Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

tRNA (adenine(58)-N(1))-methyltransferase, mitochondrial

Gene

TRMT61B

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

Functioni

Methyltransferase that catalyzes the formation of N1-methyladenine at position 58 (m1A58) in various tRNAs in mitochondrion, including tRNA(Leu) (deciphering codons UUA or UUG), tRNA(Lys) and tRNA(Ser) (deciphering codons UCA, UCU, UCG or UCC) (PubMed:23097428). Catalyzes the formation of 1-methyladenosine at position 947 of mitochondrial 16S ribosomal RNA and this modification is most likely important for mitoribosomal structure and function (PubMed:27631568). In addition to tRNA N1-methyltransferase activity, also acts as a mRNA N1-methyltransferase by mediating methylation of adenosine residues at the N1 position of MT-ND5 mRNA, leading to interfere with mitochondrial translation (PubMed:29107537).3 Publications

Caution

The identity of the enzyme catalyzing mitochondrial mRNA N1-methyltransferase is unclear. According to a report, mitochondrial mRNA N1-methyltransferase activity is catalyzed by TRMT61B (PubMed:29107537). According to a second report, it is mediated by TRMT10C (AC Q7L0Y3) (PubMed:29072297). As both reports only tested one protein (either TRMT61B or TRMT10C), it is possible that both proteins have this activity.2 Publications

Catalytic activityi

S-adenosyl-L-methionine + adenine(58) in tRNA = S-adenosyl-L-homocysteine + N1-methyladenine(58) in tRNA.PROSITE-ProRule annotation1 Publication
S-adenosyl-L-methionine + adenine in mRNA = S-adenosyl-L-homocysteine + N1-methyladenine in mRNA.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei259S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation1 Publication1
Binding sitei317S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation1 Publication1
Binding sitei335S-adenosyl-L-methioninePROSITE-ProRule annotation1 Publication1
Binding sitei463SubstrateBy similarity1

GO - Molecular functioni

  • mRNA (adenine-N1-)-methyltransferase activity Source: UniProtKB
  • rRNA (adenine) methyltransferase activity Source: UniProtKB
  • tRNA (adenine-N1-)-methyltransferase activity Source: UniProtKB

GO - Biological processi

  • mitochondrial tRNA methylation Source: UniProtKB
  • mRNA methylation Source: UniProtKB
  • protein homooligomerization Source: UniProtKB

Keywordsi

Molecular functionMethyltransferase, Transferase
Biological processtRNA processing
LigandS-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiR-HSA-6787450 tRNA modification in the mitochondrion

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA (adenine(58)-N(1))-methyltransferase, mitochondrial (EC:2.1.1.2201 Publication)
Alternative name(s):
mRNA methyladenosine-N(1)-methyltransferase1 Publication (EC:2.1.1.-1 Publication)
Gene namesi
Name:TRMT61B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiHostDB:ENSG00000171103.10
HGNCiHGNC:26070 TRMT61B
neXtProtiNX_Q9BVS5

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi335D → A: Loss of ability to catalyze the formation of 1-methyladenosine at position 947 of mitochondrial 16S ribosomal RNA. 1 Publication1

Organism-specific databases

OpenTargetsiENSG00000171103
PharmGKBiPA164726796

Polymorphism and mutation databases

BioMutaiTRMT61B
DMDMi162416224

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000311814? – 477tRNA (adenine(58)-N(1))-methyltransferase, mitochondrial
Transit peptidei1 – ?MitochondrionSequence analysis

Proteomic databases

EPDiQ9BVS5
MaxQBiQ9BVS5
PaxDbiQ9BVS5
PeptideAtlasiQ9BVS5
PRIDEiQ9BVS5

PTM databases

iPTMnetiQ9BVS5
PhosphoSitePlusiQ9BVS5

Expressioni

Gene expression databases

BgeeiENSG00000171103
ExpressionAtlasiQ9BVS5 baseline and differential
GenevisibleiQ9BVS5 HS

Organism-specific databases

HPAiHPA026747
HPA026751

Interactioni

Subunit structurei

Homooligomer; in contrast to TRMT61A, does not form a heterotetramer.2 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi120338, 39 interactors
IntActiQ9BVS5, 221 interactors
STRINGi9606.ENSP00000302801

Structurei

Secondary structure

1477
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi156 – 160Combined sources5
Beta strandi169 – 173Combined sources5
Helixi189 – 192Combined sources4
Beta strandi199 – 202Combined sources4
Beta strandi208 – 212Combined sources5
Helixi216 – 222Combined sources7
Helixi232 – 242Combined sources11
Beta strandi249 – 253Combined sources5
Helixi259 – 268Combined sources10
Beta strandi273 – 280Combined sources8
Helixi281 – 298Combined sources18
Turni299 – 301Combined sources3
Beta strandi310 – 315Combined sources6
Beta strandi329 – 334Combined sources6
Beta strandi336 – 338Combined sources3
Turni339 – 342Combined sources4
Helixi343 – 346Combined sources4
Helixi347 – 349Combined sources3
Beta strandi350 – 362Combined sources13
Helixi363 – 376Combined sources14
Beta strandi380 – 386Combined sources7
Beta strandi393 – 395Combined sources3
Beta strandi453 – 455Combined sources3
Beta strandi465 – 471Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2B25X-ray2.50A/B144-477[»]
ProteinModelPortaliQ9BVS5
SMRiQ9BVS5
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BVS5

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni77 – 79SubstrateBy similarity3
Regioni133 – 179SubstrateBy similarityAdd BLAST47
Regioni206 – 207SubstrateBy similarity2
Regioni228 – 232SubstrateBy similarity5
Regioni253 – 260SubstrateBy similarity8
Regioni278 – 279S-adenosyl-L-methionine binding1 Publication2
Regioni334 – 337SubstrateBy similarity4
Regioni358 – 365SubstrateBy similarity8

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM61 family.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2915 Eukaryota
COG2519 LUCA
GeneTreeiENSGT00510000049118
HOGENOMiHOG000245274
InParanoidiQ9BVS5
KOiK07442
OMAiIVGKFPG
OrthoDBiEOG091G050C
PhylomeDBiQ9BVS5
TreeFamiTF315053

Family and domain databases

InterProiView protein in InterPro
IPR029063 SAM-dependent_MTases
IPR014816 tRNA_MeTrfase_Gcd14
PANTHERiPTHR12133 PTHR12133, 1 hit
PfamiView protein in Pfam
PF08704 GCD14, 1 hit
SUPFAMiSSF53335 SSF53335, 1 hit
PROSITEiView protein in PROSITE
PS51620 SAM_TRM61, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q9BVS5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLMAWCRGPV LLCLRQGLGT NSFLHGLGQE PFEGARSLCC RSSPRDLRDG
60 70 80 90 100
EREHEAAQRK APGAESCPSL PLSISDIGTG CLSSLENLRL PTLREESSPR
110 120 130 140 150
ELEDSSGDQG RCGPTHQGSE DPSMLSQAQS ATEVEERHVS PSCSTSRERP
160 170 180 190 200
FQAGELILAE TGEGETKFKK LFRLNNFGLL NSNWGAVPFG KIVGKFPGQI
210 220 230 240 250
LRSSFGKQYM LRRPALEDYV VLMKRGTAIT FPKDINMILS MMDINPGDTV
260 270 280 290 300
LEAGSGSGGM SLFLSKAVGS QGRVISFEVR KDHHDLAKKN YKHWRDSWKL
310 320 330 340 350
SHVEEWPDNV DFIHKDISGA TEDIKSLTFD AVALDMLNPH VTLPVFYPHL
360 370 380 390 400
KHGGVCAVYV VNITQVIELL DGIRTCELAL SCEKISEVIV RDWLVCLAKQ
410 420 430 440 450
KNGILAQKVE SKINTDVQLD SQEKIGVKGE LFQEDDHEES HSDFPYGSFP
460 470
YVARPVHWQP GHTAFLVKLR KVKPQLN
Length:477
Mass (Da):52,965
Last modified:December 4, 2007 - v2
Checksum:iAE538B72413DED63
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti132T → I in AAH00952 (PubMed:15489334).Curated1
Sequence conflicti442S → F in BAA91300 (PubMed:14702039).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL136689 mRNA Translation: CAB66624.1
AK000635 mRNA Translation: BAA91300.1
CH471053 Genomic DNA Translation: EAX00524.1
AC097720 Genomic DNA Translation: AAY24015.1
BC000952 mRNA Translation: AAH00952.1
BC010365 mRNA Translation: AAH10365.1
CCDSiCCDS1768.1
RefSeqiNP_060380.3, NM_017910.3
UniGeneiHs.468026

Genome annotation databases

EnsembliENST00000306108; ENSP00000302801; ENSG00000171103
GeneIDi55006
KEGGihsa:55006
UCSCiuc002rmm.5 human

Similar proteinsi

Entry informationi

Entry nameiTR61B_HUMAN
AccessioniPrimary (citable) accession number: Q9BVS5
Secondary accession number(s): Q9H0Q9, Q9NWS7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: December 4, 2007
Last modified: May 23, 2018
This is version 133 of the entry and version 2 of the sequence. See 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 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health