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Protein

rRNA methyltransferase 2, mitochondrial

Gene

MRM2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methyluridine at position 1369 (Um1369) in the 16S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA.2 Publications

Catalytic activityi

S-adenosyl-L-methionine + uridine(1369) in 16S rRNA = S-adenosyl-L-homocysteine + 2'-O-methyluridine(1369) in 16S rRNA.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei112 – 1121S-adenosyl-L-methionine1 Publication
Binding sitei154 – 1541S-adenosyl-L-methionine1 Publication
Active sitei194 – 1941Proton acceptorBy similarity

GO - Molecular functioni

  • rRNA (uridine-2'-O-)-methyltransferase activity Source: BHF-UCL

GO - Biological processi

  • cell proliferation Source: BHF-UCL
  • enzyme-directed rRNA 2'-O-methylation Source: GO_Central
  • rRNA methylation Source: BHF-UCL
  • rRNA processing Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.166. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
rRNA methyltransferase 2, mitochondrial1 Publication (EC:2.1.1.-1 Publication)
Alternative name(s):
16S rRNA (uridine(1369)-2'-O)-methyltransferase1 Publication
16S rRNA [Um1369] 2'-O-methyltransferase1 Publication
Protein ftsJ homolog 21 Publication
Gene namesi
Name:MRM21 Publication
Synonyms:FJH11 Publication, FTSJ21 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:16352. MRM2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: BHF-UCL
  • nucleolus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28418.

Polymorphism and mutation databases

BioMutaiFTSJ2.
DMDMi9910866.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1818MitochondrionSequence analysisAdd
BLAST
Chaini19 – 246228rRNA methyltransferase 2, mitochondrialPRO_0000155576Add
BLAST

Proteomic databases

EPDiQ9UI43.
PaxDbiQ9UI43.
PeptideAtlasiQ9UI43.
PRIDEiQ9UI43.

PTM databases

iPTMnetiQ9UI43.
PhosphoSiteiQ9UI43.

Expressioni

Tissue specificityi

Widely expressed, with highest expression in muscle, placenta, and heart.1 Publication

Gene expression databases

BgeeiQ9UI43.
CleanExiHS_FTSJ2.
ExpressionAtlasiQ9UI43. baseline and differential.
GenevisibleiQ9UI43. HS.

Organism-specific databases

HPAiHPA019826.
HPA049622.

Interactioni

Protein-protein interaction databases

BioGridi118996. 10 interactions.
STRINGi9606.ENSP00000242257.

Structurei

Secondary structure

1
246
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi56 – 6712Combined sources
Beta strandi75 – 795Combined sources
Helixi85 – 939Combined sources
Turni94 – 974Combined sources
Beta strandi107 – 1115Combined sources
Beta strandi123 – 1253Combined sources
Helixi133 – 14210Combined sources
Helixi144 – 1463Combined sources
Beta strandi148 – 1536Combined sources
Helixi163 – 18422Combined sources
Beta strandi185 – 19511Combined sources
Helixi199 – 2013Combined sources
Helixi202 – 21110Combined sources
Beta strandi212 – 2187Combined sources
Beta strandi230 – 2378Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NYUX-ray1.76A/B51-246[»]
ProteinModelPortaliQ9UI43.
SMRiQ9UI43. Positions 51-239.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UI43.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni83 – 864S-adenosyl-L-methionine binding1 Publication
Regioni129 – 1302S-adenosyl-L-methionine binding1 Publication

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG4589. Eukaryota.
COG0293. LUCA.
HOGENOMiHOG000162366.
HOVERGENiHBG009202.
InParanoidiQ9UI43.
KOiK02427.
OMAiFLATQYH.
OrthoDBiEOG757CZN.
PhylomeDBiQ9UI43.
TreeFamiTF316701.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01547. RNA_methyltr_E.
InterProiIPR015507. rRNA-MeTfrase_E.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR10920. PTHR10920. 1 hit.
PfamiPF01728. FtsJ. 1 hit.
[Graphical view]
PIRSFiPIRSF005461. 23S_rRNA_mtase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9UI43-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGYLKLVCV SFQRQGFHTV GSRCKNRTGA EHLWLTRHLR DPFVKAAKVE
60 70 80 90 100
SYRCRSAFKL LEVNERHQIL RPGLRVLDCG AAPGAWSQVA VQKVNAAGTD
110 120 130 140 150
PSSPVGFVLG VDLLHIFPLE GATFLCPADV TDPRTSQRIL EVLPGRRADV
160 170 180 190 200
ILSDMAPNAT GFRDLDHDRL ISLCLTLLSV TPDILQPGGT FLCKTWAGSQ
210 220 230 240
SRRLQRRLTE EFQNVRIIKP EASRKESSEV YFLATQYHGR KGTVKQ
Length:246
Mass (Da):27,424
Last modified:May 1, 2000 - v1
Checksum:iDB7B9978695409D1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731G → S in AAI14515 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF093415 mRNA. Translation: AAF22488.1.
BC114514 mRNA. Translation: AAI14515.1.
CCDSiCCDS5328.1.
RefSeqiNP_037525.1. NM_013393.1.
UniGeneiHs.279877.

Genome annotation databases

EnsembliENST00000242257; ENSP00000242257; ENSG00000122687.
ENST00000440306; ENSP00000392343; ENSG00000122687.
GeneIDi29960.
KEGGihsa:29960.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF093415 mRNA. Translation: AAF22488.1.
BC114514 mRNA. Translation: AAI14515.1.
CCDSiCCDS5328.1.
RefSeqiNP_037525.1. NM_013393.1.
UniGeneiHs.279877.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NYUX-ray1.76A/B51-246[»]
ProteinModelPortaliQ9UI43.
SMRiQ9UI43. Positions 51-239.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118996. 10 interactions.
STRINGi9606.ENSP00000242257.

PTM databases

iPTMnetiQ9UI43.
PhosphoSiteiQ9UI43.

Polymorphism and mutation databases

BioMutaiFTSJ2.
DMDMi9910866.

Proteomic databases

EPDiQ9UI43.
PaxDbiQ9UI43.
PeptideAtlasiQ9UI43.
PRIDEiQ9UI43.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000242257; ENSP00000242257; ENSG00000122687.
ENST00000440306; ENSP00000392343; ENSG00000122687.
GeneIDi29960.
KEGGihsa:29960.

Organism-specific databases

CTDi29960.
GeneCardsiFTSJ2.
HGNCiHGNC:16352. MRM2.
HPAiHPA019826.
HPA049622.
MIMi606906. gene.
neXtProtiNX_Q9UI43.
PharmGKBiPA28418.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4589. Eukaryota.
COG0293. LUCA.
HOGENOMiHOG000162366.
HOVERGENiHBG009202.
InParanoidiQ9UI43.
KOiK02427.
OMAiFLATQYH.
OrthoDBiEOG757CZN.
PhylomeDBiQ9UI43.
TreeFamiTF316701.

Enzyme and pathway databases

BRENDAi2.1.1.166. 2681.

Miscellaneous databases

ChiTaRSiFTSJ2. human.
EvolutionaryTraceiQ9UI43.
GenomeRNAii29960.
PROiQ9UI43.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UI43.
CleanExiHS_FTSJ2.
ExpressionAtlasiQ9UI43. baseline and differential.
GenevisibleiQ9UI43. HS.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01547. RNA_methyltr_E.
InterProiIPR015507. rRNA-MeTfrase_E.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR10920. PTHR10920. 1 hit.
PfamiPF01728. FtsJ. 1 hit.
[Graphical view]
PIRSFiPIRSF005461. 23S_rRNA_mtase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Chromosomal localization of human FJH1."
    Jin D.-Y., Jeang K.-T.
    Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Identification and characterization of FTSJ2, a novel human nucleolar protein homologous to bacterial ribosomal RNA methyltransferase."
    Ching Y.-P., Zhou H.-J., Yuan J.-G., Qiang B.-Q., Kung H., Jin D.-Y.
    Genomics 79:2-6(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "Mitochondrial ribosomal RNA (rRNA) methyltransferase family members are positioned to modify nascent rRNA in foci near the mitochondrial DNA nucleoid."
    Lee K.W., Okot-Kotber C., LaComb J.F., Bogenhagen D.F.
    J. Biol. Chem. 288:31386-31399(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  6. "Assignment of 2'-O-methyltransferases to modification sites on the mammalian mitochondrial large subunit 16S rRNA."
    Lee K.W., Bogenhagen D.F.
    J. Biol. Chem. 289:24936-24942(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "MRM2 and MRM3 are involved in biogenesis of the large subunit of the mitochondrial ribosome."
    Rorbach J., Boesch P., Gammage P.A., Nicholls T.J., Pearce S.F., Patel D., Hauser A., Perocchi F., Minczuk M.
    Mol. Biol. Cell 25:2542-2555(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "The crystal structure of human ftsJ homolog 2 (E.coli) protein in complex with AdoMet."
    Structural genomics consortium (SGC)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 51-246 IN COMPLEX WITH S-ADENOSYL-L-METHIONINE.

Entry informationi

Entry nameiMRM2_HUMAN
AccessioniPrimary (citable) accession number: Q9UI43
Secondary accession number(s): Q24JR8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.