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Protein

Lysine--tRNA ligase

Gene

Kars

Organism
Mus musculus (Mouse)
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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei275 – 2751Substrate; via carbonyl oxygenBy similarity
Binding sitei299 – 2991SubstrateBy similarity
Binding sitei337 – 3371SubstrateBy similarity
Binding sitei339 – 3391SubstrateBy similarity
Metal bindingi485 – 4851CalciumBy similarity
Metal bindingi492 – 4921CalciumBy similarity
Binding sitei495 – 4951SubstrateBy similarity
Binding sitei499 – 4991SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi321 – 3233ATPBy similarity
Nucleotide bindingi329 – 3302ATPBy similarity
Nucleotide bindingi492 – 4932ATPBy similarity
Nucleotide bindingi548 – 5514ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.1.1.6. 3474.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1934754. Kars.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • microtubule cytoskeleton Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 595594Lysine--tRNA ligasePRO_0000152766Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei86 – 861N6-acetyllysineBy similarity
Modified residuei139 – 1391N6-acetyllysineBy similarity
Modified residuei393 – 3931PhosphoserineCombined sources
Modified residuei588 – 5881PhosphoserineCombined sources
Modified residuei589 – 5891PhosphothreonineCombined sources
Modified residuei592 – 5921PhosphoserineCombined sources
Modified residuei594 – 5941PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ99MN1.
MaxQBiQ99MN1.
PaxDbiQ99MN1.
PRIDEiQ99MN1.

PTM databases

iPTMnetiQ99MN1.
PhosphoSiteiQ99MN1.

Expressioni

Gene expression databases

BgeeiQ99MN1.
CleanExiMM_KARS.
ExpressionAtlasiQ99MN1. baseline and differential.
GenevisibleiQ99MN1. MM.

Interactioni

Subunit structurei

Homodimer (By similarity); 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.By similarity1 Publication

Protein-protein interaction databases

BioGridi220220. 2 interactions.
DIPiDIP-36058N.
IntActiQ99MN1. 3 interactions.
MINTiMINT-4136281.
STRINGi10090.ENSMUSP00000090808.

Structurei

3D structure databases

ProteinModelPortaliQ99MN1.
SMRiQ99MN1. Positions 70-574.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The N-terminal domain (1-65) is a functional tRNA-binding domain and 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. The C-terminal domain (452-597) is not required for interaction with AIMP2 (By similarity).By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1885. Eukaryota.
COG1190. LUCA.
GeneTreeiENSGT00550000074841.
HOGENOMiHOG000236577.
HOVERGENiHBG002562.
InParanoidiQ99MN1.
KOiK04567.
OrthoDBiEOG7XSTD7.
PhylomeDBiQ99MN1.

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]
PIRSFiPIRSF039101. LysRS2. 1 hit.
PRINTSiPR00982. TRNASYNTHLYS.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00499. lysS_bact. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q99MN1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATLQESEVK VDGEQKLSKN ELKRRLKAEK KLAEKEAKQK ELSEKQLNQT
60 70 80 90 100
ASAPNHTADN GVGAEEETLD PNQYYKIRSQ AVQQLKVTGE DPYPHKFHVD
110 120 130 140 150
ISLTQFIQEY SHLQPGDHLT DVTLKVAGRI HAKRASGGKL IFYDLRGEGV
160 170 180 190 200
KLQVMANSRN YKSEEEFVHI NNKLRRGDII GVEGNPGKTK KGELSIIPQE
210 220 230 240 250
ITLLSPCLHM LPHLHFGLKD KETRYRQRYL DLILNDFVRQ KFIVRSKIIT
260 270 280 290 300
YIRSFLDELG FLEIETPMMN IIPGGAVAKP FITYHNELDM NLYMRIAPEL
310 320 330 340 350
YHKMLVVGGI DRVYEIGRQF RNEGIDLTHN PEFTTCEFYM AYADYHDLME
360 370 380 390 400
ITEKMLSGMV KSITGSYKIT YHPDGPEGQA YEVDFTPPFR RISMVEELEK
410 420 430 440 450
ALGVKLPETS LFETEETRKI LDDICVAKAV ECPPPRTTAR LLDKLVGEFL
460 470 480 490 500
EVTCISPTFI CDHPQIMSPL AKWHRSKEGL TERFELFVMK KEICNAYTEL
510 520 530 540 550
NDPVRQRQLF EEQAKAKAAG DDEAMFIDEN FCTALEYGLP PTAGWGMGID
560 570 580 590
RLTMFLTDSN NIKEVLLFPA MKPEDKKETA ATTETPESTE ASPSV
Length:595
Mass (Da):67,840
Last modified:June 1, 2001 - v1
Checksum:i055889E87C11AA97
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF328904
, AF328894, AF328895, AF328896, AF328897, AF328898, AF328899, AF328900, AF328901, AF328902, AF328903 Genomic DNA. Translation: AAK19309.1.
BC036289 mRNA. Translation: AAH36289.1.
CCDSiCCDS40481.1.
RefSeqiNP_444322.1. NM_053092.3.
UniGeneiMm.196544.
Mm.410491.

Genome annotation databases

EnsembliENSMUST00000034426; ENSMUSP00000034426; ENSMUSG00000031948.
GeneIDi85305.
KEGGimmu:85305.
UCSCiuc009nne.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF328904
, AF328894, AF328895, AF328896, AF328897, AF328898, AF328899, AF328900, AF328901, AF328902, AF328903 Genomic DNA. Translation: AAK19309.1.
BC036289 mRNA. Translation: AAH36289.1.
CCDSiCCDS40481.1.
RefSeqiNP_444322.1. NM_053092.3.
UniGeneiMm.196544.
Mm.410491.

3D structure databases

ProteinModelPortaliQ99MN1.
SMRiQ99MN1. Positions 70-574.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi220220. 2 interactions.
DIPiDIP-36058N.
IntActiQ99MN1. 3 interactions.
MINTiMINT-4136281.
STRINGi10090.ENSMUSP00000090808.

PTM databases

iPTMnetiQ99MN1.
PhosphoSiteiQ99MN1.

Proteomic databases

EPDiQ99MN1.
MaxQBiQ99MN1.
PaxDbiQ99MN1.
PRIDEiQ99MN1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034426; ENSMUSP00000034426; ENSMUSG00000031948.
GeneIDi85305.
KEGGimmu:85305.
UCSCiuc009nne.3. mouse.

Organism-specific databases

CTDi3735.
MGIiMGI:1934754. Kars.

Phylogenomic databases

eggNOGiKOG1885. Eukaryota.
COG1190. LUCA.
GeneTreeiENSGT00550000074841.
HOGENOMiHOG000236577.
HOVERGENiHBG002562.
InParanoidiQ99MN1.
KOiK04567.
OrthoDBiEOG7XSTD7.
PhylomeDBiQ99MN1.

Enzyme and pathway databases

BRENDAi6.1.1.6. 3474.

Miscellaneous databases

ChiTaRSiKars. mouse.
PROiQ99MN1.
SOURCEiSearch...

Gene expression databases

BgeeiQ99MN1.
CleanExiMM_KARS.
ExpressionAtlasiQ99MN1. baseline and differential.
GenevisibleiQ99MN1. MM.

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]
PIRSFiPIRSF039101. LysRS2. 1 hit.
PRINTSiPR00982. TRNASYNTHLYS.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00499. lysS_bact. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genomic clustering of tRNA-specific adenosine deaminase ADAT1 and two tRNA synthetases."
    Maas S., Kim Y.G., Rich A.
    Mamm. Genome 12:387-393(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/SvJ.
  2. "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].
    Strain: FVB/N.
    Tissue: Mammary gland.
  3. "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.
  4. "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.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-588; THR-589; SER-592 AND SER-594, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiSYK_MOUSE
AccessioniPrimary (citable) accession number: Q99MN1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

It is likely that the same gene provides both this cytoplasmic isoform and an additional mitochondrial isoform.
Shares a bidirectional promoter with Terf2ip/Rap1.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.