Q9BW92 · SYTM_HUMAN
- ProteinThreonine--tRNA ligase, mitochondrial
- GeneTARS2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids718 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged tRNA(Thr) via its editing domain.
Catalytic activity
- ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H+ + L-threonyl-tRNA(Thr)
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
2.5 mM | L-threonine | |||||
1.1 μM | tRNA(Thr) | |||||
180 mM | L-serine |
kcat is 5.8 sec-1 for the activation reaction of L-threonine. kcat is 1.1 sec-1 for the activation reaction of L-serine. kcat is 0.061 sec-1 for the aminoacylation of tRNA(Thr) with L-threonine.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
Molecular Function | aminoacyl-tRNA editing activity | |
Molecular Function | ATP binding | |
Molecular Function | protein homodimerization activity | |
Molecular Function | threonine-tRNA ligase activity | |
Biological Process | mitochondrial threonyl-tRNA aminoacylation | |
Biological Process | threonyl-tRNA aminoacylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameThreonine--tRNA ligase, mitochondrial
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9BW92
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Combined oxidative phosphorylation deficiency 21 (COXPD21)
- Note
- DescriptionA mitochondrial disorder characterized by a lethal encephalomyopathy. Shortly after birth, affected individuals manifest axial hypotonia, limb hypertonia, psychomotor delay, and increased serum lactate. Additional features include subsarcolemmal lipofuscin-positive deposits in muscle, cerebral spongiosis, and hepatic steatosis.
- See alsoMIM:615918
Natural variants in COXPD21
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_071853 | 282 | P>L | in COXPD21; decreased expression at mRNA and protein levels; decreased threonine-tRNA ligase activity; affects both Thr activation and transfer; decreased aminoacyl-tRNA editing activity; decreased protein stability; loss of homodimerization; dbSNP:rs587777593 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_071853 | 282 | in COXPD21; decreased expression at mRNA and protein levels; decreased threonine-tRNA ligase activity; affects both Thr activation and transfer; decreased aminoacyl-tRNA editing activity; decreased protein stability; loss of homodimerization; dbSNP:rs587777593 | |||
Sequence: P → L |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 708 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, transit peptide, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000254586 | ?-718 | Threonine--tRNA ligase, mitochondrial | |||
Sequence: MALYQRWRCLRLQGLQACRLHTAVVSTPPRWLAERLGLFEELWAAQVKRLASMAQKEPRTIKISLPGGQKIDAVAWNTTPYQLARQISSTLADTAVAAQVNGEPYDLERPLETDSDLRFLTFDSPEGKAVFWHSSTHVLGAAAEQFLGAVLCRGPSTEYGFYHDFFLGKERTIRGSELPVLERICQELTAAARPFRRLEASRDQLRQLFKDNPFKLHLIEEKVTGPTATVYGCGTLVDLCQGPHLRHTGQIGGLKLLSNSSSLWRSSGAPETLQRVSGISFPTTELLRVWEAWREEAELRDHRRIGKEQELFFFHELSPGSCFFLPRGTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFAVQPPGSDRPPSSQSDDSTRHITDTLALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGLGGLTRLRCFQQDDAHIFCTTDQLEAEIQSCLDFLRSVYAVLGFSFRLALSTRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDLNSGDGAFYGPKIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKGQAGALERPVLIHRAVLGSVERLLGVLAESCGGKWPLWLSPFQVVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDADSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDNRRLGEWDLPEAVQRLVELQNTRVPNAEEIF | ||||||
Transit peptide | 1-? | Mitochondrion | ||||
Modified residue | 52 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Homodimer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9BW92 | ARL6IP1 Q15041 | 3 | EBI-1045099, EBI-714543 | |
BINARY | Q9BW92 | ASB6 Q9NWX5 | 3 | EBI-1045099, EBI-6425205 | |
BINARY | Q9BW92 | DDIT4L Q96D03 | 3 | EBI-1045099, EBI-742054 | |
BINARY | Q9BW92 | FKBP7 Q9Y680 | 3 | EBI-1045099, EBI-3918971 | |
BINARY | Q9BW92 | MAL2 Q969L2 | 3 | EBI-1045099, EBI-944295 | |
BINARY | Q9BW92 | PLIN3 O60664 | 3 | EBI-1045099, EBI-725795 | |
BINARY | Q9BW92 | SFT2D1 Q8WV19 | 3 | EBI-1045099, EBI-2854842 | |
BINARY | Q9BW92 | SLC17A9 Q9BYT1 | 3 | EBI-1045099, EBI-3940816 | |
BINARY | Q9BW92 | SYPL1 Q16563 | 3 | EBI-1045099, EBI-2800683 | |
BINARY | Q9BW92 | TARS3 A2RTX5 | 3 | EBI-1045099, EBI-1056629 | |
BINARY | Q9BW92 | TNFRSF10D Q9UBN6 | 3 | EBI-1045099, EBI-1044859 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 55-121 | TGS | ||||
Sequence: QKEPRTIKISLPGGQKIDAVAWNTTPYQLARQISSTLADTAVAAQVNGEPYDLERPLETDSDLRFLT |
Sequence similarities
Belongs to the class-II aminoacyl-tRNA synthetase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
Q9BW92-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length718
- Mass (Da)81,036
- Last updated2001-06-01 v1
- ChecksumA2F793A60483E7F9
Q9BW92-2
- Name2
- Differences from canonical
- 211-340: Missing
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_054537 | 211-340 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 269 | in Ref. 2; BAD96534 | ||||
Sequence: A → P | ||||||
Sequence conflict | 579 | in Ref. 2; BAD96534 | ||||
Sequence: E → G |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK022590 EMBL· GenBank· DDBJ | BAB14117.1 EMBL· GenBank· DDBJ | mRNA | ||
AK222814 EMBL· GenBank· DDBJ | BAD96534.1 EMBL· GenBank· DDBJ | mRNA | ||
AL356356 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471121 EMBL· GenBank· DDBJ | EAW53549.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC000541 EMBL· GenBank· DDBJ | AAH00541.1 EMBL· GenBank· DDBJ | mRNA | ||
BC007824 EMBL· GenBank· DDBJ | AAH07824.2 EMBL· GenBank· DDBJ | mRNA | ||
BC009997 EMBL· GenBank· DDBJ | AAH09997.1 EMBL· GenBank· DDBJ | mRNA |