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Reviewed, UniProtKB/Swiss-Prot Q9NSE4 (SYIM_HUMAN)

Last modified November 3, 2009. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Isoleucyl-tRNA synthetase, mitochondrial
    EC=6.1.1.5
Alternative name(s):
    Isoleucine--tRNA ligase
      Short name=IleRS
Gene names
Name: IARS2
OrganismHomo sapiens (Human) [Complete 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).

Subcellular location

Mitochondrion matrix By similarity.

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.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processisoleucyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrial matrix

Inferred from Experiment. Source: Reactome

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

isoleucine-tRNA ligase activity

Inferred from Experiment. Source: Reactome

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4848Mitochondrion Potential
Chain49 – 1012964Isoleucyl-tRNA synthetase, mitochondrial
PRO_0000233335

Regions

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

Sites

Binding site6671ATP By similarity

Amino acid modifications

Modified residue1861Phosphoserine Ref.6
Modified residue1891N6-acetyllysine Ref.8
Modified residue2331N6-acetyllysine Ref.8
Modified residue2411N6-acetyllysine Ref.8
Modified residue7751N6-acetyllysine Ref.8
Modified residue7811N6-acetyllysine Ref.8

Natural variations

Natural variant141A → V: dbSNP rs2577154.
VAR_059862
Natural variant5221I → V: dbSNP rs11800305.
VAR_034526

Experimental info

Sequence conflict6471P → L in BAB14164. Ref.5
Sequence conflict9071I → T in BAB14164. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9NSE4-1 [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: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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.
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 56-1012.
Tissue: Liver, Placenta and Skin.
[5]"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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 142-1012.
[6]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, MASS SPECTROMETRY.
Tissue: Epithelium.
[7]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-189; LYS-233; LYS-241; LYS-775 AND LYS-781, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

AY267462 mRNA. Translation: AAP94033.1.
AC103590 Genomic DNA. No translation available.
D28500 mRNA. Translation: BAA95147.1.
BC010218 mRNA. Translation: AAH10218.2.
BC040376 mRNA. Translation: AAH40376.2.
BC047880 mRNA. Translation: AAH47880.3.
AK001188 mRNA. Translation: BAA91544.1. Frameshift.
AK022665 mRNA. Translation: BAB14164.1. Different initiation.
IPIIPI00017283.
RefSeqNP_060530.3.
UniGeneHs.262823

3D structure databases

HSSPHSSP built from PDB template 1FFY based on UniProtKB P41972.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9NSE4. 2 interactions.
STRINGQ9NSE4.

PTM databases

PhosphoSiteQ9NSE4.

Proteomic databases

PRIDEQ9NSE4.

Genome annotation databases

EnsemblENST00000302637; ENSP00000303279; ENSG00000067704; Homo sapiens. [Genome view]
ENST00000366922; ENSP00000355889; ENSG00000067704; Homo sapiens. [Genome view]
GeneID55699.
KEGGhsa:55699.
NMPDRfig|9606.3.peg.3090.
UCSCuc001hmc.1. human.

Organism-specific databases

CTD55699.
GeneCardsGC01P218334.
HGNCHGNC:29685. IARS2.
HPAHPA024212.
HPA024594.
HPA024596.
PharmGKBPA142671670.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ9NSE4.
HOVERGENQ9NSE4.
OMAFPMRGNL.

Enzyme and pathway databases

BRENDA6.1.1.5. 247.
ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ9NSE4.
BgeeQ9NSE4.
CleanExHS_IARS2.
GenevestigatorQ9NSE4.
GermOnlineENSG00000067704. Homo sapiens.

Family and domain databases

InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR010663. DNA_glyclase/IsotRNA_synth_Znf.
IPR002301. Ile-tRNA-synt_Ia.
IPR015905. Ile-tRNA-synt_Ia_N.
IPR018353. Isoleucyl-tRNA_synthetase.
IPR014729. Rossmann-like_a/b/a_fold.
IPR013155. V/L/I-tRNA-synth_anticodon-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHERPTHR11946:SF9. Ile-tRNA-synt_Ia. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view]
PRINTSPR00984. TRNASYNTHILE.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00167. L-Isoleucine.
NextBio60534.

Entry information

Entry nameSYIM_HUMAN
AccessionPrimary (citable) accession number: Q9NSE4
Secondary accession number(s): Q1M2P9 expand/collapse secondary AC list , Q6PI85, Q7L439, Q86WU9, Q96D91, Q9H9Q8, Q9NW42
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: May 2, 2006
Last modified: November 3, 2009
This is version 59 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Human chromosome 1

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents