Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8BIJ6 (SYIM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isoleucine--tRNA ligase, mitochondrial

EC=6.1.1.5
Alternative name(s):
Isoleucyl-tRNA synthetase
Short name=IleRS
Gene names
Name:Iars2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1012 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02002

Subcellular location

Mitochondrion matrix By similarity HAMAP-Rule MF_02002.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4848Mitochondrion Potential
Chain49 – 1012964Isoleucine--tRNA ligase, mitochondrial HAMAP-Rule MF_02002
PRO_0000233337

Regions

Motif116 – 12611"HIGH" region By similarity
Motif664 – 6685"KMSKS" region By similarity

Sites

Binding site6671ATP By similarity

Amino acid modifications

Modified residue561N6-succinyllysine Ref.3
Modified residue741N6-acetyllysine; alternate Ref.4
Modified residue741N6-succinyllysine; alternate Ref.3
Modified residue1941N6-succinyllysine Ref.3
Modified residue2331N6-acetyllysine By similarity
Modified residue2411N6-acetyllysine; alternate By similarity
Modified residue2411N6-succinyllysine; alternate Ref.3
Modified residue4791N6-succinyllysine Ref.3
Modified residue5001N6-succinyllysine Ref.3
Modified residue7251N6-acetyllysine Ref.4
Modified residue7751N6-acetyllysine; alternate Ref.4
Modified residue7751N6-succinyllysine; alternate Ref.3
Modified residue7811N6-acetyllysine; alternate By similarity
Modified residue7811N6-succinyllysine; alternate Ref.3

Experimental info

Sequence conflict681Q → K in BAC29337. Ref.1
Sequence conflict861E → G in BAE39055. Ref.1
Sequence conflict1191N → K in BAC29337. Ref.1
Sequence conflict7091V → M in BAC34208. Ref.1
Sequence conflict8191C → Y in BAE39055. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8BIJ6 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: A4663D3A1BC3D678

FASTA1,012112,804
        10         20         30         40         50         60 
MHWGLCPRGP GAAAVAAAGS FWGPARLPSR LGCLGMTRRL VVRSVAGADS PQSSSKGGRY 

        70         80         90        100        110        120 
RDTVLLPQTS FPMKLLGRQQ SDMELEIQQK CGFSELYSWQ RERKVKTEFC LHDGPPYANG 

       130        140        150        160        170        180 
DPHVGHALNK ILKDIANRFH MMRGSKVHFV PGWDCHGLPI ETKVLSELGV DAQSLSAMEI 

       190        200        210        220        230        240 
REKARSFAQA AIEKQKSAFV RWGVMADWNN CYYTFDPKYE AKQLRVFYQM YEKGLVYRSY 

       250        260        270        280        290        300 
KPVYWSPSSR TALAEAELEY NPEHVSRSIY VRFPLLRPPP KLESLTDASS PVSVLVWTTQ 

       310        320        330        340        350        360 
PWTIPANQAI CYMPEAKYAV VKCSASGHLY ILAEDKIAPV ASALETTFDV VAAFSGVDLE 

       370        380        390        400        410        420 
GGTCSHPLTP DKVSPLLPAT HVTMAKGTGL VHTAPAHGME DYSVASQHSL PMDCLVDEGG 

       430        440        450        460        470        480 
MFTDAAGPEL QNKAVLKEGT DVVIKMLQAT KNVLKEENIV HSYPCDWRTK TPVLIRASKQ 

       490        500        510        520        530        540 
WFVNITDIKA AAKESLKTVK FIPGAALNSM TDMLDRRPYW CISRQRVWGV PIPVFHHKTK 

       550        560        570        580        590        600 
DEYLINSQTT EHIIKLVEQH GSDVWWTLPA EQLLPAEVLA QAGGPGALEY APGQDILDIW 

       610        620        630        640        650        660 
FDSGTSWSCV LQDTQQRADL YLEGKDQLGG WFQSSLLTSV ATRSKAPFRT VMVHGFTLGE 

       670        680        690        700        710        720 
KGEKMSKSLG NVINPDTIIS GGKDHSKEPP YGADILRWWI AESNVFTEVT IGPSVLSAAR 

       730        740        750        760        770        780 
DDISKLRNTL RFLLGNLTGF NPETDSVPVK NMYVIDQYML HLIQDFATKI TDSYKQYDFG 

       790        800        810        820        830        840 
KVVRLLKAFY TRELSSFYFS IVKDRLYCEN EKDPKRRSCQ TALAEILDVL VRAFAPILPH 

       850        860        870        880        890        900 
LAEEVFQHIP YVTEPKSVFR TGWINTSSIW KKPGLEEAVE SACAMRDSFL GSIPGKNAAE 

       910        920        930        940        950        960 
YEVIIVIEPG LLFEIMEMLQ AEETSSTSQL NELMMASQTT LLAQEPRERT AGDIELTGTF 

       970        980        990       1000       1010 
VINLEGGDIR EESSYKVIVV PTAREKCPRC WKHTSETADA LCPRCAEVIG AK 

« Hide

References

[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS15596.1.
RefSeqNP_941055.1. NM_198653.2.
UniGeneMm.275841.
Mm.331142.

3D structure databases

ProteinModelPortalQ8BIJ6.
SMRQ8BIJ6. Positions 99-849.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8BIJ6. 2 interactions.
MINTMINT-1840839.

PTM databases

PhosphoSiteQ8BIJ6.

Proteomic databases

MaxQBQ8BIJ6.
PaxDbQ8BIJ6.
PRIDEQ8BIJ6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027921; ENSMUSP00000027921; ENSMUSG00000026618.
GeneID381314.
KEGGmmu:381314.
UCSCuc007dyz.1. mouse.

Organism-specific databases

CTD55699.
MGIMGI:1919586. Iars2.

Phylogenomic databases

eggNOGCOG0060.
GeneTreeENSGT00550000074910.
HOGENOMHOG000246402.
HOVERGENHBG059862.
InParanoidQ8BIJ6.
KOK01870.
OMALGHRVHY.
OrthoDBEOG72JWFN.
PhylomeDBQ8BIJ6.
TreeFamTF300518.

Gene expression databases

ArrayExpressQ8BIJ6.
BgeeQ8BIJ6.
CleanExMM_IARS2.
GenevestigatorQ8BIJ6.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02002. Ile_tRNA_synth_type1.
InterProIPR001412. 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]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view]
PRINTSPR00984. TRNASYNTHILE.
SUPFAMSSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIARS2. mouse.
NextBio401882.
PROQ8BIJ6.
SOURCESearch...

Entry information

Entry nameSYIM_MOUSE
AccessionPrimary (citable) accession number: Q8BIJ6
Secondary accession number(s): Q3TKT8, Q8BIJ0, Q8BIP3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries