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protein coding gene - tef103 (SPBC839.15c) - translation elongation factor EF-1 alpha Ef1a-c

Gene summary

Standard name
tef103
Systematic ID
SPBC839.15c
Product
translation elongation factor EF-1 alpha Ef1a-c
Organism
Schizosaccharomyces pombe (fission yeast)
Synonyms
ef1a-c, efa13, EF-1aC, ef1-b
UniProt ID
P0CT55
Characterisation status
biological role published
Feature type
mRNA gene
Genomic location
chromosome II: 626004..627522 reverse strand

Annotation

Disease association

MONDO:0014625 - developmental and epileptic encephalopathy, 33

References:

MONDO:0014617 - intellectual disability, autosomal dominant 38

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GO biological process

GO:0002182 - cytoplasmic translational elongation

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GO cellular component

GO:0005853 - eukaryotic translation elongation factor 1 complex

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GO molecular function

GO:0005516 - calmodulin binding

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GO:0005525 - GTP binding

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GO:0003924 - GTPase activity

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GO:0003746 - translation elongation factor activity

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Modification

MOD:02025 - 5-glutaminyl glutamic acid

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MOD:01982 - N,N,N-trimethylglycine

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MOD:00083 - N6,N6,N6-trimethyl-L-lysine

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MOD:00084 - N6,N6-dimethyl-L-lysine

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MOD:00085 - N6-methyl-L-lysine

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MOD:00046 - O-phospho-L-serine

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MOD:00047 - O-phospho-L-threonine

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MOD:00048 - O4'-phospho-L-tyrosine

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MOD:01149 - sumoylated lysine

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MOD:01148 - ubiquitinylated lysine

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Qualitative gene expression

PomGeneEx:0000019 - protein level decreased

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PomGeneEx:0000027 - ribosomal density decreased

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PomGeneEx:0000012 - RNA level decreased

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PomGeneEx:0000011 - RNA level increased

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PomGeneEx:0000014 - RNA present

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Quantitative gene expression

PBO:0011963 - RNA level

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Single locus phenotype

FYPO:0001118 - abnormal vegetative cell morphology

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Genotypes:

FYPO:0009092 - decreased cell population growth on lysine and serine nitrogen source

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Genotypes:

FYPO:0009052 - increased cell population growth on glutamate nitrogen source

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Genotypes:

FYPO:0000245 - loss of viability in stationary phase

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Genotypes:

FYPO:0009041 - resistance to 2,2′-dipyridyl

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Genotypes:

FYPO:0009030 - resistance to amitrole

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Genotypes:

FYPO:0000067 - resistance to brefeldin A

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Genotypes:

FYPO:0000764 - resistance to cycloheximide

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Genotypes:

FYPO:0002693 - resistance to diamide

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Genotypes:

FYPO:0009038 - resistance to egtazic acid

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Genotypes:

FYPO:0001453 - resistance to ethanol

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Genotypes:

FYPO:0000830 - resistance to vanadate

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Genotypes:

FYPO:0009069 - sensitive to ciclopirox olamine

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Genotypes:

FYPO:0000842 - sensitive to ethanol during vegetative growth

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Genotypes:

FYPO:0001719 - sensitive to lithium

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Genotypes:

FYPO:0000111 - sensitive to rapamycin

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Genotypes:

FYPO:0000797 - sensitive to tert-butyl hydroperoxide

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Genotypes:

FYPO:0002701 - sensitive to torin1

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Genotypes:

FYPO:0009064 - sensitive to X-rays and rapamycin during vegetative growth.

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Genotypes:

FYPO:0002060 - viable vegetative cell population

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Genotypes:

FYPO:0002177 - viable vegetative cell with normal cell morphology

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Genotypes:

Taxonomic conservation

PBO:0011067 - conserved in bacteria

PBO:0011065 - conserved in eukaryotes

PBO:0011064 - conserved in fungi

PBO:0011069 - conserved in metazoa

PBO:0011070 - conserved in vertebrates

PBO:0006222 - predominantly single copy (one to one)

Protein features

IDNameInterPro nameDB name
PF00009GTP_EFTUT_Tr_GTP-bd_domPfam
PF03144GTP_EFTU_D2EFTu-like_2Pfam
PF22594GTP-eEF1A_CGTP-eEF1A_CPfam
cd01883EF1_alphaCDD
cd03693EF1_alpha_IICDD
cd03705EF1_alpha_IIICDD
PS00301G_TR_1G_TR_CSPROSITE patterns
PS51722G_TR_2T_Tr_GTP-bd_domPROSITE profiles
PR00315ELONGATNFCTT_Tr_GTP-bd_domPRINTS
G3DSA:2.40.30.10:FF:000003CATH-FunFam
G3DSA:2.40.30.10:FF:000005CATH-FunFam
G3DSA:3.40.50.300:FF:000211CATH-FunFam
G3DSA:2.40.30.10CATH-Gene3D
G3DSA:3.40.50.300P-loop_NTPaseCATH-Gene3D
SSF50447Transl_B-barrel_sfSUPERFAMILY
SSF50465Transl_elong_EF1A/Init_IF2_CSUPERFAMILY
SSF52540P-loop_NTPaseSUPERFAMILY
PTHR23115TRAFAC_GTPase_membersPANTHER
NF008969PRK12317.1NCBIFAM
TIGR00483EF-1_alphaTransl_elong_EF1A_euk/arcNCBIFAM
MF_00118_AEF_Tu_ATransl_elong_EF1A_euk/arcHAMAP

Orthologs

References / Literature

PMID:38269097 - Rapamycin-sensitive mechanisms confine the growth of fission yeast below the temperatures detrimental to cell physiology.
Morozumi Y et al. iScience 2024 Jan 19;27(1):108777
PMID:30726745 - Fission Yeast NDR/LATS Kinase Orb6 Regulates Exocytosis via Phosphorylation of the Exocyst Complex.
Tay YD et al. Cell Rep 2019 Feb 05;26(6):1654-1667.e7
GO_REF:0000002 - Comments
PMID:33313903 - Ribosome profiling reveals ribosome stalling on tryptophan codons and ribosome queuing upon oxidative stress in fission yeast.
Rubio A et al. Nucleic Acids Res 2021 Jan 11;49(1):383-399
PB_REF:0000006 - Disease associations from Monarch via human-pombe orthologs
PMID:10526238 - Overproduction of elongation factor 1alpha, an essential translational component, causes aberrant cell morphology by affecting the control of growth polarity in fission yeast.
Suda M et al. Genes Cells 1999 Sep;4(9):517-27
PMID:30321377 - Proteomic profiling and functional characterization of post-translational modifications of the fission yeast RNA exosome.
Telekawa C et al. Nucleic Acids Res 2018 Nov 30;46(21):11169-11183
PMID:21504829 - Yeast SREBP cleavage activation requires the Golgi Dsc E3 ligase complex.
Stewart EV et al. Mol Cell 2011 Apr 22;42(2):160-71
PMID:24818994 - The S. pombe translation initiation factor eIF4G is Sumoylated and associates with the SUMO protease Ulp2.
Jongjitwimol J et al. PLoS One 2014;9(5):e94182
PMID:9099890 - Comprehensive cloning of Schizosaccharomyces pombe genes encoding translation elongation factors.
Mita K et al. Gene 1997 Mar 18;187(2):259-66
PMID:32435206 - Posttranslational Arginylation Enzyme Arginyltransferase1 Shows Genetic Interactions With Specific Cellular Pathways in vivo .
Wiley DJ et al. Front Physiol 2020;11:427
GO_REF:0000033 - Annotation inferences using phylogenetic trees
PMID:26537787 - Targeting of SUMO substrates to a Cdc48-Ufd1-Npl4 segregase and STUbL pathway in fission yeast.
Køhler JB et al. Nat Commun 2015 Nov 05;6:8827
PMID:21652630 - Characterization of Mug33 reveals complementary roles for actin cable-dependent transport and exocyst regulators in fission yeast exocytosis.
Snaith HA et al. J Cell Sci 2011 Jul 01;124(Pt 13):2187-99
PMID:21511999 - Comparative functional genomics of the fission yeasts.
Rhind N et al. Science 2011 May 20;332(6032):930-6
PMID:36408920 - UniProt: the Universal Protein Knowledgebase in 2023.
UniProt Consortium Nucleic Acids Res 2023 Jan 06;51(D1):D523-D531
PMID:15175657 - PRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunits.
Bachand F et al. EMBO J 2004 Jul 07;23(13):2641-50
PMID:3214489 - Peptide elongation factor 1 from yeasts: purification and biochemical characterization of peptide elongation factors 1 alpha and 1 beta (gamma) from Saccharomyces carlsbergensis and Schizosaccharomyces pombe.
Miyazaki M et al. J Biochem 1988 Mar;103(3):508-21
PMID:23101633 - Quantitative analysis of fission yeast transcriptomes and proteomes in proliferating and quiescent cells.
Marguerat S et al. Cell 2012 Oct 26;151(3):671-83
PMID:27984744 - Survival in Quiescence Requires the Euchromatic Deployment of Clr4/SUV39H by Argonaute-Associated Small RNAs.
Joh RI et al. Mol Cell 2016 Dec 15;64(6):1088-1101
PMID:10593605 - Cloning of a Schizosaccharomyces pombe homologue of elongation factor 1 alpha by two-hybrid selection of calmodulin-binding proteins.
Rasmussen C et al. Biochem Cell Biol 1999;77(5):421-30
PMID:23697806 - A genome-wide resource of cell cycle and cell shape genes of fission yeast.
Hayles J et al. Open Biol 2013 May 22;3(5):130053
PMID:36630955 - Zinc-finger protein Zpr1 is a bespoke chaperone essential for eEF1A biogenesis.
Sabbarini IM et al. Mol Cell 2023 Jan 19;83(2):252-265.e13
PMID:39367033 - Quantitative proteomics and phosphoproteomics profiling of meiotic divisions in the fission yeast Schizosaccharomyces pombe.
Sivakova B et al. Sci Rep 2024 Oct 04;14(1):23105
PMID:18257517 - Phosphoproteome analysis of fission yeast.
Wilson-Grady JT et al. J Proteome Res 2008 Mar;7(3):1088-97
PMID:36478272 - Translation-complex profiling of fission yeast cells reveals dynamic rearrangements of scanning ribosomal subunits upon nutritional stress.
Duncan CDS et al. Nucleic Acids Res 2022 Dec 09;50(22):13011-13025
PMID:34250083 - Barcode sequencing and a high-throughput assay for chronological lifespan uncover ageing-associated genes in fission yeast.
Romila CA et al. Microb Cell 2021 Jul 05;8(7):146-160
PMID:36820394 - Inorganic polyphosphate abets silencing of a sub-telomeric gene cluster in fission yeast.
Sanchez AM et al. MicroPubl Biol 2023;2023
PMID:34496258 - Transcription and chromatin-based surveillance mechanism controls suppression of cryptic antisense transcription.
Heo DH et al. Cell Rep 2021 Sep 07;36(10):109671
PMID:37787768 - Broad functional profiling of fission yeast proteins using phenomics and machine learning.
Rodríguez-López M et al. Elife 2023 Oct 03;12
PMID:39476757 - Characterization of Ksg1 protein kinase-dependent phosphoproteome in the fission yeast S. pombe.
Cipak L et al. Biochem Biophys Res Commun 2024 Oct 25;736:150895
PMID:28801462 - Protein glutaminylation is a yeast-specific posttranslational modification of elongation factor 1A.
Jank T et al. J Biol Chem 2017 Sep 29;292(39):16014-16023
PMID:26896847 - Ensembl comparative genomics resources.
Herrero J et al. Database (Oxford) 2016;2016
PMID:26412298 - A Degenerate Cohort of Yeast Membrane Trafficking DUBs Mediates Cell Polarity and Survival.
Beckley JR et al. Mol Cell Proteomics 2015 Dec;14(12):3132-41
GO_REF:0000024 - Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity.
PMID:26115316 - Saccharomyces cerevisiae Eukaryotic Elongation Factor 1A (eEF1A) Is Methylated at Lys-390 by a METTL21-Like Methyltransferase.
Jakobsson ME et al. PLoS One 2015;10(6):e0131426
PMID:20473289 - Analysis of a genome-wide set of gene deletions in the fission yeast Schizosaccharomyces pombe.
Kim DU et al. Nat Biotechnol 2010 Jun;28(6):617-623