Reviewed, UniProtKB/Swiss-Prot P14868 (SYDC_HUMAN)

Names and origin

Protein names

Recommended name:
    Aspartyl-tRNA synthetase, cytoplasmic
    EC=6.1.1.12
Alternative name(s):
    Aspartate--tRNA ligase
      Short name=AspRS
    Cell proliferation-inducing gene 40 protein

Gene names

Name:	DARS
ORF Names:	PIG40

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	501 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.
Catalytic activity	ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp).
Subunit structure	Homodimer; also part of a multisubunit complex that groups AIMP1, AIMP2, EEF1A1 and tRNA ligases for Arg, Asp, Glu, Gln, Ile, Leu, Lys, Met and Pro.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	aspartyl-tRNA aminoacylation Traceable author statement. Source: ProtInc protein complex assembly Traceable author statement. Source: ProtInc
Cellular component	cytosol Inferred from Experiment. Source: Reactome soluble fraction Traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW aminoacylase activity Traceable author statement. Source: ProtInc aspartate-tRNA ligase activity Traceable author statement. Source: ProtInc nucleic acid binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GRB2	P62993	1	EBI-358730,EBI-401755
NDRG1	Q92597	1	EBI-358730,EBI-716486
PIK3R1	P27986	1	EBI-358730,EBI-79464

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 501	501	Aspartyl-tRNA synthetase, cytoplasmic		PRO_0000111010
Regions
	Region	411 – 415	5	Binding site for the 3'-end of tRNA Potential
Amino acid modifications
	Modified residue	74	1	N6-acetyllysine Ref.12
	Modified residue	238	1	Phosphoserine Ref.8
	Modified residue	249	1	Phosphoserine Ref.11
	Modified residue	374	1	N6-acetyllysine Ref.12
	Modified residue	500	1	Phosphothreonine; by PKA Potential
Natural variations
	Natural variant	426	1	L → F: dbSNP rs1803165.		VAR_027611
Experimental info
	Sequence conflict	5 – 7	3	SAS → TQ in AAA35567. Ref.1
	Sequence conflict	31	1	I → T in AAI07750. Ref.7
	Sequence conflict	38	1	Q → H in BAD96196. Ref.5
	Sequence conflict	164	1	A → Q in AAA35567. Ref.1
	Sequence conflict	312	1	Q → H in AAX07827. Ref.2
	Sequence conflict	414	1	N → K in AAA35567. Ref.1
	Sequence conflict	447	1	I → N in AAA35567. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P14868-1 [UniParc]. Last modified April 16, 2002. Version 2. Checksum: B181572DF0AF5F94	FASTA	501	57,136
	10 20 30 40 50 60 MPSASASRKS QEKPREIMDA AEDYAKERYG ISSMIQSQEK PDRVLVRVRD LTIQKADEVV 70 80 90 100 110 120 WVRARVHTSR AKGKQCFLVL RQQQFNVQAL VAVGDHASKQ MVKFAANINK ESIVDVEGVV 130 140 150 160 170 180 RKVNQKIGSC TQQDVELHVQ KIYVISLAEP RLPLQLDDAV RPEAEGEEEG RATVNQDTRL 190 200 210 220 230 240 DNRVIDLRTS TSQAVFRLQS GICHLFRETL INKGFVEIQT PKIISAASEG GANVFTVSYF 250 260 270 280 290 300 KNNAYLAQSP QLYKQMCICA DFEKVFSIGP VFRAEDSNTH RHLTEFVGLD IEMAFNYHYH 310 320 330 340 350 360 EVMEEIADTM VQIFKGLQER FQTEIQTVNK QFPCEPFKFL EPTLRLEYCE ALAMLREAGV 370 380 390 400 410 420 EMGDEDDLST PNEKLLGHLV KEKYDTDFYI LDKYPLAVRP FYTMPDPRNP KQSNSYDMFM 430 440 450 460 470 480 RGEEILSGAQ RIHDPQLLTE RALHHGIDLE KIKAYIDSFR FGAPPHAGGG IGLERVTMLF 490 500 LGLHNVRQTS MFPRDPKRLT P

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA sequence, predicted primary structure, and evolving amphiphilic helix of human aspartyl-tRNA synthetase." Jacobo-Molina A., Peterson R., Yang D.C.H. J. Biol. Chem. 264:16608-16612(1989) [PubMed: 2674137] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Identification of a cell proliferation-inducing gene." Kim J.W. Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"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].
[4]	"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]. Tissue: Heart.
[5]	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: Adipose tissue.
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: Eye.
[8]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, MASS SPECTROMETRY.
[9]	"Lysyl-tRNA synthetase interacts with EF1alpha, aspartyl-tRNA synthetase and p38 in vitro." Guzzo C.M., Yang D.C.H. Biochem. Biophys. Res. Commun. 365:718-723(2008) [PubMed: 18029264] [Abstract] Cited for: INTERACTION WITH KARS.
[10]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, MASS SPECTROMETRY.
[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-74 AND LYS-374, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J05032 mRNA. Translation: AAA35567.1. AY762100 mRNA. Translation: AAX07827.1. BT006710 mRNA. Translation: AAP35356.1. AK222476 mRNA. Translation: BAD96196.1. AK290607 mRNA. Translation: BAF83296.1. CH471058 Genomic DNA. Translation: EAX11617.1. BC000629 mRNA. Translation: AAH00629.1. BC107749 mRNA. Translation: AAI07750.1.
IPI	IPI00216951.
PIR	SYHUDT. A34393.
RefSeq	NP_001340.2.
UniGene	Hs.503787
3D structure databases
SMR	P14868. Positions 22-501.
ModBase	Search...
Protein-protein interaction databases
IntAct	P14868. 6 interactions.
STRING	P14868.
PTM databases
PhosphoSite	P14868.
2-D gel databases
OGP	P14868.
REPRODUCTION-2DPAGE	IPI00216951.
Proteomic databases
PeptideAtlas	P14868.
PRIDE	P14868.
Genome annotation databases
Ensembl	ENST00000264161; ENSP00000264161; ENSG00000115866; Homo sapiens. [Genome view]
GeneID	1615.
KEGG	hsa:1615.
UCSC	uc002tux.1. human.
Organism-specific databases
CTD	1615.
GeneCards	GC02M136380.
H-InvDB	HIX0002480.
HGNC	HGNC:2678. DARS.
HPA	HPA020451. HPA024079.
MIM	603084. gene.
PharmGKB	PA27146.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG18789.
HOGENOM	HBG745843.
HOVERGEN	P14868.
InParanoid	P14868.
OMA	RNPKQSN.
OrthoDB	EOG9QVFX4.
PhylomeDB	P14868.
Enzyme and pathway databases
BRENDA	6.1.1.12. 247.
Reactome	REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	P14868.
Bgee	P14868.
CleanEx	HS_DARS.
Genevestigator	P14868.
GermOnline	ENSG00000115866. Homo sapiens.
Family and domain databases
InterPro	IPR004364. aa-tRNA-synt_II. IPR018150. aa-tRNA-synt_II-like. IPR006195. aa-tRNA-synth_II_cons-dom. IPR002312. Asp-tRNA-synth_IIb. IPR004523. Asp-tRNA-synth_IIb_arc/euk. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. IPR004365. NA_bd_OB_tRNA-helicase. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
PANTHER	PTHR22594. aa-tRNA-synt_II. 1 hit.
Pfam	PF00152. tRNA-synt_2. 1 hit. PF01336. tRNA_anti. 1 hit. [Graphical view]
PRINTS	PR01042. TRNASYNTHASP.
TIGRFAMs	TIGR00458. aspS_arch. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00128. L-Aspartic Acid.
NextBio	6634.
SOURCE	Search...

Entry information

Entry name

SYDC_HUMAN

Accession

Primary (citable) accession number: P14868
Secondary accession number(s): A8K3J2 , Q2TNI3, Q32Q69, Q53HV4, Q53YC5, Q9BW52

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 16, 2002
Last modified:	February 9, 2010
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.