Full text data of EEF1B2
EEF1B2
(EEF1B, EF1B)
[Confidence: low (only semi-automatic identification from reviews)]
Elongation factor 1-beta; EF-1-beta
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Elongation factor 1-beta; EF-1-beta
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P24534
ID EF1B_HUMAN Reviewed; 225 AA.
AC P24534; A8K795; Q6IBH9;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 159.
DE RecName: Full=Elongation factor 1-beta;
DE Short=EF-1-beta;
GN Name=EEF1B2; Synonyms=EEF1B, EF1B;
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].
RC TISSUE=Skin fibroblast;
RX PubMed=1886777; DOI=10.1093/nar/19.16.4551;
RA Sanders J., Maassen J.A., Amons R., Moeller W.;
RT "Nucleotide sequence of human elongation factor-1 beta cDNA.";
RL Nucleic Acids Res. 19:4551-4551(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovarian granulosa cell;
RX PubMed=1710449; DOI=10.1016/0006-291X(91)91984-K;
RA von der Kammer H., Klaudiny J., Zimmer M., Scheit K.H.;
RT "Human elongation factor 1 beta: cDNA and derived amino acid
RT sequence.";
RL Biochem. Biophys. Res. Commun. 177:312-317(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Eye, and Pancreas;
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 2-11.
RC TISSUE=Liver;
RX PubMed=1286669; DOI=10.1002/elps.11501301201;
RA Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
RA Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
RA Appel R.D., Hughes G.J.;
RT "Human liver protein map: a reference database established by
RT microsequencing and gel comparison.";
RL Electrophoresis 13:992-1001(1992).
RN [10]
RP PROTEIN SEQUENCE OF 8-22; 140-157 AND 164-176, AND MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [11]
RP PROTEIN SEQUENCE OF 55-60; 79-85; 123-127 AND 164-175.
RC TISSUE=Keratinocyte;
RX PubMed=1286667; DOI=10.1002/elps.11501301199;
RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA Vandekerckhove J.;
RT "Microsequences of 145 proteins recorded in the two-dimensional gel
RT protein database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASS
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASS
RP 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-106, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASS
RP 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-95 AND SER-106,
RP AND MASS 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, 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 [19]
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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASS
RP 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-95 AND SER-106,
RP AND 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 [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-7, AND 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95 AND SER-106, AND MASS
RP 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 [24]
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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; THR-93; SER-95 AND
RP SER-106, AND 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).
CC -!- FUNCTION: EF-1-beta and EF-1-delta stimulate the exchange of GDP
CC bound to EF-1-alpha to GTP.
CC -!- SUBUNIT: EF-1 is composed of 4 subunits: alpha, beta, delta, and
CC gamma.
CC -!- INTERACTION:
CC P26641:EEF1G; NbExp=3; IntAct=EBI-354334, EBI-351467;
CC -!- INDUCTION: By homocysteine (HC), may mediate accelerated synthesis
CC of free thiol-containing proteins in response to HC-induced
CC oxidative stress.
CC -!- PTM: Phosphorylation affects the GDP/GTP exchange rate.
CC -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family.
CC -!- SIMILARITY: Contains 1 GST C-terminal domain.
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DR EMBL; X60489; CAA43019.1; -; mRNA.
DR EMBL; X60656; CAA43063.1; -; mRNA.
DR EMBL; BT007079; AAP35742.1; -; mRNA.
DR EMBL; CR456825; CAG33106.1; -; mRNA.
DR EMBL; AK291910; BAF84599.1; -; mRNA.
DR EMBL; AC007383; AAY15062.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70381.1; -; Genomic_DNA.
DR EMBL; BC000211; AAH00211.1; -; mRNA.
DR EMBL; BC004931; AAH04931.1; -; mRNA.
DR EMBL; BC067787; AAH67787.1; -; mRNA.
DR PIR; S25432; S25432.
DR RefSeq; NP_001032752.1; NM_001037663.1.
DR RefSeq; NP_001950.1; NM_001959.3.
DR RefSeq; NP_066944.1; NM_021121.3.
DR UniGene; Hs.421608; -.
DR PDB; 1B64; NMR; -; A=136-224.
DR PDBsum; 1B64; -.
DR ProteinModelPortal; P24534; -.
DR SMR; P24534; 10-72, 136-225.
DR IntAct; P24534; 22.
DR MINT; MINT-4999956; -.
DR STRING; 9606.ENSP00000236957; -.
DR PhosphoSite; P24534; -.
DR DMDM; 119163; -.
DR DOSAC-COBS-2DPAGE; P24534; -.
DR OGP; P24534; -.
DR SWISS-2DPAGE; P24534; -.
DR PaxDb; P24534; -.
DR PeptideAtlas; P24534; -.
DR PRIDE; P24534; -.
DR DNASU; 1933; -.
DR Ensembl; ENST00000236957; ENSP00000236957; ENSG00000114942.
DR Ensembl; ENST00000392221; ENSP00000376055; ENSG00000114942.
DR Ensembl; ENST00000392222; ENSP00000376056; ENSG00000114942.
DR GeneID; 1933; -.
DR KEGG; hsa:1933; -.
DR UCSC; uc002vbf.1; human.
DR CTD; 1933; -.
DR GeneCards; GC02P207024; -.
DR HGNC; HGNC:3208; EEF1B2.
DR HPA; CAB012477; -.
DR MIM; 600655; gene.
DR neXtProt; NX_P24534; -.
DR PharmGKB; PA27644; -.
DR eggNOG; COG2092; -.
DR HOGENOM; HOG000207273; -.
DR HOVERGEN; HBG000787; -.
DR InParanoid; P24534; -.
DR KO; K03232; -.
DR OMA; YESEFAS; -.
DR OrthoDB; EOG7RZ5QW; -.
DR PhylomeDB; P24534; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; EEF1B2; human.
DR EvolutionaryTrace; P24534; -.
DR GeneWiki; EEF1B2; -.
DR GenomeRNAi; 1933; -.
DR NextBio; 7829; -.
DR PMAP-CutDB; P24534; -.
DR PRO; PR:P24534; -.
DR ArrayExpress; P24534; -.
DR Bgee; P24534; -.
DR CleanEx; HS_EEF1B2; -.
DR Genevestigator; P24534; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; NAS:UniProtKB.
DR GO; GO:0003746; F:translation elongation factor activity; NAS:UniProtKB.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.30.70.60; -; 1.
DR InterPro; IPR018940; EF-1_beta_acid_region_euk.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
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; SSF47616; SSF47616; 1.
DR SUPFAM; SSF54984; SSF54984; 1.
DR PROSITE; PS00824; EF1BD_1; 1.
DR PROSITE; PS00825; EF1BD_2; 1.
DR PROSITE; PS50405; GST_CTER; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; Elongation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 225 Elongation factor 1-beta.
FT /FTId=PRO_0000155021.
FT DOMAIN 2 84 GST C-terminal.
FT MOD_RES 7 7 N6-acetyllysine.
FT MOD_RES 8 8 Phosphoserine.
FT MOD_RES 93 93 Phosphothreonine.
FT MOD_RES 95 95 Phosphoserine.
FT MOD_RES 106 106 Phosphoserine.
FT STRAND 140 150
FT HELIX 155 164
FT STRAND 171 183
FT STRAND 185 193
FT HELIX 200 207
FT TURN 211 213
FT STRAND 214 220
SQ SEQUENCE 225 AA; 24764 MW; CDE763ADBF127822 CRC64;
MGFGDLKSPA GLQVLNDYLA DKSYIEGYVP SQADVAVFEA VSSPPPADLC HALRWYNHIK
SYEKEKASLP GVKKALGKYG PADVEDTTGS GATDSKDDDD IDLFGSDDEE ESEEAKRLRE
ERLAQYESKK AKKPALVAKS SILLDVKPWD DETDMAKLEE CVRSIQADGL VWGSSKLVPV
GYGIKKLQIQ CVVEDDKVGT DMLEEQITAF EDYVQSMDVA AFNKI
//
ID EF1B_HUMAN Reviewed; 225 AA.
AC P24534; A8K795; Q6IBH9;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 159.
DE RecName: Full=Elongation factor 1-beta;
DE Short=EF-1-beta;
GN Name=EEF1B2; Synonyms=EEF1B, EF1B;
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].
RC TISSUE=Skin fibroblast;
RX PubMed=1886777; DOI=10.1093/nar/19.16.4551;
RA Sanders J., Maassen J.A., Amons R., Moeller W.;
RT "Nucleotide sequence of human elongation factor-1 beta cDNA.";
RL Nucleic Acids Res. 19:4551-4551(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovarian granulosa cell;
RX PubMed=1710449; DOI=10.1016/0006-291X(91)91984-K;
RA von der Kammer H., Klaudiny J., Zimmer M., Scheit K.H.;
RT "Human elongation factor 1 beta: cDNA and derived amino acid
RT sequence.";
RL Biochem. Biophys. Res. Commun. 177:312-317(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Eye, and Pancreas;
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 2-11.
RC TISSUE=Liver;
RX PubMed=1286669; DOI=10.1002/elps.11501301201;
RA Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
RA Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
RA Appel R.D., Hughes G.J.;
RT "Human liver protein map: a reference database established by
RT microsequencing and gel comparison.";
RL Electrophoresis 13:992-1001(1992).
RN [10]
RP PROTEIN SEQUENCE OF 8-22; 140-157 AND 164-176, AND MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [11]
RP PROTEIN SEQUENCE OF 55-60; 79-85; 123-127 AND 164-175.
RC TISSUE=Keratinocyte;
RX PubMed=1286667; DOI=10.1002/elps.11501301199;
RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA Vandekerckhove J.;
RT "Microsequences of 145 proteins recorded in the two-dimensional gel
RT protein database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASS
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASS
RP 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-106, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASS
RP 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-95 AND SER-106,
RP AND MASS 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, 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 [19]
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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASS
RP 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-95 AND SER-106,
RP AND 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 [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-7, AND 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95 AND SER-106, AND MASS
RP 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 [24]
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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; THR-93; SER-95 AND
RP SER-106, AND 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).
CC -!- FUNCTION: EF-1-beta and EF-1-delta stimulate the exchange of GDP
CC bound to EF-1-alpha to GTP.
CC -!- SUBUNIT: EF-1 is composed of 4 subunits: alpha, beta, delta, and
CC gamma.
CC -!- INTERACTION:
CC P26641:EEF1G; NbExp=3; IntAct=EBI-354334, EBI-351467;
CC -!- INDUCTION: By homocysteine (HC), may mediate accelerated synthesis
CC of free thiol-containing proteins in response to HC-induced
CC oxidative stress.
CC -!- PTM: Phosphorylation affects the GDP/GTP exchange rate.
CC -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family.
CC -!- SIMILARITY: Contains 1 GST C-terminal domain.
CC -----------------------------------------------------------------------
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DR EMBL; X60489; CAA43019.1; -; mRNA.
DR EMBL; X60656; CAA43063.1; -; mRNA.
DR EMBL; BT007079; AAP35742.1; -; mRNA.
DR EMBL; CR456825; CAG33106.1; -; mRNA.
DR EMBL; AK291910; BAF84599.1; -; mRNA.
DR EMBL; AC007383; AAY15062.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70381.1; -; Genomic_DNA.
DR EMBL; BC000211; AAH00211.1; -; mRNA.
DR EMBL; BC004931; AAH04931.1; -; mRNA.
DR EMBL; BC067787; AAH67787.1; -; mRNA.
DR PIR; S25432; S25432.
DR RefSeq; NP_001032752.1; NM_001037663.1.
DR RefSeq; NP_001950.1; NM_001959.3.
DR RefSeq; NP_066944.1; NM_021121.3.
DR UniGene; Hs.421608; -.
DR PDB; 1B64; NMR; -; A=136-224.
DR PDBsum; 1B64; -.
DR ProteinModelPortal; P24534; -.
DR SMR; P24534; 10-72, 136-225.
DR IntAct; P24534; 22.
DR MINT; MINT-4999956; -.
DR STRING; 9606.ENSP00000236957; -.
DR PhosphoSite; P24534; -.
DR DMDM; 119163; -.
DR DOSAC-COBS-2DPAGE; P24534; -.
DR OGP; P24534; -.
DR SWISS-2DPAGE; P24534; -.
DR PaxDb; P24534; -.
DR PeptideAtlas; P24534; -.
DR PRIDE; P24534; -.
DR DNASU; 1933; -.
DR Ensembl; ENST00000236957; ENSP00000236957; ENSG00000114942.
DR Ensembl; ENST00000392221; ENSP00000376055; ENSG00000114942.
DR Ensembl; ENST00000392222; ENSP00000376056; ENSG00000114942.
DR GeneID; 1933; -.
DR KEGG; hsa:1933; -.
DR UCSC; uc002vbf.1; human.
DR CTD; 1933; -.
DR GeneCards; GC02P207024; -.
DR HGNC; HGNC:3208; EEF1B2.
DR HPA; CAB012477; -.
DR MIM; 600655; gene.
DR neXtProt; NX_P24534; -.
DR PharmGKB; PA27644; -.
DR eggNOG; COG2092; -.
DR HOGENOM; HOG000207273; -.
DR HOVERGEN; HBG000787; -.
DR InParanoid; P24534; -.
DR KO; K03232; -.
DR OMA; YESEFAS; -.
DR OrthoDB; EOG7RZ5QW; -.
DR PhylomeDB; P24534; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; EEF1B2; human.
DR EvolutionaryTrace; P24534; -.
DR GeneWiki; EEF1B2; -.
DR GenomeRNAi; 1933; -.
DR NextBio; 7829; -.
DR PMAP-CutDB; P24534; -.
DR PRO; PR:P24534; -.
DR ArrayExpress; P24534; -.
DR Bgee; P24534; -.
DR CleanEx; HS_EEF1B2; -.
DR Genevestigator; P24534; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; NAS:UniProtKB.
DR GO; GO:0003746; F:translation elongation factor activity; NAS:UniProtKB.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.30.70.60; -; 1.
DR InterPro; IPR018940; EF-1_beta_acid_region_euk.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
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; SSF47616; SSF47616; 1.
DR SUPFAM; SSF54984; SSF54984; 1.
DR PROSITE; PS00824; EF1BD_1; 1.
DR PROSITE; PS00825; EF1BD_2; 1.
DR PROSITE; PS50405; GST_CTER; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; Elongation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 225 Elongation factor 1-beta.
FT /FTId=PRO_0000155021.
FT DOMAIN 2 84 GST C-terminal.
FT MOD_RES 7 7 N6-acetyllysine.
FT MOD_RES 8 8 Phosphoserine.
FT MOD_RES 93 93 Phosphothreonine.
FT MOD_RES 95 95 Phosphoserine.
FT MOD_RES 106 106 Phosphoserine.
FT STRAND 140 150
FT HELIX 155 164
FT STRAND 171 183
FT STRAND 185 193
FT HELIX 200 207
FT TURN 211 213
FT STRAND 214 220
SQ SEQUENCE 225 AA; 24764 MW; CDE763ADBF127822 CRC64;
MGFGDLKSPA GLQVLNDYLA DKSYIEGYVP SQADVAVFEA VSSPPPADLC HALRWYNHIK
SYEKEKASLP GVKKALGKYG PADVEDTTGS GATDSKDDDD IDLFGSDDEE ESEEAKRLRE
ERLAQYESKK AKKPALVAKS SILLDVKPWD DETDMAKLEE CVRSIQADGL VWGSSKLVPV
GYGIKKLQIQ CVVEDDKVGT DMLEEQITAF EDYVQSMDVA AFNKI
//
MIM
600655
*RECORD*
*FIELD* NO
600655
*FIELD* TI
*600655 EUKARYOTIC TRANSLATION ELONGATION FACTOR 1, BETA-2; EEF1B2
;;ELONGATION FACTOR 1, BETA-2A;;
read moreELONGATION FACTOR 1, BETA; EF1B
EUKARYOTIC TRANSLATION ELONGATION FACTOR 1, BETA-1, PSEUDOGENE, INCLUDED;
EEF1B1, INCLUDED; EEF1B2P1, INCLUDED;;
EUKARYOTIC TRANSLATION ELONGATION FACTOR 1, BETA-3, PSEUDOGENE, INCLUDED;
EEF1B3, INCLUDED; EEF1B2P2, INCLUDED;;
EUKARYOTIC TRANSLATION ELONGATION FACTOR 1, BETA-4, PSEUDOGENE, INCLUDED;
EEF1B4, INCLUDED; EEF1B2P3, INCLUDED
*FIELD* TX
DESCRIPTION
Eukaryotic elongation factor-1 (EF1) consists of 4 subunits, EF1-alpha
(EEF1A1; 130590), EF1-beta, EF1-gamma (EEF1G; 130593), and EF1-delta
(EEF1D; 130592). 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
Sanders et al. (1991) identified a human EF1-beta cDNA by hybridization
with a pig EF1-beta probe.
By immunofluorescence analysis, Sanders et al. (1996) found that
EF1-beta, -gamma, and -delta showed a perinuclear distribution and
colocalized with an endoplasmic reticulum resident protein in human
foreskin fibroblasts. In contrast, EF1-alpha showed strong nuclear
staining and diffuse cytoplasmic staining.
MAPPING
The EEF1B2 gene was mapped by Pizzuti et al. (1993) to chromosome 2 by
PCR analysis of a somatic cell hybrid DNA panel.
- Pseudogenes
From a cDNA library of human ovarian granulosa cells, von der Kammer et
al. (1991) isolated a cDNA that appeared to code for human EF1-beta. The
gene corresponding to this cDNA was mapped to chromosome 15 by PCR
analysis of a chromosomal hybrid panel by Pizzuti et al. (1993).
Chambers et al. (2001) determined that the gene isolated by von der
Kammer et al. (1991) is actually a processed pseudogene on chromosome 15
corresponding to an alternative splice form of EEF1B2.
Two additional pseudogenes, previously designated EEF1B3 AND EEF1B4,
were mapped to chromosome 5 and chromosome X, respectively, by Pizzuti
et al. (1993).
*FIELD* RF
1. Chambers, D. M.; Rouleau, G. A.; Abbott, C. M.: Comparative genomic
analysis of genes encoding translation elongation factor 1B-alpha
in human and mouse shows EEF1B1 to be a recent retrotransposition
event. Genomics 77: 145-148, 2001.
2. Pizzuti, A.; Gennarelli, M.; Novelli, G.; Colosimo, A.; Cicero,
S. L.; Caskey, C. T.; Dallapiccola, B.: Human elongation factor EF-1-beta:
cloning and characterization of the EF1-beta-5a gene and assignment
of EF-1-beta isoforms to chromosomes 2, 5, 15 and X. Biochem. Biophys.
Res. Commun. 197: 154-162, 1993.
3. 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.
4. Sanders, J.; Maassen, J. A.; Amons, R.; Moller, W.: Nucleotide
sequence of human elongation factor-1-beta cDNA. Nucleic Acids Res. 19:
4551, 1991.
5. von der Kammer, H.; Klaudiny, J.; Zimmer, M.; Scheit, K. H.: Human
elongation factor 1-beta: cDNA and derived amino acid sequence. Biochem.
Biophys. Res. Commun. 177: 312-317, 1991.
*FIELD* CN
Patricia A. Hartz - updated: 10/3/2008
*FIELD* CD
Alan F. Scott: 7/17/1995
*FIELD* ED
carol: 08/21/2012
carol: 8/21/2012
mgross: 10/8/2008
terry: 10/3/2008
carol: 6/1/2004
carol: 5/26/2004
terry: 8/11/1998
dkim: 7/21/1998
dkim: 6/30/1998
mark: 4/1/1996
mark: 7/17/1995
*RECORD*
*FIELD* NO
600655
*FIELD* TI
*600655 EUKARYOTIC TRANSLATION ELONGATION FACTOR 1, BETA-2; EEF1B2
;;ELONGATION FACTOR 1, BETA-2A;;
read moreELONGATION FACTOR 1, BETA; EF1B
EUKARYOTIC TRANSLATION ELONGATION FACTOR 1, BETA-1, PSEUDOGENE, INCLUDED;
EEF1B1, INCLUDED; EEF1B2P1, INCLUDED;;
EUKARYOTIC TRANSLATION ELONGATION FACTOR 1, BETA-3, PSEUDOGENE, INCLUDED;
EEF1B3, INCLUDED; EEF1B2P2, INCLUDED;;
EUKARYOTIC TRANSLATION ELONGATION FACTOR 1, BETA-4, PSEUDOGENE, INCLUDED;
EEF1B4, INCLUDED; EEF1B2P3, INCLUDED
*FIELD* TX
DESCRIPTION
Eukaryotic elongation factor-1 (EF1) consists of 4 subunits, EF1-alpha
(EEF1A1; 130590), EF1-beta, EF1-gamma (EEF1G; 130593), and EF1-delta
(EEF1D; 130592). 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
Sanders et al. (1991) identified a human EF1-beta cDNA by hybridization
with a pig EF1-beta probe.
By immunofluorescence analysis, Sanders et al. (1996) found that
EF1-beta, -gamma, and -delta showed a perinuclear distribution and
colocalized with an endoplasmic reticulum resident protein in human
foreskin fibroblasts. In contrast, EF1-alpha showed strong nuclear
staining and diffuse cytoplasmic staining.
MAPPING
The EEF1B2 gene was mapped by Pizzuti et al. (1993) to chromosome 2 by
PCR analysis of a somatic cell hybrid DNA panel.
- Pseudogenes
From a cDNA library of human ovarian granulosa cells, von der Kammer et
al. (1991) isolated a cDNA that appeared to code for human EF1-beta. The
gene corresponding to this cDNA was mapped to chromosome 15 by PCR
analysis of a chromosomal hybrid panel by Pizzuti et al. (1993).
Chambers et al. (2001) determined that the gene isolated by von der
Kammer et al. (1991) is actually a processed pseudogene on chromosome 15
corresponding to an alternative splice form of EEF1B2.
Two additional pseudogenes, previously designated EEF1B3 AND EEF1B4,
were mapped to chromosome 5 and chromosome X, respectively, by Pizzuti
et al. (1993).
*FIELD* RF
1. Chambers, D. M.; Rouleau, G. A.; Abbott, C. M.: Comparative genomic
analysis of genes encoding translation elongation factor 1B-alpha
in human and mouse shows EEF1B1 to be a recent retrotransposition
event. Genomics 77: 145-148, 2001.
2. Pizzuti, A.; Gennarelli, M.; Novelli, G.; Colosimo, A.; Cicero,
S. L.; Caskey, C. T.; Dallapiccola, B.: Human elongation factor EF-1-beta:
cloning and characterization of the EF1-beta-5a gene and assignment
of EF-1-beta isoforms to chromosomes 2, 5, 15 and X. Biochem. Biophys.
Res. Commun. 197: 154-162, 1993.
3. 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.
4. Sanders, J.; Maassen, J. A.; Amons, R.; Moller, W.: Nucleotide
sequence of human elongation factor-1-beta cDNA. Nucleic Acids Res. 19:
4551, 1991.
5. von der Kammer, H.; Klaudiny, J.; Zimmer, M.; Scheit, K. H.: Human
elongation factor 1-beta: cDNA and derived amino acid sequence. Biochem.
Biophys. Res. Commun. 177: 312-317, 1991.
*FIELD* CN
Patricia A. Hartz - updated: 10/3/2008
*FIELD* CD
Alan F. Scott: 7/17/1995
*FIELD* ED
carol: 08/21/2012
carol: 8/21/2012
mgross: 10/8/2008
terry: 10/3/2008
carol: 6/1/2004
carol: 5/26/2004
terry: 8/11/1998
dkim: 7/21/1998
dkim: 6/30/1998
mark: 4/1/1996
mark: 7/17/1995