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Reviewed, UniProtKB/Swiss-Prot P14868 (SYDC_HUMAN)

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

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length501 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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.

Ontologies

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 501501Aspartyl-tRNA synthetase, cytoplasmic
PRO_0000111010

Regions

Region411 – 4155Binding site for the 3'-end of tRNA Potential

Amino acid modifications

Modified residue2381Phosphoserine Ref.6
Modified residue5001Phosphothreonine; by PKA Potential

Natural variations

Natural variant4261L → F: dbSNP rs1803165.
VAR_027611

Experimental info

Sequence conflict5 – 73SAS → TQ in AAA35567. Ref.1
Sequence conflict311I → T in AAI07750. Ref.5
Sequence conflict381Q → H in BAD96196. Ref.4
Sequence conflict1641A → Q in AAA35567. Ref.1
Sequence conflict3121Q → H in AAX07827. Ref.2
Sequence conflict4141N → K in AAA35567. Ref.1
Sequence conflict4471I → N in AAA35567. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P14868-1 [UniParc].

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

FASTA50157,136
        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 

« Hide

References

« Hide '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.

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.
IPIIPI00216951.
PIRSYHUDT. A34393.
RefSeqNP_001340.2.
UniGeneHs.503787

3D structure databases

HSSPHSSP built from PDB template 1ASZ based on UniProtKB P04802.
ModBaseSearch...

Protein-protein interaction databases

IntActP14868. 6 interactions.

PTM databases

PhosphoSiteP14868.

2-D gel databases

OGPP14868.
REPRODUCTION-2DPAGEIPI00216951.

Proteomic databases

PeptideAtlasP14868.
PRIDEP14868.

Genome annotation databases

EnsemblENSG00000115866. Homo sapiens. [Contig view]
GeneID1615.
KEGGhsa:1615.

Organism-specific databases

GeneCardsGC02M136380.
H-InvDBHIX0002480.
HGNCHGNC:2678. DARS.
MIM603084. gene.
PharmGKBPA27146.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP14868.
OMAP14868. RNPKQSN.

Enzyme and pathway databases

BRENDA6.1.1.12. 247.

Gene expression databases

ArrayExpressP14868.
BgeeP14868.
CleanExHS_DARS.
GermOnlineENSG00000115866. Homo sapiens.

Family and domain databases

InterProIPR004364. 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]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
PANTHERPTHR22594. aa-tRNA-synt_II. 1 hit.
PfamPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti. 1 hit.
[Graphical view]
PRINTSPR01042. TRNASYNTHASP.
TIGRFAMsTIGR00458. aspS_arch. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00128. L-Aspartic Acid.
NextBio6634.
SOURCESearch...

Entry information

Entry nameSYDC_HUMAN
AccessionPrimary (citable) accession number: P14868
Secondary accession number(s): Q2TNI3 expand/collapse secondary AC list , Q32Q69, Q53HV4, Q53YC5, 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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents