EEF1B2

EEF1B2

Eukaryotic translation elongation factor 1 beta 2, also known as EEF1B2, is a human gene.cite web | title = Entrez Gene: EEF1B2 eukaryotic translation elongation factor 1 beta 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1933| accessdate = ]

PBB_Summary
section_title =
summary_text = This gene encodes a translation elongation factor. The protein is a guanine nucleotide exchange factor involved in the transfer of aminoacylated tRNAs to the ribosome. Alternative splicing results in three transcript variants which differ only in the 5' UTR.cite web | title = Entrez Gene: EEF1B2 eukaryotic translation elongation factor 1 beta 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1933| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Rasmussen HH, van Damme J, Puype M, "et al." |title=Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. |journal=Electrophoresis |volume=13 |issue= 12 |pages= 960–9 |year= 1993 |pmid= 1286667 |doi=
*cite journal | author=Hochstrasser DF, Frutiger S, Paquet N, "et al." |title=Human liver protein
journal=Electrophoresis |volume=13 |issue= 12 |pages= 992–1001 |year= 1993 |pmid= 1286669 |doi=

*cite journal | author=von der Kammer H, Klaudiny J, Zimmer M, Scheit KH |title=Human elongation factor 1 beta: cDNA and derived amino acid sequence. |journal=Biochem. Biophys. Res. Commun. |volume=177 |issue= 1 |pages= 312–7 |year= 1991 |pmid= 1710449 |doi=
*cite journal | author=Sanders J, Maassen JA, Amons R, Möller W |title=Nucleotide sequence of human elongation factor-1 beta cDNA. |journal=Nucleic Acids Res. |volume=19 |issue= 16 |pages= 4551 |year= 1991 |pmid= 1886777 |doi=
*cite journal | author=Bec G, Kerjan P, Zha XD, Waller JP |title=Valyl-tRNA synthetase from rabbit liver. I. Purification as a heterotypic complex in association with elongation factor 1. |journal=J. Biol. Chem. |volume=264 |issue= 35 |pages= 21131–7 |year= 1990 |pmid= 2556394 |doi=
*cite journal | author=Motorin YuA , Wolfson AD, Orlovsky AF, Gladilin KL |title=Mammalian valyl-tRNA synthetase forms a complex with the first elongation factor. |journal=FEBS Lett. |volume=238 |issue= 2 |pages= 262–4 |year= 1988 |pmid= 3169261 |doi=
*cite journal | author=Pizzuti A, Gennarelli M, Novelli G, "et al." |title=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. |journal=Biochem. Biophys. Res. Commun. |volume=197 |issue= 1 |pages= 154–62 |year= 1994 |pmid= 8250921 |doi=
*cite journal | author=Chen CJ, Traugh JA |title=Expression of recombinant elongation factor 1 beta from rabbit in Escherichia coli. Phosphorylation by casein kinase II. |journal=Biochim. Biophys. Acta |volume=1264 |issue= 3 |pages= 303–11 |year= 1996 |pmid= 8547318 |doi=
*cite journal | author=Béhar G, Coleclough C, Houlgatte R, "et al." |title=Human lymphocyte cDNA ordered library analyzed by 2D gel electrophoresis. 3. Analysis of individual clones. |journal=Appl. Theor. Electrophor. |volume=5 |issue= 2 |pages= 99–105 |year= 1996 |pmid= 8573604 |doi=
*cite journal | author=Sanders J, Brandsma M, Janssen GM, "et al." |title=Immunofluorescence studies of human fibroblasts demonstrate the presence of the complex of elongation factor-1 beta gamma delta in the endoplasmic reticulum. |journal=J. Cell. Sci. |volume=109 ( Pt 5) |issue= |pages= 1113–7 |year= 1996 |pmid= 8743958 |doi=
*cite journal | author=Sheu GT, Traugh JA |title=Recombinant subunits of mammalian elongation factor 1 expressed in Escherichia coli. Subunit interactions, elongation activity, and phosphorylation by protein kinase CKII. |journal=J. Biol. Chem. |volume=272 |issue= 52 |pages= 33290–7 |year= 1998 |pmid= 9407120 |doi=
*cite journal | author=Sheu GT, Traugh JA |title=A structural model for elongation factor 1 (EF-1) and phosphorylation by protein kinase CKII. |journal=Mol. Cell. Biochem. |volume=191 |issue= 1-2 |pages= 181–6 |year= 1999 |pmid= 10094407 |doi=
*cite journal | author=Pérez JM, Siegal G, Kriek J, "et al." |title=The solution structure of the guanine nucleotide exchange domain of human elongation factor 1beta reveals a striking resemblance to that of EF-Ts from Escherichia coli. |journal=Structure |volume=7 |issue= 2 |pages= 217–26 |year= 1999 |pmid= 10368288 |doi=
*cite journal | author=Chambers DM, Rouleau GA, Abbott CM |title=Comparative genomic analysis of genes encoding translation elongation factor 1B(alpha) in human and mouse shows EEF1B1 to be a recent retrotransposition event. |journal=Genomics |volume=77 |issue= 3 |pages= 145–8 |year= 2001 |pmid= 11597139 |doi= 10.1006/geno.2001.6626
*cite journal | author=Sang Lee J, Gyu Park S, Park H, "et al." |title=Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex. |journal=Biochem. Biophys. Res. Commun. |volume=291 |issue= 1 |pages= 158–64 |year= 2002 |pmid= 11829477 |doi= 10.1006/bbrc.2002.6398
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Cans C, Passer BJ, Shalak V, "et al." |title=Translationally controlled tumor protein acts as a guanine nucleotide dissociation inhibitor on the translation elongation factor eEF1A. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 24 |pages= 13892–7 |year= 2004 |pmid= 14623968 |doi= 10.1073/pnas.2335950100
*cite journal | author=Shu H, Chen S, Bi Q, "et al." |title=Identification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell line. |journal=Mol. Cell Proteomics |volume=3 |issue= 3 |pages= 279–86 |year= 2004 |pmid= 14729942 |doi= 10.1074/mcp.D300003-MCP200
*cite journal | author=Beausoleil SA, Jedrychowski M, Schwartz D, "et al." |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130–5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101
*cite journal | author=Ito T, Marintchev A, Wagner G |title=Solution structure of human initiation factor eIF2alpha reveals homology to the elongation factor eEF1B. |journal=Structure |volume=12 |issue= 9 |pages= 1693–704 |year= 2005 |pmid= 15341733 |doi= 10.1016/j.str.2004.07.010

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes


Wikimedia Foundation. 2010.

Игры ⚽ Нужен реферат?

Look at other dictionaries:

  • Translation (biology) — Diagram showing the translation of mRNA and the synthesis of proteins by a ribosome. In molecular biology and genetics, translation is the third stage of protein biosynthesis (part of the overall process of gene expression). In translation,… …   Wikipedia

  • Start codon — The start codon is generally defined as the point, sequence, at which a ribosome begins to translate a sequence of RNA into amino acids. When an RNA transcript is read from the 5 carbon to the 3 carbon by the ribosome the start codon (AUG) is the …   Wikipedia

  • Eukaryotic elongation factors — are very similar to those in prokaryotes. Elongation in eukaryotes is carried out with two elongation factors: *eEF 1, whose α and βγ subunits act as counterparts to EF Tu and EF Ts, respectively *eEF 2, the counterpart to prokaryotic EF GGenes*… …   Wikipedia

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”