Q15046 (SYK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lysine--tRNA ligase
EC=6.1.1.6

Alternative name(s):
Lysyl-tRNA synthetase
Short name=LysRS

Gene names

Name:	KARS
Synonyms:	KIAA0070

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	597 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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).
Enzyme regulation	Up-regulated by DARS and EEF1A1, but not by AIMP2.
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 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.
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.19
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 process	Host-virus interaction Protein biosynthesis
Cellular component	Cell membrane Cytoplasm Membrane Mitochondrion Nucleus Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Charcot-Marie-Tooth disease Disease mutation Neuropathy
Ligand	ATP-binding Metal-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	diadenosine tetraphosphate biosynthetic process Inferred from electronic annotation. Source: Compara lysyl-tRNA aminoacylation Inferred from direct assay Ref.2. Source: UniProtKB tRNA processing Non-traceable author statement Ref.2. Source: UniProtKB virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	aminoacyl-tRNA synthetase multienzyme complex Inferred from electronic annotation. Source: Compara 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 nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW amino acid binding Inferred from electronic annotation. Source: Compara 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...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7

Chain

2 – 597

596

Lysine--tRNA ligase

PRO_0000152765

Regions

Nucleotide binding

323 – 325

3

ATP

Nucleotide binding

331 – 332

2

ATP

Nucleotide binding

494 – 495

2

ATP

Nucleotide binding

550 – 553

4

ATP

Sites

Metal binding

487

1

Calcium

Metal binding

494

1

Calcium

Binding site

277

1

Substrate; via carbonyl oxygen

Binding site

301

1

Substrate

Binding site

339

1

Substrate

Binding site

341

1

Substrate

Binding site

497

1

Substrate

Binding site

501

1

Substrate

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.7

Modified residue

88

1

N6-acetyllysine Ref.16

Modified residue

141

1

N6-acetyllysine Ref.16

Modified residue

596

1

Phosphoserine By similarity

Natural variations

Alternative sequence

1 – 21

21

MAAVQ…KLSKN → MLTQAAVRLVRGSLRKTSWA EWGHRELRLGQLAPFTAPHK DKSFSDQRS in isoform Mitochondrial.

VSP_038481

Natural variant

105

1

L → H in CMTRIB; severely affects enzyme activity. Ref.19

VAR_064911

Natural variant

179

1

G → A.
Corresponds to variant rs11557665 [ dbSNP | Ensembl ].

VAR_052640

Natural variant

274

1

I → M in CMTRIB. Ref.19

VAR_064912

Natural variant

595

1

T → S. Ref.2 Ref.3 Ref.19
Corresponds to variant rs6834 [ dbSNP | Ensembl ].

VAR_016105

Experimental info

Mutagenesis

1 – 65

65

Missing: Loss of nuclear localization, but no effect on packaging into HIV-1. Ref.13

Isoform Mitochondrial:

Sequence conflict

48

1

R → G in AAG30114. Ref.2

Secondary structure

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597

Helix Strand Turn

Details...

Helix

73 – 89

17

Helix

105 – 112

8

Beta strand

126 – 149

24

Beta strand

152 – 159

8

Helix

160 – 162

3

Helix

166 – 175

10

Beta strand

181 – 190

10

Beta strand

196 – 207

12

Helix

223 – 228

6

Helix

230 – 236

7

Helix

238 – 260

23

Beta strand

270 – 274

5

Beta strand

277 – 279

3

Beta strand

284 – 287

4

Turn

288 – 291

4

Beta strand

292 – 296

5

Helix

301 – 309

9

Beta strand

314 – 322

9

Beta strand

328 – 330

3

Beta strand

333 – 343

11

Helix

347 – 366

20

Beta strand

367 – 373

7

Beta strand

383 – 386

4

Beta strand

392 – 395

4

Helix

396 – 404

9

Helix

411 – 413

3

Helix

417 – 429

13

Helix

440 – 451

12

Helix

453 – 455

3

Beta strand

460 – 463

4

Helix

467 – 469

3

Beta strand

477 – 479

3

Beta strand

482 – 490

9

Beta strand

493 – 501

9

Helix

505 – 521

17

Helix

531 – 537

7

Turn

538 – 540

3

Beta strand

543 – 550

8

Helix

551 – 558

8

Helix

564 – 566

3

Beta strand

568 – 570

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Cytoplasmic [UniParc]. Last modified April 16, 2002. Version 3. Checksum: E7770953332D905D	FASTA	597	68,048
	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
	Isoform Mitochondrial [UniParc]. Checksum: 294DA1CE5A137AD6	FASTA	625	71,497
	10 20 30 40 50 60 MLTQAAVRLV RGSLRKTSWA EWGHRELRLG QLAPFTAPHK DKSFSDQRSE LKRRLKAEKK 70 80 90 100 110 120 VAEKEAKQKE LSEKQLSQAT AAATNHTTDN GVGPEEESVD PNQYYKIRSQ AIHQLKVNGE 130 140 150 160 170 180 DPYPHKFHVD ISLTDFIQKY SHLQPGDHLT DITLKVAGRI HAKRASGGKL IFYDLRGEGV 190 200 210 220 230 240 KLQVMANSRN YKSEEEFIHI NNKLRRGDII GVQGNPGKTK KGELSIIPYE ITLLSPCLHM 250 260 270 280 290 300 LPHLHFGLKD KETRYRQRYL DLILNDFVRQ KFIIRSKIIT YIRSFLDELG FLEIETPMMN 310 320 330 340 350 360 IIPGGAVAKP FITYHNELDM NLYMRIAPEL YHKMLVVGGI DRVYEIGRQF RNEGIDLTHN 370 380 390 400 410 420 PEFTTCEFYM AYADYHDLME ITEKMVSGMV KHITGSYKVT YHPDGPEGQA YDVDFTPPFR 430 440 450 460 470 480 RINMVEELEK ALGMKLPETN LFETEETRKI LDDICVAKAV ECPPPRTTAR LLDKLVGEFL 490 500 510 520 530 540 EVTCINPTFI CDHPQIMSPL AKWHRSKEGL TERFELFVMK KEICNAYTEL NDPMRQRQLF 550 560 570 580 590 600 EEQAKAKAAG DDEAMFIDEN FCTALEYGLP PTAGWGMGID RVAMFLTDSN NIKEVLLFPA 610 620 MKPEDKKENV ATTDTLESTT VGTSV

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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]	"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, MASS SPECTROMETRY.
[17]	"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].
[18]	"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.
[19]	"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. , 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.
+	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.

IPI

IPI00014238.
IPI00307092.

RefSeq

NP_001123561.1. NM_001130089.1.
NP_005539.1. NM_005548.2.

UniGene

Hs.3100.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3BJU	X-ray	2.31	A/B/C/D	70-581	[»]
4DPG	X-ray	2.84	A/B/C/D/E/F/G/H	70-581	[»]

ProteinModelPortal

Q15046.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29725N.

IntAct

Q15046. 14 interactions.

MINT

MINT-5006627.

STRING

9606.ENSP00000325448.

PTM databases

PhosphoSite

Q15046.

Polymorphism databases

DMDM

20178333.

Proteomic databases

PaxDb

Q15046.

PRIDE

Q15046.

Protocols and materials databases

DNASU

3735.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000302445; ENSP00000303043; ENSG00000065427.
ENST00000319410; ENSP00000325448; ENSG00000065427.

GeneID

3735.

KEGG

hsa:3735.

UCSC

uc002feq.3. human.
uc002fer.3. human.

Organism-specific databases

CTD

3735.

GeneCards

GC16M075661.

HGNC

HGNC:6215. KARS.

HPA

HPA041345.
HPA041550.

MIM

601421. gene.
613641. phenotype.

neXtProt

NX_Q15046.

Orphanet

254334. Autosomal recessive intermediate Charcot-Marie-Tooth disease type B.

PharmGKB

PA30016.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1190.

HOGENOM

HOG000236577.

HOVERGEN

HBG002562.

KO

K04567.

OMA

EHKLEQP.

OrthoDB

EOG4KSPJH.

Enzyme and pathway databases

BRENDA

6.1.1.6. 2681.

Reactome

REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q15046.

Bgee

Q15046.

CleanEx

HS_KARS.

Genevestigator

Q15046.

GermOnline

ENSG00000065427. Homo sapiens.

Family and domain databases

Gene3D

2.40.50.140. 1 hit.

InterPro

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-helicase.
[Graphical view]

PANTHER

PTHR22594. PTHR22594. 1 hit.
PTHR22594:SF4. PTHR22594:SF4. 1 hit.

Pfam

PF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti. 1 hit.
[Graphical view]

PRINTS

PR00982. TRNASYNTHLYS.

SUPFAM

SSF50249. Nucleic_acid_OB. 1 hit.

TIGRFAMs

TIGR00499. lysS_bact. 1 hit.

PROSITE

PS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q15046.

ChEMBL

CHEMBL5575.

ChiTaRS

KARS. human.

DrugBank

DB00123. L-Lysine.

EvolutionaryTrace

Q15046.

GenomeRNAi

3735.

NextBio

14617.

SOURCE

Search...

Entry information

Entry name

SYK_HUMAN

Accession

Primary (citable) accession number: Q15046
Secondary accession number(s): A8MSK1 , D3DUK4, O14946, Q96J25, Q9HB23

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	April 16, 2002
Last modified:	May 1, 2013
This is version 122 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.