Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

C9JQM9

- C9JQM9_HUMAN

UniProt

C9JQM9 - C9JQM9_HUMAN

Protein
Submitted name:

Aspartate--tRNA ligase, cytoplasmic

Gene

DARS

Organism
Homo sapiens (Human)
Status
Unreviewed - Annotation score: 1 out of 5- Experimental evidence at protein leveli
  1. Functioni

    GO - Molecular functioni

    1. aspartate-tRNA ligase activity Source: InterPro
    2. ATP binding Source: InterPro
    3. nucleic acid binding Source: InterPro

    GO - Biological processi

    1. aspartyl-tRNA aminoacylation Source: InterPro

    Names & Taxonomyi

    Protein namesi
    Submitted name:
    Aspartate--tRNA ligase, cytoplasmicImported
    Gene namesi
    Name:DARSImported
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:2678. DARS.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: InterPro

    PTM / Processingi

    Proteomic databases

    PRIDEiC9JQM9.

    Expressioni

    Gene expression databases

    ArrayExpressiC9JQM9.
    BgeeiC9JQM9.

    Structurei

    3D structure databases

    ProteinModelPortaliC9JQM9.
    SMRiC9JQM9. Positions 1-131.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Phylogenomic databases

    HOGENOMiHOG000213672.

    Family and domain databases

    Gene3Di2.40.50.140. 1 hit.
    InterProiIPR018150. aa-tRNA-synt_II-like.
    IPR004523. Asp-tRNA_synthase.
    IPR012340. NA-bd_OB-fold.
    IPR004365. NA-bd_OB_tRNA.
    [Graphical view]
    PANTHERiPTHR22594. PTHR22594. 1 hit.
    PTHR22594:SF10. PTHR22594:SF10. 1 hit.
    PfamiPF01336. tRNA_anti-codon. 1 hit.
    [Graphical view]
    SUPFAMiSSF50249. SSF50249. 1 hit.

    Sequencei

    Sequence statusi: Fragment.

    C9JQM9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIQSQEKPDR VLVRVRDLTI QKADEVVWVR ARVHTSRAKG KQCFLVLRQQ    50
    QFNVQALVAV GDHASKQMVK FAANINKESI VDVEGVVRKV NQKIGSCTQQ 100
    DVELHVQKIY VISLAEPRLP LQLDDAVRPE AEGEE 135
    Length:135
    Mass (Da):15,282
    Last modified:November 3, 2009 - v1
    Checksum:i08A6854638AEB3B9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei135 – 1351Imported

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC011999 Genomic DNA. No translation available.
    AC093391 Genomic DNA. No translation available.

    Genome annotation databases

    EnsembliENST00000449218; ENSP00000388801; ENSG00000115866.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC011999 Genomic DNA. No translation available.
    AC093391 Genomic DNA. No translation available.

    3D structure databases

    ProteinModelPortali C9JQM9.
    SMRi C9JQM9. Positions 1-131.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi C9JQM9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000449218 ; ENSP00000388801 ; ENSG00000115866 .

    Organism-specific databases

    HGNCi HGNC:2678. DARS.
    GenAtlasi Search...

    Phylogenomic databases

    HOGENOMi HOG000213672.

    Miscellaneous databases

    ChiTaRSi DARS. human.
    NextBioi 35487428.

    Gene expression databases

    ArrayExpressi C9JQM9.
    Bgeei C9JQM9.

    Family and domain databases

    Gene3Di 2.40.50.140. 1 hit.
    InterProi IPR018150. aa-tRNA-synt_II-like.
    IPR004523. Asp-tRNA_synthase.
    IPR012340. NA-bd_OB-fold.
    IPR004365. NA-bd_OB_tRNA.
    [Graphical view ]
    PANTHERi PTHR22594. PTHR22594. 1 hit.
    PTHR22594:SF10. PTHR22594:SF10. 1 hit.
    Pfami PF01336. tRNA_anti-codon. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50249. SSF50249. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "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].
    2. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    4. Ensembl
      Submitted (JUL-2011) to UniProtKB
      Cited for: IDENTIFICATION.

    Entry informationi

    Entry nameiC9JQM9_HUMAN
    AccessioniPrimary (citable) accession number: C9JQM9
    Entry historyi
    Integrated into UniProtKB/TrEMBL: November 3, 2009
    Last sequence update: November 3, 2009
    Last modified: October 1, 2014
    This is version 34 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)
    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

    Caution

    The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

    Keywords - Technical termi

    Complete proteome, Reference proteomeImported

    External Data

    Dasty 3