SYYC_HUMAN
ID SYYC_HUMAN Reviewed; 528 AA.
AC P54577; B3KWK4; D3DPQ4; O43276; Q53EN1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 218.
DE RecName: Full=Tyrosine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.1;
DE AltName: Full=Tyrosyl-tRNA synthetase;
DE Short=TyrRS;
DE Contains:
DE RecName: Full=Tyrosine--tRNA ligase, cytoplasmic, N-terminally processed;
GN Name=YARS1 {ECO:0000312|HGNC:HGNC:12840}; Synonyms=YARS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8552597; DOI=10.1073/pnas.93.1.166;
RA Ribas de Pouplana L., Frugier M., Quinn C.L., Schimmel P.;
RT "Evidence that two present-day components needed for the genetic code
RT appeared after nucleated cells separated from eubacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:166-170(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9162081; DOI=10.1074/jbc.272.22.14420;
RA Kleeman T.A., Wei D., Simpson K.L., First E.A.;
RT "Human tyrosyl-tRNA synthetase shares amino acid sequence homology with a
RT putative cytokine.";
RL J. Biol. Chem. 272:14420-14425(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 2-16.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP PROTEIN SEQUENCE OF 2-16, ACETYLATION AT GLY-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (OCT-2004) to UniProtKB.
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND GLY-2, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-197; LYS-206; LYS-474; LYS-482
RP AND LYS-490, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205 AND SER-386, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.18 ANGSTROMS) OF 1-342, AND SUBUNIT.
RX PubMed=12427973; DOI=10.1073/pnas.242611799;
RA Yang X.-L., Skene R.J., McRee D.E., Schimmel P.;
RT "Crystal structure of a human aminoacyl-tRNA synthetase cytokine.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:15369-15374(2002).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-364 IN COMPLEX WITH TYROSINE.
RX PubMed=14671330; DOI=10.1073/pnas.2136794100;
RA Yang X.-L., Otero F.J., Skene R.J., McRee D.E., Schimmel P.,
RA Ribas de Pouplana L.;
RT "Crystal structures that suggest late development of genetic code
RT components for differentiating aromatic side chains.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:15376-15380(2003).
RN [17]
RP SUBCELLULAR LOCATION, VARIANTS CMTDIC 153-VAL--VAL-156 DEL; ARG-41 AND
RP LYS-196, AND CHARACTERIZATION OF VARIANTS CMTDIC ARG-41 AND LYS-196.
RX PubMed=16429158; DOI=10.1038/ng1727;
RA Jordanova A., Irobi J., Thomas F.P., Van Dijck P., Meerschaert K.,
RA Dewil M., Dierick I., Jacobs A., De Vriendt E., Guergueltcheva V.,
RA Rao C.V., Tournev I., Gondim F.A.A., D'Hooghe M., Van Gerwen V.,
RA Callaerts P., Van Den Bosch L., Timmermans J.-P., Robberecht W.,
RA Gettemans J., Thevelein J.M., De Jonghe P., Kremensky I., Timmerman V.;
RT "Disrupted function and axonal distribution of mutant tyrosyl-tRNA
RT synthetase in dominant intermediate Charcot-Marie-Tooth neuropathy.";
RL Nat. Genet. 38:197-202(2006).
RN [18]
RP VARIANT LYS-274.
RX PubMed=24627108; DOI=10.1007/s00415-014-7289-8;
RA Schabhuettl M., Wieland T., Senderek J., Baets J., Timmerman V.,
RA De Jonghe P., Reilly M.M., Stieglbauer K., Laich E., Windhager R., Erwa W.,
RA Trajanoski S., Strom T.M., Auer-Grumbach M.;
RT "Whole-exome sequencing in patients with inherited neuropathies: outcome
RT and challenges.";
RL J. Neurol. 261:970-982(2014).
RN [19]
RP VARIANTS IMNEPD2 LEU-213 AND ARG-525, AND INVOLVEMENT IN IMNEPD2.
RX PubMed=27633801; DOI=10.1002/ajmg.a.37973;
RG FORGE Canada Consortium, Care4Rare Canada Consortium;
RA Nowaczyk M.J., Huang L., Tarnopolsky M., Schwartzentruber J., Majewski J.,
RA Bulman D.E., Hartley T., Boycott K.M.;
RT "A novel multisystem disease associated with recessive mutations in the
RT tyrosyl-tRNA synthetase (YARS) gene.";
RL Am. J. Med. Genet. A 173:126-134(2017).
RN [20]
RP VARIANT IMNEPD2 SER-269, AND INVOLVEMENT IN IMNEPD2.
RX PubMed=29232904; DOI=10.3390/genes8120381;
RG University of Washington Center for Mendelian Genomics;
RA Tracewska-Siemiatkowska A., Haer-Wigman L., Bosch D.G.M., Nickerson D.,
RA Bamshad M.J., van de Vorst M., Rendtorff N.D., Moeller C., Kjellstroem U.,
RA Andreasson S., Cremers F.P.M., Tranebjaerg L.;
RT "An Expanded Multi-Organ Disease Phenotype Associated with Mutations in
RT YARS.";
RL Genes (Basel) 8:0-0(2017).
RN [21]
RP VARIANT IMNEPD2 THR-167, CHARACTERIZATION OF VARIANT IMNEPD2 THR-167,
RP INVOLVEMENT IN IMNEPD2, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=30304524; DOI=10.1093/hmg/ddy344;
RA Williams K.B., Brigatti K.W., Puffenberger E.G., Gonzaga-Jauregui C.,
RA Griffin L.B., Martinez E.D., Wenger O.K., Yoder M.A., Kandula V.V.R.,
RA Fox M.D., Demczko M.M., Poskitt L., Furuya K.N., Reid J.G., Overton J.D.,
RA Baras A., Miles L., Radhakrishnan K., Carson V.J., Antonellis A.,
RA Jinks R.N., Strauss K.A.;
RT "Homozygosity for a mutation affecting the catalytic domain of tyrosyl-tRNA
RT synthetase (YARS) causes multisystem disease.";
RL Hum. Mol. Genet. 28:525-538(2019).
CC -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-
CC step reaction: tyrosine is first activated by ATP to form Tyr-AMP and
CC then transferred to the acceptor end of tRNA(Tyr). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-
CC tyrosyl-tRNA(Tyr); Xref=Rhea:RHEA:10220, Rhea:RHEA-COMP:9706,
CC Rhea:RHEA-COMP:9707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58315, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78536, ChEBI:CHEBI:456215; EC=6.1.1.1;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12427973,
CC ECO:0000269|PubMed:14671330, ECO:0000269|PubMed:30304524}.
CC -!- INTERACTION:
CC P54577; Q86SG2: ANKRD23; NbExp=3; IntAct=EBI-1048893, EBI-5661893;
CC P54577; Q96DX5-3: ASB9; NbExp=3; IntAct=EBI-1048893, EBI-25843552;
CC P54577; Q8WXF7: ATL1; NbExp=3; IntAct=EBI-1048893, EBI-2410266;
CC P54577; Q14781-2: CBX2; NbExp=3; IntAct=EBI-1048893, EBI-11974585;
CC P54577; Q5M9N0-2: CCDC158; NbExp=3; IntAct=EBI-1048893, EBI-21796846;
CC P54577; Q8NHQ1-3: CEP70; NbExp=3; IntAct=EBI-1048893, EBI-11526150;
CC P54577; Q9UNS2: COPS3; NbExp=3; IntAct=EBI-1048893, EBI-350590;
CC P54577; Q9H3K2: GHITM; NbExp=3; IntAct=EBI-1048893, EBI-2868909;
CC P54577; P37235: HPCAL1; NbExp=3; IntAct=EBI-1048893, EBI-749311;
CC P54577; Q9UBF1: MAGEC2; NbExp=3; IntAct=EBI-1048893, EBI-5651487;
CC P54577; Q8N7B6-2: PACRGL; NbExp=3; IntAct=EBI-1048893, EBI-10694433;
CC P54577; P09874: PARP1; NbExp=5; IntAct=EBI-1048893, EBI-355676;
CC P54577; O75925: PIAS1; NbExp=3; IntAct=EBI-1048893, EBI-629434;
CC P54577; Q6P1M0-2: SLC27A4; NbExp=3; IntAct=EBI-1048893, EBI-12898981;
CC P54577; Q8IYM2: SLFN12; NbExp=3; IntAct=EBI-1048893, EBI-2822550;
CC P54577; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-1048893, EBI-11959123;
CC P54577; Q8IYN2: TCEAL8; NbExp=3; IntAct=EBI-1048893, EBI-2116184;
CC P54577; P17024: ZNF20; NbExp=3; IntAct=EBI-1048893, EBI-717634;
CC P54577; Q86V28; NbExp=3; IntAct=EBI-1048893, EBI-10259496;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16429158,
CC ECO:0000269|PubMed:30304524}.
CC -!- DISEASE: Charcot-Marie-Tooth disease, dominant, intermediate type, C
CC (CMTDIC) [MIM:608323]: A form of Charcot-Marie-Tooth disease, a
CC disorder of the peripheral nervous system, characterized by progressive
CC weakness and atrophy, initially of the peroneal muscles and later of
CC the distal muscles of the arms. The dominant intermediate type C is
CC characterized by clinical and pathologic features intermediate between
CC demyelinating and axonal peripheral neuropathies, and motor median
CC nerve conduction velocities ranging from 25 to 45 m/sec.
CC {ECO:0000269|PubMed:16429158}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Neurologic, endocrine, and pancreatic disease, multisystem,
CC infantile-onset 2 (IMNEPD2) [MIM:619418]: An autosomal recessive
CC disorder with variable clinical manifestations and severity. Main
CC features include cholestatic hepatitis, poor feeding, poor overall
CC growth, and hypoglycemia apparent from infancy. Most patients have
CC variable global developmental delay, sensorineural deafness, retinal
CC abnormalities with visual defects, and hypotonia. Some patients have
CC endocrine abnormalities. Brain imaging often shows dysmyelination, thin
CC corpus callosum, cerebral atrophy, and white matter abnormalities.
CC Death in early childhood may occur. {ECO:0000269|PubMed:27633801,
CC ECO:0000269|PubMed:29232904, ECO:0000269|PubMed:30304524}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB39406.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U40714; AAB39406.1; ALT_FRAME; mRNA.
DR EMBL; U89436; AAB88409.1; -; mRNA.
DR EMBL; AK125213; BAG54166.1; -; mRNA.
DR EMBL; AK223608; BAD97328.1; -; mRNA.
DR EMBL; CH471059; EAX07506.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07507.1; -; Genomic_DNA.
DR EMBL; BC001933; AAH01933.1; -; mRNA.
DR EMBL; BC004151; AAH04151.1; -; mRNA.
DR EMBL; BC016689; AAH16689.1; -; mRNA.
DR CCDS; CCDS368.1; -.
DR RefSeq; NP_003671.1; NM_003680.3.
DR PDB; 1N3L; X-ray; 1.18 A; A=1-364.
DR PDB; 1NTG; X-ray; 2.21 A; A/B/C/D=359-528.
DR PDB; 1Q11; X-ray; 1.60 A; A=1-364.
DR PDB; 4Q93; X-ray; 2.10 A; A=1-364.
DR PDB; 4QBT; X-ray; 2.10 A; A=1-364.
DR PDB; 5THH; X-ray; 1.96 A; A=4-342.
DR PDB; 5THL; X-ray; 1.60 A; A=1-364.
DR PDBsum; 1N3L; -.
DR PDBsum; 1NTG; -.
DR PDBsum; 1Q11; -.
DR PDBsum; 4Q93; -.
DR PDBsum; 4QBT; -.
DR PDBsum; 5THH; -.
DR PDBsum; 5THL; -.
DR AlphaFoldDB; P54577; -.
DR SMR; P54577; -.
DR BioGRID; 114134; 130.
DR DIP; DIP-50415N; -.
DR IntAct; P54577; 43.
DR MINT; P54577; -.
DR STRING; 9606.ENSP00000362576; -.
DR BindingDB; P54577; -.
DR ChEMBL; CHEMBL3179; -.
DR DrugBank; DB08617; 4-(2,2,2-TRIFLUOROETHYL)-L-PHENYLALANINE.
DR DrugBank; DB01766; Beta-(2-Naphthyl)-Alanine.
DR DrugBank; DB07205; N6-ISOPENTENYL-ADENOSINE-5'-MONOPHOSPHATE.
DR DrugBank; DB08371; p-Benzoyl-L-phenylalanine.
DR DrugBank; DB02709; Resveratrol.
DR DrugBank; DB03978; Tyrosinal.
DR DrugBank; DB00135; Tyrosine.
DR DrugCentral; P54577; -.
DR CarbonylDB; P54577; -.
DR GlyGen; P54577; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P54577; -.
DR MetOSite; P54577; -.
DR PhosphoSitePlus; P54577; -.
DR SwissPalm; P54577; -.
DR BioMuta; YARS; -.
DR DMDM; 13638438; -.
DR REPRODUCTION-2DPAGE; IPI00007074; -.
DR CPTAC; CPTAC-299; -.
DR CPTAC; CPTAC-300; -.
DR EPD; P54577; -.
DR jPOST; P54577; -.
DR MassIVE; P54577; -.
DR MaxQB; P54577; -.
DR PaxDb; P54577; -.
DR PeptideAtlas; P54577; -.
DR PRIDE; P54577; -.
DR ProteomicsDB; 56686; -.
DR ABCD; P54577; 2 sequenced antibodies.
DR Antibodypedia; 17005; 257 antibodies from 26 providers.
DR DNASU; 8565; -.
DR Ensembl; ENST00000373477.9; ENSP00000362576.4; ENSG00000134684.12.
DR GeneID; 8565; -.
DR KEGG; hsa:8565; -.
DR MANE-Select; ENST00000373477.9; ENSP00000362576.4; NM_003680.4; NP_003671.1.
DR UCSC; uc001bvy.2; human.
DR CTD; 8565; -.
DR DisGeNET; 8565; -.
DR GeneCards; YARS1; -.
DR GeneReviews; YARS1; -.
DR HGNC; HGNC:12840; YARS1.
DR HPA; ENSG00000134684; Low tissue specificity.
DR MalaCards; YARS1; -.
DR MIM; 603623; gene.
DR MIM; 608323; phenotype.
DR MIM; 619418; phenotype.
DR neXtProt; NX_P54577; -.
DR OpenTargets; ENSG00000134684; -.
DR Orphanet; 100045; Autosomal dominant intermediate Charcot-Marie-Tooth disease type C.
DR PharmGKB; PA37431; -.
DR VEuPathDB; HostDB:ENSG00000134684; -.
DR eggNOG; KOG2144; Eukaryota.
DR eggNOG; KOG2241; Eukaryota.
DR GeneTree; ENSGT00940000156949; -.
DR HOGENOM; CLU_035267_3_0_1; -.
DR InParanoid; P54577; -.
DR OMA; YIGFEIS; -.
DR OrthoDB; 852081at2759; -.
DR PhylomeDB; P54577; -.
DR TreeFam; TF300898; -.
DR BRENDA; 6.1.1.1; 2681.
DR PathwayCommons; P54577; -.
DR Reactome; R-HSA-379716; Cytosolic tRNA aminoacylation.
DR SignaLink; P54577; -.
DR BioGRID-ORCS; 8565; 811 hits in 1061 CRISPR screens.
DR ChiTaRS; YARS; human.
DR EvolutionaryTrace; P54577; -.
DR GeneWiki; YARS; -.
DR GenomeRNAi; 8565; -.
DR Pharos; P54577; Tchem.
DR PRO; PR:P54577; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P54577; protein.
DR Bgee; ENSG00000134684; Expressed in right adrenal gland and 208 other tissues.
DR ExpressionAtlas; P54577; baseline and differential.
DR Genevisible; P54577; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005153; F:interleukin-8 receptor binding; TAS:ProtInc.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; TAS:ProtInc.
DR CDD; cd00805; TyrRS_core; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR002547; tRNA-bd_dom.
DR InterPro; IPR002307; Tyr-tRNA-ligase.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR Pfam; PF01588; tRNA_bind; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00234; tyrS; 1.
DR PROSITE; PS50886; TRBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding;
KW Charcot-Marie-Tooth disease; Cytoplasm; Direct protein sequencing;
KW Disease variant; Ligase; Neurodegeneration; Neuropathy; Nucleotide-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; RNA-binding;
KW tRNA-binding.
FT CHAIN 1..528
FT /note="Tyrosine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000423285"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.8,
FT ECO:0007744|PubMed:19413330"
FT CHAIN 2..528
FT /note="Tyrosine--tRNA ligase, cytoplasmic, N-terminally
FT processed"
FT /id="PRO_0000055673"
FT DOMAIN 364..468
FT /note="tRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00209"
FT REGION 339..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 44..52
FT /note="'HIGH' region"
FT MOTIF 222..226
FT /note="'KMSKS' region"
FT BINDING 39
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000269|PubMed:14671330,
FT ECO:0007744|PDB:4QBT"
FT BINDING 166
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000269|PubMed:14671330,
FT ECO:0007744|PDB:4QBT"
FT BINDING 170
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000269|PubMed:14671330,
FT ECO:0007744|PDB:4QBT"
FT BINDING 173
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000269|PubMed:14671330,
FT ECO:0007744|PDB:4QBT"
FT BINDING 188
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000269|PubMed:14671330,
FT ECO:0007744|PDB:4QBT"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 2
FT /note="N-acetylglycine; in Tyrosine--tRNA ligase,
FT cytoplasmic, N-terminally processed"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330"
FT MOD_RES 197
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 206
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 474
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 482
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 490
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 41
FT /note="G -> R (in CMTDIC; partial loss of activity;
FT dbSNP:rs121908833)"
FT /evidence="ECO:0000269|PubMed:16429158"
FT /id="VAR_026681"
FT VARIANT 153..156
FT /note="Missing (in CMTDIC)"
FT /evidence="ECO:0000269|PubMed:16429158"
FT /id="VAR_026682"
FT VARIANT 167
FT /note="P -> T (in IMNEPD2; hypomorphic variant in yeast
FT complementation assays; decreased homodimerization; does
FT not affect localization to the cytoplasm)"
FT /evidence="ECO:0000269|PubMed:30304524"
FT /id="VAR_086001"
FT VARIANT 170
FT /note="Q -> H (in dbSNP:rs2128600)"
FT /id="VAR_026683"
FT VARIANT 196
FT /note="E -> K (in CMTDIC; partial loss of activity;
FT dbSNP:rs121908834)"
FT /evidence="ECO:0000269|PubMed:16429158"
FT /id="VAR_026684"
FT VARIANT 213
FT /note="P -> L (in IMNEPD2; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:27633801"
FT /id="VAR_086002"
FT VARIANT 269
FT /note="F -> S (in IMNEPD2; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:29232904"
FT /id="VAR_086003"
FT VARIANT 274
FT /note="E -> K (found in a patient with hereditary motor and
FT sensory neuropathy; unknown pathological significance;
FT dbSNP:rs758897498)"
FT /evidence="ECO:0000269|PubMed:24627108"
FT /id="VAR_073292"
FT VARIANT 525
FT /note="G -> R (in IMNEPD2; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:27633801"
FT /id="VAR_086004"
FT CONFLICT 143
FT /note="H -> R (in Ref. 4; BAD97328)"
FT /evidence="ECO:0000305"
FT HELIX 7..15
FT /evidence="ECO:0007829|PDB:1N3L"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:1N3L"
FT HELIX 24..31
FT /evidence="ECO:0007829|PDB:1N3L"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:1N3L"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:1N3L"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:1N3L"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:1N3L"
FT HELIX 75..80
FT /evidence="ECO:0007829|PDB:1N3L"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:1N3L"
FT HELIX 87..108
FT /evidence="ECO:0007829|PDB:1N3L"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:1N3L"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1N3L"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:1N3L"
FT HELIX 127..137
FT /evidence="ECO:0007829|PDB:1N3L"
FT HELIX 142..148
FT /evidence="ECO:0007829|PDB:1N3L"
FT TURN 149..152
FT /evidence="ECO:0007829|PDB:1N3L"
FT HELIX 161..176
FT /evidence="ECO:0007829|PDB:1N3L"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:1N3L"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:1N3L"
FT HELIX 189..198
FT /evidence="ECO:0007829|PDB:1N3L"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:1N3L"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:1N3L"
FT HELIX 238..246
FT /evidence="ECO:0007829|PDB:1N3L"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:1Q11"
FT HELIX 259..266
FT /evidence="ECO:0007829|PDB:1N3L"
FT TURN 267..273
FT /evidence="ECO:0007829|PDB:1N3L"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:1N3L"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:1N3L"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:1N3L"
FT HELIX 292..300
FT /evidence="ECO:0007829|PDB:1N3L"
FT HELIX 306..327
FT /evidence="ECO:0007829|PDB:1N3L"
FT HELIX 331..340
FT /evidence="ECO:0007829|PDB:1N3L"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:1NTG"
FT STRAND 370..380
FT /evidence="ECO:0007829|PDB:1NTG"
FT STRAND 388..393
FT /evidence="ECO:0007829|PDB:1NTG"
FT STRAND 395..398
FT /evidence="ECO:0007829|PDB:1NTG"
FT STRAND 400..405
FT /evidence="ECO:0007829|PDB:1NTG"
FT TURN 407..409
FT /evidence="ECO:0007829|PDB:1NTG"
FT HELIX 412..414
FT /evidence="ECO:0007829|PDB:1NTG"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:1NTG"
FT STRAND 419..423
FT /evidence="ECO:0007829|PDB:1NTG"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:1NTG"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:1NTG"
FT STRAND 442..454
FT /evidence="ECO:0007829|PDB:1NTG"
FT STRAND 466..469
FT /evidence="ECO:0007829|PDB:1NTG"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:1NTG"
FT HELIX 483..485
FT /evidence="ECO:0007829|PDB:1NTG"
FT HELIX 487..492
FT /evidence="ECO:0007829|PDB:1NTG"
FT STRAND 495..497
FT /evidence="ECO:0007829|PDB:1NTG"
FT STRAND 501..505
FT /evidence="ECO:0007829|PDB:1NTG"
FT STRAND 508..512
FT /evidence="ECO:0007829|PDB:1NTG"
FT STRAND 526..528
FT /evidence="ECO:0007829|PDB:1NTG"
SQ SEQUENCE 528 AA; 59143 MW; 00C7E88843905780 CRC64;
MGDAPSPEEK LHLITRNLQE VLGEEKLKEI LKERELKIYW GTATTGKPHV AYFVPMSKIA
DFLKAGCEVT ILFADLHAYL DNMKAPWELL ELRVSYYENV IKAMLESIGV PLEKLKFIKG
TDYQLSKEYT LDVYRLSSVV TQHDSKKAGA EVVKQVEHPL LSGLLYPGLQ ALDEEYLKVD
AQFGGIDQRK IFTFAEKYLP ALGYSKRVHL MNPMVPGLTG SKMSSSEEES KIDLLDRKED
VKKKLKKAFC EPGNVENNGV LSFIKHVLFP LKSEFVILRD EKWGGNKTYT AYVDLEKDFA
AEVVHPGDLK NSVEVALNKL LDPIREKFNT PALKKLASAA YPDPSKQKPM AKGPAKNSEP
EEVIPSRLDI RVGKIITVEK HPDADSLYVE KIDVGEAEPR TVVSGLVQFV PKEELQDRLV
VVLCNLKPQK MRGVESQGML LCASIEGINR QVEPLDPPAG SAPGEHVFVK GYEKGQPDEE
LKPKKKVFEK LQADFKISEE CIAQWKQTNF MTKLGSISCK SLKGGNIS
