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Elongation factor 1-beta (EF-1-beta)

 EF1B_HUMAN              Reviewed;         225 AA.
P24534; A8K795; Q6IBH9;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
10-OCT-2018, entry version 210.
RecName: Full=Elongation factor 1-beta;
Short=EF-1-beta;
Name=EEF1B2; Synonyms=EEF1B, EF1B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Skin fibroblast;
PubMed=1886777; DOI=10.1093/nar/19.16.4551;
Sanders J., Maassen J.A., Amons R., Moeller W.;
"Nucleotide sequence of human elongation factor-1 beta cDNA.";
Nucleic Acids Res. 19:4551-4551(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Ovarian granulosa cell;
PubMed=1710449; DOI=10.1016/0006-291X(91)91984-K;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Eye, and Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 2-11.
TISSUE=Liver;
PubMed=1286669; DOI=10.1002/elps.11501301201;
Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
Appel R.D., Hughes G.J.;
"Human liver protein map: a reference database established by
microsequencing and gel comparison.";
Electrophoresis 13:992-1001(1992).
[10]
PROTEIN SEQUENCE OF 8-22; 140-157 AND 164-176, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[11]
PROTEIN SEQUENCE OF 55-60; 79-85; 123-127 AND 164-175.
TISSUE=Keratinocyte;
PubMed=1286667; DOI=10.1002/elps.11501301199;
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel
protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[12]
INDUCTION BY HOMOCYSTEINE.
PubMed=9677419; DOI=10.1074/jbc.273.31.19840;
Chacko G., Ling Q., Hajjar K.A.;
"Induction of acute translational response genes by homocysteine.
Elongation factors-1alpha, -beta, and -delta.";
J. Biol. Chem. 273:19840-19846(1998).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Prostate cancer;
PubMed=17487921; DOI=10.1002/elps.200600782;
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
"Toward a global characterization of the phosphoproteome in prostate
cancer cells: identification of phosphoproteins in the LNCaP cell
line.";
Electrophoresis 28:2027-2034(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17693683; DOI=10.1074/mcp.M700120-MCP200;
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,
Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
network: indicating the involvement of ribonucleoside-diphosphate
reductase M2 subunit phosphorylation at residue serine 20 in canonical
Wnt signal transduction.";
Mol. Cell. Proteomics 6:1952-1967(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-95 AND SER-106,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-95 AND SER-106,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-7, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95 AND SER-106, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; THR-93; SER-95 AND
SER-106, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-95; SER-106 AND
SER-174, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND SER-106, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[29]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-147, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: EF-1-beta and EF-1-delta stimulate the exchange of GDP
bound to EF-1-alpha to GTP.
-!- SUBUNIT: EF-1 is composed of 4 subunits: alpha, beta, delta, and
gamma.
-!- INTERACTION:
P26641:EEF1G; NbExp=5; IntAct=EBI-354334, EBI-351467;
P26641-2:EEF1G; NbExp=3; IntAct=EBI-354334, EBI-10177695;
-!- INDUCTION: By homocysteine (HC), may mediate accelerated synthesis
of free thiol-containing proteins in response to HC-induced
oxidative stress. {ECO:0000269|PubMed:9677419}.
-!- PTM: Phosphorylation affects the GDP/GTP exchange rate.
-!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family.
{ECO:0000305}.
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EMBL; X60489; CAA43019.1; -; mRNA.
EMBL; X60656; CAA43063.1; -; mRNA.
EMBL; BT007079; AAP35742.1; -; mRNA.
EMBL; CR456825; CAG33106.1; -; mRNA.
EMBL; AK291910; BAF84599.1; -; mRNA.
EMBL; AC007383; AAY15062.1; -; Genomic_DNA.
EMBL; CH471063; EAW70381.1; -; Genomic_DNA.
EMBL; BC000211; AAH00211.1; -; mRNA.
EMBL; BC004931; AAH04931.1; -; mRNA.
EMBL; BC067787; AAH67787.1; -; mRNA.
CCDS; CCDS2367.1; -.
PIR; S25432; S25432.
RefSeq; NP_001032752.1; NM_001037663.1.
RefSeq; NP_001950.1; NM_001959.3.
RefSeq; NP_066944.1; NM_021121.3.
UniGene; Hs.421608; -.
PDB; 1B64; NMR; -; A=136-225.
PDB; 5DQS; X-ray; 2.10 A; D=1-88.
PDBsum; 1B64; -.
PDBsum; 5DQS; -.
ProteinModelPortal; P24534; -.
SMR; P24534; -.
BioGrid; 108253; 75.
IntAct; P24534; 37.
MINT; P24534; -.
STRING; 9606.ENSP00000236957; -.
iPTMnet; P24534; -.
PhosphoSitePlus; P24534; -.
SwissPalm; P24534; -.
BioMuta; EEF1B2; -.
DMDM; 119163; -.
DOSAC-COBS-2DPAGE; P24534; -.
OGP; P24534; -.
SWISS-2DPAGE; P24534; -.
EPD; P24534; -.
MaxQB; P24534; -.
PaxDb; P24534; -.
PeptideAtlas; P24534; -.
PRIDE; P24534; -.
ProteomicsDB; 54214; -.
TopDownProteomics; P24534; -.
DNASU; 1933; -.
Ensembl; ENST00000236957; ENSP00000236957; ENSG00000114942.
Ensembl; ENST00000392221; ENSP00000376055; ENSG00000114942.
Ensembl; ENST00000392222; ENSP00000376056; ENSG00000114942.
Ensembl; ENST00000635728; ENSP00000489993; ENSG00000283391.
Ensembl; ENST00000636275; ENSP00000490326; ENSG00000283391.
Ensembl; ENST00000637253; ENSP00000490214; ENSG00000283391.
GeneID; 1933; -.
KEGG; hsa:1933; -.
UCSC; uc002vbf.2; human.
CTD; 1933; -.
DisGeNET; 1933; -.
EuPathDB; HostDB:ENSG00000114942.13; -.
GeneCards; EEF1B2; -.
HGNC; HGNC:3208; EEF1B2.
HPA; CAB012477; -.
HPA; HPA035029; -.
MIM; 600655; gene.
neXtProt; NX_P24534; -.
OpenTargets; ENSG00000114942; -.
PharmGKB; PA27644; -.
eggNOG; KOG1668; Eukaryota.
eggNOG; COG2092; LUCA.
GeneTree; ENSGT00390000011747; -.
HOGENOM; HOG000207273; -.
HOVERGEN; HBG000787; -.
InParanoid; P24534; -.
KO; K03232; -.
OMA; PSQADVH; -.
OrthoDB; EOG091G0P0Z; -.
PhylomeDB; P24534; -.
TreeFam; TF313134; -.
Reactome; R-HSA-156842; Eukaryotic Translation Elongation.
SIGNOR; P24534; -.
ChiTaRS; EEF1B2; human.
EvolutionaryTrace; P24534; -.
GeneWiki; EEF1B2; -.
GenomeRNAi; 1933; -.
PMAP-CutDB; P24534; -.
PRO; PR:P24534; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000114942; Expressed in 88 organ(s), highest expression level in body of pancreas.
CleanEx; HS_EEF1B2; -.
ExpressionAtlas; P24534; baseline and differential.
Genevisible; P24534; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; NAS:UniProtKB.
GO; GO:0003746; F:translation elongation factor activity; NAS:UniProtKB.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0006414; P:translational elongation; TAS:Reactome.
CDD; cd00292; EF1B; 1.
Gene3D; 3.30.70.60; -; 1.
InterPro; IPR036219; eEF-1beta-like_sf.
InterPro; IPR018940; EF-1_beta_acid_region_euk.
InterPro; IPR014038; EF1B_bsu/dsu_GNE.
InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
InterPro; IPR014717; Transl_elong_EF1B/ribosomal_S6.
InterPro; IPR001326; Transl_elong_EF1B_B/D_CS.
Pfam; PF10587; EF-1_beta_acid; 1.
Pfam; PF00736; EF1_GNE; 1.
SMART; SM01182; EF-1_beta_acid; 1.
SMART; SM00888; EF1_GNE; 1.
SUPFAM; SSF47616; SSF47616; 1.
SUPFAM; SSF54984; SSF54984; 1.
PROSITE; PS00824; EF1BD_1; 1.
PROSITE; PS00825; EF1BD_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Elongation factor; Isopeptide bond;
Phosphoprotein; Protein biosynthesis; Reference proteome;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1286669}.
CHAIN 2 225 Elongation factor 1-beta.
/FTId=PRO_0000155021.
DOMAIN 2 84 GST C-terminal.
MOD_RES 7 7 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 8 8 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 42 42 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 88 88 Phosphothreonine.
{ECO:0000250|UniProtKB:O70251}.
MOD_RES 93 93 Phosphothreonine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 95 95 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 106 106 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17487921,
ECO:0000244|PubMed:17693683,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 174 174 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 147 147 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
HELIX 9 18 {ECO:0000244|PDB:5DQS}.
TURN 19 21 {ECO:0000244|PDB:5DQS}.
STRAND 23 26 {ECO:0000244|PDB:5DQS}.
HELIX 32 41 {ECO:0000244|PDB:5DQS}.
HELIX 50 60 {ECO:0000244|PDB:5DQS}.
HELIX 61 65 {ECO:0000244|PDB:5DQS}.
STRAND 69 71 {ECO:0000244|PDB:5DQS}.
HELIX 76 78 {ECO:0000244|PDB:5DQS}.
STRAND 79 81 {ECO:0000244|PDB:5DQS}.
STRAND 140 150 {ECO:0000244|PDB:1B64}.
HELIX 155 164 {ECO:0000244|PDB:1B64}.
STRAND 171 183 {ECO:0000244|PDB:1B64}.
STRAND 185 193 {ECO:0000244|PDB:1B64}.
HELIX 200 207 {ECO:0000244|PDB:1B64}.
TURN 211 213 {ECO:0000244|PDB:1B64}.
STRAND 214 220 {ECO:0000244|PDB:1B64}.
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


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