ID SYC_HUMAN STANDARD; PRT; 748 AA. AC P49589; Q9HD24; Q9HD25; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 31-JAN-2002, sequence version 3. DT 07-FEB-2006, entry version 46. DE Cysteinyl-tRNA synthetase (EC 6.1.1.16) (Cysteine--tRNA ligase) DE (CysRS). GN Name=CARS; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Brain; RX MEDLINE=95078457; PubMed=7987009; RA Cruzen M.E., Arfin S.M.; RT "Nucleotide and deduced amino acid sequence of human cysteinyl-tRNA RT synthetase."; RL DNA Seq. 4:243-248(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RX MEDLINE=21245111; PubMed=11347887; DOI=10.1515/BC.2001.049; RA Davidson E., Caffarella J., Vitseva O., Hou Y.M., King M.P.; RT "Isolation of two cDNAs encoding functional human cytoplasmic RT cysteinyl-tRNA synthetase."; RL Biol. Chem. 382:399-406(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [4] RP PHOSPHORYLATION SITE TYR-260, AND MASS SPECTROMETRY. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer RT cells."; RL Nat. Biotechnol. 23:94-101(2005). CC -!- CATALYTIC ACTIVITY: ATP + L-cysteine + tRNA(Cys) = AMP + CC diphosphate + L-cysteinyl-tRNA(Cys). CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P49589-1; Sequence=Displayed; CC Name=2; CC IsoId=P49589-2; Sequence=VSP_006312; CC Note=Found in 20% of the mRNAs; CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. CC -!- CAUTION: Ref.1 sequence differs from that shown due to a CC frameshift in position 619. 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; L06845; AAA73901.1; ALT_FRAME; mRNA. DR EMBL; AF288206; AAG00578.1; -; mRNA. DR EMBL; AF288207; AAG00579.1; -; mRNA. DR EMBL; BC002880; AAH02880.1; -; mRNA. DR HSSP; P21888; 1LI5. DR Ensembl; ENSG00000110619; Homo sapiens. DR H-InvDB; HIX0009371; -. DR HGNC; HGNC:1493; CARS. DR MIM; 123859; gene. DR GO; GO:0005737; C:cytoplasm; TAS. DR GO; GO:0005625; C:soluble fraction; TAS. DR GO; GO:0000049; F:tRNA binding; TAS. DR InterPro; IPR002308; Cys_tRNA-synt_1a. DR InterPro; IPR001412; tRNA-synt_I. DR PANTHER; PTHR10890; Cys_tRNA-synt_1a; 2. DR Pfam; PF01406; tRNA-synt_1e; 1. DR PRINTS; PR00983; TRNASYNTHCYS. DR TIGRFAMs; TIGR00435; cysS; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; FALSE_NEG. KW Alternative splicing; Aminoacyl-tRNA synthetase; ATP-binding; Ligase; KW Metal-binding; Nucleotide-binding; Phosphorylation; KW Protein biosynthesis; Zinc. FT CHAIN 1 748 Cysteinyl-tRNA synthetase. FT /FTId=PRO_0000159550. FT MOTIF 57 67 "HIGH" region. FT MOTIF 406 410 "KMSKS" region. FT METAL 55 55 Zinc (By similarity). FT METAL 348 348 Zinc (By similarity). FT METAL 373 373 Zinc (By similarity). FT METAL 377 377 Zinc (By similarity). FT BINDING 409 409 ATP (By similarity). FT MOD_RES 260 260 Phosphotyrosine. FT VARSPLIC 705 748 GLPTHDMEGKELSKGQAKKLKKLFEAQEKLYKEYLQMAQNG FT SFQ -> VSMVCPHMTWRAKSSAKGKPRS (in isoform FT 2). FT /FTId=VSP_006312. SQ SEQUENCE 748 AA; 85473 MW; D0B7A29EC03AA87F CRC64; MADSSGQQGK GRRVQPQWSP PAGTQPCRLH LYNSLTRNKE VFIPQDGKKV TWYCCGPTVY DASHMGHARS YISFDILRRV LKDYFKFDVF YCMNITDIDD KIIKRARQNH LFEQYREKRP EAAQLLEDVQ AALKPFSVKL NETTDPDKKQ MLERIQHAVQ LATEPLEKAV QSRLTGEEVN SCVEVLLEEA KDLLSDWLDS TLGCDVTDNS IFSKLPKFWE GDFHRDMEAL NVLPPDVLTR VSEYVPEIVN FVQKIVDNGY GYVSNGSVYF DTAKFASSEK HSYGKLVPEA VGDQKALQEG EGDLSISADR LSEKRSPNDF ALWKASKPGE PSWPCPWGKG RPGWHIECSA MAGTLLGASM DIHGGGFDLR FPHHDNELAQ SEAYFENDCW VRYFLHTGHL TIAGCKMSKS LKNFITIKDA LKKHSARQLR LAFLMHSWKD TLDYSSNTME SALQYEKFLN EFFLNVKDIL RAPVDITGQF EKWGEEEAEL NKNFYDKKTA IHKALCDNVD TRTVMEEMRA LVSQCNLYMA ARKAVRKRPN QALLENIALY LTHMLKIFGA VEEDSSLGFP VGGPGTSLSL EATVMPYLQV LSEFREGVRK IAREQKVPEI LQLSDALRDN ILPELGVRFE DHEGLPTVVK LVDRNTLLKE REEKRRVEEE KRKKKEEAAR RKQEQEAAKL AKMKIPPSEM FLSETDKYSK FDENGLPTHD MEGKELSKGQ AKKLKKLFEA QEKLYKEYLQ MAQNGSFQ //