Full text data of EEF1D
EEF1D
(EF1D)
[Confidence: low (only semi-automatic identification from reviews)]
Elongation factor 1-delta; EF-1-delta (Antigen NY-CO-4)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Elongation factor 1-delta; EF-1-delta (Antigen NY-CO-4)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P29692
ID EF1D_HUMAN Reviewed; 281 AA.
AC P29692; B4DDU4; D3DWK3; E9PBQ9; Q4VBZ6; Q969J1; Q96I38;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 5.
DT 22-JAN-2014, entry version 150.
DE RecName: Full=Elongation factor 1-delta;
DE Short=EF-1-delta;
DE AltName: Full=Antigen NY-CO-4;
GN Name=EEF1D; Synonyms=EF1D;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DOMAIN LEUCINE ZIPPER.
RC TISSUE=Skin fibroblast;
RX PubMed=8334168; DOI=10.1016/0167-4781(93)90097-W;
RA Sanders J.P., Raggiaschi R., Morales J., Moeller W.;
RT "The human leucine zipper-containing guanine-nucleotide exchange
RT protein elongation factor-1 delta.";
RL Biochim. Biophys. Acta 1174:87-90(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Colon carcinoma;
RX PubMed=9610721;
RX DOI=10.1002/(SICI)1097-0215(19980529)76:5<652::AID-IJC7>3.0.CO;2-P;
RA Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E.,
RA Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J.;
RT "Characterization of human colon cancer antigens recognized by
RT autologous antibodies.";
RL Int. J. Cancer 76:652-658(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
RA Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
RA Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Brain, Lung, and Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 2-10 (ISOFORM 1), ACETYLATION AT ALA-2, AND MASS
RP SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V., Potts A., Barblan J., Quadroni M.;
RL Submitted (JUL-2004) to UniProtKB.
RN [10]
RP INDUCTION BY IONIZING RADIATION.
RX PubMed=8168075;
RA Jung M., Kondratyev A.D., Dritschilo A.;
RT "Elongation factor 1 delta is enhanced following exposure to ionizing
RT radiation.";
RL Cancer Res. 54:2541-2543(1994).
RN [11]
RP INDUCTION BY HOMOCYSTEINE.
RX PubMed=9677419; DOI=10.1074/jbc.273.31.19840;
RA Chacko G., Ling Q., Hajjar K.A.;
RT "Induction of acute translational response genes by homocysteine.
RT Elongation factors-1alpha, -beta, and -delta.";
RL J. Biol. Chem. 273:19840-19846(1998).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133; THR-147 AND
RP SER-162, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND MASS
RP SPECTROMETRY.
RC TISSUE=Pituitary;
RX PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
RA Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
RT "Phosphoproteomic analysis of the human pituitary.";
RL Pituitary 9:109-120(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND SER-162, AND
RP MASS SPECTROMETRY.
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate
RT cancer cells: identification of phosphoproteins in the LNCaP cell
RT line.";
RL Electrophoresis 28:2027-2034(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa
RT cells and high confident phosphopeptide identification by cross-
RT validation of MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.M700120-MCP200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,
RA Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate
RT reductase M2 subunit phosphorylation at residue serine 20 in canonical
RT Wnt signal transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND MASS
RP SPECTROMETRY.
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133; THR-147 AND
RP SER-162, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-91 AND SER-94 (ISOFORM 2),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40 (ISOFORM 3), AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND SER-162, AND
RP MASS SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147 AND SER-162, AND
RP MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17; LYS-107 AND LYS-117, AND
RP MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND SER-162, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [28]
RP FUNCTION (ISOFORM 2), INTERACTION WITH HSF1 AND NFE2L2 (ISOFORM 2),
RP TISSUE SPECIFICITY (ISOFORM 2), DNA-BINDING (ISOFORM 2), AND
RP SUBCELLULAR LOCATION (ISOFORM 2).
RX PubMed=21597468; DOI=10.1038/embor.2011.82;
RA Kaitsuka T., Tomizawa K., Matsushita M.;
RT "Transformation of eEF1Bdelta into heat-shock response transcription
RT factor by alternative splicing.";
RL EMBO Rep. 12:673-681(2011).
RN [29]
RP PHOSPHORYLATION AT SER-162 BY CK2.
RX PubMed=21936567; DOI=10.1021/pr2008994;
RA Gyenis L., Duncan J.S., Turowec J.P., Bretner M., Litchfield D.W.;
RT "Unbiased functional proteomics strategy for protein kinase inhibitor
RT validation and identification of bona fide protein kinase substrates:
RT application to identification of as a substrate for CK2.";
RL J. Proteome Res. 10:4887-4901(2011).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND SER-162, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Isoform 1: EF-1-beta and EF-1-delta stimulate the
CC exchange of GDP bound to EF-1-alpha to GTP, regenerating EF-1-
CC alpha for another round of transfer of aminoacyl-tRNAs to the
CC ribosome.
CC -!- FUNCTION: Isoform 2: Regulates induction of heat-shock-responsive
CC genes through association with heat shock transcription factors
CC and direct DNA-binding at heat shock promoter elements (HSE).
CC -!- SUBUNIT: EF-1 is composed of 4 subunits: alpha, beta, delta
CC isoform 1, and gamma. Isoform 2 interacts with HSF1 and NFE2L2.
CC -!- INTERACTION:
CC Q5T5U3:ARHGAP21; NbExp=2; IntAct=EBI-358607, EBI-1642518;
CC O95352:ATG7; NbExp=2; IntAct=EBI-358607, EBI-987834;
CC Q08AD1:CAMSAP2; NbExp=2; IntAct=EBI-358607, EBI-1051869;
CC P26641:EEF1G; NbExp=3; IntAct=EBI-358607, EBI-351467;
CC -!- SUBCELLULAR LOCATION: Isoform 2: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P29692-1; Sequence=Displayed;
CC Name=2; Synonyms=eEF1BdeltaL;
CC IsoId=P29692-2; Sequence=VSP_037884;
CC Note=Ref.3 (AAP35906), Ref.4 (EAW82228) and Ref.5 (AAH07847)
CC sequences are in conflict in position: 189:D->E. Contains a
CC phosphoserine at position 91. Contains a phosphoserine at
CC position 94;
CC Name=3;
CC IsoId=P29692-3; Sequence=VSP_043812;
CC Note=Contains a phosphoserine at position 40;
CC Name=4;
CC IsoId=P29692-4; Sequence=VSP_045960;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Isoform 2 is specifically expressed in brain,
CC cerebellum and testis.
CC -!- INDUCTION: By homocysteine (HC), may mediate accelerated synthesis
CC of free thiol-containing proteins in response to HC-induced
CC oxidative stress. Also induced following exposure to ionizing
CC radiation.
CC -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family.
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DR EMBL; Z21507; CAA79716.1; -; mRNA.
DR EMBL; BT007242; AAP35906.1; -; mRNA.
DR EMBL; AK293339; BAG56855.1; -; mRNA.
DR EMBL; AC067930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471162; EAW82227.1; -; Genomic_DNA.
DR EMBL; CH471162; EAW82228.1; -; Genomic_DNA.
DR EMBL; CH471162; EAW82229.1; -; Genomic_DNA.
DR EMBL; CH471162; EAW82230.1; -; Genomic_DNA.
DR EMBL; CH471162; EAW82232.1; -; Genomic_DNA.
DR EMBL; BC007847; AAH07847.1; -; mRNA.
DR EMBL; BC009907; AAH09907.1; -; mRNA.
DR EMBL; BC012819; AAH12819.1; -; mRNA.
DR EMBL; BC062535; AAH62535.1; -; mRNA.
DR EMBL; BC094806; AAH94806.1; -; mRNA.
DR PIR; S34626; S34626.
DR RefSeq; NP_001123525.2; NM_001130053.2.
DR RefSeq; NP_001123527.1; NM_001130055.2.
DR RefSeq; NP_001123528.1; NM_001130056.2.
DR RefSeq; NP_001123529.1; NM_001130057.2.
DR RefSeq; NP_001182132.1; NM_001195203.1.
DR RefSeq; NP_001951.2; NM_001960.4.
DR RefSeq; NP_115754.3; NM_032378.4.
DR RefSeq; XP_005250880.1; XM_005250823.1.
DR RefSeq; XP_005250881.1; XM_005250824.1.
DR RefSeq; XP_005250882.1; XM_005250825.1.
DR RefSeq; XP_005250883.1; XM_005250826.1.
DR UniGene; Hs.333388; -.
DR UniGene; Hs.686554; -.
DR UniGene; Hs.703306; -.
DR ProteinModelPortal; P29692; -.
DR SMR; P29692; 192-281.
DR IntAct; P29692; 56.
DR MINT; MINT-1139610; -.
DR STRING; 9606.ENSP00000391944; -.
DR PhosphoSite; P29692; -.
DR DMDM; 20141357; -.
DR OGP; P29692; -.
DR PaxDb; P29692; -.
DR PRIDE; P29692; -.
DR DNASU; 1936; -.
DR Ensembl; ENST00000317198; ENSP00000317399; ENSG00000104529.
DR Ensembl; ENST00000395119; ENSP00000378551; ENSG00000104529.
DR Ensembl; ENST00000419152; ENSP00000388261; ENSG00000104529.
DR Ensembl; ENST00000423316; ENSP00000410059; ENSG00000104529.
DR Ensembl; ENST00000442189; ENSP00000391944; ENSG00000104529.
DR Ensembl; ENST00000524624; ENSP00000435697; ENSG00000104529.
DR Ensembl; ENST00000526838; ENSP00000436507; ENSG00000104529.
DR Ensembl; ENST00000528610; ENSP00000431763; ENSG00000104529.
DR Ensembl; ENST00000529272; ENSP00000434872; ENSG00000104529.
DR GeneID; 1936; -.
DR KEGG; hsa:1936; -.
DR UCSC; uc011lkl.2; human.
DR CTD; 1936; -.
DR GeneCards; GC08M144661; -.
DR H-InvDB; HIX0034587; -.
DR HGNC; HGNC:3211; EEF1D.
DR HPA; HPA045101; -.
DR MIM; 130592; gene.
DR neXtProt; NX_P29692; -.
DR PharmGKB; PA27647; -.
DR eggNOG; COG2092; -.
DR HOGENOM; HOG000207272; -.
DR HOVERGEN; HBG000787; -.
DR InParanoid; P29692; -.
DR KO; K15410; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; EEF1D; human.
DR GeneWiki; EEF1D; -.
DR GenomeRNAi; 1936; -.
DR NextBio; 7841; -.
DR PRO; PR:P29692; -.
DR ArrayExpress; P29692; -.
DR Bgee; P29692; -.
DR CleanEx; HS_EEF1D; -.
DR Genevestigator; P29692; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; TAS:ProtInc.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004871; F:signal transducer activity; IMP:UniProtKB.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0008135; F:translation factor activity, nucleic acid binding; TAS:ProtInc.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0006414; P:translational elongation; TAS:Reactome.
DR Gene3D; 3.30.70.60; -; 1.
DR InterPro; IPR018940; EF-1_beta_acid_region_euk.
DR InterPro; IPR014717; Transl_elong_EF1B/ribosomal_S6.
DR InterPro; IPR001326; Transl_elong_EF1B_B/D_CS.
DR InterPro; IPR014038; Transl_elong_fac_EF1B_bsu/dsu.
DR Pfam; PF10587; EF-1_beta_acid; 1.
DR Pfam; PF00736; EF1_GNE; 1.
DR SMART; SM00888; EF1_GNE; 1.
DR SUPFAM; SSF54984; SSF54984; 1.
DR PROSITE; PS00824; EF1BD_1; 1.
DR PROSITE; PS00825; EF1BD_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; DNA-binding; Elongation factor; Nucleus;
KW Phosphoprotein; Protein biosynthesis; Reference proteome;
KW Transcription; Transcription regulation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 281 Elongation factor 1-delta.
FT /FTId=PRO_0000155046.
FT REGION 80 115 Leucine-zipper.
FT REGION 173 281 Catalytic (GEF).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 17 17 N6-acetyllysine.
FT MOD_RES 107 107 N6-acetyllysine.
FT MOD_RES 117 117 N6-acetyllysine.
FT MOD_RES 133 133 Phosphoserine.
FT MOD_RES 147 147 Phosphothreonine.
FT MOD_RES 162 162 Phosphoserine; by CK2.
FT VAR_SEQ 1 1 M -> MRSGKASCTLETVWEDKHKYEEAERRFYEHEATQAA
FT ASAQQLPAEGPAMNGPGQDDPEDADEAEAPDGGSRRDPRKS
FT QDSRKPLQKKRKRSPKSGLGPADLALLGLSAERVWLDKSLF
FT DQAESSYRQKLADVAAQAAWPPALAPWGLCTHGNQVACHHV
FT TWGIWVNKSSFDQAERAFVEWSQALLLAPDGSRRQGTPNTG
FT QQVAVPDLAHQPSPPVNGQPPLGSLQALVREVWLEKPRYDA
FT AERGFYEALFDGHPPGKVRLQERAGLAEGARRGRRDRRGRN
FT ILGNKRAGLRRADGEAPSALPYCYFLQKDAEAPWLSKPAYD
FT SAECRHHAAEALRVAWCLEAASLSHRPGPRSGLSVSSLRPN
FT RKM (in isoform 2).
FT /FTId=VSP_037884.
FT VAR_SEQ 40 63 Missing (in isoform 3).
FT /FTId=VSP_043812.
FT VAR_SEQ 78 96 Missing (in isoform 4).
FT /FTId=VSP_045960.
FT CONFLICT 34 34 A -> R (in Ref. 1; CAA79716).
FT CONFLICT 44 44 S -> T (in Ref. 1; CAA79716).
FT CONFLICT 209 209 T -> A (in Ref. 4; BAG56855).
SQ SEQUENCE 281 AA; 31122 MW; CE778D6D5D09BD6C CRC64;
MATNFLAHEK IWFDKFKYDD AERRFYEQMN GPVAGASRQE NGASVILRDI ARARENIQKS
LAGSSGPGAS SGTSGDHGEL VVRIASLEVE NQSLRGVVQE LQQAISKLEA RLNVLEKSSP
GHRATAPQTQ HVSPMRQVEP PAKKPATPAE DDEDDDIDLF GSDNEEEDKE AAQLREERLR
QYAEKKAKKP ALVAKSSILL DVKPWDDETD MAQLEACVRS IQLDGLVWGA SKLVPVGYGI
RKLQIQCVVE DDKVGTDLLE EEITKFEEHV QSVDIAAFNK I
//
ID EF1D_HUMAN Reviewed; 281 AA.
AC P29692; B4DDU4; D3DWK3; E9PBQ9; Q4VBZ6; Q969J1; Q96I38;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 5.
DT 22-JAN-2014, entry version 150.
DE RecName: Full=Elongation factor 1-delta;
DE Short=EF-1-delta;
DE AltName: Full=Antigen NY-CO-4;
GN Name=EEF1D; Synonyms=EF1D;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DOMAIN LEUCINE ZIPPER.
RC TISSUE=Skin fibroblast;
RX PubMed=8334168; DOI=10.1016/0167-4781(93)90097-W;
RA Sanders J.P., Raggiaschi R., Morales J., Moeller W.;
RT "The human leucine zipper-containing guanine-nucleotide exchange
RT protein elongation factor-1 delta.";
RL Biochim. Biophys. Acta 1174:87-90(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Colon carcinoma;
RX PubMed=9610721;
RX DOI=10.1002/(SICI)1097-0215(19980529)76:5<652::AID-IJC7>3.0.CO;2-P;
RA Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E.,
RA Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J.;
RT "Characterization of human colon cancer antigens recognized by
RT autologous antibodies.";
RL Int. J. Cancer 76:652-658(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
RA Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
RA Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Brain, Lung, and Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 2-10 (ISOFORM 1), ACETYLATION AT ALA-2, AND MASS
RP SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V., Potts A., Barblan J., Quadroni M.;
RL Submitted (JUL-2004) to UniProtKB.
RN [10]
RP INDUCTION BY IONIZING RADIATION.
RX PubMed=8168075;
RA Jung M., Kondratyev A.D., Dritschilo A.;
RT "Elongation factor 1 delta is enhanced following exposure to ionizing
RT radiation.";
RL Cancer Res. 54:2541-2543(1994).
RN [11]
RP INDUCTION BY HOMOCYSTEINE.
RX PubMed=9677419; DOI=10.1074/jbc.273.31.19840;
RA Chacko G., Ling Q., Hajjar K.A.;
RT "Induction of acute translational response genes by homocysteine.
RT Elongation factors-1alpha, -beta, and -delta.";
RL J. Biol. Chem. 273:19840-19846(1998).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133; THR-147 AND
RP SER-162, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND MASS
RP SPECTROMETRY.
RC TISSUE=Pituitary;
RX PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
RA Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
RT "Phosphoproteomic analysis of the human pituitary.";
RL Pituitary 9:109-120(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND SER-162, AND
RP MASS SPECTROMETRY.
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate
RT cancer cells: identification of phosphoproteins in the LNCaP cell
RT line.";
RL Electrophoresis 28:2027-2034(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa
RT cells and high confident phosphopeptide identification by cross-
RT validation of MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.M700120-MCP200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,
RA Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate
RT reductase M2 subunit phosphorylation at residue serine 20 in canonical
RT Wnt signal transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND MASS
RP SPECTROMETRY.
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133; THR-147 AND
RP SER-162, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-91 AND SER-94 (ISOFORM 2),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40 (ISOFORM 3), AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND SER-162, AND
RP MASS SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147 AND SER-162, AND
RP MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17; LYS-107 AND LYS-117, AND
RP MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND SER-162, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [28]
RP FUNCTION (ISOFORM 2), INTERACTION WITH HSF1 AND NFE2L2 (ISOFORM 2),
RP TISSUE SPECIFICITY (ISOFORM 2), DNA-BINDING (ISOFORM 2), AND
RP SUBCELLULAR LOCATION (ISOFORM 2).
RX PubMed=21597468; DOI=10.1038/embor.2011.82;
RA Kaitsuka T., Tomizawa K., Matsushita M.;
RT "Transformation of eEF1Bdelta into heat-shock response transcription
RT factor by alternative splicing.";
RL EMBO Rep. 12:673-681(2011).
RN [29]
RP PHOSPHORYLATION AT SER-162 BY CK2.
RX PubMed=21936567; DOI=10.1021/pr2008994;
RA Gyenis L., Duncan J.S., Turowec J.P., Bretner M., Litchfield D.W.;
RT "Unbiased functional proteomics strategy for protein kinase inhibitor
RT validation and identification of bona fide protein kinase substrates:
RT application to identification of as a substrate for CK2.";
RL J. Proteome Res. 10:4887-4901(2011).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND SER-162, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Isoform 1: EF-1-beta and EF-1-delta stimulate the
CC exchange of GDP bound to EF-1-alpha to GTP, regenerating EF-1-
CC alpha for another round of transfer of aminoacyl-tRNAs to the
CC ribosome.
CC -!- FUNCTION: Isoform 2: Regulates induction of heat-shock-responsive
CC genes through association with heat shock transcription factors
CC and direct DNA-binding at heat shock promoter elements (HSE).
CC -!- SUBUNIT: EF-1 is composed of 4 subunits: alpha, beta, delta
CC isoform 1, and gamma. Isoform 2 interacts with HSF1 and NFE2L2.
CC -!- INTERACTION:
CC Q5T5U3:ARHGAP21; NbExp=2; IntAct=EBI-358607, EBI-1642518;
CC O95352:ATG7; NbExp=2; IntAct=EBI-358607, EBI-987834;
CC Q08AD1:CAMSAP2; NbExp=2; IntAct=EBI-358607, EBI-1051869;
CC P26641:EEF1G; NbExp=3; IntAct=EBI-358607, EBI-351467;
CC -!- SUBCELLULAR LOCATION: Isoform 2: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P29692-1; Sequence=Displayed;
CC Name=2; Synonyms=eEF1BdeltaL;
CC IsoId=P29692-2; Sequence=VSP_037884;
CC Note=Ref.3 (AAP35906), Ref.4 (EAW82228) and Ref.5 (AAH07847)
CC sequences are in conflict in position: 189:D->E. Contains a
CC phosphoserine at position 91. Contains a phosphoserine at
CC position 94;
CC Name=3;
CC IsoId=P29692-3; Sequence=VSP_043812;
CC Note=Contains a phosphoserine at position 40;
CC Name=4;
CC IsoId=P29692-4; Sequence=VSP_045960;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Isoform 2 is specifically expressed in brain,
CC cerebellum and testis.
CC -!- INDUCTION: By homocysteine (HC), may mediate accelerated synthesis
CC of free thiol-containing proteins in response to HC-induced
CC oxidative stress. Also induced following exposure to ionizing
CC radiation.
CC -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family.
CC -----------------------------------------------------------------------
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DR EMBL; Z21507; CAA79716.1; -; mRNA.
DR EMBL; BT007242; AAP35906.1; -; mRNA.
DR EMBL; AK293339; BAG56855.1; -; mRNA.
DR EMBL; AC067930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471162; EAW82227.1; -; Genomic_DNA.
DR EMBL; CH471162; EAW82228.1; -; Genomic_DNA.
DR EMBL; CH471162; EAW82229.1; -; Genomic_DNA.
DR EMBL; CH471162; EAW82230.1; -; Genomic_DNA.
DR EMBL; CH471162; EAW82232.1; -; Genomic_DNA.
DR EMBL; BC007847; AAH07847.1; -; mRNA.
DR EMBL; BC009907; AAH09907.1; -; mRNA.
DR EMBL; BC012819; AAH12819.1; -; mRNA.
DR EMBL; BC062535; AAH62535.1; -; mRNA.
DR EMBL; BC094806; AAH94806.1; -; mRNA.
DR PIR; S34626; S34626.
DR RefSeq; NP_001123525.2; NM_001130053.2.
DR RefSeq; NP_001123527.1; NM_001130055.2.
DR RefSeq; NP_001123528.1; NM_001130056.2.
DR RefSeq; NP_001123529.1; NM_001130057.2.
DR RefSeq; NP_001182132.1; NM_001195203.1.
DR RefSeq; NP_001951.2; NM_001960.4.
DR RefSeq; NP_115754.3; NM_032378.4.
DR RefSeq; XP_005250880.1; XM_005250823.1.
DR RefSeq; XP_005250881.1; XM_005250824.1.
DR RefSeq; XP_005250882.1; XM_005250825.1.
DR RefSeq; XP_005250883.1; XM_005250826.1.
DR UniGene; Hs.333388; -.
DR UniGene; Hs.686554; -.
DR UniGene; Hs.703306; -.
DR ProteinModelPortal; P29692; -.
DR SMR; P29692; 192-281.
DR IntAct; P29692; 56.
DR MINT; MINT-1139610; -.
DR STRING; 9606.ENSP00000391944; -.
DR PhosphoSite; P29692; -.
DR DMDM; 20141357; -.
DR OGP; P29692; -.
DR PaxDb; P29692; -.
DR PRIDE; P29692; -.
DR DNASU; 1936; -.
DR Ensembl; ENST00000317198; ENSP00000317399; ENSG00000104529.
DR Ensembl; ENST00000395119; ENSP00000378551; ENSG00000104529.
DR Ensembl; ENST00000419152; ENSP00000388261; ENSG00000104529.
DR Ensembl; ENST00000423316; ENSP00000410059; ENSG00000104529.
DR Ensembl; ENST00000442189; ENSP00000391944; ENSG00000104529.
DR Ensembl; ENST00000524624; ENSP00000435697; ENSG00000104529.
DR Ensembl; ENST00000526838; ENSP00000436507; ENSG00000104529.
DR Ensembl; ENST00000528610; ENSP00000431763; ENSG00000104529.
DR Ensembl; ENST00000529272; ENSP00000434872; ENSG00000104529.
DR GeneID; 1936; -.
DR KEGG; hsa:1936; -.
DR UCSC; uc011lkl.2; human.
DR CTD; 1936; -.
DR GeneCards; GC08M144661; -.
DR H-InvDB; HIX0034587; -.
DR HGNC; HGNC:3211; EEF1D.
DR HPA; HPA045101; -.
DR MIM; 130592; gene.
DR neXtProt; NX_P29692; -.
DR PharmGKB; PA27647; -.
DR eggNOG; COG2092; -.
DR HOGENOM; HOG000207272; -.
DR HOVERGEN; HBG000787; -.
DR InParanoid; P29692; -.
DR KO; K15410; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; EEF1D; human.
DR GeneWiki; EEF1D; -.
DR GenomeRNAi; 1936; -.
DR NextBio; 7841; -.
DR PRO; PR:P29692; -.
DR ArrayExpress; P29692; -.
DR Bgee; P29692; -.
DR CleanEx; HS_EEF1D; -.
DR Genevestigator; P29692; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; TAS:ProtInc.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004871; F:signal transducer activity; IMP:UniProtKB.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0008135; F:translation factor activity, nucleic acid binding; TAS:ProtInc.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0006414; P:translational elongation; TAS:Reactome.
DR Gene3D; 3.30.70.60; -; 1.
DR InterPro; IPR018940; EF-1_beta_acid_region_euk.
DR InterPro; IPR014717; Transl_elong_EF1B/ribosomal_S6.
DR InterPro; IPR001326; Transl_elong_EF1B_B/D_CS.
DR InterPro; IPR014038; Transl_elong_fac_EF1B_bsu/dsu.
DR Pfam; PF10587; EF-1_beta_acid; 1.
DR Pfam; PF00736; EF1_GNE; 1.
DR SMART; SM00888; EF1_GNE; 1.
DR SUPFAM; SSF54984; SSF54984; 1.
DR PROSITE; PS00824; EF1BD_1; 1.
DR PROSITE; PS00825; EF1BD_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; DNA-binding; Elongation factor; Nucleus;
KW Phosphoprotein; Protein biosynthesis; Reference proteome;
KW Transcription; Transcription regulation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 281 Elongation factor 1-delta.
FT /FTId=PRO_0000155046.
FT REGION 80 115 Leucine-zipper.
FT REGION 173 281 Catalytic (GEF).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 17 17 N6-acetyllysine.
FT MOD_RES 107 107 N6-acetyllysine.
FT MOD_RES 117 117 N6-acetyllysine.
FT MOD_RES 133 133 Phosphoserine.
FT MOD_RES 147 147 Phosphothreonine.
FT MOD_RES 162 162 Phosphoserine; by CK2.
FT VAR_SEQ 1 1 M -> MRSGKASCTLETVWEDKHKYEEAERRFYEHEATQAA
FT ASAQQLPAEGPAMNGPGQDDPEDADEAEAPDGGSRRDPRKS
FT QDSRKPLQKKRKRSPKSGLGPADLALLGLSAERVWLDKSLF
FT DQAESSYRQKLADVAAQAAWPPALAPWGLCTHGNQVACHHV
FT TWGIWVNKSSFDQAERAFVEWSQALLLAPDGSRRQGTPNTG
FT QQVAVPDLAHQPSPPVNGQPPLGSLQALVREVWLEKPRYDA
FT AERGFYEALFDGHPPGKVRLQERAGLAEGARRGRRDRRGRN
FT ILGNKRAGLRRADGEAPSALPYCYFLQKDAEAPWLSKPAYD
FT SAECRHHAAEALRVAWCLEAASLSHRPGPRSGLSVSSLRPN
FT RKM (in isoform 2).
FT /FTId=VSP_037884.
FT VAR_SEQ 40 63 Missing (in isoform 3).
FT /FTId=VSP_043812.
FT VAR_SEQ 78 96 Missing (in isoform 4).
FT /FTId=VSP_045960.
FT CONFLICT 34 34 A -> R (in Ref. 1; CAA79716).
FT CONFLICT 44 44 S -> T (in Ref. 1; CAA79716).
FT CONFLICT 209 209 T -> A (in Ref. 4; BAG56855).
SQ SEQUENCE 281 AA; 31122 MW; CE778D6D5D09BD6C CRC64;
MATNFLAHEK IWFDKFKYDD AERRFYEQMN GPVAGASRQE NGASVILRDI ARARENIQKS
LAGSSGPGAS SGTSGDHGEL VVRIASLEVE NQSLRGVVQE LQQAISKLEA RLNVLEKSSP
GHRATAPQTQ HVSPMRQVEP PAKKPATPAE DDEDDDIDLF GSDNEEEDKE AAQLREERLR
QYAEKKAKKP ALVAKSSILL DVKPWDDETD MAQLEACVRS IQLDGLVWGA SKLVPVGYGI
RKLQIQCVVE DDKVGTDLLE EEITKFEEHV QSVDIAAFNK I
//
MIM
130592
*RECORD*
*FIELD* NO
130592
*FIELD* TI
*130592 EUKARYOTIC TRANSLATION ELONGATION FACTOR 1, DELTA; EEF1D
;;ELONGATION FACTOR 1, DELTA; EF1D;;
read moreGUANINE NUCLEOTIDE EXCHANGE PROTEIN
*FIELD* TX
DESCRIPTION
Eukaryotic elongation factor-1 (EF1) consists of 4 subunits, EF1-alpha
(EEF1A1; 130590), EF1-beta (EEF1B2; 600655), EF1-gamma (EEF1G; 130593),
and EF1-delta. EIF-alpha-GTP transfers aminoacyl-tRNA to the ribosome,
and the release of animoacyl-tRNA from EIF-alpha-GTP is driven by GTP
hydrolysis. EF1-alpha-GDP is recycled to EF1-alpha-GTP by the EF1-beta,
-gamma, and -delta subunits (Sanders et al., 1996).
CLONING
Using Xenopus Ef1-delta to probe a human skin fibroblast cDNA library,
Sanders et al. (1993) cloned EF1-delta. The deduced 281-amino acid
protein has a calculated molecular mass of 31 kD. It has an N-terminal
leucine zipper domain and a C-terminal domain that is similar to that of
EF1-beta and is predicted to show GDP/GTP exchange activity. EF1-delta
also has a conserved serine phosphorylation site. SDS-PAGE detected
EF1-delta at an apparent molecular mass of 38 kD.
By Western blot analysis, Sanders et al. (1996) detected 1 major and 2
minor EF1-delta bands, which they attributed to variable degrees of
phosphorylation. Immunofluorescence analysis detected EF1-beta, -gamma,
and -delta in a perinuclear distribution in human foreskin fibroblasts,
and these subunits colocalized with an endoplasmic reticulum (ER)
resident protein. In contrast, EF1-alpha showed strong nuclear staining
and diffuse cytoplasmic staining.
GENE FUNCTION
Human immunodeficiency virus-1 (HIV-1) Tat protein has an N-terminal
domain that is a potent activator of transcription from the viral long
terminal repeat promoter. Tat is also essential for viral replication
and can activate or repress transcription of host cell genes. Using Tat
as bait in a yeast 2-hybrid screen of a HeLa cell cDNA library, Xiao et
al. (1998) isolated EF1-delta. Protein pull-down and Western blot
analyses confirmed direct interaction between Tat and EF1-delta.
EF1-delta specifically interacted with the Tat C-terminal domain.
Titration of purified recombinant Tat into in vitro translation
reactions showed that Tat inhibited translation of cellular, but not
viral, proteins. Xiao et al. (1998) hypothesized that by binding
EF1-delta, Tat redirects the protein synthesis machinery toward
producing large amounts of viral proteins.
Using yeast 2-hybrid analysis, Ong et al. (2003) found that kinectin
(KTN1; 600381) interacted directly with EF1-delta. Using peptide
fragments, Ong et al. (2003) showed that a 60-amino acid domain near the
kinectin C terminus was required for EF1-delta binding. Endogenous
kinectin colocalized with EF1-delta in the ER. Expression of the
kinectin EF1-delta-binding domain disrupted EF1-delta localization,
suggesting that kinectin anchors EF1-delta to the ER membrane. Ong et
al. (2003) also showed that CDC2 (116940) phosphorylated HeLa cell
EF1-delta in vitro.
*FIELD* RF
1. Ong, L.-L.; Er, C. P. N.; Ho, A.; Aung, M. T.; Yu, H.: Kinectin
anchors the translation elongation factor-1-delta to the endoplasmic
reticulum. J. Biol. Chem. 278: 32115-32123, 2003.
2. Sanders, J.; Brandsma, M.; Janssen, G. M. C.; Dijk, J.; Moller,
W.: Immunofluorescence studies of human fibroblasts demonstrate the
presence of the complex of elongation factor-1-beta-gamma-delta in
the endoplasmic reticulum. J. Cell Sci. 109: 1113-1117, 1996.
3. Sanders, J.; Raggiaschi, R.; Morales, J.; Moller, W.: The human
leucine zipper-containing guanine-nucleotide exchange protein elongation
factor-1 delta. Biochim. Biophys. Acta 1174: 87-90, 1993.
4. Xiao, H.; Neuveut, C.; Benkirane, M.; Jeang, K.-T.: Interaction
of the second coding exon of Tat with human EF-1-delta delineates
a mechanism for HIV-1-mediated shut-off of host mRNA translation. Biochem.
Biophys. Res. Commun. 244: 384-389, 1998.
*FIELD* CN
Patricia A. Hartz - updated: 10/3/2008
*FIELD* CD
Victor A. McKusick: 7/12/1991
*FIELD* ED
mgross: 10/08/2008
terry: 10/3/2008
terry: 8/11/1998
dkim: 7/21/1998
dkim: 6/30/1998
mark: 4/1/1996
carol: 3/1/1995
supermim: 3/16/1992
carol: 7/12/1991
*RECORD*
*FIELD* NO
130592
*FIELD* TI
*130592 EUKARYOTIC TRANSLATION ELONGATION FACTOR 1, DELTA; EEF1D
;;ELONGATION FACTOR 1, DELTA; EF1D;;
read moreGUANINE NUCLEOTIDE EXCHANGE PROTEIN
*FIELD* TX
DESCRIPTION
Eukaryotic elongation factor-1 (EF1) consists of 4 subunits, EF1-alpha
(EEF1A1; 130590), EF1-beta (EEF1B2; 600655), EF1-gamma (EEF1G; 130593),
and EF1-delta. EIF-alpha-GTP transfers aminoacyl-tRNA to the ribosome,
and the release of animoacyl-tRNA from EIF-alpha-GTP is driven by GTP
hydrolysis. EF1-alpha-GDP is recycled to EF1-alpha-GTP by the EF1-beta,
-gamma, and -delta subunits (Sanders et al., 1996).
CLONING
Using Xenopus Ef1-delta to probe a human skin fibroblast cDNA library,
Sanders et al. (1993) cloned EF1-delta. The deduced 281-amino acid
protein has a calculated molecular mass of 31 kD. It has an N-terminal
leucine zipper domain and a C-terminal domain that is similar to that of
EF1-beta and is predicted to show GDP/GTP exchange activity. EF1-delta
also has a conserved serine phosphorylation site. SDS-PAGE detected
EF1-delta at an apparent molecular mass of 38 kD.
By Western blot analysis, Sanders et al. (1996) detected 1 major and 2
minor EF1-delta bands, which they attributed to variable degrees of
phosphorylation. Immunofluorescence analysis detected EF1-beta, -gamma,
and -delta in a perinuclear distribution in human foreskin fibroblasts,
and these subunits colocalized with an endoplasmic reticulum (ER)
resident protein. In contrast, EF1-alpha showed strong nuclear staining
and diffuse cytoplasmic staining.
GENE FUNCTION
Human immunodeficiency virus-1 (HIV-1) Tat protein has an N-terminal
domain that is a potent activator of transcription from the viral long
terminal repeat promoter. Tat is also essential for viral replication
and can activate or repress transcription of host cell genes. Using Tat
as bait in a yeast 2-hybrid screen of a HeLa cell cDNA library, Xiao et
al. (1998) isolated EF1-delta. Protein pull-down and Western blot
analyses confirmed direct interaction between Tat and EF1-delta.
EF1-delta specifically interacted with the Tat C-terminal domain.
Titration of purified recombinant Tat into in vitro translation
reactions showed that Tat inhibited translation of cellular, but not
viral, proteins. Xiao et al. (1998) hypothesized that by binding
EF1-delta, Tat redirects the protein synthesis machinery toward
producing large amounts of viral proteins.
Using yeast 2-hybrid analysis, Ong et al. (2003) found that kinectin
(KTN1; 600381) interacted directly with EF1-delta. Using peptide
fragments, Ong et al. (2003) showed that a 60-amino acid domain near the
kinectin C terminus was required for EF1-delta binding. Endogenous
kinectin colocalized with EF1-delta in the ER. Expression of the
kinectin EF1-delta-binding domain disrupted EF1-delta localization,
suggesting that kinectin anchors EF1-delta to the ER membrane. Ong et
al. (2003) also showed that CDC2 (116940) phosphorylated HeLa cell
EF1-delta in vitro.
*FIELD* RF
1. Ong, L.-L.; Er, C. P. N.; Ho, A.; Aung, M. T.; Yu, H.: Kinectin
anchors the translation elongation factor-1-delta to the endoplasmic
reticulum. J. Biol. Chem. 278: 32115-32123, 2003.
2. Sanders, J.; Brandsma, M.; Janssen, G. M. C.; Dijk, J.; Moller,
W.: Immunofluorescence studies of human fibroblasts demonstrate the
presence of the complex of elongation factor-1-beta-gamma-delta in
the endoplasmic reticulum. J. Cell Sci. 109: 1113-1117, 1996.
3. Sanders, J.; Raggiaschi, R.; Morales, J.; Moller, W.: The human
leucine zipper-containing guanine-nucleotide exchange protein elongation
factor-1 delta. Biochim. Biophys. Acta 1174: 87-90, 1993.
4. Xiao, H.; Neuveut, C.; Benkirane, M.; Jeang, K.-T.: Interaction
of the second coding exon of Tat with human EF-1-delta delineates
a mechanism for HIV-1-mediated shut-off of host mRNA translation. Biochem.
Biophys. Res. Commun. 244: 384-389, 1998.
*FIELD* CN
Patricia A. Hartz - updated: 10/3/2008
*FIELD* CD
Victor A. McKusick: 7/12/1991
*FIELD* ED
mgross: 10/08/2008
terry: 10/3/2008
terry: 8/11/1998
dkim: 7/21/1998
dkim: 6/30/1998
mark: 4/1/1996
carol: 3/1/1995
supermim: 3/16/1992
carol: 7/12/1991