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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. When secreted, acts as a signaling molecule that induces immune response through the activation of monocyte/macrophages. 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.By similarity

Miscellaneous

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

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei275Substrate; via carbonyl oxygenBy similarity1
Binding sitei299SubstrateBy similarity1
Binding sitei337SubstrateBy similarity1
Binding sitei339SubstrateBy similarity1
Binding sitei495SubstrateBy similarity1
Binding sitei499SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi321 – 323ATPBy similarity3
Nucleotide bindingi329 – 330ATPBy similarity2
Nucleotide bindingi492 – 493ATPBy similarity2
Nucleotide bindingi548 – 551ATPBy similarity4

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAminoacyl-tRNA synthetase, Ligase, Transferase
Biological processProtein biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.1.1.6. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysine--tRNA ligase (EC:2.7.7.-By similarity, EC:6.1.1.6By similarity)
Alternative name(s):
Lysyl-tRNA synthetase
Short name:
LysRS
Gene namesi
Name:Kars
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1934754. Kars.

Subcellular locationi

  • Cytoplasmcytosol By similarity
  • Cytoplasm By similarity
  • Nucleus By similarity
  • Cell membrane By similarity; Peripheral membrane protein By similarity
  • Secreted By similarity

  • Note: Secretion is induced by TNF-alpha. Cytosolic in quiescent mast cells. Translocates into the nucleus in response to mast cell activation by immunoglobulin E.By similarity

GO - Cellular componenti

  • aminoacyl-tRNA synthetase multienzyme complex Source: CAFA
  • cytosol Source: MGI
  • extracellular space Source: MGI
  • mitochondrion Source: MGI

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001527662 – 595Lysine--tRNA ligaseAdd BLAST594

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei86N6-acetyllysineBy similarity1
Modified residuei139N6-acetyllysineBy similarity1
Modified residuei205PhosphoserineBy similarity1
Modified residuei393PhosphoserineCombined sources1
Modified residuei588PhosphoserineCombined sources1
Modified residuei589PhosphothreonineCombined sources1
Modified residuei592PhosphoserineCombined sources1
Modified residuei594PhosphoserineCombined sources1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ99MN1.
MaxQBiQ99MN1.
PaxDbiQ99MN1.
PRIDEiQ99MN1.

PTM databases

iPTMnetiQ99MN1.
PhosphoSitePlusiQ99MN1.

Expressioni

Gene expression databases

BgeeiENSMUSG00000031948.
CleanExiMM_KARS.
ExpressionAtlasiQ99MN1. baseline and differential.
GenevisibleiQ99MN1. MM.

Interactioni

Subunit structurei

Homodimer (By similarity). 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:14975237). Interacts with AIMP2 (via N-terminus) and MITF (PubMed:14975237).By similarity1 Publication

GO - Molecular functioni

  • scaffold protein binding Source: CAFA

Protein-protein interaction databases

BioGridi220220. 2 interactors.
DIPiDIP-36058N.
IntActiQ99MN1. 4 interactors.
MINTiMINT-4136281.
STRINGi10090.ENSMUSP00000090808.

Structurei

3D structure databases

ProteinModelPortaliQ99MN1.
SMRiQ99MN1.
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.
PhylomeDBiQ99MN1.

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.

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.

Similar proteinsi

Entry informationi

Entry nameiSYK_MOUSE
AccessioniPrimary (citable) accession number: Q99MN1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: June 1, 2001
Last modified: August 30, 2017
This is version 134 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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