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Q15046

- SYK_HUMAN

UniProt

Q15046 - SYK_HUMAN

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Protein

Lysine--tRNA ligase

Gene

KARS

Organism
Homo sapiens (Human)
Status
Reviewed - 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 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. 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
Complete GO annotation...

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-KW
  5. microtubule cytoskeleton Source: HPA
  6. mitochondrial matrix Source: Reactome
  7. mitochondrion Source: UniProtKB
  8. nucleus Source: UniProtKB-KW
  9. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

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 non-syndromic 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

BgeeiQ15046.
CleanExiHS_KARS.
ExpressionAtlasiQ15046. baseline and differential.
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. 64 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 70-576.
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.
GeneTreeiENSGT00550000074841.
HOGENOMiHOG000236577.
HOVERGENiHBG002562.
InParanoidiQ15046.
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

        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 BAA06688.1 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 70-576.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109938. 64 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 non-syndromic sensorineural deafness type DFNB.
PharmGKBi PA30016.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1190.
GeneTreei ENSGT00550000074841.
HOGENOMi HOG000236577.
HOVERGENi HBG002562.
InParanoidi Q15046.
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

Bgeei Q15046.
CleanExi HS_KARS.
ExpressionAtlasi Q15046. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 138 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