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Q9D0I9

- SYRC_MOUSE

UniProt

Q9D0I9 - SYRC_MOUSE

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Protein

Arginine--tRNA ligase, cytoplasmic

Gene

Rars

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript 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 (By similarity).By similarity

Catalytic activityi

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

GO - Molecular functioni

  1. arginine binding Source: Ensembl
  2. arginine-tRNA ligase activity Source: UniProtKB-EC
  3. ATP binding Source: UniProtKB-KW
  4. tRNA binding Source: Ensembl

GO - Biological processi

  1. arginyl-tRNA aminoacylation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1914297. Rars.

Subcellular locationi

GO - Cellular componenti

  1. aminoacyl-tRNA synthetase multienzyme complex Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
  3. mitochondrion Source: MGI
  4. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 660660Arginine--tRNA ligase, cytoplasmicPRO_0000151659Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9D0I9.
PaxDbiQ9D0I9.
PRIDEiQ9D0I9.

PTM databases

PhosphoSiteiQ9D0I9.

Expressioni

Gene expression databases

BgeeiQ9D0I9.
CleanExiMM_RARS.
ExpressionAtlasiQ9D0I9. baseline and differential.
GenevestigatoriQ9D0I9.

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 (By similarity). Interacts with QARS (By similarity).By similarity

Protein-protein interaction databases

BioGridi222643. 7 interactions.
IntActiQ9D0I9. 4 interactions.
MINTiMINT-1869825.
STRINGi10090.ENSMUSP00000018992.

Structurei

3D structure databases

ProteinModelPortaliQ9D0I9.
SMRiQ9D0I9. Positions 72-660.
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.
HOVERGENiHBG029238.
InParanoidiQ9D0I9.
KOiK01887.
OMAiKCFDILG.
OrthoDBiEOG764725.
PhylomeDBiQ9D0I9.
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]

Sequencei

Sequence statusi: Complete.

Q9D0I9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDGLVAQCSA RLLQQEREIK ALTAEIDRLK NCGCLEASPS LEQLREENLK
60 70 80 90 100
LKYRLNILRR SLQEERRKPT KNMININSRL QEVFGCAIRA AYPDLENPPL
110 120 130 140 150
IVTPSQQPKF GDYQCNSAMG ISQMLKAKEQ KVSPREIAEN ITKHLPNNKY
160 170 180 190 200
IDKVEIAGPG FINVHLRKDF VSEQLTSLLV NGVQLPVLGD KEKVIVDFSS
210 220 230 240 250
PNIAKEMHVG HLRSTIIGES MSRLFEFAGY DVLRLNHVGD WGTQFGMLIA
260 270 280 290 300
HLQDKFPDYL TVSPPIGDLQ AFYKESKKRF DADEEFKKRA YQCVVLLQSK
310 320 330 340 350
NPDIMKAWNL ICDVSREEFK KIYDALDITL IERGESFYQD RMKDIVKEFE
360 370 380 390 400
DKGFVQVDDG RKIVFVPGCS VPLTIVKSDG GYTYDTSDLA AIKQRLFEEK
410 420 430 440 450
ANKIIYVVDN GQAIHFQTIF AAAQMIGWYD PKVTLVTHVG FGVVLGEDKK
460 470 480 490 500
KFKTRSGETV RLMDLLEEGL KRSMDKLKEK ERDKVLTEEE LKAAQTSVAY
510 520 530 540 550
GCIKYADLSH NRLNDYIFSF DKMLDDRGNT AAYLLYAFTR IRSIARLANI
560 570 580 590 600
DEAMLQRAAR ETKIILDHEK EWKLGRCILR FPEILQKILD DLFLHTLCDY
610 620 630 640 650
IYELATTFTE FYDSCYCVEK DRQTGKVLKV NMWRMLLCEA VAAVMAKGFD
660
ILGIKPVQRM
Length:660
Mass (Da):75,674
Last modified:April 16, 2002 - v2
Checksum:i6E8EBCC590FAB81D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51V → M in BAE30955. (PubMed:16141072)Curated
Sequence conflicti178 – 1781L → H in BAB27583. (PubMed:16141072)Curated
Sequence conflicti184 – 1841Q → E in BAE40154. (PubMed:16141072)Curated
Sequence conflicti210 – 2101G → V in BAB27583. (PubMed:16141072)Curated
Sequence conflicti252 – 2521L → M in BAE38569. (PubMed:16141072)Curated
Sequence conflicti281 – 2811D → G in BAE40154. (PubMed:16141072)Curated
Sequence conflicti288 – 2881K → E in BAE40154. (PubMed:16141072)Curated
Sequence conflicti418 – 4181T → I in BAE40154. (PubMed:16141072)Curated
Sequence conflicti474 – 4741M → L in BAB27583. (PubMed:16141072)Curated
Sequence conflicti591 – 5911D → N in BAE38569. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011383 mRNA. Translation: BAB27583.1.
AK076160 mRNA. Translation: BAC36226.1.
AK149856 mRNA. Translation: BAE29127.1.
AK151966 mRNA. Translation: BAE30837.1.
AK152108 mRNA. Translation: BAE30955.1.
AK166097 mRNA. Translation: BAE38569.1.
AK168194 mRNA. Translation: BAE40154.1.
AL596084 Genomic DNA. Translation: CAI24388.1.
CH466658 Genomic DNA. Translation: EDL16275.1.
BC020132 mRNA. Translation: AAH20132.1.
CCDSiCCDS24544.1.
RefSeqiNP_080212.2. NM_025936.3.
UniGeneiMm.284906.

Genome annotation databases

EnsembliENSMUST00000018992; ENSMUSP00000018992; ENSMUSG00000018848.
GeneIDi104458.
KEGGimmu:104458.
UCSCiuc007ilh.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011383 mRNA. Translation: BAB27583.1 .
AK076160 mRNA. Translation: BAC36226.1 .
AK149856 mRNA. Translation: BAE29127.1 .
AK151966 mRNA. Translation: BAE30837.1 .
AK152108 mRNA. Translation: BAE30955.1 .
AK166097 mRNA. Translation: BAE38569.1 .
AK168194 mRNA. Translation: BAE40154.1 .
AL596084 Genomic DNA. Translation: CAI24388.1 .
CH466658 Genomic DNA. Translation: EDL16275.1 .
BC020132 mRNA. Translation: AAH20132.1 .
CCDSi CCDS24544.1.
RefSeqi NP_080212.2. NM_025936.3.
UniGenei Mm.284906.

3D structure databases

ProteinModelPortali Q9D0I9.
SMRi Q9D0I9. Positions 72-660.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 222643. 7 interactions.
IntActi Q9D0I9. 4 interactions.
MINTi MINT-1869825.
STRINGi 10090.ENSMUSP00000018992.

PTM databases

PhosphoSitei Q9D0I9.

Proteomic databases

MaxQBi Q9D0I9.
PaxDbi Q9D0I9.
PRIDEi Q9D0I9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000018992 ; ENSMUSP00000018992 ; ENSMUSG00000018848 .
GeneIDi 104458.
KEGGi mmu:104458.
UCSCi uc007ilh.2. mouse.

Organism-specific databases

CTDi 5917.
MGIi MGI:1914297. Rars.

Phylogenomic databases

eggNOGi COG0018.
GeneTreei ENSGT00530000063407.
HOVERGENi HBG029238.
InParanoidi Q9D0I9.
KOi K01887.
OMAi KCFDILG.
OrthoDBi EOG764725.
PhylomeDBi Q9D0I9.
TreeFami TF106111.

Miscellaneous databases

NextBioi 357144.
PROi Q9D0I9.
SOURCEi Search...

Gene expression databases

Bgeei Q9D0I9.
CleanExi MM_RARS.
ExpressionAtlasi Q9D0I9. baseline and differential.
Genevestigatori Q9D0I9.

Family and domain databases

Gene3Di 1.10.730.10. 1 hit.
3.30.1360.70. 1 hit.
3.40.50.620. 1 hit.
HAMAPi MF_00123. Arg_tRNA_synth.
InterProi IPR001412. 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 ]
PANTHERi PTHR11956. PTHR11956. 1 hit.
Pfami PF03485. Arg_tRNA_synt_N. 1 hit.
PF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view ]
PRINTSi PR01038. TRNASYNTHARG.
SMARTi SM01016. Arg_tRNA_synt_N. 1 hit.
SM00836. DALR_1. 1 hit.
[Graphical view ]
SUPFAMi SSF47323. SSF47323. 1 hit.
SSF55190. SSF55190. 1 hit.
TIGRFAMsi TIGR00456. argS. 1 hit.
PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow macrophage, Embryo, Embryonic head and Lung.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Strain: Czech 2.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiSYRC_MOUSE
AccessioniPrimary (citable) accession number: Q9D0I9
Secondary accession number(s): Q3THP2
, Q3TM73, Q3U8R2, Q3U930, Q5SXA8, Q8VDW1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: April 16, 2002
Last modified: November 26, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3