EEF2

EEF2
Estruturas disponíveis
PDB	Pesquisa Human UniProt: PDBe RCSB
Lista de códigos id do PDB
	4V6X
Identificadores
Nomes alternativos	EEF2
IDs externos	OMIM: 130610 HomoloGene: 134867 GeneCards: EEF2
Doenças Geneticamente Relacionadas
	spinocerebellar ataxia type 26
Targeted by Drug
	denileukin diftitox
Ontologia genética
Função molecular	• nucleotide binding; • ribosome binding; • GTP binding; • p53 binding; • translation elongation factor activity; • actin filament binding; • GO:0001948, GO:0016582 ligação a proteínas plasmáticas; • 5S rRNA binding; • protein kinase binding; • RNA binding; • GO:0006184 GTPase activity; • cadherin binding;
Componente celular	• citoplasma; • polysome; • membrane; • membrana plasmática; • aggresome; • membrane raft; • Exossoma; • núcleo celular; • polysomal ribosome; • GO:0005578 matriz extracelular; • extracellular region; • citosol; • secretory granule lumen; • ficolin-1-rich granule lumen; • sinapse; • Partículas de ribonucleoproteínas heterogéneas;
Processo biológico	• response to estradiol; • positive regulation of cytoplasmic translation; • skeletal muscle contraction; • translational elongation; • GO:0010260 envelhecimento; • positive regulation of translation; • response to endoplasmic reticulum stress; • cellular response to brain-derived neurotrophic factor stimulus; • response to ischemia; • hematopoietic progenitor cell differentiation; • peptidyl-diphthamide biosynthetic process from peptidyl-histidine; • glial cell proliferation; • skeletal muscle cell differentiation; • response to folic acid; • response to ethanol; • response to hydrogen peroxide; • síntese proteica; • protein methylation; • neutrophil degranulation;
	Sources:Amigo / QuickGO
Padrão de expressão RNA
	; ;
	Mais dados de referência de expressão
Ortólogos
	1938
	n/a
	ENSG00000167658
	n/a
	P13639
	n/a
	NM_001961
	n/a
	NP_001952
	n/a
	Wikidata
Ver/Editar Humano

Fator de alongamento eucariótico 2 é uma proteína que em humanos é codificada pelo gene EEF2.^[4]^[5]^[6]^[7] É a contraparte arqueana e eucariótica do EF-G [en] bacteriano.

Este gene codifica um membro da família de fatores de alongamento da tradução de ligação ao GTP. Esta proteína é um fator essencial para a síntese proteica. Ela promove a translocação do ribossomo dependente de GTP. Esta proteína é completamente inativada pela fosforilação da EF-2 quinase [en].^[6]

aEF2/eEF2 encontrado na maioria das arqueas e eucariotos, incluindo humanos, contém uma histidina modificada pós-traducionalmente, a diftamida [en].^[7] É o alvo da toxina diftérica [en] (de Corynebacterium diphtheriae) e da exotoxina A [en] (de Pseudomonas aeruginosa).^[8] A inativação do EF-2 por toxinas inibe a produção de proteínas no hospedeiro, causando sintomas devido à perda de função nas células afetadas.

Referências

↑ «Doenças geneticamente associadas a EEF2 ver/editar referências no wikidata»
↑ «Drogas que interagem fisicamente com Eukaryotic translation elongation factor 2 ver/editar referências no wikidata»
↑ «Human PubMed Reference:»
↑ Rapp G, Klaudiny J, Hagendorff G, Luck MR, Scheit KH (outubro de 1989). «Complete sequence of the coding region of human elongation factor 2 (EF-2) by enzymatic amplification of cDNA from human ovarian granulosa cells». Biological Chemistry Hoppe-Seyler. 370 (10): 1071–5. PMID 2610926. doi:10.1515/bchm3.1989.370.2.1071
↑ Kaneda Y, Yoshida MC, Kohno K, Uchida T, Okada Y (maio de 1984). «Chromosomal assignment of the gene for human elongation factor 2». Proceedings of the National Academy of Sciences of the United States of America. 81 (10): 3158–62. Bibcode:1984PNAS...81.3158K. PMC 345240. PMID 6427766. doi:10.1073/pnas.81.10.3158
↑ ^a ^b «Entrez Gene: EEF2 eukaryotic translation elongation factor 2»
↑ ^a ^b Narrowe AB, Spang A, Stairs CW, Caceres EF, Baker BJ, Miller CS, Ettema TJ (setembro de 2018). «Complex Evolutionary History of Translation Elongation Factor 2 and Diphthamide Biosynthesis in Archaea and Parabasalids». Genome Biology and Evolution. 10 (9): 2380–2393. PMC 6143161. PMID 30060184. doi:10.1093/gbe/evy154
↑ Jørgensen R, Merrill AR, Andersen GR (fevereiro de 2006). «The life and death of translation elongation factor 2». Biochemical Society Transactions. 34 (Pt 1): 1–6. PMID 16246167. doi:10.1042/BST20060001

Leitura adicional

Hanes J, Freudenstein J, Rapp G, Scheit KH (abril de 1992). «Construction of a plasmid containing the complete coding region of human elongation factor 2». Biological Chemistry Hoppe-Seyler. 373 (4): 201–4. PMID 1596361. doi:10.1515/bchm3.1992.373.1.201
Nygård O, Nilsson L (abril de 1990). «Kinetic determination of the effects of ADP-ribosylation on the interaction of eukaryotic elongation factor 2 with ribosomes». The Journal of Biological Chemistry. 265 (11): 6030–4. PMID 2318846. doi:10.1016/S0021-9258(19)39286-5
Rapp G, Mucha J, Einspanier R, Luck M, Scheit KH (abril de 1988). «Cloning and sequence analysis of a cDNA from human ovarian granulosa cells encoding the C-terminal part of human elongation factor 2». Biological Chemistry Hoppe-Seyler. 369 (4): 247–50. PMID 2840927. doi:10.1515/bchm3.1988.369.1.247
Kaneda Y, Hayes H, Uchida T, Yoshida MC, Okada Y (1987). «Regional assignment of five genes on human chromosome 19». Chromosoma. 95 (1): 8–12. PMID 3034518. doi:10.1007/BF00293835
Nairn AC, Palfrey HC (dezembro de 1987). «Identification of the major Mr 100,000 substrate for calmodulin-dependent protein kinase III in mammalian cells as elongation factor-2». The Journal of Biological Chemistry. 262 (36): 17299–303. PMID 3693353. doi:10.1016/S0021-9258(18)45377-X
Shestakova EA, Motuz LP, Minin AA, Gavrilova LP (abril de 1993). «Study of localization of the protein-synthesizing machinery along actin filament bundles». Cell Biology International. 17 (4): 409–16. PMID 8318952. doi:10.1006/cbir.1993.1079
Redpath NT, Price NT, Severinov KV, Proud CG (abril de 1993). «Regulation of elongation factor-2 by multisite phosphorylation». European Journal of Biochemistry. 213 (2): 689–99. PMID 8386634. doi:10.1111/j.1432-1033.1993.tb17809.x
Knebel A, Haydon CE, Morrice N, Cohen P (outubro de 2002). «Stress-induced regulation of eukaryotic elongation factor 2 kinase by SB 203580-sensitive and -insensitive pathways». The Biochemical Journal. 367 (Pt 2): 525–32. PMC 1222910. PMID 12171600. doi:10.1042/BJ20020916
Yin X, Fontoura BM, Morimoto T, Carroll RB (setembro de 2003). «Cytoplasmic complex of p53 and eEF2». Journal of Cellular Physiology. 196 (3): 474–82. PMID 12891704. doi:10.1002/jcp.10329
Ryazanova LV, Dorovkov MV, Ansari A, Ryazanov AG (janeiro de 2004). «Characterization of the protein kinase activity of TRPM7/ChaK1, a protein kinase fused to the transient receptor potential ion channel». The Journal of Biological Chemistry. 279 (5): 3708–16. PMID 14594813. doi:10.1074/jbc.M308820200
Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, et al. (agosto de 2004). «Large-scale characterization of HeLa cell nuclear phosphoproteins». Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. PMC 514446. PMID 15302935. doi:10.1073/pnas.0404720101
Elo MA, Karjalainen HM, Sironen RK, Valmu L, Redpath NT, Browne GJ, et al. (fevereiro de 2005). «High hydrostatic pressure inhibits the biosynthesis of eukaryotic elongation factor-2». Journal of Cellular Biochemistry. 94 (3): 497–507. PMID 15534876. doi:10.1002/jcb.20333
Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M (janeiro de 2005). «Nucleolar proteome dynamics». Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. PMID 15635413. doi:10.1038/nature03207
Shibatani T, David LL, McCormack AL, Frueh K, Skach WR (abril de 2005). «Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits». Biochemistry. 44 (16): 5982–92. PMID 15835887. doi:10.1021/bi047328f
Ahmed M, Forsberg J, Bergsten P (2005). «Protein profiling of human pancreatic islets by two-dimensional gel electrophoresis and mass spectrometry». Journal of Proteome Research. 4 (3): 931–40. PMID 15952740. doi:10.1021/pr050024a
Gevaert K, Staes A, Van Damme J, De Groot S, Hugelier K, Demol H, et al. (setembro de 2005). «Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC». Proteomics. 5 (14): 3589–99. PMID 16097034. doi:10.1002/pmic.200401217

Ligações externas

Peptídeo+Fator+de+Elongação+2 na Biblioteca Nacional de Medicina dos EUA, Medical Subject Headings (MeSH)

[1] «Doenças geneticamente associadas a EEF2 ver/editar referências no wikidata»

[2] «Drogas que interagem fisicamente com Eukaryotic translation elongation factor 2 ver/editar referências no wikidata»

[3] «Human PubMed Reference:»

[pmid2610926-4] Rapp G, Klaudiny J, Hagendorff G, Luck MR, Scheit KH (outubro de 1989). «Complete sequence of the coding region of human elongation factor 2 (EF-2) by enzymatic amplification of cDNA from human ovarian granulosa cells». Biological Chemistry Hoppe-Seyler. 370 (10): 1071–5. PMID 2610926. doi:10.1515/bchm3.1989.370.2.1071

[pmid6427766-5] Kaneda Y, Yoshida MC, Kohno K, Uchida T, Okada Y (maio de 1984). «Chromosomal assignment of the gene for human elongation factor 2». Proceedings of the National Academy of Sciences of the United States of America. 81 (10): 3158–62. Bibcode:1984PNAS...81.3158K. PMC 345240. PMID 6427766. doi:10.1073/pnas.81.10.3158

[entrez-6] «Entrez Gene: EEF2 eukaryotic translation elongation factor 2»

[dph-7] Narrowe AB, Spang A, Stairs CW, Caceres EF, Baker BJ, Miller CS, Ettema TJ (setembro de 2018). «Complex Evolutionary History of Translation Elongation Factor 2 and Diphthamide Biosynthesis in Archaea and Parabasalids». Genome Biology and Evolution. 10 (9): 2380–2393. PMC 6143161. PMID 30060184. doi:10.1093/gbe/evy154

[pmid16246167-8] Jørgensen R, Merrill AR, Andersen GR (fevereiro de 2006). «The life and death of translation elongation factor 2». Biochemical Society Transactions. 34 (Pt 1): 1–6. PMID 16246167. doi:10.1042/BST20060001

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