Q9Y2Z4 · SYYM_HUMAN
- ProteinTyrosine--tRNA ligase, mitochondrial
- GeneYARS2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids477 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Catalytic activity
- ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H+ + L-tyrosyl-tRNA(Tyr)
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 77 | L-tyrosine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 81 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 121 | L-tyrosine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 221 | L-tyrosine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 225 | L-tyrosine (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 228 | L-tyrosine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 244-246 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GSD | ||||||
Binding site | 247 | L-tyrosine (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 274 | ATP (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 284 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrion | |
Cellular Component | nuclear body | |
Molecular Function | ATP binding | |
Molecular Function | L-tyrosine binding | |
Molecular Function | protein homodimerization activity | |
Molecular Function | RNA binding | |
Molecular Function | tRNA binding | |
Molecular Function | tyrosine-tRNA ligase activity | |
Biological Process | mitochondrial tyrosyl-tRNA aminoacylation | |
Biological Process | translation | |
Biological Process | tRNA aminoacylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTyrosine--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 accessionQ9Y2Z4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Myopathy with lactic acidosis and sideroblastic anemia 2 (MLASA2)
- Note
- DescriptionA rare oxidative phosphorylation disorder specific to skeletal muscle and bone marrow. Affected individuals manifest sideroblastic anemia, progressive lethargy, muscle weakness, and exercise intolerance associated with persistent lactic acidemia.
- See alsoMIM:613561
Natural variants in MLASA2
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_068646 | 46 | G>D | in MLASA2; dbSNP:rs587777213 | |
VAR_064188 | 52 | F>L | in MLASA2; has a 2-fold reduction in catalytic activity and a reduction in affinity for tRNA-tyr resulting in an overall 9-fold loss of catalytic efficiency; dbSNP:rs267607180 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_068646 | 46 | in MLASA2; dbSNP:rs587777213 | |||
Sequence: G → D | ||||||
Natural variant | VAR_064188 | 52 | in MLASA2; has a 2-fold reduction in catalytic activity and a reduction in affinity for tRNA-tyr resulting in an overall 9-fold loss of catalytic efficiency; dbSNP:rs267607180 | |||
Sequence: F → L | ||||||
Natural variant | VAR_034534 | 191 | in dbSNP:rs11539445 | |||
Sequence: G → V | ||||||
Mutagenesis | 200 | Loss of tRNA ligase activity. | ||||
Sequence: S → E | ||||||
Mutagenesis | 202 | Mildly decreased tRNA ligase activity. | ||||
Sequence: Q → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 567 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 transit peptide, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-16 | Mitochondrion | ||||
Sequence: MAAPILRSFSWGRWSG | ||||||
Chain | PRO_0000035830 | 17-477 | Tyrosine--tRNA ligase, mitochondrial | |||
Sequence: TLNLSVLLPLGLRKAHSGAQGLLAAQKARGLFKDFFPETGTKIELPELFDRGTASFPQTIYCGFDPTADSLHVGHLLALLGLFHLQRAGHNVIALVGGATARLGDPSGRTKEREALETERVRANARALRLGLEALAANHQQLFTDGRSWGSFTVLDNSAWYQKQHLVDFLAAVGGHFRMGTLLSRQSVQLRLKSPEGMSLAEFFYQVLQAYDFYYLFQRYGCRVQLGGSDQLGNIMSGYEFINKLTGEDVFGITVPLITSTTGAKLGKSAGNAVWLNRDKTSPFELYQFFVRQPDDSVERYLKLFTFLPLPEIDHIMQLHVKEPERRGPQKRLAAEVTKLVHGREGLDSAKRCTQALYHSSIDALEVMSDQELKELFKEAPFSEFFLDPGTSVLDTCRKANAIPDGPRGYRMITEGGVSINHQQVTNPESVLIVGQHILKNGLSLLKIGKRNFYIIKWLQL | ||||||
Modified residue | 355 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 367 | N6-acetyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Homodimer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9Y2Z4 | AGTRAP Q6RW13-2 | 3 | EBI-1049286, EBI-11522760 | |
BINARY | Q9Y2Z4 | FAM9B Q8IZU0 | 3 | EBI-1049286, EBI-10175124 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 82-91 | 'HIGH' region | ||||
Sequence: PTADSLHVGH | ||||||
Motif | 281-285 | 'KMSKS' region | ||||
Sequence: KLGKS |
Sequence similarities
Belongs to the class-I aminoacyl-tRNA synthetase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length477
- Mass (Da)53,199
- Last updated2004-07-19 v2
- ChecksumC513B8FE1E7A09E4
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H0YHS6 | H0YHS6_HUMAN | YARS2 | 291 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 1-4 | in Ref. 1; AAD27714 | ||||
Sequence: MAAP → MGA | ||||||
Sequence conflict | 118 | in Ref. 1; AAD27714 | ||||
Sequence: R → A | ||||||
Sequence conflict | 272 | in Ref. 1; AAD27714 | ||||
Sequence: P → T | ||||||
Sequence conflict | 311 | in Ref. 1; AAD27714 | ||||
Sequence: D → E |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF132939 EMBL· GenBank· DDBJ | AAD27714.1 EMBL· GenBank· DDBJ | mRNA | ||
AK024057 EMBL· GenBank· DDBJ | BAB14806.1 EMBL· GenBank· DDBJ | mRNA | ||
AC087588 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471116 EMBL· GenBank· DDBJ | EAW88517.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471116 EMBL· GenBank· DDBJ | EAW88518.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC015625 EMBL· GenBank· DDBJ | AAH15625.1 EMBL· GenBank· DDBJ | mRNA |