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Q15046

- SYK_HUMAN

UniProt

Q15046 - SYK_HUMAN

Protein

Lysine--tRNA ligase

Gene

KARS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 3 (16 Apr 2002)
      Previous versions | rss
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    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. When secreted, acts as a signaling molecule that induces immune response through the activation of monocyte/macrophages. Catalyzes the synthesis of diadenosine oligophosphate (Ap4A), a signaling molecule involved in the activation of MITF transcriptional activity. Interacts with HIV-1 virus GAG protein, facilitating the selective packaging of tRNA3(Lys), the primer for reverse transcription initiation.2 Publications

    Catalytic activityi

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

    Enzyme regulationi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei277 – 2771Substrate; via carbonyl oxygen1 Publication
    Binding sitei301 – 3011Substrate1 Publication
    Binding sitei339 – 3391Substrate1 Publication
    Binding sitei341 – 3411Substrate1 Publication
    Metal bindingi487 – 4871Calcium
    Metal bindingi494 – 4941Calcium
    Binding sitei497 – 4971Substrate1 Publication
    Binding sitei501 – 5011Substrate1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi323 – 3253ATP1 Publication
    Nucleotide bindingi331 – 3322ATP1 Publication
    Nucleotide bindingi494 – 4952ATP1 Publication
    Nucleotide bindingi550 – 5534ATP1 Publication

    GO - Molecular functioni

    1. amino acid binding Source: Ensembl
    2. ATP binding Source: UniProtKB-KW
    3. lysine-tRNA ligase activity Source: UniProtKB
    4. metal ion binding Source: UniProtKB-KW
    5. protein binding Source: IntAct
    6. tRNA binding Source: UniProtKB

    GO - Biological processi

    1. cell death Source: UniProtKB-KW
    2. diadenosine tetraphosphate biosynthetic process Source: Ensembl
    3. gene expression Source: Reactome
    4. lysyl-tRNA aminoacylation Source: UniProtKB
    5. tRNA aminoacylation for protein translation Source: Reactome
    6. tRNA processing Source: UniProtKB
    7. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Host-virus interaction, Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi6.1.1.6. 2681.
    ReactomeiREACT_15302. Mitochondrial tRNA aminoacylation.
    REACT_15306. Cytosolic tRNA aminoacylation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysine--tRNA ligase (EC:6.1.1.6)
    Alternative name(s):
    Lysyl-tRNA synthetase
    Short name:
    LysRS
    Gene namesi
    Name:KARS
    Synonyms:KIAA0070
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:6215. KARS.

    Subcellular locationi

    GO - Cellular componenti

    1. aminoacyl-tRNA synthetase multienzyme complex Source: Ensembl
    2. cytoplasm Source: HPA
    3. cytosol Source: Reactome
    4. extracellular region Source: UniProtKB-SubCell
    5. microtubule cytoskeleton Source: HPA
    6. mitochondrial matrix Source: Reactome
    7. mitochondrion Source: UniProtKB
    8. nucleus Source: UniProtKB-SubCell
    9. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Involvement in diseasei

    Charcot-Marie-Tooth disease, recessive, intermediate type, B (CMTRIB) [MIM:613641]: A 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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti105 – 1051L → H in CMTRIB; severely affects enzyme activity. 1 Publication
    VAR_064911
    Natural varianti274 – 2741I → M in CMTRIB. 1 Publication
    VAR_064912
    Deafness, autosomal recessive, 89 (DFNB89) [MIM:613916]: A form of non-syndromic deafness characterized by bilateral, prelingual, moderate to severe hearing loss affecting all frequencies.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti145 – 1451Y → H in DFNB89. 1 Publication
    VAR_070233
    Natural varianti349 – 3491D → N in DFNB89. 1 Publication
    VAR_070234

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1 – 6565Missing: Loss of nuclear localization, but no effect on packaging into HIV-1. 1 PublicationAdd
    BLAST

    Keywords - Diseasei

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

    Organism-specific databases

    MIMi613641. phenotype.
    613916. phenotype.
    Orphaneti254334. Autosomal recessive intermediate Charcot-Marie-Tooth disease type B.
    90636. Autosomal recessive nonsyndromic sensorineural deafness type DFNB.
    PharmGKBiPA30016.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 597596Lysine--tRNA ligasePRO_0000152765Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications
    Modified residuei88 – 881N6-acetyllysine1 Publication
    Modified residuei141 – 1411N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ15046.
    PaxDbiQ15046.
    PRIDEiQ15046.

    PTM databases

    PhosphoSiteiQ15046.

    Expressioni

    Gene expression databases

    ArrayExpressiQ15046.
    BgeeiQ15046.
    CleanExiHS_KARS.
    GenevestigatoriQ15046.

    Organism-specific databases

    HPAiHPA041345.
    HPA041550.

    Interactioni

    Subunit structurei

    Homodimer; also part of a multisubunit complex that groups AIMP1, AIMP2, EEF1A1 and tRNA ligases for Arg, Asp, Glu, Gln, Ile, Leu, Lys, Met and Pro. Interacts with AIMP2 (via N-terminus) and MITF. Interacts directly with HIV-1 virus GAG protein.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AIMP2Q131553EBI-356367,EBI-745226
    RPSAP088655EBI-356367,EBI-354112

    Protein-protein interaction databases

    BioGridi109938. 62 interactions.
    DIPiDIP-29725N.
    IntActiQ15046. 21 interactions.
    MINTiMINT-1154971.
    STRINGi9606.ENSP00000325448.

    Structurei

    Secondary structure

    1
    597
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi73 – 8917
    Helixi105 – 1128
    Beta strandi126 – 14924
    Beta strandi152 – 1598
    Helixi160 – 1623
    Helixi166 – 17510
    Beta strandi181 – 19010
    Beta strandi196 – 20712
    Helixi223 – 2286
    Helixi230 – 2367
    Helixi238 – 26023
    Beta strandi270 – 2745
    Beta strandi277 – 2793
    Beta strandi284 – 2874
    Turni288 – 2914
    Beta strandi292 – 2965
    Helixi301 – 3099
    Beta strandi314 – 3229
    Beta strandi328 – 3303
    Beta strandi333 – 34311
    Helixi347 – 36620
    Beta strandi367 – 3737
    Beta strandi383 – 3864
    Beta strandi392 – 3954
    Helixi396 – 4049
    Helixi411 – 4133
    Helixi417 – 42913
    Helixi440 – 45112
    Helixi453 – 4553
    Beta strandi460 – 4634
    Helixi467 – 4693
    Beta strandi477 – 4793
    Beta strandi482 – 4909
    Beta strandi493 – 5019
    Helixi505 – 52117
    Helixi531 – 5377
    Turni538 – 5403
    Beta strandi543 – 5508
    Helixi551 – 5588
    Helixi564 – 5663
    Beta strandi568 – 5703

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BJUX-ray2.31A/B/C/D70-582[»]
    4DPGX-ray2.84A/B/C/D/E/F/G/H70-581[»]
    ProteinModelPortaliQ15046.
    SMRiQ15046. Positions 71-576.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15046.

    Family & Domainsi

    Domaini

    The N-terminal domain (1-65) of the cytoplasmic isoform is a functional tRNA-binding domain By similarity, 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.

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1190.
    HOGENOMiHOG000236577.
    HOVERGENiHBG002562.
    KOiK04567.
    OMAiMAETENK.
    OrthoDBiEOG7XSTD7.
    PhylomeDBiQ15046.
    TreeFamiTF300365.

    Family and domain databases

    Gene3Di2.40.50.140. 1 hit.
    HAMAPiMF_00252. Lys_tRNA_synth_class2.
    InterProiIPR004364. aa-tRNA-synt_II.
    IPR018150. aa-tRNA-synt_II-like.
    IPR006195. aa-tRNA-synth_II.
    IPR002313. Lys-tRNA-ligase_II.
    IPR018149. Lys-tRNA-synth_II_C.
    IPR012340. NA-bd_OB-fold.
    IPR004365. NA-bd_OB_tRNA.
    [Graphical view]
    PANTHERiPTHR22594. PTHR22594. 1 hit.
    PfamiPF00152. tRNA-synt_2. 1 hit.
    PF01336. tRNA_anti-codon. 1 hit.
    [Graphical view]
    PRINTSiPR00982. TRNASYNTHLYS.
    SUPFAMiSSF50249. SSF50249. 1 hit.
    TIGRFAMsiTIGR00499. lysS_bact. 1 hit.
    PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
    [Graphical view]

    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. Align

    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

    MAAVQAAEVK VDGSEPKLSK NELKRRLKAE KKVAEKEAKQ KELSEKQLSQ    50
    ATAAATNHTT DNGVGPEEES VDPNQYYKIR SQAIHQLKVN GEDPYPHKFH 100
    VDISLTDFIQ KYSHLQPGDH LTDITLKVAG RIHAKRASGG KLIFYDLRGE 150
    GVKLQVMANS RNYKSEEEFI HINNKLRRGD IIGVQGNPGK TKKGELSIIP 200
    YEITLLSPCL HMLPHLHFGL KDKETRYRQR YLDLILNDFV RQKFIIRSKI 250
    ITYIRSFLDE LGFLEIETPM MNIIPGGAVA KPFITYHNEL DMNLYMRIAP 300
    ELYHKMLVVG GIDRVYEIGR QFRNEGIDLT HNPEFTTCEF YMAYADYHDL 350
    MEITEKMVSG MVKHITGSYK VTYHPDGPEG QAYDVDFTPP FRRINMVEEL 400
    EKALGMKLPE TNLFETEETR KILDDICVAK AVECPPPRTT ARLLDKLVGE 450
    FLEVTCINPT FICDHPQIMS PLAKWHRSKE GLTERFELFV MKKEICNAYT 500
    ELNDPMRQRQ LFEEQAKAKA AGDDEAMFID ENFCTALEYG LPPTAGWGMG 550
    IDRVAMFLTD SNNIKEVLLF PAMKPEDKKE NVATTDTLES TTVGTSV 597
    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 BAA06688.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Isoform Mitochondrial (identifier: Q15046-2)
    Sequence conflicti48 – 481R → G in AAG30114. (PubMed:10952987)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti105 – 1051L → H in CMTRIB; severely affects enzyme activity. 1 Publication
    VAR_064911
    Natural varianti145 – 1451Y → H in DFNB89. 1 Publication
    VAR_070233
    Natural varianti179 – 1791G → A.
    Corresponds to variant rs11557665 [ dbSNP | Ensembl ].
    VAR_052640
    Natural varianti274 – 2741I → M in CMTRIB. 1 Publication
    VAR_064912
    Natural varianti349 – 3491D → N in DFNB89. 1 Publication
    VAR_070234
    Natural varianti595 – 5951T → S.3 Publications
    Corresponds to variant rs6834 [ dbSNP | Ensembl ].
    VAR_016105

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2121MAAVQ…KLSKN → MLTQAAVRLVRGSLRKTSWA EWGHRELRLGQLAPFTAPHK DKSFSDQRS in isoform Mitochondrial. 1 PublicationVSP_038481Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.3. human. [Q15046-1]
    uc002fer.3. human. [Q15046-2]

    Polymorphism databases

    DMDMi20178333.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS10923.1. [Q15046-1 ]
    CCDS45532.1. [Q15046-2 ]
    RefSeqi NP_001123561.1. NM_001130089.1. [Q15046-2 ]
    NP_005539.1. NM_005548.2. [Q15046-1 ]
    UniGenei Hs.3100.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3BJU X-ray 2.31 A/B/C/D 70-582 [» ]
    4DPG X-ray 2.84 A/B/C/D/E/F/G/H 70-581 [» ]
    ProteinModelPortali Q15046.
    SMRi Q15046. Positions 71-576.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109938. 62 interactions.
    DIPi DIP-29725N.
    IntActi Q15046. 21 interactions.
    MINTi MINT-1154971.
    STRINGi 9606.ENSP00000325448.

    Chemistry

    BindingDBi Q15046.
    ChEMBLi CHEMBL5575.
    DrugBanki DB00123. L-Lysine.

    PTM databases

    PhosphoSitei Q15046.

    Polymorphism databases

    DMDMi 20178333.

    Proteomic databases

    MaxQBi Q15046.
    PaxDbi Q15046.
    PRIDEi Q15046.

    Protocols and materials databases

    DNASUi 3735.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000302445 ; ENSP00000303043 ; ENSG00000065427 . [Q15046-1 ]
    ENST00000319410 ; ENSP00000325448 ; ENSG00000065427 . [Q15046-2 ]
    GeneIDi 3735.
    KEGGi hsa:3735.
    UCSCi uc002feq.3. human. [Q15046-1 ]
    uc002fer.3. human. [Q15046-2 ]

    Organism-specific databases

    CTDi 3735.
    GeneCardsi GC16M075661.
    HGNCi HGNC:6215. KARS.
    HPAi HPA041345.
    HPA041550.
    MIMi 601421. gene.
    613641. phenotype.
    613916. phenotype.
    neXtProti NX_Q15046.
    Orphaneti 254334. Autosomal recessive intermediate Charcot-Marie-Tooth disease type B.
    90636. Autosomal recessive nonsyndromic sensorineural deafness type DFNB.
    PharmGKBi PA30016.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1190.
    HOGENOMi HOG000236577.
    HOVERGENi HBG002562.
    KOi K04567.
    OMAi MAETENK.
    OrthoDBi EOG7XSTD7.
    PhylomeDBi Q15046.
    TreeFami TF300365.

    Enzyme and pathway databases

    BRENDAi 6.1.1.6. 2681.
    Reactomei REACT_15302. Mitochondrial tRNA aminoacylation.
    REACT_15306. Cytosolic tRNA aminoacylation.

    Miscellaneous databases

    ChiTaRSi KARS. human.
    EvolutionaryTracei Q15046.
    GeneWikii KARS_(gene).
    GenomeRNAii 3735.
    NextBioi 14617.
    PROi Q15046.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15046.
    Bgeei Q15046.
    CleanExi HS_KARS.
    Genevestigatori Q15046.

    Family and domain databases

    Gene3Di 2.40.50.140. 1 hit.
    HAMAPi MF_00252. Lys_tRNA_synth_class2.
    InterProi IPR004364. aa-tRNA-synt_II.
    IPR018150. aa-tRNA-synt_II-like.
    IPR006195. aa-tRNA-synth_II.
    IPR002313. Lys-tRNA-ligase_II.
    IPR018149. Lys-tRNA-synth_II_C.
    IPR012340. NA-bd_OB-fold.
    IPR004365. NA-bd_OB_tRNA.
    [Graphical view ]
    PANTHERi PTHR22594. PTHR22594. 1 hit.
    Pfami PF00152. tRNA-synt_2. 1 hit.
    PF01336. tRNA_anti-codon. 1 hit.
    [Graphical view ]
    PRINTSi PR00982. TRNASYNTHLYS.
    SUPFAMi SSF50249. SSF50249. 1 hit.
    TIGRFAMsi TIGR00499. lysS_bact. 1 hit.
    PROSITEi PS50862. AA_TRNA_LIGASE_II. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human lysyl-tRNA synthetase accepts nucleotide 73 variants and rescues Escherichia coli double-defective mutant."
      Shiba K., Stello T., Motegi H., Noda T., Musier-Forsyth K., Schimmel P.
      J. Biol. Chem. 272:22809-22816(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYTOPLASMIC).
      Tissue: Brain.
    2. "The human lysyl-tRNA synthetase gene encodes both the cytoplasmic and mitochondrial enzymes by means of an unusual alternative splicing of the primary transcript."
      Tolkunova E., Park H., Xia J., King M.P., Davidson E.
      J. Biol. Chem. 275:35063-35069(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL), SUBCELLULAR LOCATION, VARIANT SER-595.
    3. "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
      Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
      DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CYTOPLASMIC), VARIANT SER-595.
      Tissue: Bone marrow.
    4. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM CYTOPLASMIC).
      Tissue: Placenta.
    7. Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-10; 112-127; 142-148; 231-241; 306-314 AND 486-492, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY (ISOFORM CYTOPLASMIC).
      Tissue: Hepatoma.
    8. "Enzymatic synthesis of diadenosine tetraphosphate and diadenosine triphosphate with a purified lysyl-tRNA synthetase."
      Zamecnik P.C., Stephenson M.L., Janeway C.M., Randerath K.
      Biochem. Biophys. Res. Commun. 24:91-97(1966) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein."
      Quevillon S., Robinson J.-C., Berthonneau E., Siatecka M., Mirande M.
      J. Mol. Biol. 285:183-195(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AIMP2.
    10. "The telomeric protein Rap1 is conserved in vertebrates and is expressed from a bidirectional promoter positioned between the Rap1 and KARS genes."
      Tan M., Wei C., Price C.M.
      Gene 323:1-10(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIDIRECTIONAL PROMOTER WITH TERF2IP.
    11. "The function of lysyl-tRNA synthetase and Ap4A as signaling regulators of MITF activity in FcepsilonRI-activated mast cells."
      Lee Y.N., Nechushtan H., Figov N., Razin E.
      Immunity 20:145-151(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MIFT.
    12. "The interaction between HIV-1 Gag and human lysyl-tRNA synthetase during viral assembly."
      Javanbakht H., Halwani R., Cen S., Saadatmand J., Musier-Forsyth K., Gottlinger H., Kleiman L.
      J. Biol. Chem. 278:27644-27651(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, INTERACTION WITH HIV-1 GAG.
    13. "Cellular distribution of Lysyl-tRNA synthetase and its interaction with Gag during human immunodeficiency virus type 1 assembly."
      Halwani R., Cen S., Javanbakht H., Saadatmand J., Kim S., Shiba K., Kleiman L.
      J. Virol. 78:7553-7564(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF 1-MET--GLY-65, INTERACTION WITH AIMP2 AND HIV-1 GAG.
    14. "Human lysyl-tRNA synthetase is secreted to trigger proinflammatory response."
      Park S.G., Kim H.J., Min Y.H., Choi E.-C., Shin Y.K., Park B.-J., Lee S.W., Kim S.
      Proc. Natl. Acad. Sci. U.S.A. 102:6356-6361(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, FUNCTION.
    15. "Lysyl-tRNA synthetase interacts with EF1alpha, aspartyl-tRNA synthetase and p38 in vitro."
      Guzzo C.M., Yang D.C.H.
      Biochem. Biophys. Res. Commun. 365:718-723(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EEF1A1; AIMP2 AND DARS.
    16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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-88 AND LYS-141, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Crystal structure of tetrameric form of human lysyl-tRNA synthetase: Implications for multisynthetase complex formation."
      Guo M., Ignatov M., Musier-Forsyth K., Schimmel P., Yang X.-L.
      Proc. Natl. Acad. Sci. U.S.A. 105:2331-2336(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 70-581 IN COMPLEX WITH SUBSTRATE AND ATP.
    22. Cited for: VARIANTS CMTRIB HIS-105 AND MET-274, VARIANT SER-595.
    23. Cited for: VARIANTS DFNB89 HIS-145 AND ASN-349.

    Entry informationi

    Entry nameiSYK_HUMAN
    AccessioniPrimary (citable) accession number: Q15046
    Secondary accession number(s): A8MSK1
    , D3DUK4, O14946, Q96J25, Q9HB23
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: April 16, 2002
    Last modified: October 1, 2014
    This is version 137 of the entry and version 3 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

    Miscellaneous

    Shares a bidirectional promoter with TERF2IP/RAP1.1 Publication

    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

    External Data

    Dasty 3