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Protein

Isoleucine--tRNA ligase, mitochondrial

Gene

Iars2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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: GO_Central
  2. mitochondrial translation Source: GO_Central
Complete GO annotation...

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. cytoplasm Source: MGI
  2. cytosol Source: GO_Central
  3. mitochondrial matrix Source: UniProtKB-SubCell
  4. mitochondrion Source: MGI
Complete GO annotation...

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

BgeeiQ8BIJ6.
CleanExiMM_IARS2.
ExpressionAtlasiQ8BIJ6. baseline and differential.
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.
OMAiSYLGEHV.
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.
IPR013155. M/V/L/I-tRNA-synth_anticd-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_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

        10         20         30         40         50
MHWGLCPRGP GAAAVAAAGS FWGPARLPSR LGCLGMTRRL VVRSVAGADS
60 70 80 90 100
PQSSSKGGRY RDTVLLPQTS FPMKLLGRQQ SDMELEIQQK CGFSELYSWQ
110 120 130 140 150
RERKVKTEFC LHDGPPYANG DPHVGHALNK ILKDIANRFH MMRGSKVHFV
160 170 180 190 200
PGWDCHGLPI ETKVLSELGV DAQSLSAMEI REKARSFAQA AIEKQKSAFV
210 220 230 240 250
RWGVMADWNN CYYTFDPKYE AKQLRVFYQM YEKGLVYRSY KPVYWSPSSR
260 270 280 290 300
TALAEAELEY NPEHVSRSIY VRFPLLRPPP KLESLTDASS PVSVLVWTTQ
310 320 330 340 350
PWTIPANQAI CYMPEAKYAV VKCSASGHLY ILAEDKIAPV ASALETTFDV
360 370 380 390 400
VAAFSGVDLE GGTCSHPLTP DKVSPLLPAT HVTMAKGTGL VHTAPAHGME
410 420 430 440 450
DYSVASQHSL PMDCLVDEGG MFTDAAGPEL QNKAVLKEGT DVVIKMLQAT
460 470 480 490 500
KNVLKEENIV HSYPCDWRTK TPVLIRASKQ WFVNITDIKA AAKESLKTVK
510 520 530 540 550
FIPGAALNSM TDMLDRRPYW CISRQRVWGV PIPVFHHKTK DEYLINSQTT
560 570 580 590 600
EHIIKLVEQH GSDVWWTLPA EQLLPAEVLA QAGGPGALEY APGQDILDIW
610 620 630 640 650
FDSGTSWSCV LQDTQQRADL YLEGKDQLGG WFQSSLLTSV ATRSKAPFRT
660 670 680 690 700
VMVHGFTLGE KGEKMSKSLG NVINPDTIIS GGKDHSKEPP YGADILRWWI
710 720 730 740 750
AESNVFTEVT IGPSVLSAAR DDISKLRNTL RFLLGNLTGF NPETDSVPVK
760 770 780 790 800
NMYVIDQYML HLIQDFATKI TDSYKQYDFG KVVRLLKAFY TRELSSFYFS
810 820 830 840 850
IVKDRLYCEN EKDPKRRSCQ TALAEILDVL VRAFAPILPH LAEEVFQHIP
860 870 880 890 900
YVTEPKSVFR TGWINTSSIW KKPGLEEAVE SACAMRDSFL GSIPGKNAAE
910 920 930 940 950
YEVIIVIEPG LLFEIMEMLQ AEETSSTSQL NELMMASQTT LLAQEPRERT
960 970 980 990 1000
AGDIELTGTF VINLEGGDIR EESSYKVIVV PTAREKCPRC WKHTSETADA
1010
LCPRCAEVIG AK
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ8BIJ6.
SMRiQ8BIJ6. Positions 99-849.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8BIJ6. 2 interactions.
MINTiMINT-1840839.

PTM databases

PhosphoSiteiQ8BIJ6.

Proteomic databases

MaxQBiQ8BIJ6.
PaxDbiQ8BIJ6.
PRIDEiQ8BIJ6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi55699.
MGIiMGI:1919586. Iars2.

Phylogenomic databases

eggNOGiCOG0060.
GeneTreeiENSGT00550000074910.
HOGENOMiHOG000246402.
HOVERGENiHBG059862.
InParanoidiQ8BIJ6.
KOiK01870.
OMAiSYLGEHV.
OrthoDBiEOG72JWFN.
PhylomeDBiQ8BIJ6.
TreeFamiTF300518.

Miscellaneous databases

ChiTaRSiIars2. mouse.
NextBioi401882.
PROiQ8BIJ6.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BIJ6.
CleanExiMM_IARS2.
ExpressionAtlasiQ8BIJ6. baseline and differential.
GenevestigatoriQ8BIJ6.

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.
IPR013155. M/V/L/I-tRNA-synth_anticd-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_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]
ProtoNetiSearch...

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: March 4, 2015
This is version 100 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.