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Q8BYM8 (SYCM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length551 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 BAC30187.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 551Probable cysteine--tRNA ligase, mitochondrialPRO_0000250739

Regions

Motif65 – 7511"HIGH" region
Motif302 – 3065"KMSKS" region

Sites

Metal binding631Zinc By similarity
Metal binding2421Zinc By similarity
Metal binding2671Zinc By similarity
Metal binding2711Zinc By similarity
Binding site3051ATP By similarity

Amino acid modifications

Modified residue3141N6-acetyllysine By similarity

Experimental info

Sequence conflict2031P → PA in BAB26596. Ref.1
Sequence conflict4391I → T in BAB26596. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8BYM8 [UniParc].

Last modified October 3, 2006. Version 2.
Checksum: E71AAB981EE23013

FASTA55161,272
        10         20         30         40         50         60 
MLRARGPGPG ALLLRAALGL GRRGRSWQRP QGQDTGVQVH NSLTGRKEPL IVARSDAVSW 

        70         80         90        100        110        120 
YSCGPTVYDH AHLGHACSYV RFDIIRRILT RVFGCNVVMA MSITDVDDKI IKRANEMNVT 

       130        140        150        160        170        180 
PASLASLFEE EFKQDMAALK VLPPTVYLRV TENIPQIIAF IEGIIAHGHA YSTATGSVYF 

       190        200        210        220        230        240 
DLHARGDKYG KLVNTVPSAT AEPGDSDKRH SSDFALWKAA KPQEVFWASP WGDGRPGWHI 

       250        260        270        280        290        300 
ECSTMASEVF GSHLDIHTGG IDLAFPHHEN EIAQSEVFHQ CQQWGNYFLH SGHLHVKGTE 

       310        320        330        340        350        360 
EKMSKSLKNY ITIKDFLKTF SPDVFRLFCL RTNYRSAIEY SDSTLVEAKH LLLGLASFVE 

       370        380        390        400        410        420 
DARAYVKGQL TCGPVEEDVL WERLTSTKKA VKAALANDFD TPRAVNTILD LVHHANRQLR 

       430        440        450        460        470        480 
AVSKEASGPR SPTVFGAIIS YVEQFFETVG ISLANRQCVS GDSSTVTLRC VVDELVRFRL 

       490        500        510        520        530        540 
KVRQYALDTP GAAGEARKRQ LQERQPLLEA CDTLRQDLVT HGINVKDRGS AASTWELLDP 

       550 
RTRHQKPGDR G

« Hide

References

[1]"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. expand/collapse author list , 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].
Strain: C57BL/6J.
Tissue: Hypothalamus and Tongue.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK009937 mRNA. Translation: BAB26596.1.
AK038968 mRNA. Translation: BAC30187.1. Different initiation.
IPIIPI00896595.
RefSeqNP_077210.1. NM_024248.1.
UniGeneMm.196576.

3D structure databases

HSSPHSSP built from PDB template 1LI5 based on UniProtKB P21888.
ProteinModelPortalQ8BYM8.
SMRQ8BYM8. Positions 36-537.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8BYM8.

PTM databases

PhosphoSiteQ8BYM8.

Proteomic databases

PRIDEQ8BYM8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID71941.
KEGGmmu:71941.
UCSCuc009kvh.2. mouse.

Organism-specific databases

CTD79587.
MGIMGI:1919191. Cars2.

Phylogenomic databases

GeneTreeENSGT00390000006347.
HOGENOMHBG327651.
HOVERGENHBG094012.
InParanoidQ8BYM8.
OMAYEEDFKQ.
OrthoDBEOG4B8JCV.
PhylomeDBQ8BYM8.

Gene expression databases

ArrayExpressQ8BYM8.
BgeeQ8BYM8.
GenevestigatorQ8BYM8.
GermOnlineENSMUSG00000056228. Mus musculus.

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

SOURCESearch...

Entry information

Entry nameSYCM_MOUSE
AccessionPrimary (citable) accession number: Q8BYM8
Secondary accession number(s): Q9D6U9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 3, 2006
Last modified: January 25, 2012
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents