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Protein

Arginine--tRNA ligase, cytoplasmic

Gene

RARS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis. Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1.1 Publication

Catalytic activityi

ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg).

Kineticsi

  1. KM=3.9 µM for arginine (ATP-PPi exchange at 37 degrees Celsius)1 Publication
  2. KM=3.5 µM for arginine (arginylation at 37 degrees Celsius)1 Publication
  3. KM=1183 µM for ATP (ATP-PPi exchange at 37 Celsius)1 Publication
  4. KM=910 µM for ATP (arginylation at 37 Celsius)1 Publication
  5. KM=0.05 µM for calf liver tRNA-Arg (ATP-PPi exchange at 37 Celsius)1 Publication
  6. KM=0.41 µM for calf liver tRNA-Arg (arginylation at 37 Celsius)1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_15306. Cytosolic tRNA aminoacylation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arginine--tRNA ligase, cytoplasmic (EC:6.1.1.19)
    Alternative name(s):
    Arginyl-tRNA synthetase
    Short name:
    ArgRS
    Gene namesi
    Name:RARS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:9870. RARS.

    Subcellular locationi

    GO - Cellular componenti

    • aminoacyl-tRNA synthetase multienzyme complex Source: Ensembl
    • cytoplasm Source: HPA
    • cytosol Source: Reactome
    • extracellular exosome Source: UniProtKB
    • membrane Source: UniProtKB
    • mitochondrion Source: Ensembl
    • nucleoplasm Source: HPA
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Leukodystrophy, hypomyelinating, 9 (HLD9)1 Publication

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionAn autosomal recessive neurodegenerative disorder characterized by delayed psychomotor development, severe spasticity, nystagmus, and ataxia associated with diffuse hypomyelination apparent on brain MRI.

    See also OMIM:616140
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2 – 21D → G in HLD9. 1 Publication
    VAR_072666
    Natural varianti512 – 5121R → Q in HLD9. 1 Publication
    VAR_072667

    Keywords - Diseasei

    Disease mutation, Leukodystrophy

    Organism-specific databases

    MIMi616140. phenotype.
    PharmGKBiPA34231.

    Polymorphism and mutation databases

    BioMutaiRARS.
    DMDMi20178331.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 660660Arginine--tRNA ligase, cytoplasmicPRO_0000035797Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine3 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP54136.
    PaxDbiP54136.
    PeptideAtlasiP54136.
    PRIDEiP54136.

    PTM databases

    PhosphoSiteiP54136.

    Expressioni

    Gene expression databases

    BgeeiP54136.
    CleanExiHS_RARS.
    ExpressionAtlasiP54136. baseline and differential.
    GenevestigatoriP54136.

    Organism-specific databases

    HPAiHPA003979.
    HPA004130.

    Interactioni

    Subunit structurei

    Interacts (via N-terminus) with AIMP1 (via N-terminus); this stimulates its catalytic activity. Interacts (via N-terminus) with LARS2 (via C-terminus). Monomer; also part of a multisubunit complex that groups tRNA ligases for Arg, Asp, Glu, Gln, Ile, Leu, Lys, Met and Pro. Interacts with QARS.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LARSQ9P2J53EBI-355482,EBI-356077

    Protein-protein interaction databases

    BioGridi111852. 44 interactions.
    IntActiP54136. 8 interactions.
    MINTiMINT-5006018.
    STRINGi9606.ENSP00000231572.

    Structurei

    Secondary structure

    1
    660
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi76 – 9116Combined sources
    Beta strandi102 – 1043Combined sources
    Helixi108 – 1103Combined sources
    Beta strandi112 – 1154Combined sources
    Helixi117 – 1259Combined sources
    Helixi134 – 1429Combined sources
    Beta strandi149 – 1579Combined sources
    Turni158 – 1603Combined sources
    Beta strandi161 – 1666Combined sources
    Helixi168 – 18013Combined sources
    Beta strandi193 – 1975Combined sources
    Helixi209 – 22719Combined sources
    Beta strandi231 – 2366Combined sources
    Beta strandi241 – 2433Combined sources
    Helixi246 – 25510Combined sources
    Turni257 – 2615Combined sources
    Helixi269 – 28214Combined sources
    Helixi284 – 29815Combined sources
    Helixi302 – 32524Combined sources
    Helixi335 – 3384Combined sources
    Helixi339 – 35113Combined sources
    Beta strandi356 – 3583Combined sources
    Beta strandi361 – 3644Combined sources
    Beta strandi373 – 3764Combined sources
    Helixi384 – 39714Combined sources
    Beta strandi402 – 4098Combined sources
    Helixi410 – 4123Combined sources
    Helixi413 – 42513Combined sources
    Turni431 – 4333Combined sources
    Beta strandi434 – 4418Combined sources
    Beta strandi449 – 4513Combined sources
    Turni455 – 4573Combined sources
    Helixi462 – 47716Combined sources
    Turni478 – 4803Combined sources
    Helixi481 – 4833Combined sources
    Turni487 – 4926Combined sources
    Helixi493 – 50816Combined sources
    Beta strandi512 – 5143Combined sources
    Helixi520 – 5245Combined sources
    Beta strandi526 – 5305Combined sources
    Helixi531 – 54616Combined sources
    Turni547 – 5493Combined sources
    Helixi552 – 56110Combined sources
    Helixi569 – 57810Combined sources
    Helixi581 – 59111Combined sources
    Helixi595 – 61218Combined sources
    Beta strandi617 – 6204Combined sources
    Turni622 – 6243Combined sources
    Beta strandi627 – 6293Combined sources
    Helixi632 – 65120Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4Q2TX-ray2.40A/B73-660[»]
    4Q2XX-ray2.80A/B73-660[»]
    4Q2YX-ray2.80A/B73-660[»]
    4R3ZX-ray4.03B1-660[»]
    ProteinModelPortaliP54136.
    SMRiP54136. Positions 2-660.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 7272Could be involved in the assembly of the multisynthetase complexAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi201 – 21212"HIGH" regionAdd
    BLAST

    Domaini

    The N-terminus (AA 1-72) has two regions predicted to be alpha-helical that might be involved in the multisynthetase complex assembly.

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0018.
    GeneTreeiENSGT00530000063407.
    HOGENOMiHOG000247212.
    HOVERGENiHBG029238.
    InParanoidiP54136.
    KOiK01887.
    OMAiLDTHLEF.
    OrthoDBiEOG764725.
    PhylomeDBiP54136.
    TreeFamiTF106111.

    Family and domain databases

    Gene3Di1.10.730.10. 1 hit.
    3.30.1360.70. 1 hit.
    3.40.50.620. 1 hit.
    HAMAPiMF_00123. Arg_tRNA_synth.
    InterProiIPR001412. aa-tRNA-synth_I_CS.
    IPR001278. Arg-tRNA-ligase.
    IPR005148. Arg-tRNA-synth_N.
    IPR008909. DALR_anticod-bd.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR009080. tRNAsynth_1a_anticodon-bd.
    [Graphical view]
    PANTHERiPTHR11956. PTHR11956. 1 hit.
    PfamiPF03485. Arg_tRNA_synt_N. 1 hit.
    PF05746. DALR_1. 1 hit.
    PF00750. tRNA-synt_1d. 1 hit.
    [Graphical view]
    PRINTSiPR01038. TRNASYNTHARG.
    SMARTiSM01016. Arg_tRNA_synt_N. 1 hit.
    SM00836. DALR_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF47323. SSF47323. 1 hit.
    SSF55190. SSF55190. 1 hit.
    TIGRFAMsiTIGR00456. argS. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

    Isoform Complexed (identifier: P54136-1) [UniParc]FASTAAdd to basket

    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.

    « Hide

            10         20         30         40         50
    MDVLVSECSA RLLQQEEEIK SLTAEIDRLK NCGCLGASPN LEQLQEENLK
    60 70 80 90 100
    LKYRLNILRK SLQAERNKPT KNMINIISRL QEVFGHAIKA AYPDLENPPL
    110 120 130 140 150
    LVTPSQQAKF GDYQCNSAMG ISQMLKTKEQ KVNPREIAEN ITKHLPDNEC
    160 170 180 190 200
    IEKVEIAGPG FINVHLRKDF VSEQLTSLLV NGVQLPALGE NKKVIVDFSS
    210 220 230 240 250
    PNIAKEMHVG HLRSTIIGES ISRLFEFAGY DVLRLNHVGD WGTQFGMLIA
    260 270 280 290 300
    HLQDKFPDYL TVSPPIGDLQ VFYKESKKRF DTEEEFKKRA YQCVVLLQGK
    310 320 330 340 350
    NPDITKAWKL ICDVSRQELN KIYDALDVSL IERGESFYQD RMNDIVKEFE
    360 370 380 390 400
    DRGFVQVDDG RKIVFVPGCS IPLTIVKSDG GYTYDTSDLA AIKQRLFEEK
    410 420 430 440 450
    ADMIIYVVDN GQSVHFQTIF AAAQMIGWYD PKVTRVFHAG FGVVLGEDKK
    460 470 480 490 500
    KFKTRSGETV RLMDLLGEGL KRSMDKLKEK ERDKVLTAEE LNAAQTSVAY
    510 520 530 540 550
    GCIKYADLSH NRLNDYIFSF DKMLDDRGNT AAYLLYAFTR IRSIARLANI
    560 570 580 590 600
    DEEMLQKAAR ETKILLDHEK EWKLGRCILR FPEILQKILD DLFLHTLCDY
    610 620 630 640 650
    IYELATAFTE FYDSCYCVEK DRQTGKILKV NMWRMLLCEA VAAVMAKGFD
    660
    ILGIKPVQRM
    Length:660
    Mass (Da):75,379
    Last modified:April 16, 2002 - v2
    Checksum:iFE9FB5C910709956
    GO
    Isoform Monomeric (identifier: P54136-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-72: Missing.

    Show »
    Length:588
    Mass (Da):67,140
    Checksum:i857EA1F69F3B6A3B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti39 – 391P → S in AAB35627 (PubMed:7590355).Curated
    Sequence conflicti130 – 1312QK → PE in AAB35627 (PubMed:7590355).Curated
    Sequence conflicti135 – 1373REI → GEF in AAB35627 (PubMed:7590355).Curated
    Sequence conflicti147 – 15610DNECIEKVEI → AMDVLKRVEF in AAB35627 (PubMed:7590355).Curated
    Sequence conflicti164 – 1641V → G in AAB35627 (PubMed:7590355).Curated
    Sequence conflicti278 – 2781K → N in BAG37326 (PubMed:14702039).Curated
    Sequence conflicti308 – 3125WKLIC → YLLMS in AAB35627 (PubMed:7590355).Curated
    Sequence conflicti341 – 3411R → G in BAD96517 (Ref. 4) Curated
    Sequence conflicti358 – 3581D → G in BAG37326 (PubMed:14702039).Curated
    Sequence conflicti487 – 4871T → A in BAD96517 (Ref. 4) Curated
    Sequence conflicti567 – 5671D → V in AAB35627 (PubMed:7590355).Curated
    Sequence conflicti635 – 6406MLLCEA → ILCET in AAB35627 (PubMed:7590355).Curated
    Sequence conflicti651 – 6511I → T in AAB35627 (PubMed:7590355).Curated
    Sequence conflicti657 – 6604VQRM → GPRV in AAB35627 (PubMed:7590355).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2 – 21D → G in HLD9. 1 Publication
    VAR_072666
    Natural varianti3 – 31V → I.
    Corresponds to variant rs244903 [ dbSNP | Ensembl ].
    VAR_020106
    Natural varianti135 – 1351R → G.
    Corresponds to variant rs1059443 [ dbSNP | Ensembl ].
    VAR_052635
    Natural varianti397 – 3971F → Y.
    Corresponds to variant rs2305734 [ dbSNP | Ensembl ].
    VAR_020107
    Natural varianti512 – 5121R → Q in HLD9. 1 Publication
    VAR_072667

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7272Missing in isoform Monomeric. CuratedVSP_018905Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    S80343 mRNA. Translation: AAB35627.1.
    BT007394 mRNA. Translation: AAP36058.1.
    AK314795 mRNA. Translation: BAG37326.1.
    AK222797 mRNA. Translation: BAD96517.1.
    BC000528 mRNA. Translation: AAH00528.1.
    BC014619 mRNA. Translation: AAH14619.1.
    CCDSiCCDS4367.1. [P54136-1]
    PIRiJC4365.
    RefSeqiNP_002878.2. NM_002887.3. [P54136-1]
    UniGeneiHs.654907.

    Genome annotation databases

    EnsembliENST00000231572; ENSP00000231572; ENSG00000113643. [P54136-1]
    GeneIDi5917.
    KEGGihsa:5917.
    UCSCiuc003lzx.3. human. [P54136-1]

    Keywords - Coding sequence diversityi

    Alternative initiation, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    S80343 mRNA. Translation: AAB35627.1.
    BT007394 mRNA. Translation: AAP36058.1.
    AK314795 mRNA. Translation: BAG37326.1.
    AK222797 mRNA. Translation: BAD96517.1.
    BC000528 mRNA. Translation: AAH00528.1.
    BC014619 mRNA. Translation: AAH14619.1.
    CCDSiCCDS4367.1. [P54136-1]
    PIRiJC4365.
    RefSeqiNP_002878.2. NM_002887.3. [P54136-1]
    UniGeneiHs.654907.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4Q2TX-ray2.40A/B73-660[»]
    4Q2XX-ray2.80A/B73-660[»]
    4Q2YX-ray2.80A/B73-660[»]
    4R3ZX-ray4.03B1-660[»]
    ProteinModelPortaliP54136.
    SMRiP54136. Positions 2-660.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi111852. 44 interactions.
    IntActiP54136. 8 interactions.
    MINTiMINT-5006018.
    STRINGi9606.ENSP00000231572.

    Chemistry

    BindingDBiP54136.
    ChEMBLiCHEMBL2824.

    PTM databases

    PhosphoSiteiP54136.

    Polymorphism and mutation databases

    BioMutaiRARS.
    DMDMi20178331.

    Proteomic databases

    MaxQBiP54136.
    PaxDbiP54136.
    PeptideAtlasiP54136.
    PRIDEiP54136.

    Protocols and materials databases

    DNASUi5917.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000231572; ENSP00000231572; ENSG00000113643. [P54136-1]
    GeneIDi5917.
    KEGGihsa:5917.
    UCSCiuc003lzx.3. human. [P54136-1]

    Organism-specific databases

    CTDi5917.
    GeneCardsiGC05P167913.
    HGNCiHGNC:9870. RARS.
    HPAiHPA003979.
    HPA004130.
    MIMi107820. gene.
    616140. phenotype.
    neXtProtiNX_P54136.
    PharmGKBiPA34231.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0018.
    GeneTreeiENSGT00530000063407.
    HOGENOMiHOG000247212.
    HOVERGENiHBG029238.
    InParanoidiP54136.
    KOiK01887.
    OMAiLDTHLEF.
    OrthoDBiEOG764725.
    PhylomeDBiP54136.
    TreeFamiTF106111.

    Enzyme and pathway databases

    ReactomeiREACT_15306. Cytosolic tRNA aminoacylation.

    Miscellaneous databases

    ChiTaRSiRARS. human.
    GeneWikiiRARS_(gene).
    GenomeRNAii5917.
    NextBioi23038.
    PROiP54136.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP54136.
    CleanExiHS_RARS.
    ExpressionAtlasiP54136. baseline and differential.
    GenevestigatoriP54136.

    Family and domain databases

    Gene3Di1.10.730.10. 1 hit.
    3.30.1360.70. 1 hit.
    3.40.50.620. 1 hit.
    HAMAPiMF_00123. Arg_tRNA_synth.
    InterProiIPR001412. aa-tRNA-synth_I_CS.
    IPR001278. Arg-tRNA-ligase.
    IPR005148. Arg-tRNA-synth_N.
    IPR008909. DALR_anticod-bd.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR009080. tRNAsynth_1a_anticodon-bd.
    [Graphical view]
    PANTHERiPTHR11956. PTHR11956. 1 hit.
    PfamiPF03485. Arg_tRNA_synt_N. 1 hit.
    PF05746. DALR_1. 1 hit.
    PF00750. tRNA-synt_1d. 1 hit.
    [Graphical view]
    PRINTSiPR01038. TRNASYNTHARG.
    SMARTiSM01016. Arg_tRNA_synt_N. 1 hit.
    SM00836. DALR_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF47323. SSF47323. 1 hit.
    SSF55190. SSF55190. 1 hit.
    TIGRFAMsiTIGR00456. argS. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning and characterization of cDNA encoding a human arginyl-tRNA synthetase."
      Girjes A.A., Hobson K., Chen P., Lavin M.F.
      Gene 164:347-350(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "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.
      , 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].
    4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Liver.
    5. "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].
      Tissue: Muscle.
    6. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-11.
      Tissue: Platelet.
    7. "Precursor of pro-apoptotic cytokine modulates aminoacylation activity of tRNA synthetase."
      Park S.G., Jung K.H., Lee J.S., Jo Y.J., Motegi H., Kim S., Shiba K.
      J. Biol. Chem. 274:16673-16676(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AIMP1.
    8. "The C-terminal appended domain of human cytosolic leucyl-tRNA synthetase is indispensable in its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex."
      Ling C., Yao Y.N., Zheng Y.G., Wei H., Wang L., Wu X.F., Wang E.D.
      J. Biol. Chem. 280:34755-34763(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, INTERACTION WITH LARS2.
    9. "Two forms of human cytoplasmic arginyl-tRNA synthetase produced from two translation initiations by a single mRNA."
      Zheng Y.-G., Wei H., Ling C., Xu M.-G., Wang E.-D.
      Biochemistry 45:1338-1344(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, ALTERNATIVE INITIATION.
    10. "Proteasomes and RARS modulate AIMP1/EMAP II secretion in human cancer cell lines."
      Bottoni A., Vignali C., Piccin D., Tagliati F., Luchin A., Zatelli M.C., Uberti E.C.
      J. Cell. Physiol. 212:293-297(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH AIMP1.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Mutations in QARS, encoding glutaminyl-tRNA synthetase, cause progressive microcephaly, cerebral-cerebellar atrophy, and intractable seizures."
      Zhang X., Ling J., Barcia G., Jing L., Wu J., Barry B.J., Mochida G.H., Hill R.S., Weimer J.M., Stein Q., Poduri A., Partlow J.N., Ville D., Dulac O., Yu T.W., Lam A.T., Servattalab S., Rodriguez J.
      , Boddaert N., Munnich A., Colleaux L., Zon L.I., Soll D., Walsh C.A., Nabbout R.
      Am. J. Hum. Genet. 94:547-558(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH QARS.
    17. Cited for: INVOLVEMENT IN HLD9, VARIANTS HLD9 GLY-2 AND GLN-512.
    18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiSYRC_HUMAN
    AccessioniPrimary (citable) accession number: P54136
    Secondary accession number(s): B2RBS9, Q53GY4, Q9BWA1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: April 16, 2002
    Last modified: May 27, 2015
    This is version 154 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.