ID SYCC_HUMAN Reviewed; 748 AA. AC P49589; Q53XI8; Q9HD24; Q9HD25; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 31-JAN-2002, sequence version 3. DT 05-APR-2011, entry version 102. DE RecName: Full=Cysteinyl-tRNA synthetase, cytoplasmic; DE EC=6.1.1.16; DE AltName: Full=Cysteine--tRNA ligase; DE Short=CysRS; GN Name=CARS; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP CHROMOSOMAL TRANSLOCATION WITH ALK. RX MEDLINE=22105993; PubMed=12112524; DOI=10.1002/gcc.10033; RA Cools J., Wlodarska I., Somers R., Mentens N., Pedeutour F., Maes B., RA De Wolf-Peeters C., Pauwels P., Hagemeijer A., Marynen P.; RT "Identification of novel fusion partners of ALK, the anaplastic RT lymphoma kinase, in anaplastic large-cell lymphoma and inflammatory RT myofibroblastic tumor."; RL Genes Chromosomes Cancer 34:354-362(2002). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-260, AND MASS RP 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). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-746, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASS RP SPECTROMETRY. RC TISSUE=Embryonic kidney; RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-503, AND MASS SPECTROMETRY. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., 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 [10] 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., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). 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 -!- DISEASE: Note=A chromosomal aberration involving CARS is CC associated with inflammatory myofibroblastic tumors (IMTs). CC Translocation t(2;11)(p23;p15) with ALK. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. CC -!- SEQUENCE CAUTION: CC Sequence=AAA73901.1; Type=Frameshift; Positions=619; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/CARSID484.html"; 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; BT009913; AAP88915.1; -; mRNA. DR EMBL; BC002880; AAH02880.1; -; mRNA. DR IPI; IPI00556365; -. DR IPI; IPI00939491; -. DR RefSeq; NP_001742.1; NM_001751.5. DR RefSeq; NP_644802.1; NM_139273.3. DR UniGene; Hs.274873; -. DR ProteinModelPortal; P49589; -. DR SMR; P49589; 29-641. DR IntAct; P49589; 4. DR STRING; P49589; -. DR PhosphoSite; P49589; -. DR PRIDE; P49589; -. DR Ensembl; ENST00000397111; ENSP00000380300; ENSG00000110619. DR GeneID; 833; -. DR KEGG; hsa:833; -. DR NMPDR; fig|9606.3.peg.5048; -. DR UCSC; uc001lxg.1; human. DR UCSC; uc001lxh.1; human. DR CTD; 833; -. DR GeneCards; GC11M002810; -. DR HGNC; HGNC:1493; CARS. DR HPA; HPA002383; -. DR HPA; HPA002384; -. DR MIM; 123859; gene. DR neXtProt; NX_P49589; -. DR eggNOG; prNOG17865; -. DR GeneTree; ENSGT00390000006347; -. DR HOVERGEN; HBG002089; -. DR OrthoDB; EOG473PQS; -. DR PhylomeDB; P49589; -. DR BRENDA; 6.1.1.16; 247. DR Reactome; REACT_71; Gene Expression. DR DrugBank; DB00151; L-Cysteine. DR NextBio; 3450; -. DR ArrayExpress; P49589; -. DR Bgee; P49589; -. DR CleanEx; HS_CARS; -. DR Genevestigator; P49589; -. DR GermOnline; ENSG00000110619; Homo sapiens. DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB. DR GO; GO:0005829; C:cytosol; EXP:Reactome. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0004817; F:cysteine-tRNA ligase activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IMP:UniProtKB. DR GO; GO:0000049; F:tRNA binding; IDA:UniProtKB. DR GO; GO:0000049; F:tRNA binding; IMP:UniProtKB. DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IDA:UniProtKB. DR InterPro; IPR015803; Cys-tRNA-synt_Ia. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd. DR Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 2. DR Pfam; PF01406; tRNA-synt_1e; 1. DR PRINTS; PR00983; TRNASYNTHCYS. DR SUPFAM; SSF47323; tRNAsyn_1a_bind; 1. DR TIGRFAMs; TIGR00435; cysS; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; FALSE_NEG. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Aminoacyl-tRNA synthetase; KW ATP-binding; Chromosomal rearrangement; Complete proteome; Cytoplasm; KW Ligase; Metal-binding; Nucleotide-binding; Phosphoprotein; KW Protein biosynthesis; Proto-oncogene; Zinc. FT CHAIN 1 748 Cysteinyl-tRNA synthetase, cytoplasmic. 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 19 19 Phosphoserine. FT MOD_RES 260 260 Phosphotyrosine. FT MOD_RES 307 307 Phosphoserine (By similarity). FT MOD_RES 503 503 N6-acetyllysine. FT MOD_RES 746 746 Phosphoserine. FT VAR_SEQ 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 //