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Q15046 (SYK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysine--tRNA ligase

EC=6.1.1.6
Alternative name(s):
Lysyl-tRNA synthetase
Short name=LysRS
Gene names
Name:KARS
Synonyms:KIAA0070
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length597 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.14

Catalytic activity

ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys). HAMAP-Rule MF_00252

Enzyme regulation

Up-regulated by DARS and EEF1A1, but not by AIMP2. HAMAP-Rule MF_00252

Subunit structure

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. Ref.9 Ref.11 Ref.12 Ref.13 Ref.15

Subcellular location

Isoform Cytoplasmic: Cytoplasm. Nucleus. Cell membrane; Peripheral membrane protein. Secreted. Note: Secretion is induced by TNF-alpha. Ref.2 Ref.13 Ref.14

Isoform Mitochondrial: Mitochondrion Ref.2 Ref.13 Ref.14.

Domain

The N-terminal domain (1-65) of the cytoplasmic isoform isa 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. HAMAP-Rule MF_00252

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.23

Miscellaneous

Shares a bidirectional promoter with TERF2IP/RAP1 (Ref.10).

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Sequence caution

The sequence BAA06688.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processHost-virus interaction
Protein biosynthesis
   Cellular componentCell membrane
Cytoplasm
Membrane
Mitochondrion
Nucleus
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCharcot-Marie-Tooth disease
Deafness
Disease mutation
Neurodegeneration
Neuropathy
Non-syndromic deafness
   LigandATP-binding
Metal-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processdiadenosine tetraphosphate biosynthetic process

Inferred from electronic annotation. Source: Ensembl

gene expression

Traceable author statement. Source: Reactome

lysyl-tRNA aminoacylation

Inferred from direct assay Ref.2. Source: UniProtKB

tRNA aminoacylation for protein translation

Traceable author statement. Source: Reactome

tRNA processing

Non-traceable author statement Ref.2. Source: UniProtKB

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentaminoacyl-tRNA synthetase multienzyme complex

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

microtubule cytoskeleton

Inferred from direct assay. Source: HPA

mitochondrial matrix

Traceable author statement. Source: Reactome

mitochondrion

Inferred from direct assay Ref.2. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

amino acid binding

Inferred from electronic annotation. Source: Ensembl

lysine-tRNA ligase activity

Inferred from direct assay Ref.2. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

tRNA binding

Non-traceable author statement Ref.2. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AIMP2Q131553EBI-356367,EBI-745226

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Cytoplasmic (identifier: Q15046-1)

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.
Isoform Mitochondrial (identifier: Q15046-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 597596Lysine--tRNA ligase HAMAP-Rule MF_00252
PRO_0000152765

Regions

Nucleotide binding323 – 3253ATP HAMAP-Rule MF_00252
Nucleotide binding331 – 3322ATP HAMAP-Rule MF_00252
Nucleotide binding494 – 4952ATP HAMAP-Rule MF_00252
Nucleotide binding550 – 5534ATP HAMAP-Rule MF_00252

Sites

Metal binding4871Calcium
Metal binding4941Calcium
Binding site2771Substrate; via carbonyl oxygen
Binding site3011Substrate
Binding site3391Substrate
Binding site3411Substrate
Binding site4971Substrate
Binding site5011Substrate

Amino acid modifications

Modified residue21N-acetylalanine Ref.7 Ref.16 Ref.19 Ref.20
Modified residue881N6-acetyllysine Ref.17
Modified residue1411N6-acetyllysine Ref.17

Natural variations

Alternative sequence1 – 2121MAAVQ…KLSKN → MLTQAAVRLVRGSLRKTSWA EWGHRELRLGQLAPFTAPHK DKSFSDQRS in isoform Mitochondrial.
VSP_038481
Natural variant1051L → H in CMTRIB; severely affects enzyme activity. Ref.22
VAR_064911
Natural variant1451Y → H in DFNB89. Ref.23
VAR_070233
Natural variant1791G → A.
Corresponds to variant rs11557665 [ dbSNP | Ensembl ].
VAR_052640
Natural variant2741I → M in CMTRIB. Ref.22
VAR_064912
Natural variant3491D → N in DFNB89. Ref.23
VAR_070234
Natural variant5951T → S. Ref.2 Ref.3 Ref.22
Corresponds to variant rs6834 [ dbSNP | Ensembl ].
VAR_016105

Experimental info

Mutagenesis1 – 6565Missing: Loss of nuclear localization, but no effect on packaging into HIV-1. Ref.13
Isoform Mitochondrial:
Sequence conflict481R → G in AAG30114. Ref.2

Secondary structure

............................................................................ 597
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Cytoplasmic [UniParc].

Last modified April 16, 2002. Version 3.
Checksum: E7770953332D905D

FASTA59768,048
        10         20         30         40         50         60 
MAAVQAAEVK VDGSEPKLSK NELKRRLKAE KKVAEKEAKQ KELSEKQLSQ ATAAATNHTT 

        70         80         90        100        110        120 
DNGVGPEEES VDPNQYYKIR SQAIHQLKVN GEDPYPHKFH VDISLTDFIQ KYSHLQPGDH 

       130        140        150        160        170        180 
LTDITLKVAG RIHAKRASGG KLIFYDLRGE GVKLQVMANS RNYKSEEEFI HINNKLRRGD 

       190        200        210        220        230        240 
IIGVQGNPGK TKKGELSIIP YEITLLSPCL HMLPHLHFGL KDKETRYRQR YLDLILNDFV 

       250        260        270        280        290        300 
RQKFIIRSKI ITYIRSFLDE LGFLEIETPM MNIIPGGAVA KPFITYHNEL DMNLYMRIAP 

       310        320        330        340        350        360 
ELYHKMLVVG GIDRVYEIGR QFRNEGIDLT HNPEFTTCEF YMAYADYHDL MEITEKMVSG 

       370        380        390        400        410        420 
MVKHITGSYK VTYHPDGPEG QAYDVDFTPP FRRINMVEEL EKALGMKLPE TNLFETEETR 

       430        440        450        460        470        480 
KILDDICVAK AVECPPPRTT ARLLDKLVGE FLEVTCINPT FICDHPQIMS PLAKWHRSKE 

       490        500        510        520        530        540 
GLTERFELFV MKKEICNAYT ELNDPMRQRQ LFEEQAKAKA AGDDEAMFID ENFCTALEYG 

       550        560        570        580        590 
LPPTAGWGMG IDRVAMFLTD SNNIKEVLLF PAMKPEDKKE NVATTDTLES TTVGTSV 

« Hide

Isoform Mitochondrial [UniParc].

Checksum: 294DA1CE5A137AD6
Show »

FASTA62571,497

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]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].
[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]"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].
[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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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]"Compound heterozygosity for loss-of-function lysyl-tRNA synthetase mutations in a patient with peripheral neuropathy."
McLaughlin H.M., Sakaguchi R., Liu C., Igarashi T., Pehlivan D., Chu K., Iyer R., Cruz P., Cherukuri P.F., Hansen N.F., Mullikin J.C., Biesecker L.G., Wilson T.E., Ionasescu V., Nicholson G., Searby C., Talbot K., Vance J.M. expand/collapse author list , Zuchner S., Szigeti K., Lupski J.R., Hou Y.M., Green E.D., Antonellis A.
Am. J. Hum. Genet. 87:560-566(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CMTRIB HIS-105 AND MET-274, VARIANT SER-595.
[23]"Mutations in KARS, encoding lysyl-tRNA synthetase, cause autosomal-recessive nonsyndromic hearing impairment DFNB89."
University of Washington Center for Mendelian Genomics
Santos-Cortez R.L., Lee K., Azeem Z., Antonellis P.J., Pollock L.M., Khan S., Ullah I., Andrade-Elizondo P.B., Chiu I., Adams M.D., Basit S., Smith J.D., Nickerson D.A., McDermott B.M. Jr., Ahmad W., Leal S.M.
Am. J. Hum. Genet. 93:132-140(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DFNB89 HIS-145 AND ASN-349.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001123561.1. NM_001130089.1.
NP_005539.1. NM_005548.2.
UniGeneHs.3100.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BJUX-ray2.31A/B/C/D70-581[»]
4DPGX-ray2.84A/B/C/D/E/F/G/H70-581[»]
ProteinModelPortalQ15046.
SMRQ15046. Positions 71-576.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109938. 62 interactions.
DIPDIP-29725N.
IntActQ15046. 19 interactions.
MINTMINT-1154971.
STRING9606.ENSP00000325448.

Chemistry

BindingDBQ15046.
ChEMBLCHEMBL5575.
DrugBankDB00123. L-Lysine.

PTM databases

PhosphoSiteQ15046.

Polymorphism databases

DMDM20178333.

Proteomic databases

PaxDbQ15046.
PRIDEQ15046.

Protocols and materials databases

DNASU3735.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302445; ENSP00000303043; ENSG00000065427. [Q15046-1]
ENST00000319410; ENSP00000325448; ENSG00000065427. [Q15046-2]
GeneID3735.
KEGGhsa:3735.
UCSCuc002feq.3. human. [Q15046-1]
uc002fer.3. human. [Q15046-2]

Organism-specific databases

CTD3735.
GeneCardsGC16M075661.
HGNCHGNC:6215. KARS.
HPAHPA041345.
HPA041550.
MIM601421. gene.
613641. phenotype.
613916. phenotype.
neXtProtNX_Q15046.
Orphanet254334. Autosomal recessive intermediate Charcot-Marie-Tooth disease type B.
90636. Autosomal recessive nonsyndromic sensorineural deafness type DFNB.
PharmGKBPA30016.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1190.
HOGENOMHOG000236577.
HOVERGENHBG002562.
KOK04567.
OMADLMDFTE.
OrthoDBEOG7XSTD7.
PhylomeDBQ15046.
TreeFamTF300365.

Enzyme and pathway databases

BRENDA6.1.1.6. 2681.
ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ15046.
BgeeQ15046.
CleanExHS_KARS.
GenevestigatorQ15046.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
HAMAPMF_00252. Lys_tRNA_synth_class2.
InterProIPR004364. 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]
PANTHERPTHR22594. PTHR22594. 1 hit.
PTHR22594:SF4. PTHR22594:SF4. 1 hit.
PfamPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
PRINTSPR00982. TRNASYNTHLYS.
SUPFAMSSF50249. SSF50249. 1 hit.
TIGRFAMsTIGR00499. lysS_bact. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKARS. human.
EvolutionaryTraceQ15046.
GeneWikiKARS_(gene).
GenomeRNAi3735.
NextBio14617.
PROQ15046.
SOURCESearch...

Entry information

Entry nameSYK_HUMAN
AccessionPrimary (citable) accession number: Q15046
Secondary accession number(s): A8MSK1 expand/collapse secondary AC list , D3DUK4, O14946, Q96J25, Q9HB23
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 16, 2002
Last modified: April 16, 2014
This is version 132 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 16

Human chromosome 16: entries, gene names and cross-references to MIM

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries