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Protein

Lysine--tRNA ligase

Gene

KARS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA (PubMed:9278442, PubMed:18029264, PubMed:18272479). When secreted, acts as a signaling molecule that induces immune response through the activation of monocyte/macrophages (PubMed:15851690). Catalyzes the synthesis of the signaling molecule diadenosine tetraphosphate (Ap4A), and thereby mediates disruption of the complex between HINT1 and MITF and the concomitant activation of MITF transcriptional activity (PubMed:5338216, PubMed:14975237, PubMed:19524539, PubMed:23159739).7 Publications
(Microbial infection) Interacts with HIV-1 virus GAG protein, facilitating the selective packaging of tRNA3(Lys), the primer for reverse transcription initiation.1 Publication

Miscellaneous

Shares a bidirectional promoter with TERF2IP/RAP1.1 Publication

Catalytic activityi

ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys).3 Publications

Enzyme regulationi

Up-regulated by DARS and EEF1A1, but not by AIMP2.1 Publication

Kineticsi

Kcat is 0.31 (sec-1) for aminoacylation for tRNA(Lys).1 Publication
  1. KM=1.19 µM for tRNA(Lys)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei277Substrate; via carbonyl oxygen2 Publications1
    Binding sitei301Substrate3 Publications1
    Binding sitei339Substrate3 Publications1
    Binding sitei341Substrate3 Publications1
    Binding sitei497Substrate3 Publications1
    Binding sitei501Substrate3 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi323 – 325ATP1 Publication3
    Nucleotide bindingi331 – 332ATP1 Publication2
    Nucleotide bindingi494 – 495ATP1 Publication2
    Nucleotide bindingi550 – 553ATP1 Publication4

    GO - Molecular functioni

    • amino acid binding Source: Ensembl
    • ATP adenylyltransferase activity Source: UniProtKB
    • ATP binding Source: UniProtKB-KW
    • identical protein binding Source: IntAct
    • lysine-tRNA ligase activity Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB
    • tRNA binding Source: UniProtKB

    GO - Biological processi

    • activation of MAPK activity Source: CAFA
    • basophil activation involved in immune response Source: CAFA
    • diadenosine tetraphosphate biosynthetic process Source: UniProtKB
    • ERK1 and ERK2 cascade Source: CAFA
    • lysyl-tRNA aminoacylation Source: UniProtKB
    • negative regulation of cell proliferation Source: CAFA
    • positive regulation of cytokine production involved in inflammatory response Source: CAFA
    • positive regulation of cytokine secretion involved in immune response Source: CAFA
    • positive regulation of ERK1 and ERK2 cascade Source: CAFA
    • positive regulation of macrophage activation Source: CAFA
    • positive regulation of macrophage chemotaxis Source: CAFA
    • positive regulation of metallopeptidase activity Source: CAFA
    • positive regulation of p38MAPK cascade Source: CAFA
    • positive regulation of transcription, DNA-templated Source: CAFA
    • response to X-ray Source: Ensembl
    • tRNA aminoacylation for protein translation Source: Reactome
    • tRNA processing Source: UniProtKB
    • tumor necrosis factor-mediated signaling pathway Source: CAFA
    • viral process Source: UniProtKB-KW

    Keywordsi

    Molecular functionAminoacyl-tRNA synthetase, Ligase, Transferase
    Biological processHost-virus interaction, Protein biosynthesis
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi6.1.1.6. 2681.
    ReactomeiR-HSA-2408517. SeMet incorporation into proteins.
    R-HSA-379716. Cytosolic tRNA aminoacylation.
    R-HSA-379726. Mitochondrial tRNA aminoacylation.
    SIGNORiQ15046.

    Protein family/group databases

    MoonProtiQ15046.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysine--tRNA ligase (EC:2.7.7.-3 Publications, EC:6.1.1.63 Publications)
    Alternative name(s):
    Lysyl-tRNA synthetase
    Short name:
    LysRS
    Gene namesi
    Name:KARS
    Synonyms:KIAA0070
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 16

    Organism-specific databases

    EuPathDBiHostDB:ENSG00000065427.14.
    HGNCiHGNC:6215. KARS.
    MIMi601421. gene.
    neXtProtiNX_Q15046.

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Mitochondrion, Nucleus, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Charcot-Marie-Tooth disease, recessive, intermediate type, B (CMTRIB)1 Publication
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Recessive intermediate forms of Charcot-Marie-Tooth disease are characterized by clinical and pathologic features intermediate between demyelinating and axonal peripheral neuropathies, and motor median nerve conduction velocities ranging from 25 to 45 m/sec.
    See also OMIM:613641
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_064911105L → H in CMTRIB; severely affects enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs267607194Ensembl.1
    Natural variantiVAR_064912274I → M in CMTRIB. 1 PublicationCorresponds to variant dbSNP:rs146955132Ensembl.1
    Deafness, autosomal recessive, 89 (DFNB89)2 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA form of non-syndromic deafness characterized by bilateral, prelingual, moderate to severe hearing loss affecting all frequencies.
    See also OMIM:613916
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_070233145Y → H in DFNB89. 1 PublicationCorresponds to variant dbSNP:rs397514745Ensembl.1
    Natural variantiVAR_070234349D → N in DFNB89. 1 PublicationCorresponds to variant dbSNP:rs397514746Ensembl.1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi1 – 65Missing : Loss of nuclear localization, but no effect on packaging into HIV-1. 1 PublicationAdd BLAST65
    Mutagenesisi101V → D, R or W: Disrupts interaction with AIMP2 and the multisynthase complex. 1 Publication1
    Mutagenesisi207S → A: Strongly reduced production of diadenosine tetraphosphate (Ap4A). Reduced protein phosphorylation. 1 Publication1
    Mutagenesisi207S → D: Phosphomimetic mutant that strongly enhances translocation into the nucleus and production of diadenosine tetraphosphate (Ap4A). Almost complete loss of tRNA ligase activity. 1 Publication1
    Mutagenesisi207S → R: Strongly decreased tRNA ligase activity. 1 Publication1
    Mutagenesisi207S → Y: Almost complete loss of tRNA ligase activity. 1 Publication1
    Mutagenesisi346D → R: Induces protein aggregation. Releases from the subunit complex. 1 Publication1
    Mutagenesisi540G → Y: Disrupts interaction with AIMP2 and the multisynthase complex. Increases production of diadenosine tetraphosphate (Ap4A). Almost complete loss of tRNA ligase activity. 1 Publication1

    Keywords - Diseasei

    Charcot-Marie-Tooth disease, Deafness, Disease mutation, Neurodegeneration, Neuropathy, Non-syndromic deafness

    Organism-specific databases

    DisGeNETi3735.
    MalaCardsiKARS.
    MIMi613641. phenotype.
    613916. phenotype.
    OpenTargetsiENSG00000065427.
    Orphaneti254334. Autosomal recessive intermediate Charcot-Marie-Tooth disease type B.
    90636. Autosomal recessive non-syndromic sensorineural deafness type DFNB.
    PharmGKBiPA30016.

    Chemistry databases

    ChEMBLiCHEMBL5575.
    DrugBankiDB00123. L-Lysine.

    Polymorphism and mutation databases

    BioMutaiKARS.
    DMDMi20178333.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedCombined sources1 Publication
    ChainiPRO_00001527652 – 597Lysine--tRNA ligaseAdd BLAST596

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylalanineCombined sources1 Publication1
    Modified residuei88N6-acetyllysineCombined sources1
    Modified residuei141N6-acetyllysineCombined sources1
    Modified residuei207Phosphoserine1 Publication1
    Modified residuei590PhosphoserineBy similarity1
    Modified residuei591PhosphothreonineBy similarity1
    Modified residuei596PhosphoserineBy similarity1

    Post-translational modificationi

    Phosphorylated on a serine residue after mast cell stimulation with immunoglobulin E (IgE).By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    EPDiQ15046.
    MaxQBiQ15046.
    PaxDbiQ15046.
    PeptideAtlasiQ15046.
    PRIDEiQ15046.

    PTM databases

    iPTMnetiQ15046.
    PhosphoSitePlusiQ15046.
    SwissPalmiQ15046.

    Expressioni

    Gene expression databases

    BgeeiENSG00000065427.
    CleanExiHS_KARS.
    ExpressionAtlasiQ15046. baseline and differential.
    GenevisibleiQ15046. HS.

    Organism-specific databases

    HPAiHPA041345.
    HPA041550.

    Interactioni

    Subunit structurei

    Homodimer and tetradimer (PubMed:18272479, PubMed:23159739, PubMed:26074468, PubMed:28887846). Part of a multisubunit complex that groups tRNA ligases for Arg (RARS), Asp (DARS), Gln (QARS), Ile (IARS), Leu (LARS), Lys (KARS), Met (MARS) the bifunctional ligase for Glu and Pro (EPRS) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18 (PubMed:19131329, PubMed:19289464, PubMed:23159739). Interacts with AIMP2 (via N-terminus) and MITF (PubMed:9878398, PubMed:14975237, PubMed:15220430, PubMed:23159739, PubMed:26074468).10 Publications
    (Microbial infection) Interacts directly with HIV-1 virus GAG protein (PubMed:12756246, PubMed:15220430).2 Publications

    Binary interactionsi

    Show more details

    GO - Molecular functioni

    • identical protein binding Source: IntAct
    • protein homodimerization activity Source: UniProtKB

    Protein-protein interaction databases

    BioGridi109938. 85 interactors.
    CORUMiQ15046.
    DIPiDIP-29725N.
    IntActiQ15046. 26 interactors.
    MINTiMINT-1154971.
    STRINGi9606.ENSP00000325448.

    Chemistry databases

    BindingDBiQ15046.

    Structurei

    Secondary structure

    1597
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi73 – 89Combined sources17
    Helixi105 – 112Combined sources8
    Beta strandi126 – 137Combined sources12
    Beta strandi139 – 149Combined sources11
    Beta strandi152 – 159Combined sources8
    Helixi160 – 162Combined sources3
    Helixi166 – 175Combined sources10
    Beta strandi181 – 190Combined sources10
    Beta strandi196 – 207Combined sources12
    Turni216 – 218Combined sources3
    Helixi223 – 228Combined sources6
    Helixi230 – 236Combined sources7
    Helixi238 – 260Combined sources23
    Beta strandi270 – 274Combined sources5
    Beta strandi277 – 279Combined sources3
    Beta strandi284 – 287Combined sources4
    Turni288 – 291Combined sources4
    Beta strandi292 – 296Combined sources5
    Helixi301 – 309Combined sources9
    Beta strandi314 – 322Combined sources9
    Beta strandi328 – 330Combined sources3
    Beta strandi333 – 343Combined sources11
    Helixi347 – 366Combined sources20
    Beta strandi367 – 373Combined sources7
    Beta strandi383 – 386Combined sources4
    Beta strandi392 – 395Combined sources4
    Helixi396 – 404Combined sources9
    Helixi411 – 413Combined sources3
    Helixi417 – 429Combined sources13
    Helixi440 – 451Combined sources12
    Helixi453 – 455Combined sources3
    Beta strandi460 – 463Combined sources4
    Helixi467 – 469Combined sources3
    Beta strandi477 – 479Combined sources3
    Beta strandi482 – 490Combined sources9
    Beta strandi493 – 501Combined sources9
    Helixi505 – 519Combined sources15
    Turni520 – 522Combined sources3
    Beta strandi524 – 526Combined sources3
    Helixi531 – 538Combined sources8
    Beta strandi543 – 550Combined sources8
    Helixi551 – 558Combined sources8
    Helixi564 – 567Combined sources4
    Beta strandi568 – 570Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3BJUX-ray2.31A/B/C/D70-582[»]
    4DPGX-ray2.84A/B/C/D/E/F/G/H70-581[»]
    4YCUX-ray2.10A/B70-581[»]
    4YCWX-ray2.90A/B/E/F70-581[»]
    ProteinModelPortaliQ15046.
    SMRiQ15046.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15046.

    Family & Domainsi

    Domaini

    The N-terminal domain (1-65) of the cytoplasmic isoform is a functional tRNA-binding domain, is required for nuclear localization, is involved in the interaction with DARS, but has a repulsive role in the binding to EEF1A1. A central domain (208-259) is involved in homodimerization and is required for interaction with HIV-1 GAG and incorporation into virions. The C-terminal domain (452-597) is not required for interaction with AIMP2.2 Publications

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG1885. Eukaryota.
    COG1190. LUCA.
    GeneTreeiENSGT00550000074841.
    HOGENOMiHOG000236577.
    HOVERGENiHBG002562.
    InParanoidiQ15046.
    KOiK04567.
    OMAiEDPYPHK.
    OrthoDBiEOG091G03SI.
    PhylomeDBiQ15046.
    TreeFamiTF300365.

    Family and domain databases

    CDDicd00775. LysRS_core. 1 hit.
    HAMAPiMF_00252. Lys_tRNA_synth_class2. 1 hit.
    InterProiView protein in InterPro
    IPR004364. aa-tRNA-synt_II.
    IPR006195. aa-tRNA-synth_II.
    IPR002313. Lys-tRNA-ligase_II.
    IPR034762. Lys-tRNA-ligase_II_bac/euk.
    IPR018149. Lys-tRNA-synth_II_C.
    IPR012340. NA-bd_OB-fold.
    IPR004365. NA-bd_OB_tRNA.
    PfamiView protein in Pfam
    PF00152. tRNA-synt_2. 1 hit.
    PF01336. tRNA_anti-codon. 1 hit.
    PIRSFiPIRSF039101. LysRS2. 1 hit.
    PRINTSiPR00982. TRNASYNTHLYS.
    SUPFAMiSSF50249. SSF50249. 1 hit.
    TIGRFAMsiTIGR00499. lysS_bact. 1 hit.
    PROSITEiView protein in PROSITE
    PS50862. AA_TRNA_LIGASE_II. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform Cytoplasmic (identifier: Q15046-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MAAVQAAEVK VDGSEPKLSK NELKRRLKAE KKVAEKEAKQ KELSEKQLSQ
    60 70 80 90 100
    ATAAATNHTT DNGVGPEEES VDPNQYYKIR SQAIHQLKVN GEDPYPHKFH
    110 120 130 140 150
    VDISLTDFIQ KYSHLQPGDH LTDITLKVAG RIHAKRASGG KLIFYDLRGE
    160 170 180 190 200
    GVKLQVMANS RNYKSEEEFI HINNKLRRGD IIGVQGNPGK TKKGELSIIP
    210 220 230 240 250
    YEITLLSPCL HMLPHLHFGL KDKETRYRQR YLDLILNDFV RQKFIIRSKI
    260 270 280 290 300
    ITYIRSFLDE LGFLEIETPM MNIIPGGAVA KPFITYHNEL DMNLYMRIAP
    310 320 330 340 350
    ELYHKMLVVG GIDRVYEIGR QFRNEGIDLT HNPEFTTCEF YMAYADYHDL
    360 370 380 390 400
    MEITEKMVSG MVKHITGSYK VTYHPDGPEG QAYDVDFTPP FRRINMVEEL
    410 420 430 440 450
    EKALGMKLPE TNLFETEETR KILDDICVAK AVECPPPRTT ARLLDKLVGE
    460 470 480 490 500
    FLEVTCINPT FICDHPQIMS PLAKWHRSKE GLTERFELFV MKKEICNAYT
    510 520 530 540 550
    ELNDPMRQRQ LFEEQAKAKA AGDDEAMFID ENFCTALEYG LPPTAGWGMG
    560 570 580 590
    IDRVAMFLTD SNNIKEVLLF PAMKPEDKKE NVATTDTLES TTVGTSV
    Length:597
    Mass (Da):68,048
    Last modified:April 16, 2002 - v3
    Checksum:iE7770953332D905D
    GO
    Isoform Mitochondrial (identifier: Q15046-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-21: MAAVQAAEVKVDGSEPKLSKN → MLTQAAVRLVRGSLRKTSWAEWGHRELRLGQLAPFTAPHKDKSFSDQRS

    Note: Mitochondrial precursor. Contains a mitochondrial transit peptide at positions 1-16.Curated
    Show »
    Length:625
    Mass (Da):71,497
    Checksum:i294DA1CE5A137AD6
    GO

