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P54136 (SYRC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arginine--tRNA ligase, cytoplasmic

EC=6.1.1.19
Alternative name(s):
Arginyl-tRNA synthetase
Short name=ArgRS
Gene names
Name:RARS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length660 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10

Catalytic activity

ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg). HAMAP-Rule MF_00123

Subunit structure

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. Ref.7 Ref.8 Ref.10

Subcellular location

Cytoplasm Ref.8 Ref.9.

Domain

The N-terminus (AA 1-72) has two regions predicted to be alpha-helical that might be involved in the multisynthetase complex assembly. HAMAP-Rule MF_00123

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=3.9 µM for arginine (ATP-PPi exchange at 37 degrees Celsius) Ref.8

KM=3.5 µM for arginine (arginylation at 37 degrees Celsius)

KM=1183 µM for ATP (ATP-PPi exchange at 37 Celsius)

KM=910 µM for ATP (arginylation at 37 Celsius)

KM=0.05 µM for calf liver tRNA-Arg (ATP-PPi exchange at 37 Celsius)

KM=0.41 µM for calf liver tRNA-Arg (arginylation at 37 Celsius)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LARSQ9P2J53EBI-355482,EBI-356077

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform Complexed (identifier: P54136-1)

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.
Isoform Monomeric (identifier: P54136-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 660660Arginine--tRNA ligase, cytoplasmic HAMAP-Rule MF_00123
PRO_0000035797

Regions

Region1 – 7272Could be involved in the assembly of the multisynthetase complex HAMAP-Rule MF_00123
Motif201 – 21212"HIGH" region HAMAP-Rule MF_00123

Amino acid modifications

Modified residue11N-acetylmethionine Ref.11 Ref.14 Ref.15

Natural variations

Alternative sequence1 – 7272Missing in isoform Monomeric.
VSP_018905
Natural variant31V → I.
Corresponds to variant rs244903 [ dbSNP | Ensembl ].
VAR_020106
Natural variant1351R → G.
Corresponds to variant rs1059443 [ dbSNP | Ensembl ].
VAR_052635
Natural variant3971F → Y.
Corresponds to variant rs2305734 [ dbSNP | Ensembl ].
VAR_020107

Experimental info

Sequence conflict391P → S in AAB35627. Ref.1
Sequence conflict130 – 1312QK → PE in AAB35627. Ref.1
Sequence conflict135 – 1373REI → GEF in AAB35627. Ref.1
Sequence conflict147 – 15610DNECIEKVEI → AMDVLKRVEF in AAB35627. Ref.1
Sequence conflict1641V → G in AAB35627. Ref.1
Sequence conflict2781K → N in BAG37326. Ref.3
Sequence conflict308 – 3125WKLIC → YLLMS in AAB35627. Ref.1
Sequence conflict3411R → G in BAD96517. Ref.4
Sequence conflict3581D → G in BAG37326. Ref.3
Sequence conflict4871T → A in BAD96517. Ref.4
Sequence conflict5671D → V in AAB35627. Ref.1
Sequence conflict635 – 6406MLLCEA → ILCET in AAB35627. Ref.1
Sequence conflict6511I → T in AAB35627. Ref.1
Sequence conflict657 – 6604VQRM → GPRV in AAB35627. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform Complexed [UniParc].

Last modified April 16, 2002. Version 2.
Checksum: FE9FB5C910709956

FASTA66075,379
        10         20         30         40         50         60 
MDVLVSECSA RLLQQEEEIK SLTAEIDRLK NCGCLGASPN LEQLQEENLK LKYRLNILRK 

        70         80         90        100        110        120 
SLQAERNKPT KNMINIISRL QEVFGHAIKA AYPDLENPPL LVTPSQQAKF GDYQCNSAMG 

       130        140        150        160        170        180 
ISQMLKTKEQ KVNPREIAEN ITKHLPDNEC IEKVEIAGPG FINVHLRKDF VSEQLTSLLV 

       190        200        210        220        230        240 
NGVQLPALGE NKKVIVDFSS PNIAKEMHVG HLRSTIIGES ISRLFEFAGY DVLRLNHVGD 

       250        260        270        280        290        300 
WGTQFGMLIA HLQDKFPDYL TVSPPIGDLQ VFYKESKKRF DTEEEFKKRA YQCVVLLQGK 

       310        320        330        340        350        360 
NPDITKAWKL ICDVSRQELN KIYDALDVSL IERGESFYQD RMNDIVKEFE DRGFVQVDDG 

       370        380        390        400        410        420 
RKIVFVPGCS IPLTIVKSDG GYTYDTSDLA AIKQRLFEEK ADMIIYVVDN GQSVHFQTIF 

       430        440        450        460        470        480 
AAAQMIGWYD PKVTRVFHAG FGVVLGEDKK KFKTRSGETV RLMDLLGEGL KRSMDKLKEK 

       490        500        510        520        530        540 
ERDKVLTAEE LNAAQTSVAY GCIKYADLSH NRLNDYIFSF DKMLDDRGNT AAYLLYAFTR 

       550        560        570        580        590        600 
IRSIARLANI DEEMLQKAAR ETKILLDHEK EWKLGRCILR FPEILQKILD DLFLHTLCDY 

       610        620        630        640        650        660 
IYELATAFTE FYDSCYCVEK DRQTGKILKV NMWRMLLCEA VAAVMAKGFD ILGIKPVQRM 

« Hide

Isoform Monomeric [UniParc].

Checksum: 857EA1F69F3B6A3B
Show »

FASTA58867,140

References

« Hide 'large scale' references
[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. 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] [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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS4367.1. [P54136-1]
PIRJC4365.
RefSeqNP_002878.2. NM_002887.3. [P54136-1]
UniGeneHs.654907.

3D structure databases

ProteinModelPortalP54136.
SMRP54136. Positions 74-659.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111852. 41 interactions.
IntActP54136. 8 interactions.
MINTMINT-5006018.
STRING9606.ENSP00000231572.

Chemistry

BindingDBP54136.
ChEMBLCHEMBL2824.

PTM databases

PhosphoSiteP54136.

Polymorphism databases

DMDM20178331.

Proteomic databases

MaxQBP54136.
PaxDbP54136.
PeptideAtlasP54136.
PRIDEP54136.

Protocols and materials databases

DNASU5917.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000231572; ENSP00000231572; ENSG00000113643. [P54136-1]
GeneID5917.
KEGGhsa:5917.
UCSCuc003lzx.3. human. [P54136-1]

Organism-specific databases

CTD5917.
GeneCardsGC05P167846.
HGNCHGNC:9870. RARS.
HPAHPA003979.
HPA004130.
MIM107820. gene.
neXtProtNX_P54136.
PharmGKBPA34231.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247212.
HOVERGENHBG029238.
InParanoidP54136.
KOK01887.
OMAIRNTIND.
OrthoDBEOG764725.
PhylomeDBP54136.
TreeFamTF106111.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressP54136.
BgeeP54136.
CleanExHS_RARS.
GenevestigatorP54136.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.30.1360.70. 1 hit.
3.40.50.620. 1 hit.
HAMAPMF_00123. Arg_tRNA_synth.
InterProIPR001412. 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]
PANTHERPTHR11956. PTHR11956. 1 hit.
PfamPF03485. Arg_tRNA_synt_N. 1 hit.
PF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view]
PRINTSPR01038. TRNASYNTHARG.
SMARTSM01016. Arg_tRNA_synt_N. 1 hit.
SM00836. DALR_1. 1 hit.
[Graphical view]
SUPFAMSSF47323. SSF47323. 1 hit.
SSF55190. SSF55190. 1 hit.
TIGRFAMsTIGR00456. argS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRARS_(gene).
GenomeRNAi5917.
NextBio23038.
PROP54136.
SOURCESearch...

Entry information

Entry nameSYRC_HUMAN
AccessionPrimary (citable) accession number: P54136
Secondary accession number(s): B2RBS9, Q53GY4, Q9BWA1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: April 16, 2002
Last modified: July 9, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries