P49589 (SYCC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cysteine--tRNA ligase, cytoplasmic
EC=6.1.1.16

Alternative name(s):
Cysteinyl-tRNA synthetase
Short name=CysRS

Gene names

Name:

CARS

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	748 AA.
Sequence status	Complete.
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.
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.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Chromosomal rearrangement
Disease	Proto-oncogene
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cysteinyl-tRNA aminoacylation Inferred from direct assay PubMed 10908348PubMed 17303165Ref.2. Source: UniProtKB
Cellular_component	cytoplasm Non-traceable author statement Ref.2. Source: UniProtKB cytosol Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from direct assay PubMed 17303165. Source: UniProtKB cysteine-tRNA ligase activity Inferred from direct assay PubMed 10908348PubMed 17303165Ref.2. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein homodimerization activity Inferred from direct assay Ref.2. Source: UniProtKB tRNA binding Inferred from direct assay Ref.2. Source: UniProtKB
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 748	748	Cysteine--tRNA ligase, cytoplasmic		PRO_0000159550
Regions
	Motif	57 – 67	11	"HIGH" region
	Motif	406 – 410	5	"KMSKS" region
Sites
	Metal binding	55	1	Zinc By similarity
	Metal binding	348	1	Zinc By similarity
	Metal binding	373	1	Zinc By similarity
	Metal binding	377	1	Zinc By similarity
	Binding site	409	1	ATP By similarity
Amino acid modifications
	Modified residue	307	1	Phosphoserine By similarity
	Modified residue	503	1	N6-acetyllysine Ref.12
	Modified residue	746	1	Phosphoserine Ref.11 Ref.13
Natural variations
	Alternative sequence	9	1	G → APDYRSILSISDEAARAQAL NEHLSTRSYVQGYSLSQADV DAFRQLSAPPADPQLFHVAR WFRHIEALLGSPCGKGQPCR LQAS in isoform 3.		VSP_043571
	Alternative sequence	705 – 748	44	GLPTH…NGSFQ → VSMVCPHMTWRAKSSAKGKP RS in isoform 2.		VSP_006312

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 31, 2002. Version 3. Checksum: D0B7A29EC03AA87F	FASTA	748	85,473
	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
	Isoform 2 [UniParc]. Checksum: 92C51DF9289FE47D	FASTA	726	82,846
	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 FDENVSMVCP HMTWRAKSSA KGKPRS
	Isoform 3 [UniParc]. Checksum: C0080CD332F79B8F	FASTA	831	94,638
	10 20 30 40 50 60 MADSSGQQAP DYRSILSISD EAARAQALNE HLSTRSYVQG YSLSQADVDA FRQLSAPPAD 70 80 90 100 110 120 PQLFHVARWF RHIEALLGSP CGKGQPCRLQ ASKGRRVQPQ WSPPAGTQPC RLHLYNSLTR 130 140 150 160 170 180 NKEVFIPQDG KKVTWYCCGP TVYDASHMGH ARSYISFDIL RRVLKDYFKF DVFYCMNITD 190 200 210 220 230 240 IDDKIIKRAR QNHLFEQYRE KRPEAAQLLE DVQAALKPFS VKLNETTDPD KKQMLERIQH 250 260 270 280 290 300 AVQLATEPLE KAVQSRLTGE EVNSCVEVLL EEAKDLLSDW LDSTLGCDVT DNSIFSKLPK 310 320 330 340 350 360 FWEGDFHRDM EALNVLPPDV LTRVSEYVPE IVNFVQKIVD NGYGYVSNGS VYFDTAKFAS 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 FLNEFFLNVK DILRAPVDIT GQFEKWGEEE AELNKNFYDK KTAIHKALCD NVDTRTVMEE 610 620 630 640 650 660 MRALVSQCNL YMAARKAVRK RPNQALLENI ALYLTHMLKI FGAVEEDSSL GFPVGGPGTS 670 680 690 700 710 720 LSLEATVMPY LQVLSEFREG VRKIAREQKV PEILQLSDAL RDNILPELGV RFEDHEGLPT 730 740 750 760 770 780 VVKLVDRNTL LKEREEKRRV EEEKRKKKEE AARRKQEQEA AKLAKMKIPP SEMFLSETDK 790 800 810 820 830 YSKFDENGLP THDMEGKELS KGQAKKLKKL FEAQEKLYKE YLQMAQNGSF Q

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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), MASS SPECTROMETRY. 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].
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.
IPI	IPI00027443. IPI00556365. IPI00939491.
RefSeq	NP_001014437.1. NM_001014437.2. NP_001742.1. NM_001751.5. NP_644802.1. NM_139273.3.
UniGene	Hs.274873.
3D structure databases
ProteinModelPortal	P49589.
ModBase	Search...
Protein-protein interaction databases
IntAct	P49589. 4 interactions.
STRING	9606.ENSP00000369897.
PTM databases
PhosphoSite	P49589.
Polymorphism databases
DMDM	20141641.
Proteomic databases
PaxDb	P49589.
PRIDE	P49589.
Protocols and materials databases
DNASU	833.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000278224; ENSP00000278224; ENSG00000110619. ENST00000380525; ENSP00000369897; ENSG00000110619. ENST00000397111; ENSP00000380300; ENSG00000110619.
GeneID	833.
KEGG	hsa:833.
UCSC	uc001lxf.3. human. uc001lxg.3. human. uc001lxh.3. human.
Organism-specific databases
CTD	833.
GeneCards	GC11M003022.
H-InvDB	HIX0128660.
HGNC	HGNC:1493. CARS.
HPA	HPA002383. HPA002384.
MIM	123859. gene.
neXtProt	NX_P49589.
PharmGKB	PA26079.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0215.
HOGENOM	HOG000245252.
HOVERGEN	HBG002089.
KO	K01883.
OMA	VARWFRH.
OrthoDB	EOG473PQS.
PhylomeDB	P49589.
Enzyme and pathway databases
Reactome	REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	P49589.
Bgee	P49589.
CleanEx	HS_CARS.
Genevestigator	P49589.
GermOnline	ENSG00000110619. Homo sapiens.
Family and domain databases
Gene3D	3.40.50.620. 2 hits.
InterPro	IPR015803. Cys-tRNA-ligase. IPR024909. Cys-tRNA/MSH_ligase. IPR014729. Rossmann-like_a/b/a_fold. IPR009080. tRNAsynth_1a_anticodon-bd. [Graphical view]
PANTHER	PTHR10890. PTHR10890. 1 hit.
Pfam	PF01406. tRNA-synt_1e. 1 hit. [Graphical view]
PRINTS	PR00983. TRNASYNTHCYS.
SUPFAM	SSF47323. tRNAsyn_1a_bind. 1 hit.
TIGRFAMs	TIGR00435. cysS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. False negative. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CARS. human.
DrugBank	DB00151. L-Cysteine.
GenomeRNAi	833.
NextBio	3450.
SOURCE	Search...

Entry information

Entry name

SYCC_HUMAN

Accession

Primary (citable) accession number: P49589
Secondary accession number(s): Q53XI8 , Q5HYE4, Q9HD24, Q9HD25

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	January 31, 2002
Last modified:	May 29, 2013
This is version 124 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.