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

Tyrosine--tRNA ligase, mitochondrial

Gene

YARS2

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

Functioni

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).2 Publications

Catalytic activityi

ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei77TyrosineCombined sources1 Publication1
Binding sitei81ATPCombined sources1 Publication1
Binding sitei121TyrosineCombined sources1 Publication1
Binding sitei221TyrosineCombined sources1 Publication1
Binding sitei225TyrosineCombined sources1 Publication1
Binding sitei228TyrosineCombined sources1 Publication1
Binding sitei247TyrosineCombined sources1 Publication1
Binding sitei274ATP; via amide nitrogen and carbonyl oxygenCombined sources1 Publication1
Binding sitei284ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi244 – 246ATPCombined sources1 Publication3

GO - Molecular functioni

  • ATP binding Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL
  • RNA binding Source: UniProtKB
  • tRNA binding Source: BHF-UCL
  • tyrosine binding Source: BHF-UCL
  • tyrosine-tRNA ligase activity Source: BHF-UCL

GO - Biological processi

  • mitochondrial tyrosyl-tRNA aminoacylation Source: BHF-UCL
  • translation Source: UniProtKB
  • tRNA aminoacylation Source: BHF-UCL
  • tRNA aminoacylation for protein translation Source: Reactome

Keywordsi

Molecular functionAminoacyl-tRNA synthetase, Ligase
Biological processProtein biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.1.1.1 2681
ReactomeiR-HSA-379726 Mitochondrial tRNA aminoacylation

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine--tRNA ligase, mitochondrial (EC:6.1.1.12 Publications)
Alternative name(s):
Tyrosyl-tRNA synthetase
Short name:
TyrRS1 Publication
Gene namesi
Name:YARS2
ORF Names:CGI-04
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

EuPathDBiHostDB:ENSG00000139131.12
HGNCiHGNC:24249 YARS2
MIMi610957 gene
neXtProtiNX_Q9Y2Z4

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

Involvement in diseasei

Myopathy with lactic acidosis and sideroblastic anemia 2 (MLASA2)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease 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 also OMIM:613561
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06864646G → D in MLASA2. 1 PublicationCorresponds to variant dbSNP:rs587777213EnsemblClinVar.1
Natural variantiVAR_06418852F → 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. 1 PublicationCorresponds to variant dbSNP:rs267607180EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi200S → E: Loss of tRNA ligase activity. 1 Publication1
Mutagenesisi202Q → A: Mildly decreased tRNA ligase activity. 1 Publication1

Keywords - Diseasei

Disease mutation, Primary mitochondrial disease

Organism-specific databases

DisGeNETi51067
MalaCardsiYARS2
MIMi613561 phenotype
OpenTargetsiENSG00000139131
Orphaneti2598 Mitochondrial myopathy and sideroblastic anemia
PharmGKBiPA142670559

Chemistry databases

DrugBankiDB00135 L-Tyrosine

Polymorphism and mutation databases

BioMutaiYARS2
DMDMi50401709

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 16MitochondrionSequence analysisAdd BLAST16
ChainiPRO_000003583017 – 477Tyrosine--tRNA ligase, mitochondrialAdd BLAST461

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei355N6-acetyllysineCombined sources1
Modified residuei367N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9Y2Z4
MaxQBiQ9Y2Z4
PaxDbiQ9Y2Z4
PeptideAtlasiQ9Y2Z4
PRIDEiQ9Y2Z4
ProteomicsDBi85948

PTM databases

iPTMnetiQ9Y2Z4
PhosphoSitePlusiQ9Y2Z4
SwissPalmiQ9Y2Z4

Expressioni

Gene expression databases

BgeeiENSG00000139131
CleanExiHS_YARS2
ExpressionAtlasiQ9Y2Z4 baseline and differential
GenevisibleiQ9Y2Z4 HS

Organism-specific databases

HPAiHPA038721
HPA057610
HPA074097

Interactioni

Subunit structurei

Homodimer.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FAM9BQ8IZU03EBI-1049286,EBI-10175124

GO - Molecular functioni

  • protein homodimerization activity Source: BHF-UCL

Protein-protein interaction databases

BioGridi119258, 53 interactors
DIPiDIP-29487N
IntActiQ9Y2Z4, 20 interactors
MINTiQ9Y2Z4
STRINGi9606.ENSP00000320658

Structurei

Secondary structure

1477
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi38 – 45Combined sources8
Beta strandi50 – 52Combined sources3
Helixi61 – 64Combined sources4
Beta strandi67 – 70Combined sources4
Beta strandi75 – 80Combined sources6
Beta strandi83 – 86Combined sources4
Helixi89 – 103Combined sources15
Beta strandi107 – 112Combined sources6
Helixi116 – 118Combined sources3
Helixi134 – 158Combined sources25
Beta strandi168 – 172Combined sources5
Helixi174 – 177Combined sources4
Helixi182 – 189Combined sources8
Helixi190 – 192Combined sources3
Helixi195 – 200Combined sources6
Helixi202 – 208Combined sources7
Beta strandi210 – 212Combined sources3
Helixi216 – 236Combined sources21
Beta strandi240 – 244Combined sources5
Helixi245 – 247Combined sources3
Helixi248 – 261Combined sources14
Beta strandi267 – 271Combined sources5
Beta strandi291 – 293Combined sources3
Turni294 – 296Combined sources3
Helixi299 – 307Combined sources9
Helixi311 – 321Combined sources11
Helixi326 – 338Combined sources13
Helixi340 – 342Combined sources3
Helixi344 – 372Combined sources29

3D structure databases

ProteinModelPortaliQ9Y2Z4
SMRiQ9Y2Z4
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y2Z4

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi82 – 91"HIGH" regionCurated10
Motifi281 – 285"KMSKS" regionCurated5

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2623 Eukaryota
COG0162 LUCA
GeneTreeiENSGT00390000013709
HOGENOMiHOG000242790
HOVERGENiHBG056052
InParanoidiQ9Y2Z4
KOiK01866
OMAiVNYMMAK
OrthoDBiEOG091G06NG
PhylomeDBiQ9Y2Z4
TreeFamiTF105974

Family and domain databases

CDDicd00805 TyrRS_core, 1 hit
Gene3Di3.10.290.10, 1 hit
3.40.50.620, 1 hit
InterProiView protein in InterPro
IPR001412 aa-tRNA-synth_I_CS
IPR002305 aa-tRNA-synth_Ic
IPR014729 Rossmann-like_a/b/a_fold
IPR036986 S4_RNA-bd_sf
IPR002307 Tyr-tRNA-ligase
IPR024088 Tyr-tRNA-ligase_bac-type
PANTHERiPTHR11766 PTHR11766, 1 hit
PfamiView protein in Pfam
PF00579 tRNA-synt_1b, 1 hit
PRINTSiPR01040 TRNASYNTHTYR
TIGRFAMsiTIGR00234 tyrS, 1 hit
PROSITEiView protein in PROSITE
PS00178 AA_TRNA_LIGASE_I, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q9Y2Z4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPILRSFS WGRWSGTLNL SVLLPLGLRK AHSGAQGLLA AQKARGLFKD
60 70 80 90 100
FFPETGTKIE LPELFDRGTA SFPQTIYCGF DPTADSLHVG HLLALLGLFH
110 120 130 140 150
LQRAGHNVIA LVGGATARLG DPSGRTKERE ALETERVRAN ARALRLGLEA
160 170 180 190 200
LAANHQQLFT DGRSWGSFTV LDNSAWYQKQ HLVDFLAAVG GHFRMGTLLS
210 220 230 240 250
RQSVQLRLKS PEGMSLAEFF YQVLQAYDFY YLFQRYGCRV QLGGSDQLGN
260 270 280 290 300
IMSGYEFINK LTGEDVFGIT VPLITSTTGA KLGKSAGNAV WLNRDKTSPF
310 320 330 340 350
ELYQFFVRQP DDSVERYLKL FTFLPLPEID HIMQLHVKEP ERRGPQKRLA
360 370 380 390 400
AEVTKLVHGR EGLDSAKRCT QALYHSSIDA LEVMSDQELK ELFKEAPFSE
410 420 430 440 450
FFLDPGTSVL DTCRKANAIP DGPRGYRMIT EGGVSINHQQ VTNPESVLIV
460 470
GQHILKNGLS LLKIGKRNFY IIKWLQL
Length:477
Mass (Da):53,199
Last modified:July 19, 2004 - v2
Checksum:iC513B8FE1E7A09E4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1 – 4MAAP → MGA in AAD27714 (PubMed:10810093).Curated4
Sequence conflicti118R → A in AAD27714 (PubMed:10810093).Curated1
Sequence conflicti272P → T in AAD27714 (PubMed:10810093).Curated1
Sequence conflicti311D → E in AAD27714 (PubMed:10810093).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06864646G → D in MLASA2. 1 PublicationCorresponds to variant dbSNP:rs587777213EnsemblClinVar.1
Natural variantiVAR_06418852F → 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. 1 PublicationCorresponds to variant dbSNP:rs267607180EnsemblClinVar.1
Natural variantiVAR_034534191G → V1 PublicationCorresponds to variant dbSNP:rs11539445EnsemblClinVar.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF132939 mRNA Translation: AAD27714.1
AK024057 mRNA Translation: BAB14806.1
AC087588 Genomic DNA No translation available.
CH471116 Genomic DNA Translation: EAW88517.1
CH471116 Genomic DNA Translation: EAW88518.1
BC015625 mRNA Translation: AAH15625.1
CCDSiCCDS31770.1
RefSeqiNP_001035526.1, NM_001040436.2
UniGeneiHs.505231
Hs.706015

Genome annotation databases

EnsembliENST00000324868; ENSP00000320658; ENSG00000139131
GeneIDi51067
KEGGihsa:51067
UCSCiuc001rli.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiSYYM_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2Z4
Secondary accession number(s): D3DUW8, Q9H817
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: July 18, 2018
This is version 157 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. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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