Reviewed,
UniProtKB/Swiss-Prot Q91WQ3 (SYYC_MOUSE)
Last modified
October 13, 2009.
Version 67.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Tyrosyl-tRNA synthetase, cytoplasmic EC=6.1.1.1 Alternative name(s): Tyrosyl--tRNA ligase Short name=TyrRS | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 528 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
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 By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the class-I aminoacyl-tRNA synthetase family. Contains 1 tRNA-binding domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding RNA-binding tRNA-binding |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| PTM | Acetylation |
| Gene Ontology (GO) | |
| Biological process | tyrosyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW tRNA bindingInferred from electronic annotation. Source: UniProtKB-KW tyrosine-tRNA ligase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 528 | 527 | Tyrosyl-tRNA synthetase, cytoplasmic | PRO_0000055674 | |||||
Regions | |||||||||
| Domain | 364 – 468 | 105 | tRNA-binding | ||||||
| Motif | 44 – 52 | 9 | "HIGH" region | ||||||
| Motif | 222 – 226 | 5 | "KMSKS" region | ||||||
Sites | |||||||||
| Binding site | 39 | 1 | Tyrosine By similarity | ||||||
| Binding site | 166 | 1 | Tyrosine By similarity | ||||||
| Binding site | 170 | 1 | Tyrosine By similarity | ||||||
| Binding site | 173 | 1 | Tyrosine By similarity | ||||||
| Binding site | 188 | 1 | Tyrosine By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylglycine By similarity | ||||||
| Modified residue | 197 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 206 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 272 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 474 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 482 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 490 | 1 | N6-acetyllysine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 11 | 1 | L → M in BAC26120. Ref.1 | ||||||
| Sequence conflict | 29 | 1 | E → K in BAE24073. Ref.1 | ||||||
| Sequence conflict | 195 | 1 | A → S in BAC36424. Ref.1 | ||||||
| Sequence conflict | 294 | 1 | E → Q in BAC36424. Ref.1 | ||||||
| Sequence conflict | 320 | 1 | L → W in BAC36424. Ref.1 | ||||||
| Sequence conflict | 377 | 1 | S → R in BAC36424. Ref.1 | ||||||
Sequences
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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. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Bone marrow, Brain cortex, Egg, Embryo, Skin, Testis and Thymus. |
| [2] | "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: Kidney and Liver. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AK028785 mRNA. Translation: BAC26120.1. AK043837 mRNA. Translation: BAC31674.1. AK076634 mRNA. Translation: BAC36424.1. AK139579 mRNA. Translation: BAE24073.1. AK145356 mRNA. Translation: BAE26384.1. AK151880 mRNA. Translation: BAE30766.1. AK169708 mRNA. Translation: BAE41320.1. BC013552 mRNA. Translation: AAH13552.1. BC022143 mRNA. Translation: AAH22143.1. BC026615 mRNA. Translation: AAH26615.1. | |
| IPI | IPI00314153. |
| RefSeq | NP_598912.3. |
| UniGene | Mm.145488 Mm.410673 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1N3L based on UniProtKB P54577. |
| SMR | Q91WQ3. Positions 3-341, 4-342, 359-527, 360-528. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q91WQ3. |
PTM databases | |
| PhosphoSite | Q91WQ3. |
Proteomic databases | |
| PRIDE | Q91WQ3. |
Genome annotation databases | |
| Ensembl | ENSMUST00000001365; ENSMUSP00000001365; ENSMUSG00000028811; Mus musculus. [Genome view] ENSMUST00000106054; ENSMUSP00000101669; ENSMUSG00000028811; Mus musculus. [Genome view] |
| GeneID | 107271. |
| KEGG | mmu:107271. |
| NMPDR | fig|10090.3.peg.10424. |
| UCSC | uc008uwk.1. mouse. |
Organism-specific databases | |
| CTD | 107271. |
| MGI | MGI:2147627. Yars. |
Phylogenomic databases | |
| HOGENOM | Q91WQ3. |
| HOVERGEN | Q91WQ3. |
Enzyme and pathway databases | |
| BRENDA | 6.1.1.1. 244. |
Gene expression databases | |
| ArrayExpress | Q91WQ3. |
| Bgee | Q91WQ3. |
| CleanEx | MM_YARS. |
| Genevestigator | Q91WQ3. |
| GermOnline | ENSMUSG00000028811. Mus musculus. |
Family and domain databases | |
| InterPro | IPR002305. aa-tRNA-synth_Ib. IPR012340. NA-bd_OB-fold. IPR014729. Rossmann-like_a/b/a_fold. IPR002547. tRNA_bd. IPR015624. Tyr-tRNA-synth_Ib_arc/euk. IPR002307. Tyr-tRNA-synth_Ib_bac/mito. [Graphical view] |
| Gene3D | G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit. G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit. |
| PANTHER | PTHR11946:SF8. Tyr-tRNA_synth. 1 hit. |
| Pfam | PF00579. tRNA-synt_1b. 1 hit. PF01588. tRNA_bind. 1 hit. [Graphical view] |
| PRINTS | PR01040. TRNASYNTHTYR. |
| TIGRFAMs | TIGR00234. tyrS. 1 hit. |
| PROSITE | PS50886. TRBD. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 358652. |
| SOURCE | Search... |
Entry information
| Entry name | SYYC_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q91WQ3 Secondary accession number(s): Q3TEC8 Q8C183 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
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 |

Clusters with


