P14868 (SYDC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aspartate--tRNA ligase, cytoplasmic
EC=6.1.1.12

Alternative name(s):
Aspartyl-tRNA synthetase
Short name=AspRS
Cell proliferation-inducing gene 40 protein

Gene names

Name:	DARS
ORF Names:	PIG40

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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 Reference proteome
Gene Ontology (GO)
Biological_process	aspartyl-tRNA aminoacylation Traceable author statement PubMed 8449960. Source: ProtInc protein complex assembly Traceable author statement PubMed 8449960. Source: ProtInc
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW aminoacylase activity Traceable author statement PubMed 8449960. Source: ProtInc aspartate-tRNA ligase activity Traceable author statement PubMed 8449960. Source: ProtInc nucleic acid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GRB2	P62993	2	EBI-358730,EBI-401755

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 501	501	Aspartate--tRNA ligase, 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.9
	Modified residue	249	1	Phosphoserine Ref.11
	Modified residue	374	1	N6-acetyllysine Ref.9
	Modified residue	500	1	Phosphothreonine; by PKA Potential
Natural variations
	Natural variant	426	1	L → F. Corresponds to variant rs1803165 [ dbSNP | Ensembl ].		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 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Eye.
[8]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KARS.
[9]	"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: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-74 AND LYS-374, MASS SPECTROMETRY.
[10]	"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].
[11]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, 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. CH471058 Genomic DNA. Translation: EAX11620.1. BC000629 mRNA. Translation: AAH00629.1. BC107749 mRNA. Translation: AAI07750.1.
IPI	IPI00216951.
PIR	SYHUDT. A34393.
RefSeq	NP_001340.2. NM_001349.2.
UniGene	Hs.503787.
3D structure databases
ProteinModelPortal	P14868.
ModBase	Search...
Protein-protein interaction databases
IntAct	P14868. 9 interactions.
MINT	MINT-141082.
STRING	9606.ENSP00000264161.
PTM databases
PhosphoSite	P14868.
Polymorphism databases
DMDM	20178330.
2D gel databases
OGP	P14868.
REPRODUCTION-2DPAGE	IPI00216951.
Proteomic databases
PaxDb	P14868.
PeptideAtlas	P14868.
PRIDE	P14868.
Protocols and materials databases
DNASU	1615.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000264161; ENSP00000264161; ENSG00000115866.
GeneID	1615.
KEGG	hsa:1615.
UCSC	uc002tux.1. human.
Organism-specific databases
CTD	1615.
GeneCards	GC02M136686.
HGNC	HGNC:2678. DARS.
HPA	HPA020451. HPA029804. HPA029805.
MIM	603084. gene.
neXtProt	NX_P14868.
PharmGKB	PA27146.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0017.
HOVERGEN	HBG001028.
InParanoid	P14868.
KO	K01876.
OMA	IDLRTTT.
OrthoDB	EOG470TH2.
PhylomeDB	P14868.
Enzyme and pathway databases
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
Gene3D	2.40.50.140. 1 hit.
InterPro	IPR004364. aa-tRNA-synt_II. IPR018150. aa-tRNA-synt_II-like. IPR006195. aa-tRNA-synth_II. IPR004523. Asp-tRNA_synthase. IPR002312. Asp/Asn-tRNA-synth_IIb. IPR012340. NA-bd_OB-fold. IPR004365. NA-bd_OB_tRNA-helicase. [Graphical view]
PANTHER	PTHR22594. PTHR22594. 1 hit. PTHR22594:SF10. PTHR22594:SF10. 1 hit.
Pfam	PF00152. tRNA-synt_2. 1 hit. PF01336. tRNA_anti. 1 hit. [Graphical view]
PRINTS	PR01042. TRNASYNTHASP.
SUPFAM	SSF50249. Nucleic_acid_OB. 1 hit.
TIGRFAMs	TIGR00458. aspS_nondisc. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	DARS. human.
DrugBank	DB00128. L-Aspartic Acid.
GenomeRNAi	1615.
NextBio	6634.
SOURCE	Search...

Entry information

Entry name

SYDC_HUMAN

Accession

Primary (citable) accession number: P14868
Secondary accession number(s): A8K3J2 , D3DP77, Q2TNI3, Q32Q69, Q53HV4, Q53YC5, Q9BW52

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 16, 2002
Last modified:	May 1, 2013
This is version 137 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.