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Protein

Isoleucine--tRNA ligase, mitochondrial

Gene

IARS2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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. gene expression Source: Reactome
  2. isoleucyl-tRNA aminoacylation Source: GO_Central
  3. mitochondrial translation Source: GO_Central
  4. tRNA aminoacylation for protein translation Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_15302. Mitochondrial tRNA aminoacylation.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:29685. IARS2.

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: GO_Central
  3. mitochondrial matrix Source: Reactome
  4. mitochondrion Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671670.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4848MitochondrionSequence AnalysisAdd
BLAST
Chaini49 – 1012964Isoleucine--tRNA ligase, mitochondrialPRO_0000233335Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei74 – 741N6-acetyllysine; alternateBy similarity
Modified residuei74 – 741N6-succinyllysine; alternateBy similarity
Modified residuei189 – 1891N6-acetyllysine1 Publication
Modified residuei194 – 1941N6-succinyllysineBy similarity
Modified residuei233 – 2331N6-acetyllysine1 Publication
Modified residuei241 – 2411N6-acetyllysine; alternate1 Publication
Modified residuei241 – 2411N6-succinyllysine; alternateBy similarity
Modified residuei479 – 4791N6-succinyllysineBy similarity
Modified residuei500 – 5001N6-succinyllysineBy similarity
Modified residuei725 – 7251N6-acetyllysineBy similarity
Modified residuei775 – 7751N6-acetyllysine; alternate1 Publication
Modified residuei775 – 7751N6-succinyllysine; alternateBy similarity
Modified residuei781 – 7811N6-acetyllysine; alternate1 Publication
Modified residuei781 – 7811N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9NSE4.
PaxDbiQ9NSE4.
PRIDEiQ9NSE4.

PTM databases

PhosphoSiteiQ9NSE4.

Expressioni

Gene expression databases

BgeeiQ9NSE4.
CleanExiHS_IARS2.
ExpressionAtlasiQ9NSE4. baseline and differential.
GenevestigatoriQ9NSE4.

Organism-specific databases

HPAiHPA024212.
HPA024594.
HPA024596.

Interactioni

Protein-protein interaction databases

BioGridi120824. 23 interactions.
IntActiQ9NSE4. 2 interactions.
MINTiMINT-1490144.

Structurei

3D structure databases

ProteinModelPortaliQ9NSE4.
SMRiQ9NSE4. Positions 60-1009.
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.
HOVERGENiHBG059862.
InParanoidiQ9NSE4.
KOiK01870.
OMAiSYLGEHV.
PhylomeDBiQ9NSE4.
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.

Q9NSE4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRWGLRPRGP GAAALATARS LWGTPRLPCS PGWQGATKRL LVRSVSGASN
60 70 80 90 100
HQPNSNSGRY RDTVLLPQTS FPMKLLGRQQ PDTELEIQQK CGFSELYSWQ
110 120 130 140 150
RERKVKTEFC LHDGPPYANG DPHVGHALNK ILKDIANRFH MMNGSKIHFV
160 170 180 190 200
PGWDCHGLPI EIKVLSELGR EAQNLSAMEI RKKARSFAKA AIEKQKSAFI
210 220 230 240 250
RWGIMADWNN CYYTFDGKYE AKQLRTFYQM YDKGLVYRSY KPVFWSPSSR
260 270 280 290 300
TALAEAELEY NPEHVSRSIY VKFPLLKPSP KLASLIDGSS PVSILVWTTQ
310 320 330 340 350
PWTIPANEAV CYMPESKYAV VKCSKSGDLY VLAADKVASV ASTLETTFET
360 370 380 390 400
ISTLSGVDLE NGTCSHPLIP DKASPLLPAN HVTMAKGTGL VHTAPAHGME
410 420 430 440 450
DYGVASQHNL PMDCLVDEDG VFTDVAGPEL QNKAVLEEGT DVVIKMLQTA
460 470 480 490 500
KNLLKEEKLV HSYPYDWRTK KPVVIRASKQ WFINITDIKT AAKELLKKVK
510 520 530 540 550
FIPGSALNGM VEMMDRRPYW CISRQRVWGV PIPVFHHKTK DEYLINSQTT
560 570 580 590 600
EHIVKLVEQH GSDIWWTLPP EQLLPKEVLS EVGGPDALEY VPGQDILDIW
610 620 630 640 650
FDSGTSWSYV LPGPDQRADL YLEGKDQLGG WFQSSLLTSV AARKRAPYKT
660 670 680 690 700
VIVHGFTLGE KGEKMSKSLG NVIHPDVVVN GGQDQSKEPP YGADVLRWWV
710 720 730 740 750
ADSNVFTEVA IGPSVLNAAR DDISKLRNTL RFLLGNVADF NPETDSIPVN
760 770 780 790 800
DMYVIDQYML HLLQDLANKI TELYKQYDFG KVVRLLRTFY TRELSNFYFS
810 820 830 840 850
IIKDRLYCEK ENDPKRRSCQ TALVEILDVI VRSFAPILPH LAEEVFQHIP
860 870 880 890 900
YIKEPKSVFR TGWISTSSIW KKPGLEEAVE SACAMRDSFL GSIPGKNAAE
910 920 930 940 950
YKVITVIEPG LLFEIIEMLQ SEETSSTSQL NELMMASEST LLAQEPREMT
960 970 980 990 1000
ADVIELKGKF LINLEGGDIR EESSYKVIVM PTTKEKCPRC WKYTAESSDT
1010
LCPRCAEVVS GK
Length:1,012
Mass (Da):113,792
Last modified:May 2, 2006 - v2
Checksum:i7AAAC0C9DAD7A8C7
GO

Sequence cautioni

The sequence BAA91544.1 differs from that shown. Reason: Frameshift at position 879. Curated
The sequence BAB14164.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti647 – 6471P → L in BAB14164. (PubMed:14702039)Curated
Sequence conflicti907 – 9071I → T in BAB14164. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti14 – 141A → V.
Corresponds to variant rs2577154 [ dbSNP | Ensembl ].
VAR_059862
Natural varianti522 – 5221I → V.
Corresponds to variant rs11800305 [ dbSNP | Ensembl ].
VAR_034526

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1523.1.
RefSeqiNP_060530.3. NM_018060.3.
UniGeneiHs.262823.

Genome annotation databases

EnsembliENST00000366922; ENSP00000355889; ENSG00000067704.
GeneIDi55699.
KEGGihsa:55699.
UCSCiuc001hmc.3. human.

Polymorphism databases

DMDMi94730583.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1523.1.
RefSeqiNP_060530.3. NM_018060.3.
UniGeneiHs.262823.

3D structure databases

ProteinModelPortaliQ9NSE4.
SMRiQ9NSE4. Positions 60-1009.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120824. 23 interactions.
IntActiQ9NSE4. 2 interactions.
MINTiMINT-1490144.

Chemistry

DrugBankiDB00167. L-Isoleucine.

PTM databases

PhosphoSiteiQ9NSE4.

Polymorphism databases

DMDMi94730583.

Proteomic databases

MaxQBiQ9NSE4.
PaxDbiQ9NSE4.
PRIDEiQ9NSE4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366922; ENSP00000355889; ENSG00000067704.
GeneIDi55699.
KEGGihsa:55699.
UCSCiuc001hmc.3. human.

Organism-specific databases

CTDi55699.
GeneCardsiGC01P220267.
HGNCiHGNC:29685. IARS2.
HPAiHPA024212.
HPA024594.
HPA024596.
MIMi612801. gene.
neXtProtiNX_Q9NSE4.
PharmGKBiPA142671670.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0060.
GeneTreeiENSGT00550000074910.
HOVERGENiHBG059862.
InParanoidiQ9NSE4.
KOiK01870.
OMAiSYLGEHV.
PhylomeDBiQ9NSE4.
TreeFamiTF300518.

Enzyme and pathway databases

ReactomeiREACT_15302. Mitochondrial tRNA aminoacylation.

Miscellaneous databases

GenomeRNAii55699.
NextBioi60534.
PROiQ9NSE4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NSE4.
CleanExiHS_IARS2.
ExpressionAtlasiQ9NSE4. baseline and differential.
GenevestigatoriQ9NSE4.

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

« Hide 'large scale' publications
  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.
    , 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. 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.
    , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSYIM_HUMAN
AccessioniPrimary (citable) accession number: Q9NSE4
Secondary accession number(s): B2RPG8
, Q1M2P9, Q6PI85, Q7L439, Q86WU9, Q96D91, Q9H9Q8, Q9NW42
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: May 2, 2006
Last modified: February 4, 2015
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. 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.