Aspartyl-tRNA synthetase, cytoplasmic

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Reviewed, UniProtKB/Swiss-Prot P14868 (SYDC_HUMAN)

Last modified June 16, 2009. Version 96. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	501 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp).
Subunit structure	Homodimer; also part of a multisubunit complex that groups 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.

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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	Phosphoprotein
Gene Ontology (GO)
Biological process	aspartyl-tRNA aminoacylation Traceable author statement. Source: ProtInc protein complex assembly Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Traceable author statement. Source: ProtInc 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...

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Binary interactions

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

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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

Binding site for the 3'-end of tRNA Potential

Amino acid modifications

Modified residue

238

Phosphoserine Ref.6

Modified residue

500

Phosphothreonine; by PKA Potential

Natural variations

Natural variant

426

L → F: dbSNP rs1803165.

VAR_027611

Experimental info

Sequence conflict

5 – 7

SAS → TQ in AAA35567. Ref.1

Sequence conflict

I → T in AAI07750. Ref.5

Sequence conflict

Q → H in BAD96196. Ref.4

Sequence conflict

164

A → Q in AAA35567. Ref.1

Sequence conflict

312

Q → H in AAX07827. Ref.2

Sequence conflict

414

N → K in AAA35567. Ref.1

Sequence conflict

447

I → N in AAA35567. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P14868-1 [UniParc].

Last modified April 16, 2002. Version 2.
Checksum: B181572DF0AF5F94
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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

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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]	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.
[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: Eye.
[6]	"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.
[7]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	J05032 mRNA. Translation: AAA35567.1. AY762100 mRNA. Translation: AAX07827.1. BT006710 mRNA. Translation: AAP35356.1. AK222476 mRNA. Translation: BAD96196.1. 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
HSSP	HSSP built from PDB template 1ASZ based on UniProtKB P04802.
ModBase	Search...
Protein-protein interaction databases
IntAct	P14868. 6 interactions.
PTM databases
PhosphoSite	P14868.
2-D gel databases
OGP	P14868.
REPRODUCTION-2DPAGE	IPI00216951.
Proteomic databases
PeptideAtlas	P14868.
PRIDE	P14868.
Genome annotation databases
Ensembl	ENSG00000115866. Homo sapiens. [Contig view]
GeneID	1615.
KEGG	hsa:1615.
Organism-specific databases
GeneCards	GC02M136380.
H-InvDB	HIX0002480.
HGNC	HGNC:2678. DARS.
MIM	603084. gene.
PharmGKB	PA27146.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P14868.
OMA	P14868. RNPKQSN.
Enzyme and pathway databases
BRENDA	6.1.1.12. 247.
Gene expression databases
ArrayExpress	P14868.
Bgee	P14868.
CleanEx	HS_DARS.
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-reg. IPR002312. Asp-tRNA-synth_IIb. IPR004523. Asp-tRNA-synth_IIb_arc/euk. IPR012340. NA-bd_OB-fold. 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...

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Entry information

Entry name

SYDC_HUMAN

Accession

Primary (citable) accession number: P14868
Secondary accession number(s): Q2TNI3

Q9BW52

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 16, 2002
Last modified:	June 16, 2009
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents