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protein coding gene - mrm202 (SPAPB17E12.10c) - mitochondrial 2' O-ribose methyltransferase Mrm2-like

Gene summary

Standard name
mrm202
Systematic ID
SPAPB17E12.10c
Product
mitochondrial 2' O-ribose methyltransferase Mrm2-like
Organism
Schizosaccharomyces pombe (fission yeast)
UniProt ID
Q8TFH4
Characterisation status
biological role inferred
Feature type
mRNA gene
Genomic location
chromosome I: 1280495..1282822 reverse strand

Annotation

Disease association

MONDO:0032815 - mitochondrial DNA depletion syndrome 17

References:

GO biological process

GO:0000963 - mitochondrial RNA processing

References:

GO:0000027 - ribosomal large subunit assembly

References:

GO:0031167 - rRNA methylation

References:

GO cellular component

GO:0005759 - mitochondrial matrix

References:

GO molecular function

GO:0008650 - rRNA (uridine-2'-O-ribose)-methyltransferase activity

References:

Qualitative gene expression

PomGeneEx:0000018 - protein level increased

References:

PomGeneEx:0000012 - RNA level decreased

References:

PomGeneEx:0000011 - RNA level increased

References:

Quantitative gene expression

PBO:0011963 - RNA level

References:

Single locus phenotype

FYPO:0002111 - inviable tapered vegetative cell

References:

Genotypes:

FYPO:0002061 - inviable vegetative cell population

References:

Genotypes:

Taxonomic conservation

PBO:0011065 - conserved in eukaryotes

PBO:0011071 - conserved in eukaryotes only

PBO:0011064 - conserved in fungi

PBO:0011069 - conserved in metazoa

PBO:0011070 - conserved in vertebrates

Protein features

IDNameInterPro nameDB name
PF01728FtsJRNA_MeTrfase_FtsJ_domPFAM
cd02440AdoMet_MTasesCDD
PS51257PROKAR_LIPOPROTEINPROSITE_PROFILES
SSF53335S-adenosyl-L-methionine-dependent methyltransferasesSAM-dependent_MTases_sfSUPERFAMILY
G3DSA:3.40.50.150Vaccinia Virus protein VP39SAM-dependent_MTases_sfGENE3D
PTHR10920RIBOSOMAL RNA METHYLTRANSFERASERNA_methyltr_RlmEPANTHER

Orthologs

References / Literature

GO_REF:0000111 - Gene Ontology annotations Inferred by Curator (IC) using at least one Inferred by Sequence Similarity (ISS) annotation to support the inference
PB_REF:0000006 - Disease associations from Monarch via human-pombe orthologs
PMID:27611590 - Pfh1 Is an Accessory Replicative Helicase that Interacts with the Replisome to Facilitate Fork Progression and Preserve Genome Integrity.
McDonald KR et al. PLoS Genet 2016 Sep;12(9):e1006238
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: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:31626996 - Multiplexed proteome profiling of carbon source perturbations in two yeast species with SL-SP3-TMT.
Paulo JA et al. J Proteomics 2020 Jan 06;210:103531
PMID:23163955 - Analysis of stress-induced duplex destabilization (SIDD) properties of replication origins, genes and intergenes in the fission yeast, Schizosaccharomyces pombe.
Yadav MP et al. BMC Res Notes 2012 Nov 19;5:643
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
GO_REF:0000033 - Annotation inferences using phylogenetic trees
GO_REF:0000036 - Manual annotations that require more than one source of functional data to support the assignment of the associated GO term
PMID:21511999 - Comparative functional genomics of the fission yeasts.
Rhind N et al. Science 2011 May 20;332(6032):930-6
GO_REF:0000024 - Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity.
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
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