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Q9NSE4

- SYIM_HUMAN

UniProt

Q9NSE4 - SYIM_HUMAN

Protein

Isoleucine--tRNA ligase, mitochondrial

Gene

IARS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 2 (02 May 2006)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei667 – 6671ATPBy similarity

    GO - Molecular functioni

    1. aminoacyl-tRNA editing activity Source: InterPro
    2. ATP binding Source: UniProtKB-KW
    3. isoleucine-tRNA ligase activity Source: UniProtKB-EC

    GO - Biological processi

    1. gene expression Source: Reactome
    2. isoleucyl-tRNA aminoacylation Source: InterPro
    3. 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_15302. Mitochondrial tRNA aminoacylation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isoleucine--tRNA ligase, mitochondrial (EC:6.1.1.5)
    Alternative name(s):
    Isoleucyl-tRNA synthetase
    Short name:
    IleRS
    Gene namesi
    Name:IARS2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:29685. IARS2.

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. mitochondrial matrix Source: Reactome
    3. mitochondrion Source: HPA

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142671670.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4848MitochondrionSequence AnalysisAdd
    BLAST
    Chaini49 – 1012964Isoleucine--tRNA ligase, mitochondrialPRO_0000233335Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei74 – 741N6-acetyllysine; alternateBy similarity
    Modified residuei74 – 741N6-succinyllysine; alternateBy similarity
    Modified residuei189 – 1891N6-acetyllysine1 Publication
    Modified residuei194 – 1941N6-succinyllysineBy similarity
    Modified residuei233 – 2331N6-acetyllysine1 Publication
    Modified residuei241 – 2411N6-acetyllysine; alternate1 Publication
    Modified residuei241 – 2411N6-succinyllysine; alternateBy similarity
    Modified residuei479 – 4791N6-succinyllysineBy similarity
    Modified residuei500 – 5001N6-succinyllysineBy similarity
    Modified residuei725 – 7251N6-acetyllysineBy similarity
    Modified residuei775 – 7751N6-acetyllysine; alternate1 Publication
    Modified residuei775 – 7751N6-succinyllysine; alternateBy similarity
    Modified residuei781 – 7811N6-acetyllysine; alternate1 Publication
    Modified residuei781 – 7811N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9NSE4.
    PaxDbiQ9NSE4.
    PRIDEiQ9NSE4.

    PTM databases

    PhosphoSiteiQ9NSE4.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9NSE4.
    BgeeiQ9NSE4.
    CleanExiHS_IARS2.
    GenevestigatoriQ9NSE4.

    Organism-specific databases

    HPAiHPA024212.
    HPA024594.
    HPA024596.

    Interactioni

    Protein-protein interaction databases

    BioGridi120824. 19 interactions.
    IntActiQ9NSE4. 1 interaction.
    MINTiMINT-1490144.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NSE4.
    SMRiQ9NSE4. Positions 60-1009.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi116 – 12611"HIGH" regionBy similarityAdd
    BLAST
    Motifi664 – 6685"KMSKS" regionBy similarity

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0060.
    HOVERGENiHBG059862.
    InParanoidiQ9NSE4.
    KOiK01870.
    OMAiEYPEGHI.
    PhylomeDBiQ9NSE4.
    TreeFamiTF300518.

    Family and domain databases

    Gene3Di1.10.730.10. 1 hit.
    3.40.50.620. 2 hits.
    3.90.740.10. 1 hit.
    HAMAPiMF_02002. Ile_tRNA_synth_type1.
    InterProiIPR001412. aa-tRNA-synth_I_CS.
    IPR002300. aa-tRNA-synth_Ia.
    IPR002301. Ile-tRNA-ligase.
    IPR023585. Ile-tRNA-ligase_type1.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR009080. tRNAsynth_1a_anticodon-bd.
    IPR013155. V/L/I-tRNA-synth_anticodon-bd.
    IPR009008. Val/Leu/Ile-tRNA-synth_edit.
    IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
    [Graphical view]
    PANTHERiPTHR11946:SF9. PTHR11946:SF9. 1 hit.
    PfamiPF08264. Anticodon_1. 1 hit.
    PF00133. tRNA-synt_1. 1 hit.
    PF06827. zf-FPG_IleRS. 1 hit.
    [Graphical view]
    PRINTSiPR00984. TRNASYNTHILE.
    SUPFAMiSSF47323. SSF47323. 1 hit.
    SSF50677. SSF50677. 1 hit.
    TIGRFAMsiTIGR00392. ileS. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9NSE4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRWGLRPRGP GAAALATARS LWGTPRLPCS PGWQGATKRL LVRSVSGASN     50
    HQPNSNSGRY RDTVLLPQTS FPMKLLGRQQ PDTELEIQQK CGFSELYSWQ 100
    RERKVKTEFC LHDGPPYANG DPHVGHALNK ILKDIANRFH MMNGSKIHFV 150
    PGWDCHGLPI EIKVLSELGR EAQNLSAMEI RKKARSFAKA AIEKQKSAFI 200
    RWGIMADWNN CYYTFDGKYE AKQLRTFYQM YDKGLVYRSY KPVFWSPSSR 250
    TALAEAELEY NPEHVSRSIY VKFPLLKPSP KLASLIDGSS PVSILVWTTQ 300
    PWTIPANEAV CYMPESKYAV VKCSKSGDLY VLAADKVASV ASTLETTFET 350
    ISTLSGVDLE NGTCSHPLIP DKASPLLPAN HVTMAKGTGL VHTAPAHGME 400
    DYGVASQHNL PMDCLVDEDG VFTDVAGPEL QNKAVLEEGT DVVIKMLQTA 450
    KNLLKEEKLV HSYPYDWRTK KPVVIRASKQ WFINITDIKT AAKELLKKVK 500
    FIPGSALNGM VEMMDRRPYW CISRQRVWGV PIPVFHHKTK DEYLINSQTT 550
    EHIVKLVEQH GSDIWWTLPP EQLLPKEVLS EVGGPDALEY VPGQDILDIW 600
    FDSGTSWSYV LPGPDQRADL YLEGKDQLGG WFQSSLLTSV AARKRAPYKT 650
    VIVHGFTLGE KGEKMSKSLG NVIHPDVVVN GGQDQSKEPP YGADVLRWWV 700
    ADSNVFTEVA IGPSVLNAAR DDISKLRNTL RFLLGNVADF NPETDSIPVN 750
    DMYVIDQYML HLLQDLANKI TELYKQYDFG KVVRLLRTFY TRELSNFYFS 800
    IIKDRLYCEK ENDPKRRSCQ TALVEILDVI VRSFAPILPH LAEEVFQHIP 850
    YIKEPKSVFR TGWISTSSIW KKPGLEEAVE SACAMRDSFL GSIPGKNAAE 900
    YKVITVIEPG LLFEIIEMLQ SEETSSTSQL NELMMASEST LLAQEPREMT 950
    ADVIELKGKF LINLEGGDIR EESSYKVIVM PTTKEKCPRC WKYTAESSDT 1000
    LCPRCAEVVS GK 1012
    Length:1,012
    Mass (Da):113,792
    Last modified:May 2, 2006 - v2
    Checksum:i7AAAC0C9DAD7A8C7
    GO

    Sequence cautioni

    The sequence BAA91544.1 differs from that shown. Reason: Frameshift at position 879.
    The sequence BAB14164.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti647 – 6471P → L in BAB14164. (PubMed:14702039)Curated
    Sequence conflicti907 – 9071I → T in BAB14164. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti14 – 141A → V.
    Corresponds to variant rs2577154 [ dbSNP | Ensembl ].
    VAR_059862
    Natural varianti522 – 5221I → V.
    Corresponds to variant rs11800305 [ dbSNP | Ensembl ].
    VAR_034526

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY267462 mRNA. Translation: AAP94033.1.
    AC103590 Genomic DNA. No translation available.
    D28500 mRNA. Translation: BAA95147.1.
    CH471100 Genomic DNA. Translation: EAW93305.1.
    BC010218 mRNA. Translation: AAH10218.2.
    BC040376 mRNA. Translation: AAH40376.2.
    BC047880 mRNA. Translation: AAH47880.3.
    BC137438 mRNA. Translation: AAI37439.1.
    AK001188 mRNA. Translation: BAA91544.1. Frameshift.
    AK022665 mRNA. Translation: BAB14164.1. Different initiation.
    CCDSiCCDS1523.1.
    RefSeqiNP_060530.3. NM_018060.3.
    UniGeneiHs.262823.

    Genome annotation databases

    EnsembliENST00000302637; ENSP00000303279; ENSG00000067704.
    GeneIDi55699.
    KEGGihsa:55699.
    UCSCiuc001hmc.3. human.

    Polymorphism databases

    DMDMi94730583.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY267462 mRNA. Translation: AAP94033.1 .
    AC103590 Genomic DNA. No translation available.
    D28500 mRNA. Translation: BAA95147.1 .
    CH471100 Genomic DNA. Translation: EAW93305.1 .
    BC010218 mRNA. Translation: AAH10218.2 .
    BC040376 mRNA. Translation: AAH40376.2 .
    BC047880 mRNA. Translation: AAH47880.3 .
    BC137438 mRNA. Translation: AAI37439.1 .
    AK001188 mRNA. Translation: BAA91544.1 . Frameshift.
    AK022665 mRNA. Translation: BAB14164.1 . Different initiation.
    CCDSi CCDS1523.1.
    RefSeqi NP_060530.3. NM_018060.3.
    UniGenei Hs.262823.

    3D structure databases

    ProteinModelPortali Q9NSE4.
    SMRi Q9NSE4. Positions 60-1009.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120824. 19 interactions.
    IntActi Q9NSE4. 1 interaction.
    MINTi MINT-1490144.

    Chemistry

    DrugBanki DB00167. L-Isoleucine.

    PTM databases

    PhosphoSitei Q9NSE4.

    Polymorphism databases

    DMDMi 94730583.

    Proteomic databases

    MaxQBi Q9NSE4.
    PaxDbi Q9NSE4.
    PRIDEi Q9NSE4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000302637 ; ENSP00000303279 ; ENSG00000067704 .
    GeneIDi 55699.
    KEGGi hsa:55699.
    UCSCi uc001hmc.3. human.

    Organism-specific databases

    CTDi 55699.
    GeneCardsi GC01P220267.
    HGNCi HGNC:29685. IARS2.
    HPAi HPA024212.
    HPA024594.
    HPA024596.
    MIMi 612801. gene.
    neXtProti NX_Q9NSE4.
    PharmGKBi PA142671670.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0060.
    HOVERGENi HBG059862.
    InParanoidi Q9NSE4.
    KOi K01870.
    OMAi EYPEGHI.
    PhylomeDBi Q9NSE4.
    TreeFami TF300518.

    Enzyme and pathway databases

    Reactomei REACT_15302. Mitochondrial tRNA aminoacylation.

    Miscellaneous databases

    GenomeRNAii 55699.
    NextBioi 60534.
    PROi Q9NSE4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NSE4.
    Bgeei Q9NSE4.
    CleanExi HS_IARS2.
    Genevestigatori Q9NSE4.

    Family and domain databases

    Gene3Di 1.10.730.10. 1 hit.
    3.40.50.620. 2 hits.
    3.90.740.10. 1 hit.
    HAMAPi MF_02002. Ile_tRNA_synth_type1.
    InterProi IPR001412. aa-tRNA-synth_I_CS.
    IPR002300. aa-tRNA-synth_Ia.
    IPR002301. Ile-tRNA-ligase.
    IPR023585. Ile-tRNA-ligase_type1.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR009080. tRNAsynth_1a_anticodon-bd.
    IPR013155. V/L/I-tRNA-synth_anticodon-bd.
    IPR009008. Val/Leu/Ile-tRNA-synth_edit.
    IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
    [Graphical view ]
    PANTHERi PTHR11946:SF9. PTHR11946:SF9. 1 hit.
    Pfami PF08264. Anticodon_1. 1 hit.
    PF00133. tRNA-synt_1. 1 hit.
    PF06827. zf-FPG_IleRS. 1 hit.
    [Graphical view ]
    PRINTSi PR00984. TRNASYNTHILE.
    SUPFAMi SSF47323. SSF47323. 1 hit.
    SSF50677. SSF50677. 1 hit.
    TIGRFAMsi TIGR00392. ileS. 1 hit.
    PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of human mitochondrial isoleucine tRNA synthetase gene."
      Shan Y.X., Guo Z.K., Huang C.Q., Ye G.M., Tang W.W., Yu L.
      Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Structure and evolution of two human isoleucyl-tRNA synthetases."
      Shiba K., Suzuki N., Shigesada K., Schimmel P., Noda T.
      Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-1012.
      Tissue: Brain.
    5. "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].
      Tissue: Brain, Liver, Placenta and Skin.
    6. "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] OF 142-1012.
    7. "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-189; LYS-233; LYS-241; LYS-775 AND LYS-781, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSYIM_HUMAN
    AccessioniPrimary (citable) accession number: Q9NSE4
    Secondary accession number(s): B2RPG8
    , Q1M2P9, Q6PI85, Q7L439, Q86WU9, Q96D91, Q9H9Q8, Q9NW42
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2006
    Last sequence update: May 2, 2006
    Last modified: October 1, 2014
    This is version 109 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

    Complete proteome, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. Human chromosome 1
      Human chromosome 1: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3