Reviewed, UniProtKB/Swiss-Prot Q9ER72 (SYCC_MOUSE)

Names and origin

Protein names

Recommended name:
    Cysteinyl-tRNA synthetase, cytoplasmic
    EC=6.1.1.16
Alternative name(s):
    Cysteine--tRNA ligase
      Short name=CysRS

Gene names

Name:

Cars

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	831 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys).
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	cysteinyl-tRNA aminoacylation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cysteine-tRNA ligase activity Inferred from sequence or structural similarity. Source: UniProtKB tRNA binding Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9ER72-1)

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: Q9ER72-2)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 831	831	Cysteinyl-tRNA synthetase, cytoplasmic		PRO_0000159551
Regions
	Motif	140 – 150	11	"HIGH" region
	Motif	489 – 493	5	"KMSKS" region
Sites
	Metal binding	138	1	Zinc By similarity
	Metal binding	431	1	Zinc By similarity
	Metal binding	456	1	Zinc By similarity
	Metal binding	460	1	Zinc By similarity
	Binding site	492	1	ATP By similarity
Amino acid modifications
	Modified residue	343	1	Phosphotyrosine By similarity
	Modified residue	390	1	Phosphoserine Ref.5
	Modified residue	829	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	9 – 92	84	AADYR…RLQAS → G in isoform 2.		VSP_010258
Experimental info
	Sequence conflict	161	1	R → P in AAH30473. Ref.3
	Sequence conflict	164	1	L → R in AAH30473. Ref.3
	Sequence conflict	310	1	M → K in BAC28234. Ref.2
	Sequence conflict	313	1	L → P in BAA29032. Ref.4
	Sequence conflict	742	1	E → G in BAC28234. Ref.2
	Sequence conflict	771	1	S → G in CAC16398. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 10, 2004. Version 2. Checksum: 5FE338D27AE32B92	FASTA	831	94,860
	10 20 30 40 50 60 MAGSSAEQAA DYRSILSISD EAARVQALDQ HLSTRSYIQG YSLSQADVDV FRQLSAPPAD 70 80 90 100 110 120 SRLFHVARWF RHIEALLGGP QGRDEPCRLQ ASKGRRVQPQ WSPPAGTEPC RLRLYNSLTR 130 140 150 160 170 180 NKDVFIPQDG KKVTWYCCGP TVYDASHMGH ARSYISFDIL RRVLRDYFQY DVFYCMNITD 190 200 210 220 230 240 IDDKIIRRAR QNYLFEQYRE QKPPATQLLK DVRDAMKPFS VKLSETTDPD KRQMLERIQN 250 260 270 280 290 300 SVKLATEPLE QAVRSSLSGE EVDSKVQVLL EEAKDLLSDW LDSTGGSEVT DNSIFSKLPK 310 320 330 340 350 360 FWEEEFHKDM EALNVLPPDV LTRVSEYVPE IVNFVQKIVD NGYGYASNGS VYFDTAKFAA 370 380 390 400 410 420 SEKHSYGKLV PEAVGDQKAL QEGEGDLSIS ADRLSEKRSP NDFALWKASK PGEPSWPCPW 430 440 450 460 470 480 GKGRPGWHIE CSAMAGTLLG ASMDIHGGGF DLRFPHHDNE LAQSEAYFEN DCWVRYFLHT 490 500 510 520 530 540 GHLTIAGCKM SKSLKNFITI KDALKKHSAR QLRLAFLMHS WKDTLDYSSN TMESALQYEK 550 560 570 580 590 600 FMNEFFLNVK DILRAPVDIT GQFEKWEAEE VELNKNFYGK KTAVHEALCD NIDTRTVMEE 610 620 630 640 650 660 MRALVSQCNL YMAARKAERR RPNRALLENI AMYLTHMLKI FGAIEEESPL GFPVGGPGTN 670 680 690 700 710 720 LNLESTVMPY LQVLSEFREG VRKIAREKKV LEVLQLSDAL RDDILPELGV RFEDHEGLPT 730 740 750 760 770 780 VVKLVDRDTL LKEKEGKKRA EEEKRRKKEE AARKKQEQEA AKLAKMKIPP SEMFLSEVNK 790 800 810 820 830 YSKFDENGLP THDTEGKELS KGQAKKLKKL FEAQEKLYKE YLQMLQNGSL Q
