation available.

    Show »
    Length:487
    Mass (Da):56,150
    Checksum:i3FF3FDCBDAFE1A4C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti102 – 1021A → V in AAH13918. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 44MAAG → MAERWVAPAVLRRARFASTF FLSPQIYAHKDGDLRSAFFI LSFKRGEFIPFLNW in isoform 2. 1 PublicationVSP_056204

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X63526 mRNA. Translation: CAA45089.1.
    Z11531 mRNA. Translation: CAA77630.1.
    AK300203 mRNA. Translation: BAG61974.1.
    AP001363 Genomic DNA. No translation available.
    AP002990 Genomic DNA. No translation available.
    BC000384 mRNA. Translation: AAH00384.1.
    BC006509 mRNA. Translation: AAH06509.1.
    BC006520 mRNA. Translation: AAH06520.1.
    BC007949 mRNA. Translation: AAH07949.2.
    BC009865 mRNA. Translation: AAH09865.1.
    BC013918 mRNA. Translation: AAH13918.1.
    BC015813 mRNA. Translation: AAH15813.1.
    BC021974 mRNA. Translation: AAH21974.2.
    BC028179 mRNA. Translation: AAH28179.1.
    BC031012 mRNA. Translation: AAH31012.1.
    BC067738 mRNA. Translation: AAH67738.1.
    M55409 mRNA. Translation: AAC18414.1.
    AF119850 mRNA. Translation: AAF69604.1.
    CCDSiCCDS44626.1.
    PIRiS22655.
    RefSeqiNP_001395.1. NM_001404.4.
    UniGeneiHs.144835.
    Hs.444467.

    Genome annotation databases

    EnsembliENST00000329251; ENSP00000331901; ENSG00000254772.
    ENST00000378019; ENSP00000367258; ENSG00000254772.
    GeneIDi1937.
    KEGGihsa:1937.
    UCSCiuc001ntm.1. human.

    Polymorphism databases

    DMDMi119165.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X63526 mRNA. Translation: CAA45089.1 .
    Z11531 mRNA. Translation: CAA77630.1 .
    AK300203 mRNA. Translation: BAG61974.1 .
    AP001363 Genomic DNA. No translation available.
    AP002990 Genomic DNA. No translation available.
    BC000384 mRNA. Translation: AAH00384.1 .
    BC006509 mRNA. Translation: AAH06509.1 .
    BC006520 mRNA. Translation: AAH06520.1 .
    BC007949 mRNA. Translation: AAH07949.2 .
    BC009865 mRNA. Translation: AAH09865.1 .
    BC013918 mRNA. Translation: AAH13918.1 .
    BC015813 mRNA. Translation: AAH15813.1 .
    BC021974 mRNA. Translation: AAH21974.2 .
    BC028179 mRNA. Translation: AAH28179.1 .
    BC031012 mRNA. Translation: AAH31012.1 .
    BC067738 mRNA. Translation: AAH67738.1 .
    M55409 mRNA. Translation: AAC18414.1 .
    AF119850 mRNA. Translation: AAF69604.1 .
    CCDSi CCDS44626.1.
    PIRi S22655.
    RefSeqi NP_001395.1. NM_001404.4.
    UniGenei Hs.144835.
    Hs.444467.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PBU NMR - A 276-437 [» ]
    ProteinModelPortali P26641.
    SMRi P26641. Positions 1-202, 276-437.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108257. 123 interactions.
    DIPi DIP-32516N.
    IntActi P26641. 113 interactions.
    MINTi MINT-1191315.

    PTM databases

    PhosphoSitei P26641.

    Polymorphism databases

    DMDMi 119165.

    2D gel databases

    OGPi P26641.

    Proteomic databases

    MaxQBi P26641.
    PaxDbi P26641.
    PRIDEi P26641.

    Protocols and materials databases

    DNASUi 1937.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000329251 ; ENSP00000331901 ; ENSG00000254772 .
    ENST00000378019 ; ENSP00000367258 ; ENSG00000254772 .
    GeneIDi 1937.
    KEGGi hsa:1937.
    UCSCi uc001ntm.1. human.

    Organism-specific databases

    CTDi 1937.
    GeneCardsi GC11M062332.
    HGNCi HGNC:3213. EEF1G.
    HPAi HPA040688.
    MIMi 130593. gene.
    neXtProti NX_P26641.
    PharmGKBi PA27649.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0625.
    HOGENOMi HOG000235245.
    HOVERGENi HBG051444.
    InParanoidi P26641.
    KOi K03233.
    OrthoDBi EOG72G177.
    PhylomeDBi P26641.
    TreeFami TF314343.

    Enzyme and pathway databases

    Reactomei REACT_1477. Eukaryotic Translation Elongation.

    Miscellaneous databases

    ChiTaRSi EEF1G. human.
    EvolutionaryTracei P26641.
    GeneWikii EEF1G.
    GenomeRNAii 1937.
    NextBioi 7847.
    PROi P26641.
    SOURCEi Search...

    Gene expression databases

    CleanExi HS_EEF1G.
    Genevestigatori P26641.

    Family and domain databases

    Gene3Di 1.20.1050.10. 1 hit.
    3.30.70.1010. 1 hit.
    3.40.30.10. 1 hit.
    InterProi IPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    IPR001662. Transl_elong_EF1_G_con.
    [Graphical view ]
    Pfami PF00647. EF1G. 1 hit.
    PF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    SSF89942. SSF89942. 1 hit.
    PROSITEi PS50040. EF1G_C. 1 hit.
    PS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Elongation factor-1 messenger-RNA levels in cultured cells are high compared to tissue and are not drastically affected further by oncogenic transformation."
      Sanders J., Maassen J.A., Moeller W.
      Nucleic Acids Res. 20:5907-5910(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Human cDNAs encoding elongation factor 1 gamma and the ribosomal protein L19."
      Kumabe T., Schma Y., Yamamoto T.
      Nucleic Acids Res. 20:2598-2598(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "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] (ISOFORM 2).
      Tissue: Placenta.
    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] (ISOFORM 1).
      Tissue: Bone marrow, Eye, Liver, Lung, Muscle, Testis and Uterus.
    6. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-14.
      Tissue: Platelet.
    7. Bienvenut W.V.
      Submitted (OCT-2004) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-14, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    8. "Expression of elongation factor-1 gamma-related sequence in human pancreatic cancer."
      Lew Y., Jones D.V., Mars W.M., Evans D., Byrd D., Frazier M.L.
      Pancreas 7:144-152(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 80-437 (ISOFORM 1).
      Tissue: Pancreatic carcinoma.
    9. "Functional prediction of the coding sequences of 79 new genes deduced by analysis of cDNA clones from human fetal liver."
      Zhang C., Yu Y., Zhang S., Wei H., Zhang Y., Zhou G., Bi J., Liu M., He F.
      Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 121-437 (ISOFORM 1).
      Tissue: Fetal liver.
    10. "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection."
      Leong W.F., Chow V.T.
      Cell. Microbiol. 8:565-580(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
    11. "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].
    12. "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-147 AND LYS-434, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: MALONYLATION AT LYS-434.
    15. "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].
    16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "1H, 15N and 13C resonance assignments of the highly conserved 19 kDa C-terminal domain from human elongation factor 1Bgamma."
      Vanwetswinkel S., Kriek J., Andersen G.R., Dijk J., Siegal G.
      J. Biomol. NMR 26:189-190(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 276-437.

    Entry informationi

    Entry nameiEF1G_HUMAN
    AccessioniPrimary (citable) accession number: P26641
    Secondary accession number(s): B4DTG2
    , Q6PJ62, Q6PK31, Q96CU2, Q9P196
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 164 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3