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Protein

Tyrosine--tRNA ligase, mitochondrial

Gene

Yars2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei279 – 2791ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine--tRNA ligase, mitochondrial (EC:6.1.1.1)
Alternative name(s):
Tyrosyl-tRNA synthetase
Short name:
TyrRS
Gene namesi
Name:Yars2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1917370. Yars2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 472Tyrosine--tRNA ligase, mitochondrialPRO_0000035831
Transit peptidei1 – ?MitochondrionSequence analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei350 – 3501N6-acetyllysineBy similarity
Modified residuei362 – 3621N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ8BYL4.
MaxQBiQ8BYL4.
PaxDbiQ8BYL4.
PRIDEiQ8BYL4.

PTM databases

iPTMnetiQ8BYL4.
PhosphoSiteiQ8BYL4.

Expressioni

Gene expression databases

BgeeiQ8BYL4.
CleanExiMM_YARS2.
ExpressionAtlasiQ8BYL4. baseline and differential.
GenevisibleiQ8BYL4. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000055277.

Structurei

3D structure databases

ProteinModelPortaliQ8BYL4.
SMRiQ8BYL4. Positions 31-469.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi77 – 8610"HIGH" region
Motifi276 – 2805"KMSKS" region

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2623. Eukaryota.
COG0162. LUCA.
GeneTreeiENSGT00390000013709.
HOGENOMiHOG000242790.
HOVERGENiHBG056052.
InParanoidiQ8BYL4.
KOiK01866.
OMAiAINQETD.
OrthoDBiEOG73804M.
PhylomeDBiQ8BYL4.
TreeFamiTF105974.

Family and domain databases

Gene3Di3.10.290.10. 1 hit.
3.40.50.620. 1 hit.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002942. S4_RNA-bd.
IPR002307. Tyr-tRNA-ligase.
IPR024088. Tyr-tRNA-ligase_bac-type.
[Graphical view]
PANTHERiPTHR11766. PTHR11766. 1 hit.
PfamiPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PRINTSiPR01040. TRNASYNTHTYR.
TIGRFAMsiTIGR00234. tyrS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8BYL4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPMLRRLC RVPQSLVWLR GSRAVRPGAR GMLVAPRARG LFKEFFPESG
60 70 80 90 100
TKTELPELFD RRRAGSSPQT VYCGFDPTGD SLHVGHLLTL LGLFHFQRAG
110 120 130 140 150
HNVIALVGGS TALLGDPSGR TKGREALSAE CVRANAHALR RGLEALAANH
160 170 180 190 200
ARLFADGRPW GSFTVLDNAA WFQEQHLVDF LATVGGHFRM GTLLSRLSVQ
210 220 230 240 250
SRLKSPEGMS LAEFFYQVLQ AYDFYYLFQH YGCRVQLGGS DQLGNIMSGY
260 270 280 290 300
EFIHKLTGED VFGITVPLIT STTGAKLGKS AGNAVWLNRE KTSPFELYQF
310 320 330 340 350
FVRQQDDSVE RYLKLFTFLP LPEIDHIMQL HVKEPEKRVA QKRLAAEVTK
360 370 380 390 400
LVHGQEGLDS AKRCTQALYH SSIEALEVMS DQELKELFKE ASFSELVLDP
410 420 430 440 450
GTSVIDTCRK ANAIPDGPRG YRMITEGGVS INHRQVTNPE SVLVIGQHIL
460 470
KNGLSLLKIG KRNFYIIKWL QL
Length:472
Mass (Da):52,597
Last modified:July 19, 2004 - v2
Checksum:i7775B040E3E8A2F1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC060295 mRNA. Translation: AAH60295.1.
AK039123 mRNA. Translation: BAC30245.1.
CCDSiCCDS27983.1.
RefSeqiNP_937889.1. NM_198246.2.
UniGeneiMm.37486.

Genome annotation databases

EnsembliENSMUST00000059955; ENSMUSP00000055277; ENSMUSG00000022792.
GeneIDi70120.
KEGGimmu:70120.
UCSCiuc007yie.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC060295 mRNA. Translation: AAH60295.1.
AK039123 mRNA. Translation: BAC30245.1.
CCDSiCCDS27983.1.
RefSeqiNP_937889.1. NM_198246.2.
UniGeneiMm.37486.

3D structure databases

ProteinModelPortaliQ8BYL4.
SMRiQ8BYL4. Positions 31-469.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000055277.

PTM databases

iPTMnetiQ8BYL4.
PhosphoSiteiQ8BYL4.

Proteomic databases

EPDiQ8BYL4.
MaxQBiQ8BYL4.
PaxDbiQ8BYL4.
PRIDEiQ8BYL4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000059955; ENSMUSP00000055277; ENSMUSG00000022792.
GeneIDi70120.
KEGGimmu:70120.
UCSCiuc007yie.2. mouse.

Organism-specific databases

CTDi51067.
MGIiMGI:1917370. Yars2.

Phylogenomic databases

eggNOGiKOG2623. Eukaryota.
COG0162. LUCA.
GeneTreeiENSGT00390000013709.
HOGENOMiHOG000242790.
HOVERGENiHBG056052.
InParanoidiQ8BYL4.
KOiK01866.
OMAiAINQETD.
OrthoDBiEOG73804M.
PhylomeDBiQ8BYL4.
TreeFamiTF105974.

Miscellaneous databases

PROiQ8BYL4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BYL4.
CleanExiMM_YARS2.
ExpressionAtlasiQ8BYL4. baseline and differential.
GenevisibleiQ8BYL4. MM.

Family and domain databases

Gene3Di3.10.290.10. 1 hit.
3.40.50.620. 1 hit.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002942. S4_RNA-bd.
IPR002307. Tyr-tRNA-ligase.
IPR024088. Tyr-tRNA-ligase_bac-type.
[Graphical view]
PANTHERiPTHR11766. PTHR11766. 1 hit.
PfamiPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PRINTSiPR01040. TRNASYNTHTYR.
TIGRFAMsiTIGR00234. tyrS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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].
    Tissue: Jaw and Limb.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 70-472.
    Strain: C57BL/6J.
    Tissue: Hypothalamus.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Spleen and Testis.
  4. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-362, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSYYM_MOUSE
AccessioniPrimary (citable) accession number: Q8BYL4
Secondary accession number(s): Q6PAH7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: June 8, 2016
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. 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.