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Protein

Probable arginine--tRNA ligase, mitochondrial

Gene

Rars2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

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

Names & Taxonomyi

Protein namesi
Recommended name:
Probable arginine--tRNA ligase, mitochondrial (EC:6.1.1.19)
Alternative name(s):
Arginyl-tRNA synthetase
Short name:
ArgRS
Gene namesi
Name:Rars2
Synonyms:Rarsl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1923596. Rars2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1616MitochondrionSequence AnalysisAdd
BLAST
Chaini17 – 578562Probable arginine--tRNA ligase, mitochondrialPRO_0000250732Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei568 – 5681N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ3U186.
PaxDbiQ3U186.
PRIDEiQ3U186.

PTM databases

PhosphoSiteiQ3U186.

Expressioni

Gene expression databases

BgeeiQ3U186.
ExpressionAtlasiQ3U186. baseline and differential.
GenevisibleiQ3U186. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000029968.

Structurei

3D structure databases

ProteinModelPortaliQ3U186.
SMRiQ3U186. Positions 31-578.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi133 – 14412"HIGH" regionAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0018.
GeneTreeiENSGT00530000063407.
HOGENOMiHOG000247211.
HOVERGENiHBG057355.
InParanoidiQ3U186.
KOiK01887.
OMAiACNKNEP.
OrthoDBiEOG7DNNTT.
PhylomeDBiQ3U186.
TreeFamiTF300888.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.30.1360.70. 1 hit.
3.40.50.620. 1 hit.
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.
PfamiPF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view]
PRINTSiPR01038. TRNASYNTHARG.
SMARTiSM00836. 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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q3U186-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MACGFRRSIA CQLSRVLALP PESLIKSISA VPVSKKEEVA DFQLSVDSLL
60 70 80 90 100
EDNNHKSQVD TQDQARRLAE KLKCDTVVTA ISAGPRTLNF KINRELLTKA
110 120 130 140 150
VLQQVTEDGC KYGLKSELFS DLPKKRIVVE FSSPNIAKKF HVGHLRSTII
160 170 180 190 200
GNFIANLKEA LGHQVTRINY IGDWGMQFGL LGTGFQLFGY EEKLQTNPLQ
210 220 230 240 250
HLFDVYVQVN KEATDDKNVT KLAHEFFHRL EMGDTQALSL WQRFRDLSIE
260 270 280 290 300
EYTQIYKRLG IYFDEYSGES FYREKSQDVL KLLDSKGLLQ KTAEGNVVVD
310 320 330 340 350
LSGTGDLSSV CTVMRSDGTS LYATRDLAAA IHRMDKYNFD TMIYVADKGQ
360 370 380 390 400
RRHFQQVFQM LKIMGYDWAE RCQHVPFGIV KGMKTRRGGV TFLEDVLNEV
410 420 430 440 450
QSRMLQNMAS IKTTKQLENP QETAERVGLA AVIIQDFRGT LLSDYQFSWD
460 470 480 490 500
RVFQSRGDTG VFLQYTHARL CSLEETFGCG YLNDSNVACL QEPQSVSILQ
510 520 530 540 550
HLLRFDEVLY LSSQDLQPKH IVSYLLTLSH LAAVAHKTLQ VKDSPPDVAG
560 570
ARLHLFKAVR SVLANGMKLL GITPVCRM
Length:578
Mass (Da):65,336
Last modified:October 11, 2005 - v1
Checksum:i5255FAFA8F873C27
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti306 – 3061D → G in AAH24878 (PubMed:15489334).Curated
Sequence conflicti540 – 5401Q → K in AAH24878 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK156182 mRNA. Translation: BAE33614.1.
BC024878 mRNA. Translation: AAH24878.1.
CCDSiCCDS18029.1.
RefSeqiNP_852071.2. NM_181406.3.
UniGeneiMm.22363.

Genome annotation databases

EnsembliENSMUST00000029968; ENSMUSP00000029968; ENSMUSG00000028292.
GeneIDi109093.
KEGGimmu:109093.
UCSCiuc008sgf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK156182 mRNA. Translation: BAE33614.1.
BC024878 mRNA. Translation: AAH24878.1.
CCDSiCCDS18029.1.
RefSeqiNP_852071.2. NM_181406.3.
UniGeneiMm.22363.

3D structure databases

ProteinModelPortaliQ3U186.
SMRiQ3U186. Positions 31-578.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000029968.

PTM databases

PhosphoSiteiQ3U186.

Proteomic databases

MaxQBiQ3U186.
PaxDbiQ3U186.
PRIDEiQ3U186.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029968; ENSMUSP00000029968; ENSMUSG00000028292.
GeneIDi109093.
KEGGimmu:109093.
UCSCiuc008sgf.2. mouse.

Organism-specific databases

CTDi57038.
MGIiMGI:1923596. Rars2.

Phylogenomic databases

eggNOGiCOG0018.
GeneTreeiENSGT00530000063407.
HOGENOMiHOG000247211.
HOVERGENiHBG057355.
InParanoidiQ3U186.
KOiK01887.
OMAiACNKNEP.
OrthoDBiEOG7DNNTT.
PhylomeDBiQ3U186.
TreeFamiTF300888.

Miscellaneous databases

NextBioi361640.
PROiQ3U186.
SOURCEiSearch...

Gene expression databases

BgeeiQ3U186.
ExpressionAtlasiQ3U186. baseline and differential.
GenevisibleiQ3U186. MM.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.30.1360.70. 1 hit.
3.40.50.620. 1 hit.
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.
PfamiPF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view]
PRINTSiPR01038. TRNASYNTHARG.
SMARTiSM00836. 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

  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: NOD.
    Tissue: Spleen.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II.
    Tissue: Mammary gland.
  3. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-568, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSYRM_MOUSE
AccessioniPrimary (citable) accession number: Q3U186
Secondary accession number(s): Q8QZU7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 11, 2005
Last modified: June 24, 2015
This is version 80 of the entry and version 1 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

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.