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Protein

Cysteine--tRNA ligase, cytoplasmic

Gene

Cars

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi138 – 1381ZincBy similarity
Metal bindingi431 – 4311ZincBy similarity
Metal bindingi456 – 4561ZincBy similarity
Metal bindingi460 – 4601ZincBy similarity
Binding sitei492 – 4921ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine--tRNA ligase, cytoplasmic (EC:6.1.1.16)
Alternative name(s):
Cysteinyl-tRNA synthetase
Short name:
CysRS
Gene namesi
Name:Cars
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1351477. Cars.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 831830Cysteine--tRNA ligase, cytoplasmicPRO_0000159551Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei102 – 1021PhosphoserineCombined sources
Modified residuei388 – 3881PhosphoserineBy similarity
Modified residuei390 – 3901PhosphoserineCombined sources
Modified residuei829 – 8291PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9ER72.
MaxQBiQ9ER72.
PaxDbiQ9ER72.
PeptideAtlasiQ9ER72.
PRIDEiQ9ER72.

PTM databases

iPTMnetiQ9ER72.
PhosphoSiteiQ9ER72.

Expressioni

Gene expression databases

BgeeiQ9ER72.
CleanExiMM_CARS.
ExpressionAtlasiQ9ER72. baseline and differential.
GenevisibleiQ9ER72. MM.

Interactioni

Subunit structurei

Monomer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ9ER72. 1 interaction.
MINTiMINT-4136240.
STRINGi10090.ENSMUSP00000010899.

Structurei

3D structure databases

ProteinModelPortaliQ9ER72.
SMRiQ9ER72. Positions 101-217, 305-535.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi140 – 15011"HIGH" regionAdd
BLAST
Motifi489 – 4935"KMSKS" region

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2007. Eukaryota.
COG0215. LUCA.
GeneTreeiENSGT00390000006347.
HOVERGENiHBG002089.
InParanoidiQ9ER72.
KOiK01883.
OMAiFDILKLC.
OrthoDBiEOG7J70F0.
PhylomeDBiQ9ER72.
TreeFamiTF300384.

Family and domain databases

Gene3Di3.40.50.620. 2 hits.
HAMAPiMF_00041. Cys_tRNA_synth.
InterProiIPR015803. Cys-tRNA-ligase.
IPR024909. Cys-tRNA/MSH_ligase.
IPR010987. Glutathione-S-Trfase_C-like.
IPR014729. Rossmann-like_a/b/a_fold.
IPR032678. tRNA-synt_1_cat_dom.
IPR009080. tRNAsynth_Ia_anticodon-bd.
[Graphical view]
PANTHERiPTHR10890. PTHR10890. 1 hit.
PfamiPF01406. tRNA-synt_1e. 1 hit.
[Graphical view]
PRINTSiPR00983. TRNASYNTHCYS.
SUPFAMiSSF47323. SSF47323. 1 hit.
SSF47616. SSF47616. 1 hit.
TIGRFAMsiTIGR00435. cysS. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9ER72-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAGSSAEQAA DYRSILSISD EAARVQALDQ HLSTRSYIQG YSLSQADVDV
60 70 80 90 100
FRQLSAPPAD SRLFHVARWF RHIEALLGGP QGRDEPCRLQ ASKGRRVQPQ
110 120 130 140 150
WSPPAGTEPC RLRLYNSLTR NKDVFIPQDG KKVTWYCCGP TVYDASHMGH
160 170 180 190 200
ARSYISFDIL RRVLRDYFQY DVFYCMNITD IDDKIIRRAR QNYLFEQYRE
210 220 230 240 250
QKPPATQLLK DVRDAMKPFS VKLSETTDPD KRQMLERIQN SVKLATEPLE
260 270 280 290 300
QAVRSSLSGE EVDSKVQVLL EEAKDLLSDW LDSTGGSEVT DNSIFSKLPK
310 320 330 340 350
FWEEEFHKDM EALNVLPPDV LTRVSEYVPE IVNFVQKIVD NGYGYASNGS
360 370 380 390 400
VYFDTAKFAA SEKHSYGKLV PEAVGDQKAL QEGEGDLSIS ADRLSEKRSP
410 420 430 440 450
NDFALWKASK PGEPSWPCPW GKGRPGWHIE CSAMAGTLLG ASMDIHGGGF
460 470 480 490 500
DLRFPHHDNE LAQSEAYFEN DCWVRYFLHT GHLTIAGCKM SKSLKNFITI
510 520 530 540 550
KDALKKHSAR QLRLAFLMHS WKDTLDYSSN TMESALQYEK FMNEFFLNVK
560 570 580 590 600
DILRAPVDIT GQFEKWEAEE VELNKNFYGK KTAVHEALCD NIDTRTVMEE
610 620 630 640 650
MRALVSQCNL YMAARKAERR RPNRALLENI AMYLTHMLKI FGAIEEESPL
660 670 680 690 700
GFPVGGPGTN LNLESTVMPY LQVLSEFREG VRKIAREKKV LEVLQLSDAL
710 720 730 740 750
RDDILPELGV RFEDHEGLPT VVKLVDRDTL LKEKEGKKRA EEEKRRKKEE
760 770 780 790 800
AARKKQEQEA AKLAKMKIPP SEMFLSEVNK YSKFDENGLP THDTEGKELS
810 820 830
KGQAKKLKKL FEAQEKLYKE YLQMLQNGSL Q
Length:831
Mass (Da):94,860
Last modified:May 10, 2004 - v2
Checksum:i5FE338D27AE32B92
GO
Isoform 2 (identifier: Q9ER72-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     9-92: AADYRSILSI...RDEPCRLQAS → G

Show »
Length:748
Mass (Da):85,551
Checksum:i48E21E753893755E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti161 – 1611R → P in AAH30473 (PubMed:15489334).Curated
Sequence conflicti164 – 1641L → R in AAH30473 (PubMed:15489334).Curated
Sequence conflicti310 – 3101M → K in BAC28234 (PubMed:16141072).Curated
Sequence conflicti313 – 3131L → P in BAA29032 (Ref. 4) Curated
Sequence conflicti742 – 7421E → G in BAC28234 (PubMed:16141072).Curated
Sequence conflicti771 – 7711S → G in CAC16398 (PubMed:11063728).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei9 – 9284AADYR…RLQAS → G in isoform 2. 1 PublicationVSP_010258Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ276505 Genomic DNA. Translation: CAC16398.1.
AJ276796 mRNA. Translation: CAC16403.1.
AK033328 mRNA. Translation: BAC28234.1.
AK037227 mRNA. Translation: BAC29766.1.
AK077558 mRNA. Translation: BAC36862.1.
BC030473 mRNA. Translation: AAH30473.1.
BC054717 mRNA. Translation: AAH54717.1.
BC058954 mRNA. Translation: AAH58954.1.
AB015589 mRNA. Translation: BAA29032.1.
CCDSiCCDS40198.1. [Q9ER72-1]
CCDS57597.1. [Q9ER72-2]
RefSeqiNP_001239522.1. NM_001252593.1. [Q9ER72-2]
NP_038770.3. NM_013742.5. [Q9ER72-1]
UniGeneiMm.125659.

Genome annotation databases

EnsembliENSMUST00000010899; ENSMUSP00000010899; ENSMUSG00000010755. [Q9ER72-1]
ENSMUST00000105909; ENSMUSP00000101529; ENSMUSG00000010755. [Q9ER72-2]
GeneIDi27267.
KEGGimmu:27267.
UCSCiuc009kpn.2. mouse. [Q9ER72-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ276505 Genomic DNA. Translation: CAC16398.1.
AJ276796 mRNA. Translation: CAC16403.1.
AK033328 mRNA. Translation: BAC28234.1.
AK037227 mRNA. Translation: BAC29766.1.
AK077558 mRNA. Translation: BAC36862.1.
BC030473 mRNA. Translation: AAH30473.1.
BC054717 mRNA. Translation: AAH54717.1.
BC058954 mRNA. Translation: AAH58954.1.
AB015589 mRNA. Translation: BAA29032.1.
CCDSiCCDS40198.1. [Q9ER72-1]
CCDS57597.1. [Q9ER72-2]
RefSeqiNP_001239522.1. NM_001252593.1. [Q9ER72-2]
NP_038770.3. NM_013742.5. [Q9ER72-1]
UniGeneiMm.125659.

3D structure databases

ProteinModelPortaliQ9ER72.
SMRiQ9ER72. Positions 101-217, 305-535.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9ER72. 1 interaction.
MINTiMINT-4136240.
STRINGi10090.ENSMUSP00000010899.

PTM databases

iPTMnetiQ9ER72.
PhosphoSiteiQ9ER72.

Proteomic databases

EPDiQ9ER72.
MaxQBiQ9ER72.
PaxDbiQ9ER72.
PeptideAtlasiQ9ER72.
PRIDEiQ9ER72.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000010899; ENSMUSP00000010899; ENSMUSG00000010755. [Q9ER72-1]
ENSMUST00000105909; ENSMUSP00000101529; ENSMUSG00000010755. [Q9ER72-2]
GeneIDi27267.
KEGGimmu:27267.
UCSCiuc009kpn.2. mouse. [Q9ER72-1]

Organism-specific databases

CTDi833.
MGIiMGI:1351477. Cars.

Phylogenomic databases

eggNOGiKOG2007. Eukaryota.
COG0215. LUCA.
GeneTreeiENSGT00390000006347.
HOVERGENiHBG002089.
InParanoidiQ9ER72.
KOiK01883.
OMAiFDILKLC.
OrthoDBiEOG7J70F0.
PhylomeDBiQ9ER72.
TreeFamiTF300384.

Miscellaneous databases

ChiTaRSiCars. mouse.
PROiQ9ER72.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ER72.
CleanExiMM_CARS.
ExpressionAtlasiQ9ER72. baseline and differential.
GenevisibleiQ9ER72. MM.

Family and domain databases

Gene3Di3.40.50.620. 2 hits.
HAMAPiMF_00041. Cys_tRNA_synth.
InterProiIPR015803. Cys-tRNA-ligase.
IPR024909. Cys-tRNA/MSH_ligase.
IPR010987. Glutathione-S-Trfase_C-like.
IPR014729. Rossmann-like_a/b/a_fold.
IPR032678. tRNA-synt_1_cat_dom.
IPR009080. tRNAsynth_Ia_anticodon-bd.
[Graphical view]
PANTHERiPTHR10890. PTHR10890. 1 hit.
PfamiPF01406. tRNA-synt_1e. 1 hit.
[Graphical view]
PRINTSiPR00983. TRNASYNTHCYS.
SUPFAMiSSF47323. SSF47323. 1 hit.
SSF47616. SSF47616. 1 hit.
TIGRFAMsiTIGR00435. cysS. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and functional comparison in the Beckwith-Wiedemann region: implications for a novel imprinting centre and extended imprinting."
    Engemann S., Stroedicke M., Paulsen M., Franck O., Reinhardt R., Lane N., Reik W., Walter J.
    Hum. Mol. Genet. 9:2691-2706(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
    Strain: 129/Sv.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Skin and Testis.
  3. "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).
    Strain: C57BL/6J.
    Tissue: Brain and Retina.
  4. "Mouse cysteinyl-tRNA synthetase mRNA, partial cds."
    Yatsuki H., Mukai T.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE OF 129-614.
    Strain: C57BL/10.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-390, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiSYCC_MOUSE
AccessioniPrimary (citable) accession number: Q9ER72
Secondary accession number(s): O88303
, Q8BP81, Q8CAY7, Q8CCE3, Q8K0S4, Q9ER68
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: July 6, 2016
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.