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A2RTX5 (SYTC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 73. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable threonine--tRNA ligase 2, cytoplasmic

EC=6.1.1.3
Alternative name(s):
Threonyl-tRNA synthetase
Short name=ThrRS
Threonyl-tRNA synthetase-like protein 2
Gene names
Name:TARSL2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length802 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-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr). HAMAP-Rule MF_00184

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00184.

Sequence similarities

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

Sequence caution

The sequence BAB71554.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processthreonyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

threonine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: A2RTX5-1)

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: A2RTX5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     225-319: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 802801Probable threonine--tRNA ligase 2, cytoplasmic HAMAP-Rule MF_00184
PRO_0000333828

Regions

Coiled coil3 – 2321 Potential
Coiled coil76 – 9621 Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.5

Natural variations

Alternative sequence225 – 31995Missing in isoform 2.
VSP_033562

Experimental info

Sequence conflict961A → G in BAB71241. Ref.1
Sequence conflict1661V → A in BAB71241. Ref.1
Sequence conflict2101R → C in BAB71241. Ref.1
Sequence conflict3371I → N in AAH69346. Ref.3
Sequence conflict3371I → N in AAH69811. Ref.3
Sequence conflict5131F → C in BAB71554. Ref.1
Sequence conflict5331R → G in BAB71554. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: EE83EB934B503E59

FASTA80292,646
        10         20         30         40         50         60 
MAAEALAAEA VASRLERQEE DIRWLWSEVE RLRDEQLNAP YSCQAEGPCL TREVAQLRAE 

        70         80         90        100        110        120 
NCDLRHRLCS LRLCLAEERS RQATLESAEL EAAQEAGAQP PPSQSQDKDM KKKKMKESEA 

       130        140        150        160        170        180 
DSEVKHQPIF IKERLKLFEI LKKDHQLLLA IYGKKGDTSN IITVRVADGQ TVQGEVWKTT 

       190        200        210        220        230        240 
PYQVAAEISQ ELAESTVIAK VNGELWDLDR PLEGDSSLEL LTFDNEEAQA VYWHSSAHIL 

       250        260        270        280        290        300 
GEAMELYYGG HLCYGPPIEN GFYYDMFIED RAVSSTELSA LENICKAIIK EKQPFERLEV 

       310        320        330        340        350        360 
SKEILLEMFK YNKFKCRILN EKVNTATTTV YRCGPLIDLC KGPHVRHTGK IKTIKIFKNS 

       370        380        390        400        410        420 
STYWEGNPEM ETLQRIYGIS FPDNKMMRDW EKFQEEAKNR DHRKIGKEQE LFFFHDLSPG 

       430        440        450        460        470        480 
SCFFLPRGAF IYNTLTDFIR EEYHKRDFTE VLSPNMYNSK LWEASGHWQH YSENMFTFEI 

       490        500        510        520        530        540 
EKDTFALKPM NCPGHCLMFA HRPRSWREMP IRFADFGVLH RNELSGTLSG LTRVRRFQQD 

       550        560        570        580        590        600 
DAHIFCTVEQ IEEEIKGCLQ FLQSVYSTFG FSFQLNLSTR PENFLGEIEM WNEAEKQLQN 

       610        620        630        640        650        660 
SLMDFGEPWK MNPGDGAFYG PKIDIKIKDA IGRYHQCATI QLDFQLPIRF NLTYVSKDGD 

       670        680        690        700        710        720 
DKKRPVIIHR AILGSVERMI AILSENYGGK WPFWLSPRQV MVIPVGPTCE KYALQVSSEF 

       730        740        750        760        770        780 
FEEGFMADVD LDHSCTLNKK IRNAQLAQYN FILVVGEKEK IDNAVNVRTR DNKIHGEILV 

       790        800 
TSAIDKLKNL RKTRTLNAEE AF 

« Hide

Isoform 2 [UniParc].

Checksum: 060179AFC7232B3B
Show »

FASTA70781,561

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 315-802 (ISOFORM 1).
Tissue: Cerebellum.
[2]Mural R.J., Istrail S., Sutton G.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. expand/collapse author list , 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].
[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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-802 (ISOFORMS 1/2).
Tissue: Brain and Lung.
[4]"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].
[5]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK056653 mRNA. Translation: BAB71241.1.
AK057734 mRNA. Translation: BAB71554.1. Different initiation.
CH471101 Genomic DNA. Translation: EAX02316.1.
BC069346 mRNA. Translation: AAH69346.1.
BC069811 mRNA. Translation: AAH69811.1.
BC074887 mRNA. Translation: AAH74887.1.
BC132671 mRNA. Translation: AAI32672.1.
BC136315 mRNA. Translation: AAI36316.1.
CCDSCCDS10394.1. [A2RTX5-1]
RefSeqNP_689547.2. NM_152334.2. [A2RTX5-1]
UniGeneHs.657163.

3D structure databases

ProteinModelPortalA2RTX5.
SMRA2RTX5. Positions 162-800.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125822. 1 interaction.
STRING9606.ENSP00000338093.

PTM databases

PhosphoSiteA2RTX5.

Proteomic databases

MaxQBA2RTX5.
PaxDbA2RTX5.
PRIDEA2RTX5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000335968; ENSP00000338093; ENSG00000185418. [A2RTX5-1]
GeneID123283.
KEGGhsa:123283.
UCSCuc002bxm.3. human. [A2RTX5-1]

Organism-specific databases

CTD123283.
GeneCardsGC15M102193.
HGNCHGNC:24728. TARSL2.
neXtProtNX_A2RTX5.
PharmGKBPA128394753.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0441.
HOGENOMHOG000003878.
HOVERGENHBG059513.
InParanoidA2RTX5.
KOK01868.
OMAHFKLQKI.
OrthoDBEOG7JDQX3.
PhylomeDBA2RTX5.
TreeFamTF300858.

Gene expression databases

ArrayExpressA2RTX5.
BgeeA2RTX5.
CleanExHS_TARSL2.
GenevestigatorA2RTX5.

Family and domain databases

Gene3D3.10.20.30. 1 hit.
3.40.50.800. 1 hit.
HAMAPMF_00184. Thr_tRNA_synth.
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR012675. Beta-grasp_dom.
IPR004095. TGS.
IPR012676. TGS-like.
IPR002320. Thr-tRNA-ligase_IIa.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
PfamPF03129. HGTP_anticodon. 1 hit.
PF02824. TGS. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSPR01047. TRNASYNTHTHR.
SMARTSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMSSF52954. SSF52954. 1 hit.
SSF55186. SSF55186. 1 hit.
SSF81271. SSF81271. 1 hit.
TIGRFAMsTIGR00418. thrS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi123283.
NextBio81100.
PROA2RTX5.

Entry information

Entry nameSYTC2_HUMAN
AccessionPrimary (citable) accession number: A2RTX5
Secondary accession number(s): B2RMP7 expand/collapse secondary AC list , Q6B0A1, Q6IS76, Q96LW3, Q96MP4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 6, 2007
Last modified: July 9, 2014
This is version 73 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

SIMILARITY comments

Index of protein domains and families

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries