Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Aspartate--tRNA ligase, cytoplasmic

Gene

DARS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei229 – 2291AspartateBy similarity
Binding sitei273 – 2731AspartateBy similarity
Binding sitei424 – 4241ATPBy similarity
Binding sitei427 – 4271AspartateBy similarity
Binding sitei431 – 4311AspartateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi273 – 2753ATPBy similarity
Nucleotide bindingi281 – 2833ATPBy similarity
Nucleotide bindingi472 – 4754ATPBy similarity

GO - Molecular functioni

  • aminoacylase activity Source: ProtInc
  • aspartate-tRNA ligase activity Source: ProtInc
  • ATP binding Source: UniProtKB-KW
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • aspartyl-tRNA aminoacylation Source: ProtInc
  • gene expression Source: Reactome
  • protein complex assembly Source: ProtInc
  • translation Source: ProtInc
  • tRNA aminoacylation for protein translation Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.1.1.12. 2681.
ReactomeiREACT_15306. Cytosolic tRNA aminoacylation.

Names & Taxonomyi

Protein namesi
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 namesi
Name:DARS
ORF Names:PIG40
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:2678. DARS.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Hypomyelination with brainstem and spinal cord involvement and leg spasticity (HBSL)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal recessive leukoencephalopathy characterized by onset in the first year of life of severe spasticity, mainly affecting the lower limbs and resulting in an inability to achieve independent ambulation. Affected individuals show delayed motor development and nystagmus; some may have mild mental retardation. Brain MRI shows hypomyelination and white matter lesions in the cerebrum, brainstem, cerebellum, and spinal cord.

See also OMIM:615281
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti256 – 2561M → L in HBSL. 1 Publication
VAR_070038
Natural varianti274 – 2741A → V in HBSL. 1 Publication
VAR_070039
Natural varianti367 – 3671D → Y in HBSL. 1 Publication
VAR_070040
Natural varianti460 – 4601R → H in HBSL. 1 Publication
VAR_070041
Natural varianti464 – 4641P → L in HBSL. 1 Publication
VAR_070042
Natural varianti487 – 4871R → C in HBSL. 1 Publication
VAR_070043
Natural varianti494 – 4941R → C in HBSL. 1 Publication
VAR_070044
Natural varianti494 – 4941R → G in HBSL. 1 Publication
VAR_070045

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi615281. phenotype.
Orphaneti363412. Hypomyelination with brain stem and spinal cord involvement and leg spasticity.
PharmGKBiPA27146.

Chemistry

DrugBankiDB00128. L-Aspartic Acid.

Polymorphism and mutation databases

BioMutaiDARS.
DMDMi20178330.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 501501Aspartate--tRNA ligase, cytoplasmicPRO_0000111010Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei74 – 741N6-acetyllysine1 Publication
Modified residuei249 – 2491Phosphoserine1 Publication
Modified residuei374 – 3741N6-acetyllysine1 Publication
Modified residuei500 – 5001Phosphothreonine; by PKASequence Analysis

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP14868.
PaxDbiP14868.
PeptideAtlasiP14868.
PRIDEiP14868.

2D gel databases

OGPiP14868.
REPRODUCTION-2DPAGEIPI00216951.

PTM databases

PhosphoSiteiP14868.

Expressioni

Tissue specificityi

Expression in the developing and adult brain shows similar patterns. Highly expressed in the ventricular and subventricular zones, including hippocampal subfields, the midlateral temporaal cortex and the frontal polar cortex. The cerebellum, cereral cortex, hippocampus, and lateral ventricle show preferential neuronal expression. Expression in the peripheral neurons is evident in the colon.1 Publication

Gene expression databases

BgeeiP14868.
CleanExiHS_DARS.
ExpressionAtlasiP14868. baseline and differential.
GenevestigatoriP14868.

Organism-specific databases

HPAiHPA020451.
HPA029804.
HPA029805.

Interactioni

Subunit structurei

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
AIMP2Q131557EBI-358730,EBI-745226
GRB2P629932EBI-358730,EBI-401755

Protein-protein interaction databases

BioGridi107984. 58 interactions.
IntActiP14868. 14 interactions.
MINTiMINT-141082.
STRINGi9606.ENSP00000264161.

Structurei

Secondary structure

1
501
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi26 – 283Combined sources
Beta strandi29 – 313Combined sources
Helixi48 – 503Combined sources
Helixi53 – 553Combined sources
Beta strandi59 – 7214Combined sources
Beta strandi75 – 828Combined sources
Beta strandi85 – 939Combined sources
Turni94 – 963Combined sources
Helixi99 – 1079Combined sources
Beta strandi113 – 12210Combined sources
Beta strandi134 – 14613Combined sources
Helixi156 – 1605Combined sources
Helixi176 – 1816Combined sources
Helixi183 – 1864Combined sources
Helixi190 – 21223Combined sources
Helixi250 – 25910Combined sources
Beta strandi264 – 2718Combined sources
Beta strandi286 – 2949Combined sources
Helixi300 – 32021Combined sources
Helixi322 – 33110Combined sources
Beta strandi344 – 3474Combined sources
Helixi348 – 35710Combined sources
Helixi370 – 38415Combined sources
Beta strandi387 – 3926Combined sources
Helixi396 – 3983Combined sources
Beta strandi407 – 4093Combined sources
Beta strandi412 – 4209Combined sources
Beta strandi423 – 4319Combined sources
Helixi435 – 44410Combined sources
Helixi450 – 4523Combined sources
Helixi453 – 4575Combined sources
Turni458 – 4614Combined sources
Beta strandi466 – 4727Combined sources
Helixi473 – 4819Combined sources
Helixi486 – 4894Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4J15X-ray2.24A/B1-501[»]
ProteinModelPortaliP14868.
SMRiP14868. Positions 21-495.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni251 – 2544AspartateBy similarity
Regioni411 – 4155Binding site for the 3'-end of tRNASequence Analysis

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0017.
GeneTreeiENSGT00550000074880.
HOVERGENiHBG001028.
InParanoidiP14868.
KOiK01876.
OMAiIWLRARV.
OrthoDBiEOG7P5T0X.
PhylomeDBiP14868.
TreeFamiTF105676.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004523. Asp-tRNA_synthase_arc.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
[Graphical view]
PANTHERiPTHR22594. PTHR22594. 1 hit.
PTHR22594:SF10. PTHR22594:SF10. 1 hit.
PfamiPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
PRINTSiPR01042. TRNASYNTHASP.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00458. aspS_nondisc. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P14868-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MPSASASRKS QEKPREIMDA AEDYAKERYG ISSMIQSQEK PDRVLVRVRD
60 70 80 90 100
LTIQKADEVV WVRARVHTSR AKGKQCFLVL RQQQFNVQAL VAVGDHASKQ
110 120 130 140 150
MVKFAANINK ESIVDVEGVV RKVNQKIGSC TQQDVELHVQ KIYVISLAEP
160 170 180 190 200
RLPLQLDDAV RPEAEGEEEG RATVNQDTRL DNRVIDLRTS TSQAVFRLQS
210 220 230 240 250
GICHLFRETL INKGFVEIQT PKIISAASEG GANVFTVSYF KNNAYLAQSP
260 270 280 290 300
QLYKQMCICA DFEKVFSIGP VFRAEDSNTH RHLTEFVGLD IEMAFNYHYH
310 320 330 340 350
EVMEEIADTM VQIFKGLQER FQTEIQTVNK QFPCEPFKFL EPTLRLEYCE
360 370 380 390 400
ALAMLREAGV EMGDEDDLST PNEKLLGHLV KEKYDTDFYI LDKYPLAVRP
410 420 430 440 450
FYTMPDPRNP KQSNSYDMFM RGEEILSGAQ RIHDPQLLTE RALHHGIDLE
460 470 480 490 500
KIKAYIDSFR FGAPPHAGGG IGLERVTMLF LGLHNVRQTS MFPRDPKRLT

P
Length:501
Mass (Da):57,136
Last modified:April 16, 2002 - v2
Checksum:iB181572DF0AF5F94
GO
Isoform 2 (identifier: P14868-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-100: Missing.

Note: No experimental confirmation available.

Show »
Length:401
Mass (Da):45,771
Checksum:i0383EB6177DD0739
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 73SAS → TQ in AAA35567 (PubMed:2674137).Curated
Sequence conflicti31 – 311I → T in AAI07750 (PubMed:15489334).Curated
Sequence conflicti38 – 381Q → H in BAD96196 (Ref. 5) Curated
Sequence conflicti164 – 1641A → Q in AAA35567 (PubMed:2674137).Curated
Sequence conflicti312 – 3121Q → H in AAX07827 (Ref. 2) Curated
Sequence conflicti414 – 4141N → K in AAA35567 (PubMed:2674137).Curated
Sequence conflicti447 – 4471I → N in AAA35567 (PubMed:2674137).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti256 – 2561M → L in HBSL. 1 Publication
VAR_070038
Natural varianti274 – 2741A → V in HBSL. 1 Publication
VAR_070039
Natural varianti367 – 3671D → Y in HBSL. 1 Publication
VAR_070040
Natural varianti426 – 4261L → F.
Corresponds to variant rs1803165 [ dbSNP | Ensembl ].
VAR_027611
Natural varianti460 – 4601R → H in HBSL. 1 Publication
VAR_070041
Natural varianti464 – 4641P → L in HBSL. 1 Publication
VAR_070042
Natural varianti487 – 4871R → C in HBSL. 1 Publication
VAR_070043
Natural varianti494 – 4941R → C in HBSL. 1 Publication
VAR_070044
Natural varianti494 – 4941R → G in HBSL. 1 Publication
VAR_070045

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 100100Missing in isoform 2. 1 PublicationVSP_056192Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05032 mRNA. Translation: AAA35567.1.
AY762100 mRNA. Translation: AAX07827.1.
BT006710 mRNA. Translation: AAP35356.1.
AK290607 mRNA. Translation: BAF83296.1.
AK222476 mRNA. Translation: BAD96196.1.
CR749809 mRNA. Translation: CAH18669.1.
AC011999 Genomic DNA. No translation available.
AC093391 Genomic DNA. No translation available.
CH471058 Genomic DNA. Translation: EAX11617.1.
CH471058 Genomic DNA. Translation: EAX11620.1.
BC000629 mRNA. Translation: AAH00629.1.
BC107749 mRNA. Translation: AAI07750.1.
CCDSiCCDS2180.1. [P14868-1]
PIRiA34393. SYHUDT.
RefSeqiNP_001280241.1. NM_001293312.1. [P14868-2]
NP_001340.2. NM_001349.3. [P14868-1]
UniGeneiHs.503787.
Hs.595819.

Genome annotation databases

EnsembliENST00000264161; ENSP00000264161; ENSG00000115866. [P14868-1]
GeneIDi1615.
KEGGihsa:1615.
UCSCiuc002tux.1. human. [P14868-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05032 mRNA. Translation: AAA35567.1.
AY762100 mRNA. Translation: AAX07827.1.
BT006710 mRNA. Translation: AAP35356.1.
AK290607 mRNA. Translation: BAF83296.1.
AK222476 mRNA. Translation: BAD96196.1.
CR749809 mRNA. Translation: CAH18669.1.
AC011999 Genomic DNA. No translation available.
AC093391 Genomic DNA. No translation available.
CH471058 Genomic DNA. Translation: EAX11617.1.
CH471058 Genomic DNA. Translation: EAX11620.1.
BC000629 mRNA. Translation: AAH00629.1.
BC107749 mRNA. Translation: AAI07750.1.
CCDSiCCDS2180.1. [P14868-1]
PIRiA34393. SYHUDT.
RefSeqiNP_001280241.1. NM_001293312.1. [P14868-2]
NP_001340.2. NM_001349.3. [P14868-1]
UniGeneiHs.503787.
Hs.595819.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4J15X-ray2.24A/B1-501[»]
ProteinModelPortaliP14868.
SMRiP14868. Positions 21-495.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107984. 58 interactions.
IntActiP14868. 14 interactions.
MINTiMINT-141082.
STRINGi9606.ENSP00000264161.

Chemistry

DrugBankiDB00128. L-Aspartic Acid.

PTM databases

PhosphoSiteiP14868.

Polymorphism and mutation databases

BioMutaiDARS.
DMDMi20178330.

2D gel databases

OGPiP14868.
REPRODUCTION-2DPAGEIPI00216951.

Proteomic databases

MaxQBiP14868.
PaxDbiP14868.
PeptideAtlasiP14868.
PRIDEiP14868.

Protocols and materials databases

DNASUi1615.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264161; ENSP00000264161; ENSG00000115866. [P14868-1]
GeneIDi1615.
KEGGihsa:1615.
UCSCiuc002tux.1. human. [P14868-1]

Organism-specific databases

CTDi1615.
GeneCardsiGC02M136686.
HGNCiHGNC:2678. DARS.
HPAiHPA020451.
HPA029804.
HPA029805.
MIMi603084. gene.
615281. phenotype.
neXtProtiNX_P14868.
Orphaneti363412. Hypomyelination with brain stem and spinal cord involvement and leg spasticity.
PharmGKBiPA27146.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0017.
GeneTreeiENSGT00550000074880.
HOVERGENiHBG001028.
InParanoidiP14868.
KOiK01876.
OMAiIWLRARV.
OrthoDBiEOG7P5T0X.
PhylomeDBiP14868.
TreeFamiTF105676.

Enzyme and pathway databases

BRENDAi6.1.1.12. 2681.
ReactomeiREACT_15306. Cytosolic tRNA aminoacylation.

Miscellaneous databases

ChiTaRSiDARS. human.
GeneWikiiDARS_(gene).
GenomeRNAii1615.
NextBioi6634.
PROiP14868.
SOURCEiSearch...

Gene expression databases

BgeeiP14868.
CleanExiHS_DARS.
ExpressionAtlasiP14868. baseline and differential.
GenevestigatoriP14868.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004523. Asp-tRNA_synthase_arc.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
[Graphical view]
PANTHERiPTHR22594. PTHR22594. 1 hit.
PTHR22594:SF10. PTHR22594:SF10. 1 hit.
PfamiPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
PRINTSiPR01042. TRNASYNTHASP.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00458. aspS_nondisc. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1).
  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] (ISOFORM 1).
  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] (ISOFORM 1).
  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] (ISOFORM 1).
    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] (ISOFORM 1).
    Tissue: Adipose tissue.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Embryo.
  7. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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] (ISOFORM 1).
    Tissue: Eye.
  10. "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.
  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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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.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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: TISSUE SPECIFICITY, VARIANTS HBSL LEU-256; VAL-274; TYR-367; HIS-460; LEU-464; CYS-487; CYS-494 AND GLY-494.
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSYDC_HUMAN
AccessioniPrimary (citable) accession number: P14868
Secondary accession number(s): A8K3J2
, D3DP77, Q2TNI3, Q32Q69, Q53HV4, Q53YC5, Q68CR9, Q9BW52
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 16, 2002
Last modified: May 27, 2015
This is version 159 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.