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Reviewed, UniProtKB/Swiss-Prot Q9Y2Z4 (SYYM_HUMAN)

Last modified July 7, 2009. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Tyrosyl-tRNA synthetase, mitochondrial
    EC=6.1.1.1
Alternative name(s):
    Tyrosine--tRNA ligase
      Short name=TyrRS
Gene names
Name: YARS2
ORF Names: CGI-04
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length477 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr) By similarity.

Catalytic activity

ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr).

Subunit structure

Homodimer. Ref.4

Subcellular location

Mitochondrion matrix. Ref.4

Sequence similarities

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

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Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processtyrosyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction. Source: IntAct

tyrosine-tRNA ligase activity Ref.1

Non-traceable author statement. Source: UniProtKB

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

CDC20Q128341EBI-1049286,EBI-367462

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1616Mitochondrion Potential
Chain17 – 477461Tyrosyl-tRNA synthetase, mitochondrial
PRO_0000035830

Regions

Motif82 – 9110"HIGH" region
Motif281 – 2855"KMSKS" region

Sites

Binding site2841ATP By similarity

Amino acid modifications

Modified residue4261Phosphotyrosine Ref.5
Modified residue4351Phosphoserine Ref.5

Natural variations

Natural variant1911G → V: dbSNP rs11539445. Ref.1
VAR_034534

Experimental info

Sequence conflict1 – 44MAAP → MGA Ref.1
Sequence conflict1181R → A in AAD27714. Ref.1
Sequence conflict2721P → T in AAD27714. Ref.1
Sequence conflict3111D → E in AAD27714. Ref.1

Secondary structure

1 ................................................... 477
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q9Y2Z4-1 [UniParc].

Last modified July 19, 2004. Version 2.
Checksum: C513B8FE1E7A09E4

FASTA47753,199
        10         20         30         40         50         60 
MAAPILRSFS WGRWSGTLNL SVLLPLGLRK AHSGAQGLLA AQKARGLFKD FFPETGTKIE 

        70         80         90        100        110        120 
LPELFDRGTA SFPQTIYCGF DPTADSLHVG HLLALLGLFH LQRAGHNVIA LVGGATARLG 

       130        140        150        160        170        180 
DPSGRTKERE ALETERVRAN ARALRLGLEA LAANHQQLFT DGRSWGSFTV LDNSAWYQKQ 

       190        200        210        220        230        240 
HLVDFLAAVG GHFRMGTLLS RQSVQLRLKS PEGMSLAEFF YQVLQAYDFY YLFQRYGCRV 

       250        260        270        280        290        300 
QLGGSDQLGN IMSGYEFINK LTGEDVFGIT VPLITSTTGA KLGKSAGNAV WLNRDKTSPF 

       310        320        330        340        350        360 
ELYQFFVRQP DDSVERYLKL FTFLPLPEID HIMQLHVKEP ERRGPQKRLA AEVTKLVHGR 

       370        380        390        400        410        420 
EGLDSAKRCT QALYHSSIDA LEVMSDQELK ELFKEAPFSE FFLDPGTSVL DTCRKANAIP 

       430        440        450        460        470 
DGPRGYRMIT EGGVSINHQQ VTNPESVLIV GQHILKNGLS LLKIGKRNFY IIKWLQL

« Hide

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References

« Hide 'large scale' references
[1]"Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
Genome Res. 10:703-713(2000) [PubMed: 10810093] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-191.
[2]"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].
[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].
Tissue: Eye.
[4]"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: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
[5]"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.
Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-426 AND SER-435, MASS SPECTROMETRY.
[6]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AF132939 mRNA. Translation: AAD27714.1.
AK024057 mRNA. Translation: BAB14806.1.
BC015625 mRNA. Translation: AAH15625.1.
IPIIPI00165092.
RefSeqNP_001035526.1.
UniGeneHs.505231

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2PIDX-ray2.20A/B32-375[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ9Y2Z4. 1 interaction.

PTM databases

PhosphoSiteQ9Y2Z4.

Proteomic databases

PeptideAtlasQ9Y2Z4.
PRIDEQ9Y2Z4.

Genome annotation databases

EnsemblENSG00000139131. Homo sapiens. [Contig view]
GeneID51067.
KEGGhsa:51067.
NMPDRfig|9606.3.peg.7381.
UCSCuc001rli.1. human.

Organism-specific databases

GeneCardsGC12M032789.
HGNCHGNC:24249. YARS2.
MIM610957. gene.
PharmGKBPA142670559.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ9Y2Z4.
HOVERGENQ9Y2Z4.
OMAQ9Y2Z4. TFYIGFD.

Enzyme and pathway databases

BRENDA6.1.1.1. 247.
ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ9Y2Z4.
BgeeQ9Y2Z4.
CleanExHS_YARS2.
GermOnlineENSG00000139131. Homo sapiens.

Family and domain databases

InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ib.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002307. Tyr-tRNA-synth_Ib_bac/mito.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHERPTHR11766. Tyr_tRNA-synt_1b. 1 hit.
PfamPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PRINTSPR01040. TRNASYNTHTYR.
TIGRFAMsTIGR00234. tyrS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00135. L-Tyrosine.
NextBio53667.
SOURCESearch...

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Entry information

Entry nameSYYM_HUMAN
AccessionPrimary (citable) accession number: Q9Y2Z4
Secondary accession number(s): Q9H817
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: July 7, 2009
This is version 63 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Human chromosome 12

Human chromosome 12: 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents