SYYC_MOUSE
ID SYYC_MOUSE Reviewed; 528 AA.
AC Q91WQ3; Q3TEC8; Q3U9A1; Q3UTA7; Q8BVT2; Q8C183;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 158.
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; Synonyms=Yars;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Bone marrow, Brain cortex, Egg, Embryo, Skin, Testis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, and Liver;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK028785; BAC26120.1; -; mRNA.
DR EMBL; AK043837; BAC31674.1; -; mRNA.
DR EMBL; AK076634; BAC36424.1; -; mRNA.
DR EMBL; AK139579; BAE24073.1; -; mRNA.
DR EMBL; AK145356; BAE26384.1; -; mRNA.
DR EMBL; AK151880; BAE30766.1; -; mRNA.
DR EMBL; AK169708; BAE41320.1; -; mRNA.
DR EMBL; BC013552; AAH13552.1; -; mRNA.
DR EMBL; BC022143; AAH22143.1; -; mRNA.
DR EMBL; BC026615; AAH26615.1; -; mRNA.
DR CCDS; CCDS18685.2; -.
DR RefSeq; NP_598912.4; NM_134151.4.
DR AlphaFoldDB; Q91WQ3; -.
DR SMR; Q91WQ3; -.
DR BioGRID; 223230; 5.
DR DIP; DIP-61502N; -.
DR IntAct; Q91WQ3; 1.
DR STRING; 10090.ENSMUSP00000101669; -.
DR iPTMnet; Q91WQ3; -.
DR PhosphoSitePlus; Q91WQ3; -.
DR SwissPalm; Q91WQ3; -.
DR EPD; Q91WQ3; -.
DR jPOST; Q91WQ3; -.
DR MaxQB; Q91WQ3; -.
DR PaxDb; Q91WQ3; -.
DR PeptideAtlas; Q91WQ3; -.
DR PRIDE; Q91WQ3; -.
DR ProteomicsDB; 262990; -.
DR Antibodypedia; 17005; 257 antibodies from 26 providers.
DR DNASU; 107271; -.
DR Ensembl; ENSMUST00000106054; ENSMUSP00000101669; ENSMUSG00000028811.
DR GeneID; 107271; -.
DR KEGG; mmu:107271; -.
DR CTD; 107271; -.
DR MGI; MGI:2147627; Yars.
DR VEuPathDB; HostDB:ENSMUSG00000028811; -.
DR eggNOG; KOG2144; Eukaryota.
DR eggNOG; KOG2241; Eukaryota.
DR GeneTree; ENSGT00940000156949; -.
DR InParanoid; Q91WQ3; -.
DR OMA; YIGFEIS; -.
DR OrthoDB; 852081at2759; -.
DR BioGRID-ORCS; 107271; 26 hits in 75 CRISPR screens.
DR ChiTaRS; Yars; mouse.
DR PRO; PR:Q91WQ3; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q91WQ3; protein.
DR Bgee; ENSMUSG00000028811; Expressed in yolk sac and 258 other tissues.
DR ExpressionAtlas; Q91WQ3; baseline and differential.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006437; P:tyrosyl-tRNA aminoacylation; IEA:InterPro.
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 Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; RNA-binding; tRNA-binding.
FT CHAIN 1..528
FT /note="Tyrosine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000423286"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT CHAIN 2..528
FT /note="Tyrosine--tRNA ligase, cytoplasmic, N-terminally
FT processed"
FT /id="PRO_0000055674"
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:0000250"
FT BINDING 166
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT MOD_RES 2
FT /note="N-acetylglycine; in Tyrosine--tRNA ligase,
FT cytoplasmic, N-terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT MOD_RES 197
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT MOD_RES 206
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT MOD_RES 474
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT MOD_RES 482
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT MOD_RES 490
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT CONFLICT 11
FT /note="L -> M (in Ref. 1; BAC26120)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="E -> K (in Ref. 1; BAE24073)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="A -> S (in Ref. 1; BAC36424)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="E -> Q (in Ref. 1; BAC36424)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="L -> W (in Ref. 1; BAC36424)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="S -> R (in Ref. 1; BAC36424)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 528 AA; 59105 MW; 39D852D4C5701D0B CRC64;
MGDAPSPEEK LHLITRNLQE VLGEEKLKEI LKERELKVYW GTATTGKPHV AYFVPMSKIA
DFLKAGCEVT ILFADLHAYL DNMKAPWELL ELRTSYYENV IKAMLESIGV PLEKLKFIKG
TDYQLSKEYT LDVYRLSSVV TQHDAKKAGA EVVKQVEHPL LSGLLYPGLQ ALDEEYLKVD
AQFGGVDQRK IFTFAEKYLP ALGYSKRVHL MNPMVPGLTG SKMSSSEEES KIDLLDRKED
VKKKLKKAFC EPGNVENNGV LSFIKHVLFP LKSEFVILRD EKWGGNKTYT VYLELEKDFA
AEVVHPGDLK NSVEVALNKL LDPIREKFNT PALKKLASAA YPDPSKQKPP AKGPAKNSEP
EEVIPSRLDI RVGKILSVEK HPDADSLYVE KIDVGEAEPR TVVSGLVQFV PKEELQDRLV
VVLCNLKPQK MRGVDSQGML LCASVEGVSR QVEPLDPPAG SAPGERVFVQ GYEKGQPDEE
LKPKKKVFEK LQADFKISEE CIAQWKQTNF MTKLGFVSCK SLKGGNIS
