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P14868

- SYDC_HUMAN

UniProt

P14868 - SYDC_HUMAN

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Protein

Aspartate--tRNA ligase, cytoplasmic

Gene

DARS

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. aminoacylase activity Source: ProtInc
  2. aspartate-tRNA ligase activity Source: ProtInc
  3. ATP binding Source: UniProtKB-KW
  4. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. aspartyl-tRNA aminoacylation Source: ProtInc
  2. gene expression Source: Reactome
  3. protein complex assembly Source: ProtInc
  4. translation Source: ProtInc
  5. 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

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: Chromosome 2

Organism-specific databases

HGNCiHGNC:2678. DARS.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
  4. 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) [MIM:615281]: An 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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
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.

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
GRB2P629932EBI-358730,EBI-401755

Protein-protein interaction databases

BioGridi107984. 56 interactions.
IntActiP14868. 13 interactions.
MINTiMINT-141082.
STRINGi9606.ENSP00000264161.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiFCVGPVF.
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.
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. Align

Isoform 1 (identifier: P14868) [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. 1 PublicationCurated
Sequence conflicti164 – 1641A → Q in AAA35567. (PubMed:2674137)Curated
Sequence conflicti312 – 3121Q → H in AAX07827. 1 PublicationCurated
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:
EMBL
GenBank
DDBJ
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.
NP_001340.2. NM_001349.3.
UniGeneiHs.503787.
Hs.595819.

Genome annotation databases

EnsembliENST00000264161; ENSP00000264161; ENSG00000115866. [P14868-1]
ENST00000537273; ENSP00000444192; ENSG00000115866. [P14868-2]
GeneIDi1615.
KEGGihsa:1615.
UCSCiuc002tux.1. human. [P14868-1]

Polymorphism databases

DMDMi20178330.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS2180.1. [P14868-1 ]
PIRi A34393. SYHUDT.
RefSeqi NP_001280241.1. NM_001293312.1.
NP_001340.2. NM_001349.3.
UniGenei Hs.503787.
Hs.595819.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4J15 X-ray 2.24 A/B 1-501 [» ]
ProteinModelPortali P14868.
SMRi P14868. Positions 21-495.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107984. 56 interactions.
IntActi P14868. 13 interactions.
MINTi MINT-141082.
STRINGi 9606.ENSP00000264161.

Chemistry

DrugBanki DB00128. L-Aspartic Acid.

PTM databases

PhosphoSitei P14868.

Polymorphism databases

DMDMi 20178330.

2D gel databases

OGPi P14868.
REPRODUCTION-2DPAGE IPI00216951.

Proteomic databases

MaxQBi P14868.
PaxDbi P14868.
PeptideAtlasi P14868.
PRIDEi P14868.

Protocols and materials databases

DNASUi 1615.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264161 ; ENSP00000264161 ; ENSG00000115866 . [P14868-1 ]
ENST00000537273 ; ENSP00000444192 ; ENSG00000115866 . [P14868-2 ]
GeneIDi 1615.
KEGGi hsa:1615.
UCSCi uc002tux.1. human. [P14868-1 ]

Organism-specific databases

CTDi 1615.
GeneCardsi GC02M136686.
HGNCi HGNC:2678. DARS.
HPAi HPA020451.
HPA029804.
HPA029805.
MIMi 603084. gene.
615281. phenotype.
neXtProti NX_P14868.
Orphaneti 363412. Hypomyelination with brain stem and spinal cord involvement and leg spasticity.
PharmGKBi PA27146.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0017.
GeneTreei ENSGT00550000074880.
HOVERGENi HBG001028.
InParanoidi P14868.
KOi K01876.
OMAi FCVGPVF.
OrthoDBi EOG7P5T0X.
PhylomeDBi P14868.
TreeFami TF105676.

Enzyme and pathway databases

Reactomei REACT_15306. Cytosolic tRNA aminoacylation.

Miscellaneous databases

ChiTaRSi DARS. human.
GeneWikii DARS_(gene).
GenomeRNAii 1615.
NextBioi 6634.
PROi P14868.
SOURCEi Search...

Gene expression databases

Bgeei P14868.
CleanExi HS_DARS.
ExpressionAtlasi P14868. baseline and differential.
Genevestigatori P14868.

Family and domain databases

Gene3Di 2.40.50.140. 1 hit.
InterProi 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.
[Graphical view ]
PANTHERi PTHR22594. PTHR22594. 1 hit.
PTHR22594:SF10. PTHR22594:SF10. 1 hit.
Pfami PF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view ]
PRINTSi PR01042. TRNASYNTHASP.
SUPFAMi SSF50249. SSF50249. 1 hit.
TIGRFAMsi TIGR00458. aspS_nondisc. 1 hit.
PROSITEi PS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: TISSUE SPECIFICITY, VARIANTS HBSL LEU-256; VAL-274; TYR-367; HIS-460; LEU-464; CYS-487; CYS-494 AND GLY-494.

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: October 29, 2014
This is version 153 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