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Elongation factor 1-beta 2 (EF-1-beta 2) (Elongation factor 1-beta' 2) (EF-1-beta' 2) (Elongation factor 1B-alpha 2) (eEF-1B alpha 2)

 EF1B2_ARATH             Reviewed;         224 AA.
Q9SCX3;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
23-MAY-2018, entry version 126.
RecName: Full=Elongation factor 1-beta 2;
Short=EF-1-beta 2;
AltName: Full=Elongation factor 1-beta' 2;
Short=EF-1-beta' 2;
AltName: Full=Elongation factor 1B-alpha 2;
AltName: Full=eEF-1B alpha 2;
OrderedLocusNames=At5g19510; ORFNames=T20D1.30;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
PubMed=10618495; DOI=10.1016/S0014-5793(99)01694-4;
Hericourt F., Jupin I.;
"Molecular cloning and characterization of the Arabidopsis thaliana
alpha-subunit of elongation factor 1B.";
FEBS Lett. 464:148-152(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22092075; DOI=10.1021/pr200917t;
Aryal U.K., Krochko J.E., Ross A.R.;
"Identification of phosphoproteins in Arabidopsis thaliana leaves
using polyethylene glycol fractionation, immobilized metal-ion
affinity chromatography, two-dimensional gel electrophoresis and mass
spectrometry.";
J. Proteome Res. 11:425-437(2012).
[6]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
-!- FUNCTION: EF-1-beta and EF-1-delta stimulate the exchange of GDP
bound to EF-1-alpha to GTP. {ECO:0000269|PubMed:10618495}.
-!- SUBUNIT: EF-1 is composed of 4 subunits: alpha, beta (1B-
alpha=beta'), delta (1B-beta), and gamma (1B-gamma).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family.
{ECO:0000305}.
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EMBL; AJ249597; CAB64730.1; -; mRNA.
EMBL; AF296830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CP002688; AED92719.1; -; Genomic_DNA.
EMBL; AF360304; AAK26014.1; -; mRNA.
EMBL; AY056354; AAL07240.1; -; mRNA.
PIR; PA0110; PA0110.
PIR; T52558; T52558.
RefSeq; NP_568375.2; NM_121956.3.
UniGene; At.20397; -.
UniGene; At.72989; -.
ProteinModelPortal; Q9SCX3; -.
SMR; Q9SCX3; -.
BioGrid; 17347; 1.
STRING; 3702.AT5G19510.1; -.
iPTMnet; Q9SCX3; -.
PaxDb; Q9SCX3; -.
PRIDE; Q9SCX3; -.
EnsemblPlants; AT5G19510.1; AT5G19510.1; AT5G19510.
GeneID; 832071; -.
Gramene; AT5G19510.1; AT5G19510.1; AT5G19510.
KEGG; ath:AT5G19510; -.
Araport; AT5G19510; -.
TAIR; locus:2180806; AT5G19510.
eggNOG; KOG1668; Eukaryota.
eggNOG; COG2092; LUCA.
HOGENOM; HOG000207273; -.
InParanoid; Q9SCX3; -.
KO; K03232; -.
OMA; WVARMAS; -.
OrthoDB; EOG09360N88; -.
PhylomeDB; Q9SCX3; -.
Reactome; R-ATH-156842; Eukaryotic Translation Elongation.
PRO; PR:Q9SCX3; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9SCX3; baseline and differential.
Genevisible; Q9SCX3; AT.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
GO; GO:0042742; P:defense response to bacterium; IEP:TAIR.
CDD; cd00292; EF1B; 1.
Gene3D; 3.30.70.60; -; 1.
InterPro; IPR036219; eEF-1beta-like_sf.
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; PF00736; EF1_GNE; 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;
Acetylation; Complete proteome; Elongation factor;
Protein biosynthesis; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 224 Elongation factor 1-beta 2.
/FTId=PRO_0000155032.
DOMAIN 14 65 GST C-terminal.
COMPBIAS 82 97 Ala-rich.
COMPBIAS 98 104 Poly-Asp.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895}.
SEQUENCE 224 AA; 24201 MW; F9BF9178A60CB3B4 CRC64;
MAVTFSDLHT EEGVKSVEEH LAGKTYISGD QLSVDDVKVY AAVPVKPSDA FPNASKWYES
VASQLAKSFP GKAVGVQFGG SAAAAPAVEA EAPAAAADDD DDMDLFGDET EEEKKAAEER
EAAKKDTKKP KESGKSSVLM DVKPWDDETD MKKLEEAVRG VEMPGLFWGA SKLVPVGYGI
KKLTIMFTIV DDLVSPDNLI EDFLTSEPNN EYIQSCDIVA FNKI


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