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Q9NSE4 (SYIM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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 caution

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

The sequence BAB14164.1 differs from that shown. Reason: Erroneous initiation.

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_0000233335

Regions

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

Sites

Binding site6671ATP By similarity

Amino acid modifications

Modified residue741N6-acetyllysine; alternate By similarity
Modified residue741N6-succinyllysine; alternate By similarity
Modified residue1891N6-acetyllysine Ref.7
Modified residue1941N6-succinyllysine By similarity
Modified residue2331N6-acetyllysine Ref.7
Modified residue2411N6-acetyllysine; alternate Ref.7
Modified residue2411N6-succinyllysine; alternate By similarity
Modified residue4791N6-succinyllysine By similarity
Modified residue5001N6-succinyllysine By similarity
Modified residue7251N6-acetyllysine By similarity
Modified residue7751N6-acetyllysine; alternate Ref.7
Modified residue7751N6-succinyllysine; alternate By similarity
Modified residue7811N6-acetyllysine; alternate Ref.7
Modified residue7811N6-succinyllysine; alternate By similarity

Natural variations

Natural variant141A → V.
Corresponds to variant rs2577154 [ dbSNP | Ensembl ].
VAR_059862
Natural variant5221I → V.
Corresponds to variant rs11800305 [ dbSNP | Ensembl ].
VAR_034526

Experimental info

Sequence conflict6471P → L in BAB14164. Ref.6
Sequence conflict9071I → T in BAB14164. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q9NSE4 [UniParc].

Last modified May 2, 2006. Version 2.
Checksum: 7AAAC0C9DAD7A8C7

FASTA1,012113,792
        10         20         30         40         50         60 
MRWGLRPRGP GAAALATARS LWGTPRLPCS PGWQGATKRL LVRSVSGASN HQPNSNSGRY 

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

       130        140        150        160        170        180 
DPHVGHALNK ILKDIANRFH MMNGSKIHFV PGWDCHGLPI EIKVLSELGR EAQNLSAMEI 

       190        200        210        220        230        240 
RKKARSFAKA AIEKQKSAFI RWGIMADWNN CYYTFDGKYE AKQLRTFYQM YDKGLVYRSY 

       250        260        270        280        290        300 
KPVFWSPSSR TALAEAELEY NPEHVSRSIY VKFPLLKPSP KLASLIDGSS PVSILVWTTQ 

       310        320        330        340        350        360 
PWTIPANEAV CYMPESKYAV VKCSKSGDLY VLAADKVASV ASTLETTFET ISTLSGVDLE 

       370        380        390        400        410        420 
NGTCSHPLIP DKASPLLPAN HVTMAKGTGL VHTAPAHGME DYGVASQHNL PMDCLVDEDG 

       430        440        450        460        470        480 
VFTDVAGPEL QNKAVLEEGT DVVIKMLQTA KNLLKEEKLV HSYPYDWRTK KPVVIRASKQ 

       490        500        510        520        530        540 
WFINITDIKT AAKELLKKVK FIPGSALNGM VEMMDRRPYW CISRQRVWGV PIPVFHHKTK 

       550        560        570        580        590        600 
DEYLINSQTT EHIVKLVEQH GSDIWWTLPP EQLLPKEVLS EVGGPDALEY VPGQDILDIW 

       610        620        630        640        650        660 
FDSGTSWSYV LPGPDQRADL YLEGKDQLGG WFQSSLLTSV AARKRAPYKT VIVHGFTLGE 

       670        680        690        700        710        720 
KGEKMSKSLG NVIHPDVVVN GGQDQSKEPP YGADVLRWWV ADSNVFTEVA IGPSVLNAAR 

       730        740        750        760        770        780 
DDISKLRNTL RFLLGNVADF NPETDSIPVN DMYVIDQYML HLLQDLANKI TELYKQYDFG 

       790        800        810        820        830        840 
KVVRLLRTFY TRELSNFYFS IIKDRLYCEK ENDPKRRSCQ TALVEILDVI VRSFAPILPH 

       850        860        870        880        890        900 
LAEEVFQHIP YIKEPKSVFR TGWISTSSIW KKPGLEEAVE SACAMRDSFL GSIPGKNAAE 

       910        920        930        940        950        960 
YKVITVIEPG LLFEIIEMLQ SEETSSTSQL NELMMASEST LLAQEPREMT ADVIELKGKF 

       970        980        990       1000       1010 
LINLEGGDIR EESSYKVIVM PTTKEKCPRC WKYTAESSDT LCPRCAEVVS GK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_060530.3. NM_018060.3.
UniGeneHs.262823.

3D structure databases

ProteinModelPortalQ9NSE4.
SMRQ9NSE4. Positions 60-1009.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120824. 17 interactions.
MINTMINT-1490144.

Chemistry

DrugBankDB00167. L-Isoleucine.

PTM databases

PhosphoSiteQ9NSE4.

Polymorphism databases

DMDM94730583.

Proteomic databases

PaxDbQ9NSE4.
PRIDEQ9NSE4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302637; ENSP00000303279; ENSG00000067704.
GeneID55699.
KEGGhsa:55699.
UCSCuc001hmc.3. human.

Organism-specific databases

CTD55699.
GeneCardsGC01P220267.
HGNCHGNC:29685. IARS2.
HPAHPA024212.
HPA024594.
HPA024596.
MIM612801. gene.
neXtProtNX_Q9NSE4.
PharmGKBPA142671670.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0060.
HOVERGENHBG059862.
InParanoidQ9NSE4.
KOK01870.
OMAKGRSEWC.
PhylomeDBQ9NSE4.
TreeFamTF300518.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ9NSE4.
BgeeQ9NSE4.
CleanExHS_IARS2.
GenevestigatorQ9NSE4.

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

GenomeRNAi55699.
NextBio60534.
PROQ9NSE4.
SOURCESearch...

Entry information

Entry nameSYIM_HUMAN
AccessionPrimary (citable) accession number: Q9NSE4
Secondary accession number(s): B2RPG8 expand/collapse secondary AC list , Q1M2P9, Q6PI85, Q7L439, Q86WU9, Q96D91, Q9H9Q8, Q9NW42
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: May 2, 2006
Last modified: April 16, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries