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Q9HA77 (SYCM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable cysteine--tRNA ligase, mitochondrial

EC=6.1.1.16
Alternative name(s):
Cysteinyl-tRNA synthetase
Short name=CysRS
Gene names
Name:CARS2
ORF Names:OK/SW-cl.10
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length564 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).

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

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

Sequence caution

The sequence BAB93499.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcysteinyl-tRNA aminoacylation

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular componentcytosol

Inferred from Biological aspect of Ancestor. Source: RefGenome

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cysteine-tRNA ligase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 564Probable cysteine--tRNA ligase, mitochondrialPRO_0000250741

Regions

Motif80 – 9011"HIGH" region
Motif317 – 3215"KMSKS" region

Sites

Metal binding781Zinc By similarity
Metal binding2571Zinc By similarity
Metal binding2821Zinc By similarity
Metal binding2861Zinc By similarity
Binding site3201ATP By similarity

Amino acid modifications

Modified residue3291N6-acetyllysine Ref.6

Natural variations

Natural variant4401E → K.
Corresponds to variant rs965189 [ dbSNP | Ensembl ].
VAR_034523
Natural variant5551Q → P. Ref.3
Corresponds to variant rs1043886 [ dbSNP | Ensembl ].
VAR_034524

Experimental info

Sequence conflict182 – 20221RGNAY…KSRGD → SWERLFNGKRQCLLRSESLE ET in BAB93499. Ref.4
Sequence conflict207 – 22317LVGVV…ADSDK → IGRRGPWSSPETSGLLTS in BAB93499. Ref.4
Sequence conflict2271S → N in BAB93499. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9HA77 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 92F8B615E6657D50

FASTA56462,224
        10         20         30         40         50         60 
MLRTTRGPGL GPPLLQAALG LGRAGWHWPA GRAASGGRGR AWLQPTGRET GVQVYNSLTG 

        70         80         90        100        110        120 
RKEPLIVAHA EAASWYSCGP TVYDHAHLGH ACSYVRFDII RRILTKVFGC SIVMVMGITD 

       130        140        150        160        170        180 
VDDKIIKRAN EMNISPASLA SLYEEDFKQD MAALKVLPPT VYLRVTENIP QIISFIEGII 

       190        200        210        220        230        240 
ARGNAYSTAK GNVYFDLKSR GDKYGKLVGV VPGPVGEPAD SDKRHASDFA LWKAAKPQEV 

       250        260        270        280        290        300 
FWASPWGPGR PGWHIECSAI ASMVFGSQLD IHSGGIDLAF PHHENEIAQC EVFHQCEQWG 

       310        320        330        340        350        360 
NYFLHSGHLH AKGKEEKMSK SLKNYITIKD FLKTFSPDVF RFFCLRSSYR SAIDYSDSAM 

       370        380        390        400        410        420 
LQAQQLLLGL GSFLEDARAY MKGQLACGSV REAMLWERLS STKRAVKAAL ADDFDTPRVV 

       430        440        450        460        470        480 
DAILGLAHHG NGQLRASLKE PEGPRSPAVF GAIISYFEQF FETVGISLAN QQYVSGDGSE 

       490        500        510        520        530        540 
ATLHGVVDEL VRFRQKVRQF ALAMPEATGD ARRQQLLERQ PLLEACDTLR RGLTAHGINI 

       550        560 
KDRSSTTSTW ELLDQRTKDQ KSAG 

« Hide

References

« Hide 'large scale' references
[1]"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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary gland.
[2]"The DNA sequence and analysis of human chromosome 13."
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
Nature 428:522-528(2004) [PubMed: 15057823] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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], VARIANT PRO-555.
Tissue: Lung.
[4]"Identification of immuno-peptidmics that recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
Shichijo S., Itoh K.
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-564.
Tissue: Colon adenocarcinoma.
[5]"Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS."
Bonnefond L., Fender A., Rudinger-Thirion J., Giege R., Florentz C., Sissler M.
Biochemistry 44:4805-4816(2005) [PubMed: 15779907] [Abstract]
Cited for: IDENTIFICATION.
[6]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-329, MASS SPECTROMETRY.
[7]"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: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK022180 mRNA. Translation: BAB13978.1.
AL157820, AL139385 Genomic DNA. Translation: CAI16971.1.
AL139385, AL157820 Genomic DNA. Translation: CAI17004.1.
BC007220 mRNA. Translation: AAH07220.1.
AB062436 mRNA. Translation: BAB93499.1. Different initiation.
IPIIPI00336016.
RefSeqNP_078813.1. NM_024537.2.
UniGeneHs.508725.

3D structure databases

HSSPHSSP built from PDB template 1LI5 based on UniProtKB P21888.
ProteinModelPortalQ9HA77.
SMRQ9HA77. Positions 51-552.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9HA77. 1 interaction.
STRINGQ9HA77.

PTM databases

PhosphoSiteQ9HA77.

Polymorphism databases

DMDM74761587.

Proteomic databases

PeptideAtlasQ9HA77.
PRIDEQ9HA77.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000257347; ENSP00000257347; ENSG00000134905.
GeneID79587.
KEGGhsa:79587.
NMPDRfig|9606.3.peg.9087.
UCSCuc001vrd.1. human.

Organism-specific databases

CTD79587.
GeneCardsGC13M111293.
HGNCHGNC:25695. CARS2.
MIM612800. gene.
neXtProtNX_Q9HA77.
PharmGKBPA162381083.
GenAtlasSearch...

Phylogenomic databases

GeneTreeENSGT00390000006347.
HOGENOMHBG327651.
HOVERGENHBG094012.
InParanoidQ9HA77.
OMAYEEDFKQ.
OrthoDBEOG4B8JCV.
PhylomeDBQ9HA77.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ9HA77.
BgeeQ9HA77.
CleanExHS_CARS2.
GenevestigatorQ9HA77.
GermOnlineENSG00000134905. Homo sapiens.

Family and domain databases

InterProIPR015803. Cys-tRNA-synt.
IPR024909. Cys-tRNA/MSH_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
KOK01883.
PANTHERPTHR10890. Cys_tRNA-synt_1a. 1 hit.
PfamPF01406. tRNA-synt_1e. 1 hit.
[Graphical view]
PRINTSPR00983. TRNASYNTHCYS.
SUPFAMSSF47323. tRNAsyn_1a_bind. 1 hit.
TIGRFAMsTIGR00435. CysS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]
ProtoNetSearch...

Other

DrugBankDB00151. L-Cysteine.
NextBio68590.
SOURCESearch...

Entry information

Entry nameSYCM_HUMAN
AccessionPrimary (citable) accession number: Q9HA77
Secondary accession number(s): Q8NI84, Q96IV4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: March 1, 2001
Last modified: January 25, 2012
This is version 94 of the entry and version 1 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

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families