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P29692

- EF1D_HUMAN

UniProt

P29692 - EF1D_HUMAN

Protein

Elongation factor 1-delta

Gene

EEF1D

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 5 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Isoform 1: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP, regenerating EF-1-alpha for another round of transfer of aminoacyl-tRNAs to the ribosome.
    Isoform 2: Regulates induction of heat-shock-responsive genes through association with heat shock transcription factors and direct DNA-binding at heat shock promoter elements (HSE).

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. signal transducer activity Source: UniProtKB
    4. translation elongation factor activity Source: UniProtKB-KW
    5. translation factor activity, nucleic acid binding Source: ProtInc

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. gene expression Source: Reactome
    3. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    4. regulation of transcription, DNA-templated Source: UniProtKB-KW
    5. signal transduction Source: GOC
    6. transcription, DNA-templated Source: UniProtKB-KW
    7. translation Source: Reactome
    8. translational elongation Source: Reactome

    Keywords - Molecular functioni

    Elongation factor

    Keywords - Biological processi

    Protein biosynthesis, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_1477. Eukaryotic Translation Elongation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Elongation factor 1-delta
    Short name:
    EF-1-delta
    Alternative name(s):
    Antigen NY-CO-4
    Gene namesi
    Name:EEF1D
    Synonyms:EF1D
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:3211. EEF1D.

    Subcellular locationi

    Isoform 2 : Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. eukaryotic translation elongation factor 1 complex Source: ProtInc
    4. nucleolus Source: HPA
    5. nucleus Source: UniProt

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27647.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 281280Elongation factor 1-deltaPRO_0000155046Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei17 – 171N6-acetyllysine1 Publication
    Modified residuei107 – 1071N6-acetyllysine1 Publication
    Modified residuei117 – 1171N6-acetyllysine; alternate1 Publication
    Modified residuei117 – 1171N6-succinyllysine; alternateBy similarity
    Modified residuei133 – 1331Phosphoserine9 Publications
    Modified residuei147 – 1471Phosphothreonine3 Publications
    Modified residuei162 – 1621Phosphoserine; by CK212 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP29692.
    PaxDbiP29692.
    PRIDEiP29692.

    2D gel databases

    OGPiP29692.

    PTM databases

    PhosphoSiteiP29692.

    Expressioni

    Tissue specificityi

    Isoform 2 is specifically expressed in brain, cerebellum and testis.

    Inductioni

    By homocysteine (HC), may mediate accelerated synthesis of free thiol-containing proteins in response to HC-induced oxidative stress. Also induced following exposure to ionizing radiation.2 Publications

    Gene expression databases

    ArrayExpressiP29692.
    BgeeiP29692.
    CleanExiHS_EEF1D.
    GenevestigatoriP29692.

    Organism-specific databases

    HPAiHPA045101.
    HPA051002.

    Interactioni

    Subunit structurei

    EF-1 is composed of 4 subunits: alpha, beta, delta isoform 1, and gamma. Isoform 2 interacts with HSF1 and NFE2L2.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARHGAP21Q5T5U32EBI-358607,EBI-1642518
    ATG7O953522EBI-358607,EBI-987834
    CAMSAP2Q08AD12EBI-358607,EBI-1051869
    EEF1GP266413EBI-358607,EBI-351467

    Protein-protein interaction databases

    BioGridi108256. 69 interactions.
    IntActiP29692. 58 interactions.
    MINTiMINT-1139610.
    STRINGi9606.ENSP00000391944.

    Structurei

    3D structure databases

    ProteinModelPortaliP29692.
    SMRiP29692. Positions 192-281.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni80 – 11536Leucine-zipperAdd
    BLAST
    Regioni173 – 281109Catalytic (GEF)Add
    BLAST

    Sequence similaritiesi

    Belongs to the EF-1-beta/EF-1-delta family.Curated

    Phylogenomic databases

    eggNOGiCOG2092.
    HOGENOMiHOG000207272.
    HOVERGENiHBG000787.
    InParanoidiP29692.
    KOiK15410.
    PhylomeDBiP29692.
    TreeFamiTF313134.

    Family and domain databases

    Gene3Di3.30.70.60. 1 hit.
    InterProiIPR018940. EF-1_beta_acid_region_euk.
    IPR014717. Transl_elong_EF1B/ribosomal_S6.
    IPR001326. Transl_elong_EF1B_B/D_CS.
    IPR014038. Transl_elong_fac_EF1B_bsu/dsu.
    [Graphical view]
    PfamiPF10587. EF-1_beta_acid. 1 hit.
    PF00736. EF1_GNE. 1 hit.
    [Graphical view]
    SMARTiSM00888. EF1_GNE. 1 hit.
    [Graphical view]
    SUPFAMiSSF54984. SSF54984. 1 hit.
    PROSITEiPS00824. EF1BD_1. 1 hit.
    PS00825. EF1BD_2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P29692-1) [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

    MATNFLAHEK IWFDKFKYDD AERRFYEQMN GPVAGASRQE NGASVILRDI    50
    ARARENIQKS LAGSSGPGAS SGTSGDHGEL VVRIASLEVE NQSLRGVVQE 100
    LQQAISKLEA RLNVLEKSSP GHRATAPQTQ HVSPMRQVEP PAKKPATPAE 150
    DDEDDDIDLF GSDNEEEDKE AAQLREERLR QYAEKKAKKP ALVAKSSILL 200
    DVKPWDDETD MAQLEACVRS IQLDGLVWGA SKLVPVGYGI RKLQIQCVVE 250
    DDKVGTDLLE EEITKFEEHV QSVDIAAFNK I 281
    Length:281
    Mass (Da):31,122
    Last modified:January 23, 2007 - v5
    Checksum:iCE778D6D5D09BD6C
    GO
    Isoform 2 (identifier: P29692-2) [UniParc]FASTAAdd to Basket

    Also known as: eEF1BdeltaL

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MRSGKASCTL...VSSLRPNRKM

    Note: Contains a phosphoserine at position 91. Contains a phosphoserine at position 94.Curated

    Show »
    Length:647
    Mass (Da):71,408
    Checksum:iA4CADBF40FCFCC09
    GO
    Isoform 3 (identifier: P29692-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         40-63: Missing.

    Note: Contains a phosphoserine at position 40.

    Show »
    Length:257
    Mass (Da):28,558
    Checksum:iE38BA673BE18FBE5
    GO
    Isoform 4 (identifier: P29692-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         78-96: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:262
    Mass (Da):29,071
    Checksum:i7F9682E53B69BC17
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti34 – 341A → R in CAA79716. (PubMed:8334168)Curated
    Sequence conflicti44 – 441S → T in CAA79716. (PubMed:8334168)Curated
    Sequence conflicti209 – 2091T → A in BAG56855. (PubMed:14702039)Curated
    Isoform 2 (identifier: P29692-2)
    Sequence conflicti189 – 1891D → E in AAP35906. 1 PublicationCurated
    Sequence conflicti189 – 1891D → E in EAW82228. (PubMed:14702039)Curated
    Sequence conflicti189 – 1891D → E in AAH07847. (PubMed:16421571)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MRSGKASCTLETVWEDKHKY EEAERRFYEHEATQAAASAQ QLPAEGPAMNGPGQDDPEDA DEAEAPDGGSRRDPRKSQDS RKPLQKKRKRSPKSGLGPAD LALLGLSAERVWLDKSLFDQ AESSYRQKLADVAAQAAWPP ALAPWGLCTHGNQVACHHVT WGIWVNKSSFDQAERAFVEW SQALLLAPDGSRRQGTPNTG QQVAVPDLAHQPSPPVNGQP PLGSLQALVREVWLEKPRYD AAERGFYEALFDGHPPGKVR LQERAGLAEGARRGRRDRRG RNILGNKRAGLRRADGEAPS ALPYCYFLQKDAEAPWLSKP AYDSAECRHHAAEALRVAWC LEAASLSHRPGPRSGLSVSS LRPNRKM in isoform 2. 2 PublicationsVSP_037884
    Alternative sequencei40 – 6324Missing in isoform 3. 1 PublicationVSP_043812Add
    BLAST
    Alternative sequencei78 – 9619Missing in isoform 4. 1 PublicationVSP_045960Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z21507 mRNA. Translation: CAA79716.1.
    BT007242 mRNA. Translation: AAP35906.1.
    AK293339 mRNA. Translation: BAG56855.1.
    AC067930 Genomic DNA. No translation available.
    CH471162 Genomic DNA. Translation: EAW82227.1.
    CH471162 Genomic DNA. Translation: EAW82228.1.
    CH471162 Genomic DNA. Translation: EAW82229.1.
    CH471162 Genomic DNA. Translation: EAW82230.1.
    CH471162 Genomic DNA. Translation: EAW82232.1.
    BC007847 mRNA. Translation: AAH07847.1.
    BC009907 mRNA. Translation: AAH09907.1.
    BC012819 mRNA. Translation: AAH12819.1.
    BC062535 mRNA. Translation: AAH62535.1.
    BC094806 mRNA. Translation: AAH94806.1.
    CCDSiCCDS47930.1. [P29692-3]
    CCDS56559.1. [P29692-4]
    CCDS6404.1. [P29692-2]
    CCDS6405.1. [P29692-1]
    PIRiS34626.
    RefSeqiNP_001123525.2. NM_001130053.2.
    NP_001123527.1. NM_001130055.2. [P29692-1]
    NP_001123528.1. NM_001130056.2. [P29692-3]
    NP_001123529.1. NM_001130057.2. [P29692-1]
    NP_001182132.1. NM_001195203.1. [P29692-4]
    NP_001276879.1. NM_001289950.1. [P29692-1]
    NP_001951.2. NM_001960.4. [P29692-1]
    NP_115754.3. NM_032378.4.
    XP_005250880.1. XM_005250823.1. [P29692-2]
    XP_005250881.1. XM_005250824.1. [P29692-2]
    XP_005250883.1. XM_005250826.1. [P29692-3]
    XP_006716584.1. XM_006716521.1. [P29692-2]
    XP_006716585.1. XM_006716522.1. [P29692-2]
    XP_006716586.1. XM_006716523.1. [P29692-2]
    XP_006716587.1. XM_006716524.1. [P29692-2]
    XP_006716588.1. XM_006716525.1. [P29692-1]
    XP_006725131.1. XM_006725068.1. [P29692-2]
    XP_006725132.1. XM_006725069.1. [P29692-2]
    XP_006725133.1. XM_006725070.1. [P29692-2]
    XP_006725134.1. XM_006725071.1. [P29692-2]
    XP_006725135.1. XM_006725072.1. [P29692-2]
    XP_006725136.1. XM_006725073.1. [P29692-2]
    XP_006725138.1. XM_006725075.1. [P29692-1]
    XP_006725139.1. XM_006725076.1. [P29692-3]
    UniGeneiHs.333388.
    Hs.686554.
    Hs.703306.

    Genome annotation databases

    EnsembliENST00000317198; ENSP00000317399; ENSG00000104529. [P29692-1]
    ENST00000395119; ENSP00000378551; ENSG00000104529. [P29692-1]
    ENST00000419152; ENSP00000388261; ENSG00000104529. [P29692-1]
    ENST00000423316; ENSP00000410059; ENSG00000104529. [P29692-2]
    ENST00000442189; ENSP00000391944; ENSG00000104529. [P29692-2]
    ENST00000524624; ENSP00000435697; ENSG00000104529. [P29692-3]
    ENST00000526838; ENSP00000436507; ENSG00000104529. [P29692-4]
    ENST00000528610; ENSP00000431763; ENSG00000104529. [P29692-3]
    ENST00000529272; ENSP00000434872; ENSG00000104529. [P29692-1]
    GeneIDi1936.
    KEGGihsa:1936.
    UCSCiuc003yyp.2. human. [P29692-2]
    uc003yys.3. human. [P29692-1]
    uc003yyv.3. human. [P29692-3]

    Polymorphism databases

    DMDMi20141357.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z21507 mRNA. Translation: CAA79716.1 .
    BT007242 mRNA. Translation: AAP35906.1 .
    AK293339 mRNA. Translation: BAG56855.1 .
    AC067930 Genomic DNA. No translation available.
    CH471162 Genomic DNA. Translation: EAW82227.1 .
    CH471162 Genomic DNA. Translation: EAW82228.1 .
    CH471162 Genomic DNA. Translation: EAW82229.1 .
    CH471162 Genomic DNA. Translation: EAW82230.1 .
    CH471162 Genomic DNA. Translation: EAW82232.1 .
    BC007847 mRNA. Translation: AAH07847.1 .
    BC009907 mRNA. Translation: AAH09907.1 .
    BC012819 mRNA. Translation: AAH12819.1 .
    BC062535 mRNA. Translation: AAH62535.1 .
    BC094806 mRNA. Translation: AAH94806.1 .
    CCDSi CCDS47930.1. [P29692-3 ]
    CCDS56559.1. [P29692-4 ]
    CCDS6404.1. [P29692-2 ]
    CCDS6405.1. [P29692-1 ]
    PIRi S34626.
    RefSeqi NP_001123525.2. NM_001130053.2.
    NP_001123527.1. NM_001130055.2. [P29692-1 ]
    NP_001123528.1. NM_001130056.2. [P29692-3 ]
    NP_001123529.1. NM_001130057.2. [P29692-1 ]
    NP_001182132.1. NM_001195203.1. [P29692-4 ]
    NP_001276879.1. NM_001289950.1. [P29692-1 ]
    NP_001951.2. NM_001960.4. [P29692-1 ]
    NP_115754.3. NM_032378.4.
    XP_005250880.1. XM_005250823.1. [P29692-2 ]
    XP_005250881.1. XM_005250824.1. [P29692-2 ]
    XP_005250883.1. XM_005250826.1. [P29692-3 ]
    XP_006716584.1. XM_006716521.1. [P29692-2 ]
    XP_006716585.1. XM_006716522.1. [P29692-2 ]
    XP_006716586.1. XM_006716523.1. [P29692-2 ]
    XP_006716587.1. XM_006716524.1. [P29692-2 ]
    XP_006716588.1. XM_006716525.1. [P29692-1 ]
    XP_006725131.1. XM_006725068.1. [P29692-2 ]
    XP_006725132.1. XM_006725069.1. [P29692-2 ]
    XP_006725133.1. XM_006725070.1. [P29692-2 ]
    XP_006725134.1. XM_006725071.1. [P29692-2 ]
    XP_006725135.1. XM_006725072.1. [P29692-2 ]
    XP_006725136.1. XM_006725073.1. [P29692-2 ]
    XP_006725138.1. XM_006725075.1. [P29692-1 ]
    XP_006725139.1. XM_006725076.1. [P29692-3 ]
    UniGenei Hs.333388.
    Hs.686554.
    Hs.703306.

    3D structure databases

    ProteinModelPortali P29692.
    SMRi P29692. Positions 192-281.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108256. 69 interactions.
    IntActi P29692. 58 interactions.
    MINTi MINT-1139610.
    STRINGi 9606.ENSP00000391944.

    PTM databases

    PhosphoSitei P29692.

    Polymorphism databases

    DMDMi 20141357.

    2D gel databases

    OGPi P29692.

    Proteomic databases

    MaxQBi P29692.
    PaxDbi P29692.
    PRIDEi P29692.

    Protocols and materials databases

    DNASUi 1936.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000317198 ; ENSP00000317399 ; ENSG00000104529 . [P29692-1 ]
    ENST00000395119 ; ENSP00000378551 ; ENSG00000104529 . [P29692-1 ]
    ENST00000419152 ; ENSP00000388261 ; ENSG00000104529 . [P29692-1 ]
    ENST00000423316 ; ENSP00000410059 ; ENSG00000104529 . [P29692-2 ]
    ENST00000442189 ; ENSP00000391944 ; ENSG00000104529 . [P29692-2 ]
    ENST00000524624 ; ENSP00000435697 ; ENSG00000104529 . [P29692-3 ]
    ENST00000526838 ; ENSP00000436507 ; ENSG00000104529 . [P29692-4 ]
    ENST00000528610 ; ENSP00000431763 ; ENSG00000104529 . [P29692-3 ]
    ENST00000529272 ; ENSP00000434872 ; ENSG00000104529 . [P29692-1 ]
    GeneIDi 1936.
    KEGGi hsa:1936.
    UCSCi uc003yyp.2. human. [P29692-2 ]
    uc003yys.3. human. [P29692-1 ]
    uc003yyv.3. human. [P29692-3 ]

    Organism-specific databases

    CTDi 1936.
    GeneCardsi GC08M144661.
    H-InvDB HIX0034587.
    HGNCi HGNC:3211. EEF1D.
    HPAi HPA045101.
    HPA051002.
    MIMi 130592. gene.
    neXtProti NX_P29692.
    PharmGKBi PA27647.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2092.
    HOGENOMi HOG000207272.
    HOVERGENi HBG000787.
    InParanoidi P29692.
    KOi K15410.
    PhylomeDBi P29692.
    TreeFami TF313134.

    Enzyme and pathway databases

    Reactomei REACT_1477. Eukaryotic Translation Elongation.

    Miscellaneous databases

    ChiTaRSi EEF1D. human.
    GeneWikii EEF1D.
    GenomeRNAii 1936.
    NextBioi 7841.
    PROi P29692.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P29692.
    Bgeei P29692.
    CleanExi HS_EEF1D.
    Genevestigatori P29692.

    Family and domain databases

    Gene3Di 3.30.70.60. 1 hit.
    InterProi IPR018940. EF-1_beta_acid_region_euk.
    IPR014717. Transl_elong_EF1B/ribosomal_S6.
    IPR001326. Transl_elong_EF1B_B/D_CS.
    IPR014038. Transl_elong_fac_EF1B_bsu/dsu.
    [Graphical view ]
    Pfami PF10587. EF-1_beta_acid. 1 hit.
    PF00736. EF1_GNE. 1 hit.
    [Graphical view ]
    SMARTi SM00888. EF1_GNE. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54984. SSF54984. 1 hit.
    PROSITEi PS00824. EF1BD_1. 1 hit.
    PS00825. EF1BD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The human leucine zipper-containing guanine-nucleotide exchange protein elongation factor-1 delta."
      Sanders J.P., Raggiaschi R., Morales J., Moeller W.
      Biochim. Biophys. Acta 1174:87-90(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DOMAIN LEUCINE ZIPPER.
      Tissue: Skin fibroblast.
    2. "Characterization of human colon cancer antigens recognized by autologous antibodies."
      Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E., Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J.
      Int. J. Cancer 76:652-658(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Colon carcinoma.
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    4. "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 4).
    5. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORMS 1; 2 AND 3).
      Tissue: Brain, Lung and Muscle.
    9. Bienvenut W.V., Potts A., Barblan J., Quadroni M.
      Submitted (JUL-2004) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-10 (ISOFORM 1), ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    10. "Elongation factor 1 delta is enhanced following exposure to ionizing radiation."
      Jung M., Kondratyev A.D., Dritschilo A.
      Cancer Res. 54:2541-2543(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY IONIZING RADIATION.
    11. "Induction of acute translational response genes by homocysteine. Elongation factors-1alpha, -beta, and -delta."
      Chacko G., Ling Q., Hajjar K.A.
      J. Biol. Chem. 273:19840-19846(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY HOMOCYSTEINE.
    12. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133; THR-147 AND SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Pituitary.
    14. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
      Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
      Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Prostate cancer.
    15. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
      Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
      Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    17. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    19. "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-133; THR-147 AND SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91 AND SER-94 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    22. "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].
    23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "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 THR-147 AND SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    25. "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-17; LYS-107 AND LYS-117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "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-133 AND SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "Transformation of eEF1Bdelta into heat-shock response transcription factor by alternative splicing."
      Kaitsuka T., Tomizawa K., Matsushita M.
      EMBO Rep. 12:673-681(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION (ISOFORM 2), INTERACTION WITH HSF1 AND NFE2L2 (ISOFORM 2), TISSUE SPECIFICITY (ISOFORM 2), DNA-BINDING (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2).
    29. "Unbiased functional proteomics strategy for protein kinase inhibitor validation and identification of bona fide protein kinase substrates: application to identification of as a substrate for CK2."
      Gyenis L., Duncan J.S., Turowec J.P., Bretner M., Litchfield D.W.
      J. Proteome Res. 10:4887-4901(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-162 BY CK2.
    30. "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-133 AND SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. "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].
    32. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiEF1D_HUMAN
    AccessioniPrimary (citable) accession number: P29692
    Secondary accession number(s): B4DDU4
    , D3DWK3, E9PBQ9, Q4VBZ6, Q969J1, Q96I38
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 158 of the entry and version 5 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3