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Protein

Tyrosine--tRNA ligase, mitochondrial

Gene

YARS2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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).1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei77 – 771TyrosineBy similarity
Binding sitei221 – 2211TyrosineBy similarity
Binding sitei225 – 2251TyrosineBy similarity
Binding sitei228 – 2281TyrosineBy similarity
Binding sitei247 – 2471TyrosineBy similarity
Binding sitei284 – 2841ATPBy similarity

GO - Molecular functioni

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

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
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-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:6.1.1.1)
Alternative name(s):
Tyrosyl-tRNA synthetase
Short name:
TyrRS
Gene namesi
Name:YARS2
ORF Names:CGI-04
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:24249. YARS2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: GO_Central
  • mitochondrial matrix Source: Reactome
  • mitochondrion Source: UniProtKB
Complete GO annotation...

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti46 – 461G → D in MLASA2. 1 Publication
Corresponds to variant rs587777213 [ dbSNP | Ensembl ].
VAR_068646
Natural varianti52 – 521F → 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 Publication
Corresponds to variant rs267607180 [ dbSNP | Ensembl ].
VAR_064188

Keywords - Diseasei

Disease mutation

Organism-specific databases

MalaCardsiYARS2.
MIMi613561. phenotype.
Orphaneti2598. Mitochondrial myopathy and sideroblastic anemia.
PharmGKBiPA142670559.

Chemistry

DrugBankiDB00135. L-Tyrosine.

Polymorphism and mutation databases

BioMutaiYARS2.
DMDMi50401709.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1616MitochondrionSequence analysisAdd
BLAST
Chaini17 – 477461Tyrosine--tRNA ligase, mitochondrialPRO_0000035830Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei355 – 3551N6-acetyllysineCombined sources
Modified residuei367 – 3671N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9Y2Z4.
MaxQBiQ9Y2Z4.
PaxDbiQ9Y2Z4.
PeptideAtlasiQ9Y2Z4.
PRIDEiQ9Y2Z4.

PTM databases

iPTMnetiQ9Y2Z4.
PhosphoSiteiQ9Y2Z4.
SwissPalmiQ9Y2Z4.

Expressioni

Gene expression databases

BgeeiQ9Y2Z4.
CleanExiHS_YARS2.
ExpressionAtlasiQ9Y2Z4. baseline and differential.
GenevisibleiQ9Y2Z4. HS.

Organism-specific databases

HPAiHPA038721.
HPA057610.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

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

GO - Molecular functioni

  • protein homodimerization activity Source: BHF-UCL

Protein-protein interaction databases

BioGridi119258. 42 interactions.
DIPiDIP-29487N.
IntActiQ9Y2Z4. 11 interactions.
MINTiMINT-4832075.
STRINGi9606.ENSP00000320658.

Structurei

Secondary structure

1
477
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi38 – 458Combined sources
Beta strandi50 – 523Combined sources
Helixi61 – 644Combined sources
Beta strandi67 – 704Combined sources
Beta strandi75 – 806Combined sources
Beta strandi83 – 864Combined sources
Helixi89 – 10315Combined sources
Beta strandi107 – 1126Combined sources
Helixi116 – 1183Combined sources
Helixi134 – 15825Combined sources
Beta strandi168 – 1725Combined sources
Helixi174 – 1774Combined sources
Helixi182 – 1898Combined sources
Helixi190 – 1923Combined sources
Helixi195 – 2006Combined sources
Helixi202 – 2087Combined sources
Beta strandi210 – 2123Combined sources
Helixi216 – 23621Combined sources
Beta strandi240 – 2445Combined sources
Helixi245 – 2473Combined sources
Helixi248 – 26114Combined sources
Beta strandi267 – 2715Combined sources
Beta strandi291 – 2933Combined sources
Turni294 – 2963Combined sources
Helixi299 – 3079Combined sources
Helixi311 – 32111Combined sources
Helixi326 – 33813Combined sources
Helixi340 – 3423Combined sources
Helixi344 – 37229Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PIDX-ray2.20A/B32-375[»]
3ZXIX-ray2.75A/B32-375[»]
ProteinModelPortaliQ9Y2Z4.
SMRiQ9Y2Z4. Positions 37-474.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y2Z4.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi82 – 9110"HIGH" regionCurated
Motifi281 – 2855"KMSKS" regionCurated

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2623. Eukaryota.
COG0162. LUCA.
GeneTreeiENSGT00390000013709.
HOGENOMiHOG000242790.
HOVERGENiHBG056052.
InParanoidiQ9Y2Z4.
KOiK01866.
OMAiAINQETD.
OrthoDBiEOG73804M.
PhylomeDBiQ9Y2Z4.
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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 44MAAP → MGA in AAD27714 (PubMed:10810093).Curated
Sequence conflicti118 – 1181R → A in AAD27714 (PubMed:10810093).Curated
Sequence conflicti272 – 2721P → T in AAD27714 (PubMed:10810093).Curated
Sequence conflicti311 – 3111D → E in AAD27714 (PubMed:10810093).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti46 – 461G → D in MLASA2. 1 Publication
Corresponds to variant rs587777213 [ dbSNP | Ensembl ].
VAR_068646
Natural varianti52 – 521F → 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 Publication
Corresponds to variant rs267607180 [ dbSNP | Ensembl ].
VAR_064188
Natural varianti191 – 1911G → V.1 Publication
Corresponds to variant rs11539445 [ dbSNP | Ensembl ].
VAR_034534

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

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PIDX-ray2.20A/B32-375[»]
3ZXIX-ray2.75A/B32-375[»]
ProteinModelPortaliQ9Y2Z4.
SMRiQ9Y2Z4. Positions 37-474.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119258. 42 interactions.
DIPiDIP-29487N.
IntActiQ9Y2Z4. 11 interactions.
MINTiMINT-4832075.
STRINGi9606.ENSP00000320658.

Chemistry

DrugBankiDB00135. L-Tyrosine.

PTM databases

iPTMnetiQ9Y2Z4.
PhosphoSiteiQ9Y2Z4.
SwissPalmiQ9Y2Z4.

Polymorphism and mutation databases

BioMutaiYARS2.
DMDMi50401709.

Proteomic databases

EPDiQ9Y2Z4.
MaxQBiQ9Y2Z4.
PaxDbiQ9Y2Z4.
PeptideAtlasiQ9Y2Z4.
PRIDEiQ9Y2Z4.

Protocols and materials databases

DNASUi51067.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi51067.
GeneCardsiYARS2.
HGNCiHGNC:24249. YARS2.
HPAiHPA038721.
HPA057610.
MalaCardsiYARS2.
MIMi610957. gene.
613561. phenotype.
neXtProtiNX_Q9Y2Z4.
Orphaneti2598. Mitochondrial myopathy and sideroblastic anemia.
PharmGKBiPA142670559.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2623. Eukaryota.
COG0162. LUCA.
GeneTreeiENSGT00390000013709.
HOGENOMiHOG000242790.
HOVERGENiHBG056052.
InParanoidiQ9Y2Z4.
KOiK01866.
OMAiAINQETD.
OrthoDBiEOG73804M.
PhylomeDBiQ9Y2Z4.
TreeFamiTF105974.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiYARS2. human.
EvolutionaryTraceiQ9Y2Z4.
GenomeRNAii51067.
PROiQ9Y2Z4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y2Z4.
CleanExiHS_YARS2.
ExpressionAtlasiQ9Y2Z4. baseline and differential.
GenevisibleiQ9Y2Z4. HS.

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

« Hide 'large scale' publications
  1. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
    Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
    Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-191.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Eye.
  6. "Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS."
    Bonnefond L., Fender A., Rudinger-Thirion J., Giege R., Florentz C., Sissler M.
    Biochemistry 44:4805-4816(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
  7. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-355, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Mutation of the mitochondrial tyrosyl-tRNA synthetase gene, YARS2, causes myopathy, lactic acidosis, and sideroblastic anemia--MLASA syndrome."
    Riley L.G., Cooper S., Hickey P., Rudinger-Thirion J., McKenzie M., Compton A., Lim S.C., Thorburn D., Ryan M.T., Giege R., Bahlo M., Christodoulou J.
    Am. J. Hum. Genet. 87:52-59(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MLASA2 LEU-52, CHARACTERIZATION OF VARIANT MLASA2 LEU-52.
  11. "A novel mutation in YARS2 causes myopathy with lactic acidosis and sideroblastic anemia."
    Sasarman F., Nishimura T., Thiffault I., Shoubridge E.A.
    Hum. Mutat. 33:1201-1206(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MLASA2 ASP-46.

Entry informationi

Entry nameiSYYM_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2Z4
Secondary accession number(s): D3DUW8, Q9H817
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: July 6, 2016
This is version 138 of the entry and version 2 of the sequence. [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

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.