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Q8BIJ6

- SYIM_MOUSE

UniProt

Q8BIJ6 - SYIM_MOUSE

Protein

Isoleucine--tRNA ligase, mitochondrial

Gene

Iars2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      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. isoleucyl-tRNA aminoacylation Source: InterPro

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1919586. Iars2.

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4848MitochondrionSequence AnalysisAdd
    BLAST
    Chaini49 – 1012964Isoleucine--tRNA ligase, mitochondrialPRO_0000233337Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei56 – 561N6-succinyllysine1 Publication
    Modified residuei74 – 741N6-acetyllysine; alternate1 Publication
    Modified residuei74 – 741N6-succinyllysine; alternate1 Publication
    Modified residuei194 – 1941N6-succinyllysine1 Publication
    Modified residuei233 – 2331N6-acetyllysineBy similarity
    Modified residuei241 – 2411N6-acetyllysine; alternateBy similarity
    Modified residuei241 – 2411N6-succinyllysine; alternate1 Publication
    Modified residuei479 – 4791N6-succinyllysine1 Publication
    Modified residuei500 – 5001N6-succinyllysine1 Publication
    Modified residuei725 – 7251N6-acetyllysine1 Publication
    Modified residuei775 – 7751N6-acetyllysine; alternate1 Publication
    Modified residuei775 – 7751N6-succinyllysine; alternate1 Publication
    Modified residuei781 – 7811N6-acetyllysine; alternateBy similarity
    Modified residuei781 – 7811N6-succinyllysine; alternate1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ8BIJ6.
    PaxDbiQ8BIJ6.
    PRIDEiQ8BIJ6.

    PTM databases

    PhosphoSiteiQ8BIJ6.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8BIJ6.
    BgeeiQ8BIJ6.
    CleanExiMM_IARS2.
    GenevestigatoriQ8BIJ6.

    Interactioni

    Protein-protein interaction databases

    IntActiQ8BIJ6. 2 interactions.
    MINTiMINT-1840839.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BIJ6.
    SMRiQ8BIJ6. Positions 99-849.
    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.
    GeneTreeiENSGT00550000074910.
    HOGENOMiHOG000246402.
    HOVERGENiHBG059862.
    InParanoidiQ8BIJ6.
    KOiK01870.
    OMAiLGHRVHY.
    OrthoDBiEOG72JWFN.
    PhylomeDBiQ8BIJ6.
    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.

    Q8BIJ6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHWGLCPRGP GAAAVAAAGS FWGPARLPSR LGCLGMTRRL VVRSVAGADS     50
    PQSSSKGGRY RDTVLLPQTS FPMKLLGRQQ SDMELEIQQK CGFSELYSWQ 100
    RERKVKTEFC LHDGPPYANG DPHVGHALNK ILKDIANRFH MMRGSKVHFV 150
    PGWDCHGLPI ETKVLSELGV DAQSLSAMEI REKARSFAQA AIEKQKSAFV 200
    RWGVMADWNN CYYTFDPKYE AKQLRVFYQM YEKGLVYRSY KPVYWSPSSR 250
    TALAEAELEY NPEHVSRSIY VRFPLLRPPP KLESLTDASS PVSVLVWTTQ 300
    PWTIPANQAI CYMPEAKYAV VKCSASGHLY ILAEDKIAPV ASALETTFDV 350
    VAAFSGVDLE GGTCSHPLTP DKVSPLLPAT HVTMAKGTGL VHTAPAHGME 400
    DYSVASQHSL PMDCLVDEGG MFTDAAGPEL QNKAVLKEGT DVVIKMLQAT 450
    KNVLKEENIV HSYPCDWRTK TPVLIRASKQ WFVNITDIKA AAKESLKTVK 500
    FIPGAALNSM TDMLDRRPYW CISRQRVWGV PIPVFHHKTK DEYLINSQTT 550
    EHIIKLVEQH GSDVWWTLPA EQLLPAEVLA QAGGPGALEY APGQDILDIW 600
    FDSGTSWSCV LQDTQQRADL YLEGKDQLGG WFQSSLLTSV ATRSKAPFRT 650
    VMVHGFTLGE KGEKMSKSLG NVINPDTIIS GGKDHSKEPP YGADILRWWI 700
    AESNVFTEVT IGPSVLSAAR DDISKLRNTL RFLLGNLTGF NPETDSVPVK 750
    NMYVIDQYML HLIQDFATKI TDSYKQYDFG KVVRLLKAFY TRELSSFYFS 800
    IVKDRLYCEN EKDPKRRSCQ TALAEILDVL VRAFAPILPH LAEEVFQHIP 850
    YVTEPKSVFR TGWINTSSIW KKPGLEEAVE SACAMRDSFL GSIPGKNAAE 900
    YEVIIVIEPG LLFEIMEMLQ AEETSSTSQL NELMMASQTT LLAQEPRERT 950
    AGDIELTGTF VINLEGGDIR EESSYKVIVV PTAREKCPRC WKHTSETADA 1000
    LCPRCAEVIG AK 1012
    Length:1,012
    Mass (Da):112,804
    Last modified:March 1, 2003 - v1
    Checksum:iA4663D3A1BC3D678
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti68 – 681Q → K in BAC29337. (PubMed:16141072)Curated
    Sequence conflicti86 – 861E → G in BAE39055. (PubMed:16141072)Curated
    Sequence conflicti119 – 1191N → K in BAC29337. (PubMed:16141072)Curated
    Sequence conflicti709 – 7091V → M in BAC34208. (PubMed:16141072)Curated
    Sequence conflicti819 – 8191C → Y in BAE39055. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK166832 mRNA. Translation: BAE39055.1.
    AK036182 mRNA. Translation: BAC29337.1.
    AK048653 mRNA. Translation: BAC33410.1.
    AK050358 mRNA. Translation: BAC34208.1.
    BC052403 mRNA. Translation: AAH52403.1.
    CCDSiCCDS15596.1.
    RefSeqiNP_941055.1. NM_198653.2.
    UniGeneiMm.275841.
    Mm.331142.

    Genome annotation databases

    EnsembliENSMUST00000027921; ENSMUSP00000027921; ENSMUSG00000026618.
    GeneIDi381314.
    KEGGimmu:381314.
    UCSCiuc007dyz.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK166832 mRNA. Translation: BAE39055.1 .
    AK036182 mRNA. Translation: BAC29337.1 .
    AK048653 mRNA. Translation: BAC33410.1 .
    AK050358 mRNA. Translation: BAC34208.1 .
    BC052403 mRNA. Translation: AAH52403.1 .
    CCDSi CCDS15596.1.
    RefSeqi NP_941055.1. NM_198653.2.
    UniGenei Mm.275841.
    Mm.331142.

    3D structure databases

    ProteinModelPortali Q8BIJ6.
    SMRi Q8BIJ6. Positions 99-849.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8BIJ6. 2 interactions.
    MINTi MINT-1840839.

    PTM databases

    PhosphoSitei Q8BIJ6.

    Proteomic databases

    MaxQBi Q8BIJ6.
    PaxDbi Q8BIJ6.
    PRIDEi Q8BIJ6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000027921 ; ENSMUSP00000027921 ; ENSMUSG00000026618 .
    GeneIDi 381314.
    KEGGi mmu:381314.
    UCSCi uc007dyz.1. mouse.

    Organism-specific databases

    CTDi 55699.
    MGIi MGI:1919586. Iars2.

    Phylogenomic databases

    eggNOGi COG0060.
    GeneTreei ENSGT00550000074910.
    HOGENOMi HOG000246402.
    HOVERGENi HBG059862.
    InParanoidi Q8BIJ6.
    KOi K01870.
    OMAi LGHRVHY.
    OrthoDBi EOG72JWFN.
    PhylomeDBi Q8BIJ6.
    TreeFami TF300518.

    Miscellaneous databases

    ChiTaRSi IARS2. mouse.
    NextBioi 401882.
    PROi Q8BIJ6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8BIJ6.
    Bgeei Q8BIJ6.
    CleanExi MM_IARS2.
    Genevestigatori Q8BIJ6.

    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Cerebellum, Head and Liver.
    2. "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].
      Strain: C57BL/6.
    3. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-56; LYS-74; LYS-194; LYS-241; LYS-479; LYS-500; LYS-775 AND LYS-781, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast and Liver.
    4. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-74; LYS-725 AND LYS-775, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiSYIM_MOUSE
    AccessioniPrimary (citable) accession number: Q8BIJ6
    Secondary accession number(s): Q3TKT8, Q8BIJ0, Q8BIP3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2006
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 95 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3