Full text data of CARS
CARS
[Confidence: low (only semi-automatic identification from reviews)]
Cysteine--tRNA ligase, cytoplasmic; 6.1.1.16 (Cysteinyl-tRNA synthetase; CysRS)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Cysteine--tRNA ligase, cytoplasmic; 6.1.1.16 (Cysteinyl-tRNA synthetase; CysRS)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P49589
ID SYCC_HUMAN Reviewed; 748 AA.
AC P49589; Q53XI8; Q5HYE4; Q9HD24; Q9HD25;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 31-JAN-2002, sequence version 3.
DT 22-JAN-2014, entry version 130.
DE RecName: Full=Cysteine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.16;
DE AltName: Full=Cysteinyl-tRNA synthetase;
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 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 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 3).
RC TISSUE=Testis;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Cervix;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
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 [9]
RP CHROMOSOMAL TRANSLOCATION WITH ALK.
RX 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [11]
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 [12]
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.,
RA Walther T.C., 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-746, PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-79 (ISOFORM 3), AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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=3;
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 Name=3;
CC IsoId=P49589-3; Sequence=VSP_043571;
CC Note=Contains a phosphoserine at position 79;
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";
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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; AK302644; BAG63885.1; -; mRNA.
DR EMBL; BX647906; CAI46108.1; -; mRNA.
DR EMBL; AC108448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471158; EAX02541.1; -; Genomic_DNA.
DR EMBL; BC002880; AAH02880.1; -; mRNA.
DR RefSeq; NP_001014437.1; NM_001014437.2.
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; 18-134, 214-496.
DR IntAct; P49589; 4.
DR STRING; 9606.ENSP00000369897; -.
DR DrugBank; DB00151; L-Cysteine.
DR PhosphoSite; P49589; -.
DR DMDM; 20141641; -.
DR PaxDb; P49589; -.
DR PRIDE; P49589; -.
DR DNASU; 833; -.
DR Ensembl; ENST00000278224; ENSP00000278224; ENSG00000110619.
DR Ensembl; ENST00000380525; ENSP00000369897; ENSG00000110619.
DR Ensembl; ENST00000397111; ENSP00000380300; ENSG00000110619.
DR GeneID; 833; -.
DR KEGG; hsa:833; -.
DR UCSC; uc001lxh.3; human.
DR CTD; 833; -.
DR GeneCards; GC11M003022; -.
DR H-InvDB; HIX0128660; -.
DR HGNC; HGNC:1493; CARS.
DR HPA; HPA002383; -.
DR HPA; HPA002384; -.
DR MIM; 123859; gene.
DR neXtProt; NX_P49589; -.
DR Orphanet; 178342; Inflammatory myofibroblastic tumor.
DR PharmGKB; PA26079; -.
DR eggNOG; COG0215; -.
DR HOGENOM; HOG000245252; -.
DR HOVERGEN; HBG002089; -.
DR KO; K01883; -.
DR OMA; RTNVYIN; -.
DR PhylomeDB; P49589; -.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; CARS; human.
DR GenomeRNAi; 833; -.
DR NextBio; 3450; -.
DR PRO; PR:P49589; -.
DR ArrayExpress; P49589; -.
DR Bgee; P49589; -.
DR CleanEx; HS_CARS; -.
DR Genevestigator; P49589; -.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS: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:0000049; F:tRNA binding; IDA:UniProtKB.
DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IDA:UniProtKB.
DR Gene3D; 3.40.50.620; -; 2.
DR InterPro; IPR015803; Cys-tRNA-ligase.
DR InterPro; IPR024909; Cys-tRNA/MSH_ligase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd.
DR PANTHER; PTHR10890; PTHR10890; 1.
DR Pfam; PF01406; tRNA-synt_1e; 1.
DR PRINTS; PR00983; TRNASYNTHCYS.
DR SUPFAM; SSF47323; SSF47323; 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; Reference proteome; Zinc.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 748 Cysteine--tRNA ligase, 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 2 2 N-acetylalanine.
FT MOD_RES 503 503 N6-acetyllysine.
FT MOD_RES 746 746 Phosphoserine.
FT VAR_SEQ 9 9 G -> APDYRSILSISDEAARAQALNEHLSTRSYVQGYSLS
FT QADVDAFRQLSAPPADPQLFHVARWFRHIEALLGSPCGKGQ
FT PCRLQAS (in isoform 3).
FT /FTId=VSP_043571.
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
//
ID SYCC_HUMAN Reviewed; 748 AA.
AC P49589; Q53XI8; Q5HYE4; Q9HD24; Q9HD25;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 31-JAN-2002, sequence version 3.
DT 22-JAN-2014, entry version 130.
DE RecName: Full=Cysteine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.16;
DE AltName: Full=Cysteinyl-tRNA synthetase;
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 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 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 3).
RC TISSUE=Testis;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Cervix;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
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 [9]
RP CHROMOSOMAL TRANSLOCATION WITH ALK.
RX 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [11]
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 [12]
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.,
RA Walther T.C., 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-746, PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-79 (ISOFORM 3), AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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=3;
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 Name=3;
CC IsoId=P49589-3; Sequence=VSP_043571;
CC Note=Contains a phosphoserine at position 79;
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 -----------------------------------------------------------------------
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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; AK302644; BAG63885.1; -; mRNA.
DR EMBL; BX647906; CAI46108.1; -; mRNA.
DR EMBL; AC108448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471158; EAX02541.1; -; Genomic_DNA.
DR EMBL; BC002880; AAH02880.1; -; mRNA.
DR RefSeq; NP_001014437.1; NM_001014437.2.
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; 18-134, 214-496.
DR IntAct; P49589; 4.
DR STRING; 9606.ENSP00000369897; -.
DR DrugBank; DB00151; L-Cysteine.
DR PhosphoSite; P49589; -.
DR DMDM; 20141641; -.
DR PaxDb; P49589; -.
DR PRIDE; P49589; -.
DR DNASU; 833; -.
DR Ensembl; ENST00000278224; ENSP00000278224; ENSG00000110619.
DR Ensembl; ENST00000380525; ENSP00000369897; ENSG00000110619.
DR Ensembl; ENST00000397111; ENSP00000380300; ENSG00000110619.
DR GeneID; 833; -.
DR KEGG; hsa:833; -.
DR UCSC; uc001lxh.3; human.
DR CTD; 833; -.
DR GeneCards; GC11M003022; -.
DR H-InvDB; HIX0128660; -.
DR HGNC; HGNC:1493; CARS.
DR HPA; HPA002383; -.
DR HPA; HPA002384; -.
DR MIM; 123859; gene.
DR neXtProt; NX_P49589; -.
DR Orphanet; 178342; Inflammatory myofibroblastic tumor.
DR PharmGKB; PA26079; -.
DR eggNOG; COG0215; -.
DR HOGENOM; HOG000245252; -.
DR HOVERGEN; HBG002089; -.
DR KO; K01883; -.
DR OMA; RTNVYIN; -.
DR PhylomeDB; P49589; -.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; CARS; human.
DR GenomeRNAi; 833; -.
DR NextBio; 3450; -.
DR PRO; PR:P49589; -.
DR ArrayExpress; P49589; -.
DR Bgee; P49589; -.
DR CleanEx; HS_CARS; -.
DR Genevestigator; P49589; -.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS: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:0000049; F:tRNA binding; IDA:UniProtKB.
DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IDA:UniProtKB.
DR Gene3D; 3.40.50.620; -; 2.
DR InterPro; IPR015803; Cys-tRNA-ligase.
DR InterPro; IPR024909; Cys-tRNA/MSH_ligase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd.
DR PANTHER; PTHR10890; PTHR10890; 1.
DR Pfam; PF01406; tRNA-synt_1e; 1.
DR PRINTS; PR00983; TRNASYNTHCYS.
DR SUPFAM; SSF47323; SSF47323; 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; Reference proteome; Zinc.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 748 Cysteine--tRNA ligase, 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 2 2 N-acetylalanine.
FT MOD_RES 503 503 N6-acetyllysine.
FT MOD_RES 746 746 Phosphoserine.
FT VAR_SEQ 9 9 G -> APDYRSILSISDEAARAQALNEHLSTRSYVQGYSLS
FT QADVDAFRQLSAPPADPQLFHVARWFRHIEALLGSPCGKGQ
FT PCRLQAS (in isoform 3).
FT /FTId=VSP_043571.
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
//
MIM
123859
*RECORD*
*FIELD* NO
123859
*FIELD* TI
*123859 CYSTEINYL-tRNA SYNTHETASE; CARS
CARS/ALK FUSION GENE, INCLUDED
*FIELD* TX
read moreDESCRIPTION
The attachment of each of the 20 naturally occurring amino acids to
their cognate tRNA isoaccepting families is catalyzed by a specific
aminoacyl-tRNA synthetase, such as CARS (Cruzen et al., 1993).
MAPPING
Cruzen et al. (1993) assigned the CARS gene to chromosome 11 by analysis
of a panel of human/Chinese hamster somatic cell hybrids. By
fluorescence in situ hybridization, they refined the location to
chromosome 11p15.5.
CYTOGENETICS
In a patient with ALK (105590)-positive anaplastic large-cell lymphoma,
Cools et al. (2002) identified a t(2;11;2)(p23;p15;q31) rearrangement
that resulted in splicing of exons of the CARS gene from chromosome
11p15 to exons of the ALK gene from chromosome 2p23. The predicted
fusion protein contains 606 N-terminal amino acids of CARS fused to 562
amino acids of ALK, including the ALK kinase domain.
*FIELD* RF
1. Cools, J.; Wlodarska, I.; Somers, R.; Mentens, N.; Pedeutour, F.;
Maes, B.; De Wolf-Peeters, C.; Pauwels, P.; Hagemeijer, A.; Marynen,
P.: Identification of novel fusion partners of ALK, the anaplastic
lymphoma kinase, in anaplastic large-cell lymphoma and inflammatory
myofibroblastic tumor. Genes Chromosomes Cancer 34: 354-362, 2002.
2. Cruzen, M. E.; Bengtsson, U.; McMahon, J.; Wasmuth, J. J.; Arfin,
S. M.: Assignment of the cysteinyl-tRNA synthetase gene (CARS) to
11p15.5. Genomics 15: 692-693, 1993.
*FIELD* CN
Patricia A. Hartz - updated: 2/17/2011
*FIELD* CD
Victor A. McKusick: 4/14/1993
*FIELD* ED
mgross: 02/23/2011
terry: 2/17/2011
carol: 4/14/1993
*RECORD*
*FIELD* NO
123859
*FIELD* TI
*123859 CYSTEINYL-tRNA SYNTHETASE; CARS
CARS/ALK FUSION GENE, INCLUDED
*FIELD* TX
read moreDESCRIPTION
The attachment of each of the 20 naturally occurring amino acids to
their cognate tRNA isoaccepting families is catalyzed by a specific
aminoacyl-tRNA synthetase, such as CARS (Cruzen et al., 1993).
MAPPING
Cruzen et al. (1993) assigned the CARS gene to chromosome 11 by analysis
of a panel of human/Chinese hamster somatic cell hybrids. By
fluorescence in situ hybridization, they refined the location to
chromosome 11p15.5.
CYTOGENETICS
In a patient with ALK (105590)-positive anaplastic large-cell lymphoma,
Cools et al. (2002) identified a t(2;11;2)(p23;p15;q31) rearrangement
that resulted in splicing of exons of the CARS gene from chromosome
11p15 to exons of the ALK gene from chromosome 2p23. The predicted
fusion protein contains 606 N-terminal amino acids of CARS fused to 562
amino acids of ALK, including the ALK kinase domain.
*FIELD* RF
1. Cools, J.; Wlodarska, I.; Somers, R.; Mentens, N.; Pedeutour, F.;
Maes, B.; De Wolf-Peeters, C.; Pauwels, P.; Hagemeijer, A.; Marynen,
P.: Identification of novel fusion partners of ALK, the anaplastic
lymphoma kinase, in anaplastic large-cell lymphoma and inflammatory
myofibroblastic tumor. Genes Chromosomes Cancer 34: 354-362, 2002.
2. Cruzen, M. E.; Bengtsson, U.; McMahon, J.; Wasmuth, J. J.; Arfin,
S. M.: Assignment of the cysteinyl-tRNA synthetase gene (CARS) to
11p15.5. Genomics 15: 692-693, 1993.
*FIELD* CN
Patricia A. Hartz - updated: 2/17/2011
*FIELD* CD
Victor A. McKusick: 4/14/1993
*FIELD* ED
mgross: 02/23/2011
terry: 2/17/2011
carol: 4/14/1993