	Isoform 2. Checksum: 48E21E753893755E	FASTA	748	85,551
	10 20 30 40 50 60 MAGSSAEQGK GRRVQPQWSP PAGTEPCRLR LYNSLTRNKD VFIPQDGKKV TWYCCGPTVY 70 80 90 100 110 120 DASHMGHARS YISFDILRRV LRDYFQYDVF YCMNITDIDD KIIRRARQNY LFEQYREQKP 130 140 150 160 170 180 PATQLLKDVR DAMKPFSVKL SETTDPDKRQ MLERIQNSVK LATEPLEQAV RSSLSGEEVD 190 200 210 220 230 240 SKVQVLLEEA KDLLSDWLDS TGGSEVTDNS IFSKLPKFWE EEFHKDMEAL NVLPPDVLTR 250 260 270 280 290 300 VSEYVPEIVN FVQKIVDNGY GYASNGSVYF DTAKFAASEK 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 SALQYEKFMN EFFLNVKDIL RAPVDITGQF 490 500 510 520 530 540 EKWEAEEVEL NKNFYGKKTA VHEALCDNID TRTVMEEMRA LVSQCNLYMA ARKAERRRPN 550 560 570 580 590 600 RALLENIAMY LTHMLKIFGA IEEESPLGFP VGGPGTNLNL ESTVMPYLQV LSEFREGVRK 610 620 630 640 650 660 IAREKKVLEV LQLSDALRDD ILPELGVRFE DHEGLPTVVK LVDRDTLLKE KEGKKRAEEE 670 680 690 700 710 720 KRRKKEEAAR KKQEQEAAKL AKMKIPPSEM FLSEVNKYSK FDENGLPTHD TEGKELSKGQ 730 740 AKKLKKLFEA QEKLYKEYLQ MLQNGSLQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 11063728] [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: 16141072] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6. 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]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00331422. IPI00410740.
RefSeq	NP_038770.3.
UniGene	Mm.125659
3D structure databases
HSSP	HSSP built from PDB template 1LI5 based on UniProtKB P21888.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9ER72.
PTM databases
PhosphoSite	Q9ER72.
Proteomic databases
PRIDE	Q9ER72.
Genome annotation databases
Ensembl	ENSMUST00000010899; ENSMUSP00000010899; ENSMUSG00000010755; Mus musculus. [Genome view] ENSMUST00000105909; ENSMUSP00000101529; ENSMUSG00000010755; Mus musculus. [Genome view]
GeneID	27267.
KEGG	mmu:27267.
UCSC	uc009kpn.1. mouse. uc009kpo.1. mouse.
Organism-specific databases
CTD	27267.
MGI	MGI:1351477. Cars.
Phylogenomic databases
HOVERGEN	Q9ER72.
OMA	QCNLYMA.
Enzyme and pathway databases
BRENDA	6.1.1.16. 244.
Gene expression databases
ArrayExpress	Q9ER72.
Bgee	Q9ER72.
CleanEx	MM_CARS.
Genevestigator	Q9ER72.
GermOnline	ENSMUSG00000010755. Mus musculus.
Family and domain databases
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR015804. Cys-tRNA-synt_Ia_C. IPR015803. Cys-tRNA-synt_Ia_N. IPR002308. Cys-tRNA-synth_1a. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHER	PTHR10890. Cys_tRNA-synt_1a. 1 hit.
Pfam	PF01406. tRNA-synt_1e. 1 hit. [Graphical view]
PRINTS	PR00983. TRNASYNTHCYS.
TIGRFAMs	TIGR00435. cysS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	305168.
SOURCE	Search...

Entry information

Entry name

SYCC_MOUSE

Accession

Primary (citable) accession number: Q9ER72
Secondary accession number(s): O88303 , Q8BP81, Q8CAY7, Q8CCE3, Q8K0S4, Q9ER68

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2004
Last sequence update:	May 10, 2004
Last modified:	November 3, 2009
This is version 64 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)