    Sequence cautioni

    The sequence BAA06688 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Isoform Mitochondrial (identifier: Q15046-2)
    Sequence conflicti48R → G in AAG30114 (PubMed:10952987).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_064911105L → H in CMTRIB; severely affects enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs267607194Ensembl.1
    Natural variantiVAR_070233145Y → H in DFNB89. 1 PublicationCorresponds to variant dbSNP:rs397514745Ensembl.1
    Natural variantiVAR_052640179G → A. Corresponds to variant dbSNP:rs11557665Ensembl.1
    Natural variantiVAR_064912274I → M in CMTRIB. 1 PublicationCorresponds to variant dbSNP:rs146955132Ensembl.1
    Natural variantiVAR_070234349D → N in DFNB89. 1 PublicationCorresponds to variant dbSNP:rs397514746Ensembl.1
    Natural variantiVAR_079741350L → H Found in a patient with hypertrophic cardiomyopathy and mild intellectual disability together with proximal muscle weakness; unknown pathological significance. 1 Publication1
    Natural variantiVAR_079742390P → R Found in a patient with hypertrophic cardiomyopathy and mild intellectual disability together with proximal muscle weakness; unknown pathological significance. 1 Publication1
    Natural variantiVAR_079743438R → W Found in patients with severe infantile visual loss with progressive microcephaly and developmental delay as well as seizures and abnormal subcortical white matter; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs761527468Ensembl.1
    Natural variantiVAR_079744477R → H Probable disease-associated mutation found in a family with sensorineural hearing loss and leukoencephalopathy; decreases tRNA-lysine aminoacylation; induces protein aggregation; releases from the subunit complex; no effect on cytoplasmic location; no effect on oligomerization. 1 PublicationCorresponds to variant dbSNP:rs778748895Ensembl.1
    Natural variantiVAR_079745505P → S Probable disease-associated mutation found in a family with sensorineural hearing loss and leukoencephalopathy; decreases tRNA-lysine aminoacylation; slightly induces protein aggregation; no effect on cytoplasmic location; no effect on oligomerization. 1 Publication1
    Natural variantiVAR_079746525E → K Found in patients with severe infantile visual loss with progressive microcephaly and developmental delay as well as seizures and abnormal subcortical white matter; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs770522582Ensembl.1
    Natural variantiVAR_016105595T → S3 PublicationsCorresponds to variant dbSNP:rs6834Ensembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_0384811 – 21MAAVQ…KLSKN → MLTQAAVRLVRGSLRKTSWA EWGHRELRLGQLAPFTAPHK DKSFSDQRS in isoform Mitochondrial. 1 PublicationAdd BLAST21

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D32053 mRNA. Translation: BAA22084.1.
    AF285758 mRNA. Translation: AAG30114.1.
    D31890 mRNA. Translation: BAA06688.1. Different initiation.
    AC025287 Genomic DNA. No translation available.
    CH471114 Genomic DNA. Translation: EAW95622.1.
    CH471114 Genomic DNA. Translation: EAW95624.1.
    BC004132 mRNA. Translation: AAH04132.1.
    CCDSiCCDS10923.1. [Q15046-1]
    CCDS45532.1. [Q15046-2]
    RefSeqiNP_001123561.1. NM_001130089.1. [Q15046-2]
    NP_005539.1. NM_005548.2. [Q15046-1]
    UniGeneiHs.3100.

    Genome annotation databases

    EnsembliENST00000302445; ENSP00000303043; ENSG00000065427. [Q15046-1]
    ENST00000319410; ENSP00000325448; ENSG00000065427. [Q15046-2]
    GeneIDi3735.
    KEGGihsa:3735.
    UCSCiuc002feq.4. human. [Q15046-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Similar proteinsi

    Entry informationi

    Entry nameiSYK_HUMAN
    AccessioniPrimary (citable) accession number: Q15046
    Secondary accession number(s): A8MSK1
    , D3DUK4, O14946, Q96J25, Q9HB23
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: April 16, 2002
    Last modified: January 31, 2018
    This is version 171 of the entry and version 3 of the sequence. See 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. Human chromosome 16
      Human chromosome 16: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families