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)

D3DP78

- D3DP78_HUMAN

UniProt

D3DP78 - D3DP78_HUMAN

Protein
Submitted name:

Aspartyl-tRNA synthetase, isoform CRA_b

Gene

DARS

Organism
Homo sapiens (Human)
Status
Unreviewed - Annotation score: 1 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 33 (01 Oct 2014)
      Sequence version 1 (23 Mar 2010)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    GO - Molecular functioni

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

    GO - Biological processi

    1. aspartyl-tRNA aminoacylation Source: InterPro

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetaseUniRule annotationImported, Ligase

    Keywords - Biological processi

    Protein biosynthesisUniRule annotation

    Keywords - Ligandi

    ATP-bindingUniRule annotation, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Submitted name:
    Aspartyl-tRNA synthetase, isoform CRA_bImported
    Gene namesi
    Name:DARSImported
    ORF Names:hCG_25752Imported
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: InterPro

    Structurei

    3D structure databases

    SMRiD3DP78. Positions 1-468.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the class-II aminoacyl-tRNA synthetase family.UniRule annotation

    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]

    Sequencei

    Sequence statusi: Complete.

    D3DP78-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIQSQEKPDR VLVRVRDLTI QKADEVVWVR ARVHTSRAKG KQCFLVLRQQ    50
    QFNVQALVAV GDHASKQMVK FAANINKESI VDVEGVVRKV NQKIGSCTQQ 100
    DVELHVQKIY VISLAEPRLP LQLDDAVRPE AEGEEEGRAT VNQDTRLDNR 150
    VIDLRTSTSQ AVFRLQSGIC HLFRETLINK GFVEIQTPKI ISAASEGGAN 200
    VFTVSYFKNN AYLAQSPQLY KQMCICADFE KVFSIGPVFR AEDSNTHRHL 250
    TEFVGLDIEM AFNYHYHEVM EEIADTMVQI FKGLQERFQT EIQTVNKQFP 300
    CEPFKFLEPT LRLEYCEALA MLREAGVEMG DEDDLSTPNE KLLGHLVKEK 350
    YDTDFYILDK YPLAVRPFYT MPDPRNPKQS NSYDMFMRGE EILSGAQRIH 400
    DPQLLTERAL HHGIDLEKIK AYIDSFRFGA PPHAGGGIGL ERVTMLFLGL 450
    HNVRQTSMFP RDPKRLTP 468
    Length:468
    Mass (Da):53,464
    Last modified:March 23, 2010 - v1
    Checksum:i92F9E738158A442A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH471058 Genomic DNA. Translation: EAX11618.1.
    CH471058 Genomic DNA. Translation: EAX11619.1.
    UniGeneiHs.503787.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH471058 Genomic DNA. Translation: EAX11618.1 .
    CH471058 Genomic DNA. Translation: EAX11619.1 .
    UniGenei Hs.503787.

    3D structure databases

    SMRi D3DP78. Positions 1-468.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    ChiTaRSi DARS. human.
    NextBioi 35489815.

    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. "The sequence of the human genome."
      Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.
      , Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R., Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D., McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B., Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.
      Science 291:1304-1351(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE.

    Entry informationi

    Entry nameiD3DP78_HUMAN
    AccessioniPrimary (citable) accession number: D3DP78
    Entry historyi
    Integrated into UniProtKB/TrEMBL: March 23, 2010
    Last sequence update: March 23, 2010
    Last modified: October 1, 2014
    This is version 33 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.