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P49589 (SYCC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cysteine--tRNA ligase, cytoplasmic

EC=6.1.1.16
Alternative name(s):
Cysteinyl-tRNA synthetase
Short name=CysRS
Gene names
Name:CARS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length748 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys). HAMAP-Rule MF_00041

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00041

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00041

Subcellular location

Cytoplasm HAMAP-Rule MF_00041.

Involvement in disease

A chromosomal aberration involving CARS is associated with inflammatory myofibroblastic tumors (IMTs). Translocation t(2;11)(p23;p15) with ALK.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Sequence caution

The sequence AAA73901.1 differs from that shown. Reason: Frameshift at position 619.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P49589-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P49589-2)

The sequence of this isoform differs from the canonical sequence as follows:
     705-748: GLPTHDMEGKELSKGQAKKLKKLFEAQEKLYKEYLQMAQNGSFQ → VSMVCPHMTWRAKSSAKGKPRS
Note: Found in 20% of the mRNAs.
Isoform 3 (identifier: P49589-3)

The sequence of this isoform differs from the canonical sequence as follows:
     9-9: G → APDYRSILSI...KGQPCRLQAS
Note: Contains a phosphoserine at position 79.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.15
Chain2 – 748747Cysteine--tRNA ligase, cytoplasmic HAMAP-Rule MF_00041
PRO_0000159550

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_00041
Motif406 – 4105"KMSKS" region HAMAP-Rule MF_00041

Sites

Metal binding551Zinc By similarity
Metal binding3481Zinc By similarity
Metal binding3731Zinc By similarity
Metal binding3771Zinc By similarity
Binding site4091ATP By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.15
Modified residue5031N6-acetyllysine Ref.12
Modified residue7461Phosphoserine Ref.11 Ref.13

Natural variations

Alternative sequence91G → APDYRSILSISDEAARAQAL NEHLSTRSYVQGYSLSQADV DAFRQLSAPPADPQLFHVAR WFRHIEALLGSPCGKGQPCR LQAS in isoform 3.
VSP_043571
Alternative sequence705 – 74844GLPTH…NGSFQ → VSMVCPHMTWRAKSSAKGKP RS in isoform 2.
VSP_006312

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 31, 2002. Version 3.
Checksum: D0B7A29EC03AA87F

FASTA74885,473
        10         20         30         40         50         60 
MADSSGQQGK GRRVQPQWSP PAGTQPCRLH LYNSLTRNKE VFIPQDGKKV TWYCCGPTVY 

        70         80         90        100        110        120 
DASHMGHARS YISFDILRRV LKDYFKFDVF YCMNITDIDD KIIKRARQNH LFEQYREKRP 

       130        140        150        160        170        180 
EAAQLLEDVQ AALKPFSVKL NETTDPDKKQ MLERIQHAVQ LATEPLEKAV QSRLTGEEVN 

       190        200        210        220        230        240 
SCVEVLLEEA KDLLSDWLDS TLGCDVTDNS IFSKLPKFWE GDFHRDMEAL NVLPPDVLTR 

       250        260        270        280        290        300 
VSEYVPEIVN FVQKIVDNGY GYVSNGSVYF DTAKFASSEK HSYGKLVPEA VGDQKALQEG 

       310        320        330        340        350        360 
EGDLSISADR LSEKRSPNDF ALWKASKPGE PSWPCPWGKG RPGWHIECSA MAGTLLGASM 

       370        380        390        400        410        420 
DIHGGGFDLR FPHHDNELAQ SEAYFENDCW VRYFLHTGHL TIAGCKMSKS LKNFITIKDA 

       430        440        450        460        470        480 
LKKHSARQLR LAFLMHSWKD TLDYSSNTME SALQYEKFLN EFFLNVKDIL RAPVDITGQF 

       490        500        510        520        530        540 
EKWGEEEAEL NKNFYDKKTA IHKALCDNVD TRTVMEEMRA LVSQCNLYMA ARKAVRKRPN 

       550        560        570        580        590        600 
QALLENIALY LTHMLKIFGA VEEDSSLGFP VGGPGTSLSL EATVMPYLQV LSEFREGVRK 

       610        620        630        640        650        660 
IAREQKVPEI LQLSDALRDN ILPELGVRFE DHEGLPTVVK LVDRNTLLKE REEKRRVEEE 

       670        680        690        700        710        720 
KRKKKEEAAR RKQEQEAAKL AKMKIPPSEM FLSETDKYSK FDENGLPTHD MEGKELSKGQ 

       730        740 
AKKLKKLFEA QEKLYKEYLQ MAQNGSFQ 

« Hide

Isoform 2 [UniParc].

Checksum: 92C51DF9289FE47D
Show »

FASTA72682,846
Isoform 3 [UniParc].

Checksum: C0080CD332F79B8F
Show »

FASTA83194,638

References

« Hide 'large scale' references
[1]"Nucleotide and deduced amino acid sequence of human cysteinyl-tRNA synthetase."
Cruzen M.E., Arfin S.M.
DNA Seq. 4:243-248(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Brain.
[2]"Isolation of two cDNAs encoding functional human cytoplasmic cysteinyl-tRNA synthetase."
Davidson E., Caffarella J., Vitseva O., Hou Y.M., King M.P.
Biol. Chem. 382:399-406(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Testis.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Cervix.
[6]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Lung.
[9]"Identification of novel fusion partners of ALK, the anaplastic lymphoma kinase, in anaplastic large-cell lymphoma and inflammatory myofibroblastic tumor."
Cools J., Wlodarska I., Somers R., Mentens N., Pedeutour F., Maes B., De Wolf-Peeters C., Pauwels P., Hagemeijer A., Marynen P.
Genes Chromosomes Cancer 34:354-362(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH ALK.
[10]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-746, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-503, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-746, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L06845 mRNA. Translation: AAA73901.1. Frameshift.
AF288206 mRNA. Translation: AAG00578.1.
AF288207 mRNA. Translation: AAG00579.1.
BT009913 mRNA. Translation: AAP88915.1.
AK302644 mRNA. Translation: BAG63885.1.
BX647906 mRNA. Translation: CAI46108.1.
AC108448 Genomic DNA. No translation available.
AC131971 Genomic DNA. No translation available.
CH471158 Genomic DNA. Translation: EAX02541.1.
BC002880 mRNA. Translation: AAH02880.1.
CCDSCCDS41600.1. [P49589-3]
CCDS41602.1. [P49589-2]
CCDS7742.1. [P49589-1]
RefSeqNP_001014437.1. NM_001014437.2. [P49589-3]
NP_001742.1. NM_001751.5. [P49589-1]
NP_644802.1. NM_139273.3. [P49589-2]
UniGeneHs.274873.

3D structure databases

ProteinModelPortalP49589.
SMRP49589. Positions 18-134, 214-496.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107283. 32 interactions.
IntActP49589. 4 interactions.
STRING9606.ENSP00000369897.

Chemistry

DrugBankDB00151. L-Cysteine.

PTM databases

PhosphoSiteP49589.

Polymorphism databases

DMDM20141641.

Proteomic databases

MaxQBP49589.
PaxDbP49589.
PRIDEP49589.

Protocols and materials databases

DNASU833.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000278224; ENSP00000278224; ENSG00000110619. [P49589-2]
ENST00000380525; ENSP00000369897; ENSG00000110619. [P49589-3]
ENST00000397111; ENSP00000380300; ENSG00000110619. [P49589-1]
GeneID833.
KEGGhsa:833.
UCSCuc001lxf.3. human. [P49589-3]
uc001lxg.3. human. [P49589-2]
uc001lxh.3. human. [P49589-1]

Organism-specific databases

CTD833.
GeneCardsGC11M003022.
H-InvDBHIX0128660.
HGNCHGNC:1493. CARS.
HPAHPA002383.
HPA002384.
MIM123859. gene.
neXtProtNX_P49589.
Orphanet178342. Inflammatory myofibroblastic tumor.
PharmGKBPA26079.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0215.
HOGENOMHOG000245252.
HOVERGENHBG002089.
KOK01883.
OMAEMFLSES.
PhylomeDBP49589.
TreeFamTF300384.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressP49589.
BgeeP49589.
CleanExHS_CARS.
GenevestigatorP49589.

Family and domain databases

Gene3D3.40.50.620. 2 hits.
HAMAPMF_00041. Cys_tRNA_synth.
InterProIPR015803. Cys-tRNA-ligase.
IPR024909. Cys-tRNA/MSH_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
PANTHERPTHR10890. PTHR10890. 1 hit.
PfamPF01406. tRNA-synt_1e. 1 hit.
[Graphical view]
PRINTSPR00983. TRNASYNTHCYS.
SUPFAMSSF47323. SSF47323. 1 hit.
TIGRFAMsTIGR00435. cysS. 1 hit.
ProtoNetSearch...

Other

ChiTaRSCARS. human.
GenomeRNAi833.
NextBio3450.
PROP49589.
SOURCESearch...

Entry information

Entry nameSYCC_HUMAN
AccessionPrimary (citable) accession number: P49589
Secondary accession number(s): Q53XI8 expand/collapse secondary AC list , Q5HYE4, Q9HD24, Q9HD25
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 31, 2002
Last modified: July 9, 2014
This is version 136 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries