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P14868

- SYDC_HUMAN

UniProt

P14868 - SYDC_HUMAN

Protein

Aspartate--tRNA ligase, cytoplasmic

Gene

DARS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 2 (16 Apr 2002)
      Previous versions | rss
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    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
    5. protein binding Source: IntAct

    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

    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

    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

    ArrayExpressiP14868.
    BgeeiP14868.
    CleanExiHS_DARS.
    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. 52 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.
    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: P14868-1) [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

    MPSASASRKS QEKPREIMDA AEDYAKERYG ISSMIQSQEK PDRVLVRVRD    50
    LTIQKADEVV WVRARVHTSR AKGKQCFLVL RQQQFNVQAL VAVGDHASKQ 100
    MVKFAANINK ESIVDVEGVV RKVNQKIGSC TQQDVELHVQ KIYVISLAEP 150
    RLPLQLDDAV RPEAEGEEEG RATVNQDTRL DNRVIDLRTS TSQAVFRLQS 200
    GICHLFRETL INKGFVEIQT PKIISAASEG GANVFTVSYF KNNAYLAQSP 250
    QLYKQMCICA DFEKVFSIGP VFRAEDSNTH RHLTEFVGLD IEMAFNYHYH 300
    EVMEEIADTM VQIFKGLQER FQTEIQTVNK QFPCEPFKFL EPTLRLEYCE 350
    ALAMLREAGV EMGDEDDLST PNEKLLGHLV KEKYDTDFYI LDKYPLAVRP 400
    FYTMPDPRNP KQSNSYDMFM RGEEILSGAQ RIHDPQLLTE RALHHGIDLE 450
    KIKAYIDSFR FGAPPHAGGG IGLERVTMLF LGLHNVRQTS MFPRDPKRLT 500
    P 501
    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.
    PIRiA34393. SYHUDT.
    RefSeqiNP_001340.2. NM_001349.3.
    UniGeneiHs.503787.

    Genome annotation databases

    EnsembliENST00000264161; ENSP00000264161; ENSG00000115866.
    ENST00000537273; ENSP00000444192; ENSG00000115866.
    GeneIDi1615.
    KEGGihsa:1615.
    UCSCiuc002tux.1. human.

    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.
    PIRi A34393. SYHUDT.
    RefSeqi NP_001340.2. NM_001349.3.
    UniGenei Hs.503787.

    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. 52 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 .
    ENST00000537273 ; ENSP00000444192 ; ENSG00000115866 .
    GeneIDi 1615.
    KEGGi hsa:1615.
    UCSCi uc002tux.1. human.

    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.
    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

    ArrayExpressi P14868.
    Bgeei P14868.
    CleanExi HS_DARS.
    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

    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 1, 2014
    This is version 152 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