P54136 (SYRC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Arginine--tRNA ligase, cytoplasmic
EC=6.1.1.19

Alternative name(s):
Arginyl-tRNA synthetase
Short name=ArgRS

Gene names

Name:

RARS

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	660 AA.
Sequence status	Complete.
Protein existence	Evidence 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).
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.
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)

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative initiation Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	arginyl-tRNA aminoacylation Traceable author statement. Source: ProtInc
Cellular component	cytosol Traceable author statement. Source: Reactome nucleus Inferred from direct assay. Source: HPA soluble fraction Traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW arginine-tRNA ligase activity Traceable author statement. Source: Reactome protein binding Inferred from physical interaction Ref.8. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
LARS	Q9P2J5	3	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 660	660	Arginine--tRNA ligase, cytoplasmic		PRO_0000035797
Regions
	Region	1 – 72	72	Could be involved in the assembly of the multisynthetase complex
	Motif	201 – 212	12	"HIGH" region
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine Ref.11
	Modified residue	38	1	Phosphoserine Ref.11
	Modified residue	60	1	N6-acetyllysine Ref.12
	Modified residue	205	1	N6-acetyllysine Ref.12
Natural variations
	Alternative sequence	1 – 72	72	Missing in isoform Monomeric.		VSP_018905
	Natural variant	3	1	V → I. Corresponds to variant rs244903 [ dbSNP | Ensembl ].		VAR_020106
	Natural variant	135	1	R → G. Corresponds to variant rs1059443 [ dbSNP | Ensembl ].		VAR_052635
	Natural variant	397	1	F → Y. Corresponds to variant rs2305734 [ dbSNP | Ensembl ].		VAR_020107
Experimental info
	Sequence conflict	39	1	P → S in AAB35627. Ref.1
	Sequence conflict	130 – 131	2	QK → PE in AAB35627. Ref.1
	Sequence conflict	135 – 137	3	REI → GEF in AAB35627. Ref.1
	Sequence conflict	147 – 156	10	DNECIEKVEI → AMDVLKRVEF in AAB35627. Ref.1
	Sequence conflict	164	1	V → G in AAB35627. Ref.1
	Sequence conflict	278	1	K → N in BAG37326. Ref.3
	Sequence conflict	308 – 312	5	WKLIC → YLLMS in AAB35627. Ref.1
	Sequence conflict	341	1	R → G in BAD96517. Ref.4
	Sequence conflict	358	1	D → G in BAG37326. Ref.3
	Sequence conflict	487	1	T → A in BAD96517. Ref.4
	Sequence conflict	567	1	D → V in AAB35627. Ref.1
	Sequence conflict	635 – 640	6	MLLCEA → ILCET in AAB35627. Ref.1
	Sequence conflict	651	1	I → T in AAB35627. Ref.1
	Sequence conflict	657 – 660	4	VQRM → GPRV in AAB35627. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform Complexed [UniParc]. Last modified April 16, 2002. Version 2. Checksum: FE9FB5C910709956	FASTA	660	75,379
	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
	Isoform Monomeric [UniParc]. Checksum: 857EA1F69F3B6A3B	FASTA	588	67,140
	10 20 30 40 50 60 MINIISRLQE VFGHAIKAAY PDLENPPLLV TPSQQAKFGD YQCNSAMGIS QMLKTKEQKV 70 80 90 100 110 120 NPREIAENIT KHLPDNECIE KVEIAGPGFI NVHLRKDFVS EQLTSLLVNG VQLPALGENK 130 140 150 160 170 180 KVIVDFSSPN IAKEMHVGHL RSTIIGESIS RLFEFAGYDV LRLNHVGDWG TQFGMLIAHL 190 200 210 220 230 240 QDKFPDYLTV SPPIGDLQVF YKESKKRFDT EEEFKKRAYQ CVVLLQGKNP DITKAWKLIC 250 260 270 280 290 300 DVSRQELNKI YDALDVSLIE RGESFYQDRM NDIVKEFEDR GFVQVDDGRK IVFVPGCSIP 310 320 330 340 350 360 LTIVKSDGGY TYDTSDLAAI KQRLFEEKAD MIIYVVDNGQ SVHFQTIFAA AQMIGWYDPK 370 380 390 400 410 420 VTRVFHAGFG VVLGEDKKKF KTRSGETVRL MDLLGEGLKR SMDKLKEKER DKVLTAEELN 430 440 450 460 470 480 AAQTSVAYGC IKYADLSHNR LNDYIFSFDK MLDDRGNTAA YLLYAFTRIR SIARLANIDE 490 500 510 520 530 540 EMLQKAARET KILLDHEKEW KLGRCILRFP EILQKILDDL FLHTLCDYIY ELATAFTEFY 550 560 570 580 DSCYCVEKDR QTGKILKVNM WRMLLCEAVA AVMAKGFDIL GIKPVQRM

References

	« Hide 'large scale' referencesShow '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: 7590355] [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: 14702039] [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: 15489334] [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: 12665801] [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: 10358004] [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: 16055448] [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: 16430231] [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: 17443684] [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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60 AND LYS-205, MASS SPECTROMETRY.
[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: 21269460] [Abstract] Cited for: 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.
IPI	IPI00004860. IPI00759723.
PIR	JC4365.
RefSeq	NP_002878.2. NM_002887.3.
UniGene	Hs.654907.
3D structure databases
ProteinModelPortal	P54136.
SMR	P54136. Positions 56-660.
ModBase	Search...
Protein-protein interaction databases
IntAct	P54136. 5 interactions.
MINT	MINT-5006018.
STRING	P54136.
PTM databases
PhosphoSite	P54136.
Polymorphism databases
DMDM	20178331.
Proteomic databases
PeptideAtlas	P54136.
PRIDE	P54136.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000231572; ENSP00000231572; ENSG00000113643.
GeneID	5917.
KEGG	hsa:5917.
NMPDR	fig|9606.3.peg.26131.
UCSC	uc003lzx.1. human.
Organism-specific databases
CTD	5917.
GeneCards	GC05P167846.
H-InvDB	HIX0005391.
HGNC	HGNC:9870. RARS.
HPA	HPA003979. HPA004130.
MIM	107820. gene.
neXtProt	NX_P54136.
PharmGKB	PA34231.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG08635.
GeneTree	ENSGT00530000063407.
HOGENOM	HBG695395.
HOVERGEN	HBG029238.
InParanoid	P54136.
OMA	YREAKKH.
OrthoDB	EOG4D52X9.
PhylomeDB	P54136.
Enzyme and pathway databases
Reactome	REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	P54136.
Bgee	P54136.
CleanEx	HS_RARS.
Genevestigator	P54136.
Family and domain databases
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR001278. Arg-tRNA-synth_Ia. IPR015945. Arg-tRNA-synth_Ia_core. IPR005148. Arg-tRNA-synth_N. IPR008909. DALR_anticod-bd. IPR014729. Rossmann-like_a/b/a_fold. IPR009080. tRNAsynth_1a_anticodon-bd. [Graphical view]
Gene3D	G3DSA:3.30.1360.70. Arg-tRNA-synth_Ic_N. 1 hit. G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KO	K01887.
PANTHER	PTHR11956. Arg_tRNA-synt_1c. 1 hit.
Pfam	PF03485. Arg_tRNA_synt_N. 1 hit. PF05746. DALR_1. 1 hit. PF00750. tRNA-synt_1d. 1 hit. [Graphical view]
PRINTS	PR01038. TRNASYNTHARG.
SMART	SM01016. Arg_tRNA_synt_N. 1 hit. SM00836. DALR_1. 1 hit. [Graphical view]
SUPFAM	SSF55190. Arg-tRNA-synth_Ic_N. 1 hit. SSF47323. tRNAsyn_1a_bind. 1 hit.
TIGRFAMs	TIGR00456. ArgS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	23038.
SOURCE	Search...

Entry information

Entry name

SYRC_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 120 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.