EF1D_HUMAN
ID EF1D_HUMAN Reviewed; 281 AA.
AC P29692; B4DDU4; D3DWK3; E9PBQ9; Q4VBZ6; Q969J1; Q96I38;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 226.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 protein
RT 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 autologous
RT 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 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., 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., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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
RP IDENTIFICATION BY MASS 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 SER-162, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 cancer
RT cells: identification of phosphoproteins in the LNCaP cell line.";
RL Electrophoresis 28:2027-2034(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 cells
RT and high confident phosphopeptide identification by cross-validation of
RT 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 IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Li S.-J.,
RA 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 reductase
RT M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal
RT transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 sequential
RT 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 SER-162, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-91 AND SER-94 (ISOFORM 2), PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-40 (ISOFORM 3), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
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 IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT 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., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT 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., Buerckstuemmer T.,
RA 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), TISSUE
RP SPECIFICITY (ISOFORM 2), DNA-BINDING (ISOFORM 2), AND SUBCELLULAR LOCATION
RP (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 factor
RT 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [31]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-44; SER-60; SER-86;
RP SER-119; THR-129; SER-133; THR-147 AND SER-162, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; THR-73; THR-129; SER-133
RP AND SER-162, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [34]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: [Isoform 1]: EF-1-beta and EF-1-delta stimulate the exchange
CC of GDP bound to EF-1-alpha to GTP, regenerating EF-1-alpha for another
CC round of transfer of aminoacyl-tRNAs to the ribosome.
CC -!- FUNCTION: [Isoform 2]: Regulates induction of heat-shock-responsive
CC genes through association with heat shock transcription factors and
CC direct DNA-binding at heat shock promoter elements (HSE).
CC -!- SUBUNIT: EF-1 is composed of 4 subunits: alpha, beta, delta isoform 1,
CC and gamma. Isoform 2 interacts with HSF1 and NFE2L2.
CC -!- INTERACTION:
CC P29692; Q5T5U3: ARHGAP21; NbExp=2; IntAct=EBI-358607, EBI-1642518;
CC P29692; O95352: ATG7; NbExp=2; IntAct=EBI-358607, EBI-987834;
CC P29692; Q08AD1: CAMSAP2; NbExp=2; IntAct=EBI-358607, EBI-1051869;
CC P29692; P26641: EEF1G; NbExp=4; IntAct=EBI-358607, EBI-351467;
CC P29692; P26641-2: EEF1G; NbExp=3; IntAct=EBI-358607, EBI-10177695;
CC P29692; Q96DN0: ERP27; NbExp=4; IntAct=EBI-358607, EBI-953772;
CC P29692; P42858: HTT; NbExp=6; IntAct=EBI-358607, EBI-466029;
CC P29692; P61244: MAX; NbExp=2; IntAct=EBI-358607, EBI-751711;
CC P29692; Q8IUQ4: SIAH1; NbExp=4; IntAct=EBI-358607, EBI-747107;
CC P29692; P00441: SOD1; NbExp=3; IntAct=EBI-358607, EBI-990792;
CC P29692; P13693: TPT1; NbExp=3; IntAct=EBI-358607, EBI-1783169;
CC P29692; Q67020: PA; Xeno; NbExp=2; IntAct=EBI-358607, EBI-11514477;
CC P29692-2; Q969K4: ABTB1; NbExp=4; IntAct=EBI-5280572, EBI-7223971;
CC P29692-2; Q99996-3: AKAP9; NbExp=3; IntAct=EBI-5280572, EBI-11022349;
CC P29692-2; Q15699: ALX1; NbExp=3; IntAct=EBI-5280572, EBI-750671;
CC P29692-2; Q86TI2-2: DPP9; NbExp=3; IntAct=EBI-5280572, EBI-21529239;
CC P29692-2; P26641: EEF1G; NbExp=4; IntAct=EBI-5280572, EBI-351467;
CC P29692-2; P26641-2: EEF1G; NbExp=3; IntAct=EBI-5280572, EBI-10177695;
CC P29692-2; O75344: FKBP6; NbExp=3; IntAct=EBI-5280572, EBI-744771;
CC P29692-2; Q15012: LAPTM4A; NbExp=3; IntAct=EBI-5280572, EBI-723416;
CC P29692-2; Q8N7X4: MAGEB6; NbExp=3; IntAct=EBI-5280572, EBI-6447163;
CC P29692-2; O95563: MPC2; NbExp=3; IntAct=EBI-5280572, EBI-719403;
CC P29692-2; O15534: PER1; NbExp=3; IntAct=EBI-5280572, EBI-2557276;
CC P29692-2; Q5T6S3: PHF19; NbExp=3; IntAct=EBI-5280572, EBI-2339674;
CC P29692-2; Q8TCT7-2: SPPL2B; NbExp=3; IntAct=EBI-5280572, EBI-8345366;
CC P29692-2; P21980-2: TGM2; NbExp=3; IntAct=EBI-5280572, EBI-25842075;
CC P29692-2; P13693: TPT1; NbExp=3; IntAct=EBI-5280572, EBI-1783169;
CC P29692-2; P45880: VDAC2; NbExp=3; IntAct=EBI-5280572, EBI-354022;
CC P29692-2; O43257: ZNHIT1; NbExp=3; IntAct=EBI-5280572, EBI-347522;
CC P29692-2; Q86V28; NbExp=3; IntAct=EBI-5280572, EBI-10259496;
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus
CC {ECO:0000269|PubMed:21597468}.
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 Name=3;
CC IsoId=P29692-3; Sequence=VSP_043812;
CC Name=4;
CC IsoId=P29692-4; Sequence=VSP_045960;
CC -!- TISSUE SPECIFICITY: Isoform 2 is specifically expressed in brain,
CC cerebellum and testis.
CC -!- INDUCTION: By homocysteine (HC), may mediate accelerated synthesis of
CC free thiol-containing proteins in response to HC-induced oxidative
CC stress. Also induced following exposure to ionizing radiation.
CC {ECO:0000269|PubMed:8168075, ECO:0000269|PubMed:9677419}.
CC -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family. {ECO:0000305}.
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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 CCDS; CCDS47930.1; -. [P29692-3]
DR CCDS; CCDS56559.1; -. [P29692-4]
DR CCDS; CCDS6404.1; -. [P29692-2]
DR CCDS; CCDS6405.1; -. [P29692-1]
DR PIR; S34626; S34626.
DR RefSeq; NP_001123525.2; NM_001130053.3. [P29692-2]
DR RefSeq; NP_001123527.1; NM_001130055.3. [P29692-1]
DR RefSeq; NP_001123528.1; NM_001130056.3. [P29692-3]
DR RefSeq; NP_001123529.1; NM_001130057.3. [P29692-1]
DR RefSeq; NP_001182132.1; NM_001195203.2. [P29692-4]
DR RefSeq; NP_001276879.1; NM_001289950.2. [P29692-1]
DR RefSeq; NP_001304672.1; NM_001317743.2. [P29692-3]
DR RefSeq; NP_001317575.1; NM_001330646.1. [P29692-3]
DR RefSeq; NP_001951.2; NM_001960.5. [P29692-1]
DR RefSeq; NP_115754.3; NM_032378.5. [P29692-2]
DR RefSeq; XP_005250880.1; XM_005250823.1. [P29692-2]
DR RefSeq; XP_006716585.1; XM_006716522.1. [P29692-2]
DR RefSeq; XP_006716586.1; XM_006716523.1. [P29692-2]
DR RefSeq; XP_006716587.1; XM_006716524.1. [P29692-2]
DR RefSeq; XP_006716588.1; XM_006716525.1. [P29692-1]
DR RefSeq; XP_011515207.1; XM_011516905.2. [P29692-2]
DR RefSeq; XP_011515208.1; XM_011516906.2. [P29692-2]
DR RefSeq; XP_016868659.1; XM_017013170.1. [P29692-2]
DR PDB; 2MVM; NMR; -; A=153-192.
DR PDB; 2MVN; NMR; -; A=153-192.
DR PDB; 2N51; NMR; -; A=153-281.
DR PDB; 5JPO; X-ray; 2.00 A; E=1-30.
DR PDBsum; 2MVM; -.
DR PDBsum; 2MVN; -.
DR PDBsum; 2N51; -.
DR PDBsum; 5JPO; -.
DR AlphaFoldDB; P29692; -.
DR BMRB; P29692; -.
DR SMR; P29692; -.
DR BioGRID; 108256; 261.
DR IntAct; P29692; 151.
DR MINT; P29692; -.
DR STRING; 9606.ENSP00000410059; -.
DR ChEMBL; CHEMBL4295739; -.
DR iPTMnet; P29692; -.
DR MetOSite; P29692; -.
DR PhosphoSitePlus; P29692; -.
DR SwissPalm; P29692; -.
DR BioMuta; EEF1D; -.
DR DMDM; 20141357; -.
DR OGP; P29692; -.
DR CPTAC; CPTAC-500; -.
DR CPTAC; CPTAC-501; -.
DR EPD; P29692; -.
DR jPOST; P29692; -.
DR MassIVE; P29692; -.
DR MaxQB; P29692; -.
DR PaxDb; P29692; -.
DR PeptideAtlas; P29692; -.
DR PRIDE; P29692; -.
DR ProteomicsDB; 19276; -.
DR ProteomicsDB; 54603; -. [P29692-1]
DR ProteomicsDB; 54604; -. [P29692-2]
DR ProteomicsDB; 54605; -. [P29692-3]
DR TopDownProteomics; P29692-1; -. [P29692-1]
DR TopDownProteomics; P29692-3; -. [P29692-3]
DR TopDownProteomics; P29692-4; -. [P29692-4]
DR Antibodypedia; 27948; 340 antibodies from 30 providers.
DR DNASU; 1936; -.
DR Ensembl; ENST00000317198.10; ENSP00000317399.6; ENSG00000104529.19. [P29692-1]
DR Ensembl; ENST00000395119.7; ENSP00000378551.3; ENSG00000104529.19. [P29692-1]
DR Ensembl; ENST00000419152.7; ENSP00000388261.2; ENSG00000104529.19. [P29692-1]
DR Ensembl; ENST00000442189.6; ENSP00000391944.2; ENSG00000104529.19. [P29692-2]
DR Ensembl; ENST00000524624.5; ENSP00000435697.1; ENSG00000104529.19. [P29692-3]
DR Ensembl; ENST00000526838.5; ENSP00000436507.1; ENSG00000104529.19. [P29692-4]
DR Ensembl; ENST00000528610.5; ENSP00000431763.1; ENSG00000104529.19. [P29692-3]
DR Ensembl; ENST00000529272.5; ENSP00000434872.1; ENSG00000104529.19. [P29692-1]
DR Ensembl; ENST00000529516.6; ENSP00000431742.2; ENSG00000104529.19. [P29692-4]
DR Ensembl; ENST00000530191.6; ENSP00000436542.2; ENSG00000104529.19. [P29692-1]
DR Ensembl; ENST00000530445.6; ENSP00000436933.2; ENSG00000104529.19. [P29692-1]
DR Ensembl; ENST00000531218.6; ENSP00000434448.2; ENSG00000104529.19. [P29692-1]
DR Ensembl; ENST00000533494.6; ENSP00000433412.2; ENSG00000104529.19. [P29692-1]
DR Ensembl; ENST00000534377.6; ENSP00000431460.2; ENSG00000104529.19. [P29692-3]
DR Ensembl; ENST00000534380.6; ENSP00000433611.2; ENSG00000104529.19. [P29692-1]
DR Ensembl; ENST00000614575.4; ENSP00000478340.2; ENSG00000273594.4. [P29692-1]
DR Ensembl; ENST00000615067.4; ENSP00000479653.1; ENSG00000273594.4. [P29692-1]
DR Ensembl; ENST00000615698.4; ENSP00000483527.1; ENSG00000273594.4. [P29692-1]
DR Ensembl; ENST00000618139.4; ENSP00000484536.2; ENSG00000104529.19. [P29692-2]
DR Ensembl; ENST00000619144.4; ENSP00000477608.1; ENSG00000273594.4. [P29692-2]
DR Ensembl; ENST00000620155.3; ENSP00000480505.1; ENSG00000273594.4. [P29692-2]
DR Ensembl; ENST00000631698.1; ENSP00000488672.1; ENSG00000273594.4. [P29692-4]
DR Ensembl; ENST00000632587.1; ENSP00000487680.1; ENSG00000273594.4. [P29692-1]
DR Ensembl; ENST00000632675.1; ENSP00000488026.1; ENSG00000273594.4. [P29692-3]
DR Ensembl; ENST00000632965.1; ENSP00000488275.1; ENSG00000273594.4. [P29692-3]
DR GeneID; 1936; -.
DR KEGG; hsa:1936; -.
DR MANE-Select; ENST00000618139.4; ENSP00000484536.2; NM_001130053.5; NP_001123525.3. [P29692-2]
DR UCSC; uc003yyr.4; human. [P29692-1]
DR CTD; 1936; -.
DR DisGeNET; 1936; -.
DR GeneCards; EEF1D; -.
DR HGNC; HGNC:3211; EEF1D.
DR HPA; ENSG00000104529; Low tissue specificity.
DR MalaCards; EEF1D; -.
DR MIM; 130592; gene.
DR neXtProt; NX_P29692; -.
DR OpenTargets; ENSG00000104529; -.
DR PharmGKB; PA27647; -.
DR VEuPathDB; HostDB:ENSG00000104529; -.
DR eggNOG; KOG1668; Eukaryota.
DR GeneTree; ENSGT00950000183014; -.
DR HOGENOM; CLU_020166_0_0_1; -.
DR InParanoid; P29692; -.
DR OMA; RVWLDKP; -.
DR OrthoDB; 1464823at2759; -.
DR PhylomeDB; P29692; -.
DR TreeFam; TF313134; -.
DR PathwayCommons; P29692; -.
DR Reactome; R-HSA-156842; Eukaryotic Translation Elongation.
DR SignaLink; P29692; -.
DR SIGNOR; P29692; -.
DR BioGRID-ORCS; 1936; 13 hits in 1077 CRISPR screens.
DR ChiTaRS; EEF1D; human.
DR GeneWiki; EEF1D; -.
DR GenomeRNAi; 1936; -.
DR Pharos; P29692; Tbio.
DR PRO; PR:P29692; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P29692; protein.
DR Bgee; ENSG00000104529; Expressed in calcaneal tendon and 95 other tissues.
DR ExpressionAtlas; P29692; baseline and differential.
DR Genevisible; P29692; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; TAS:ProtInc.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0031072; F:heat shock protein binding; IPI:UniProtKB.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0008135; F:translation factor activity, RNA binding; TAS:ProtInc.
DR GO; GO:0071479; P:cellular response to ionizing radiation; IDA:UniProtKB.
DR GO; GO:0009299; P:mRNA transcription; IDA:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; HMP:UniProtKB.
DR GO; GO:0010941; P:regulation of cell death; IMP:UniProtKB.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR CDD; cd00292; EF1B; 1.
DR Gene3D; 3.30.70.60; -; 1.
DR InterPro; IPR036219; eEF-1beta-like_sf.
DR InterPro; IPR018940; EF-1_beta_acid_region_euk.
DR InterPro; IPR014038; EF1B_bsu/dsu_GNE.
DR InterPro; IPR014717; Transl_elong_EF1B/ribosomal_S6.
DR InterPro; IPR001326; Transl_elong_EF1B_B/D_CS.
DR Pfam; PF10587; EF-1_beta_acid; 1.
DR Pfam; PF00736; EF1_GNE; 1.
DR SMART; SM01182; EF-1_beta_acid; 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 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW DNA-binding; Elongation factor; Nucleus; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..281
FT /note="Elongation factor 1-delta"
FT /id="PRO_0000155046"
FT REGION 80..115
FT /note="Leucine-zipper"
FT REGION 118..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..281
FT /note="Catalytic (GEF)"
FT COMPBIAS 151..165
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 73
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FR9"
FT MOD_RES 107
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 117
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 117
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P57776"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 129
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17487921, ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 147
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 162
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:21936567,
FT ECO:0007744|PubMed:16807684, ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17487921, ECO:0007744|PubMed:17693683,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1
FT /note="M -> MRSGKASCTLETVWEDKHKYEEAERRFYEHEATQAAASAQQLPAEGP
FT AMNGPGQDDPEDADEAEAPDGGSRRDPRKSQDSRKPLQKKRKRSPKSGLGPADLALLGL
FT SAERVWLDKSLFDQAESSYRQKLADVAAQAAWPPALAPWGLCTHGNQVACHHVTWGIWV
FT NKSSFDQAERAFVEWSQALLLAPDGSRRQGTPNTGQQVAVPDLAHQPSPPVNGQPPLGS
FT LQALVREVWLEKPRYDAAERGFYEALFDGHPPGKVRLQERAGLAEGARRGRRDRRGRNI
FT LGNKRAGLRRADGEAPSALPYCYFLQKDAEAPWLSKPAYDSAECRHHAAEALRVAWCLE
FT AASLSHRPGPRSGLSVSSLRPNRKM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_037884"
FT VAR_SEQ 40..63
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043812"
FT VAR_SEQ 78..96
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045960"
FT CONFLICT 34
FT /note="A -> R (in Ref. 1; CAA79716)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="S -> T (in Ref. 1; CAA79716)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="T -> A (in Ref. 4; BAG56855)"
FT /evidence="ECO:0000305"
FT HELIX 2..9
FT /evidence="ECO:0007829|PDB:5JPO"
FT HELIX 15..27
FT /evidence="ECO:0007829|PDB:5JPO"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:2MVM"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:2MVM"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:2MVN"
FT HELIX 169..185
FT /evidence="ECO:0007829|PDB:2MVM"
FT TURN 187..190
FT /evidence="ECO:0007829|PDB:2MVN"
FT STRAND 195..206
FT /evidence="ECO:0007829|PDB:2N51"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:2N51"
FT STRAND 226..235
FT /evidence="ECO:0007829|PDB:2N51"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:2N51"
FT STRAND 241..250
FT /evidence="ECO:0007829|PDB:2N51"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:2N51"
FT HELIX 256..265
FT /evidence="ECO:0007829|PDB:2N51"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:2N51"
FT STRAND 270..280
FT /evidence="ECO:0007829|PDB:2N51"
FT MOD_RES P29692-2:91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES P29692-2:94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CONFLICT P29692-2:189
FT /note="D -> E (in Ref. 3; AAP35906, 4; EAW82228 and 5;
FT AAH07847)"
FT /evidence="ECO:0000305"
FT MOD_RES P29692-3:40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
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
