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WARS1 tryptophanyl-tRNA synthetase 1 [ Homo sapiens (human) ]

Gene ID: 7453, updated on 27-Nov-2024

Summary

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Official Symbol
WARS1provided by HGNC
Official Full Name
tryptophanyl-tRNA synthetase 1provided by HGNC
Primary source
HGNC:HGNC:12729
See related
Ensembl:ENSG00000140105 MIM:191050; AllianceGenome:HGNC:12729
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Homo sapiens
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as
HMN9; WARS; HMND9; IFI53; IFP53; GAMMA-2; NEDMSBA
Summary
Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. Two forms of tryptophanyl-tRNA synthetase exist, a cytoplasmic form, named WARS, and a mitochondrial form, named WARS2. Tryptophanyl-tRNA synthetase (WARS) catalyzes the aminoacylation of tRNA(trp) with tryptophan and is induced by interferon. Tryptophanyl-tRNA synthetase belongs to the class I tRNA synthetase family. Four transcript variants encoding two different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]
Expression
Broad expression in placenta (RPKM 128.2), appendix (RPKM 87.1) and 24 other tissues See more
Orthologs
mouse all
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Genomic context

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See WARS1 in Genome Data Viewer
Location:
14q32.2
Exon count:
15
Annotation release Status Assembly Chr Location
RS_2024_08 current GRCh38.p14 (GCF_000001405.40) 14 NC_000014.9 (100333790..100376327, complement)
RS_2024_08 current T2T-CHM13v2.0 (GCF_009914755.1) 14 NC_060938.1 (94566811..94609425, complement)
RS_2024_09 previous assembly GRCh37.p13 (GCF_000001405.25) 14 NC_000014.8 (100800127..100842664, complement)

Chromosome 14 - NC_000014.9Genomic Context describing neighboring genes Neighboring gene RNA, 7SL, cytoplasmic 523, pseudogene Neighboring gene ATAC-STARR-seq lymphoblastoid active region 9038 Neighboring gene solute carrier family 25 member 47 Neighboring gene OCT4-NANOG-H3K27ac-H3K4me1 hESC enhancer GRCh37_chr14:100837597-100838513 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 9039 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 9040 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 6090 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 6091 Neighboring gene NADH:ubiquinone oxidoreductase subunit B3 pseudogene 4 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr14:100848141-100849101 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr14:100849328-100849837 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr14:100860083-100860587 Neighboring gene WD repeat domain 25 Neighboring gene BRD4-independent group 4 enhancer GRCh37_chr14:100863901-100865100 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr14:100870227-100870728 Neighboring gene uncharacterized LOC105370664 Neighboring gene H3K27ac hESC enhancer GRCh37_chr14:100876203-100876704 Neighboring gene H3K27ac hESC enhancer GRCh37_chr14:100876705-100877204 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr14:100885967-100886468 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr14:100886469-100886968 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr14:100893614-100894278 Neighboring gene CDK7 strongly-dependent group 2 enhancer GRCh37_chr14:100904917-100906116 Neighboring gene Sharpr-MPRA regulatory region 12420 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr14:100913795-100914295 Neighboring gene uncharacterized LOC124903383

Genomic regions, transcripts, and products

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Go to nucleotide: Graphics FASTA GenBank

Expression

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  • Project title: HPA RNA-seq normal tissues
  • Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
  • BioProject: PRJEB4337
  • Publication: PMID 24309898
  • Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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Related articles in PubMed

  1. The prognostic significance of tryptophanyl-tRNA synthetase in colorectal cancer. Ghanipour A, et al. Cancer Epidemiol Biomarkers Prev, 2009 Nov. PMID 19900940
  2. Recognition by tryptophanyl-tRNA synthetases of discriminator base on tRNATrp from three biological domains. Guo Q, et al. J Biol Chem, 2002 Apr 19. PMID 11834741
  3. Biologically active fragment of a human tRNA synthetase inhibits fluid shear stress-activated responses of endothelial cells. Tzima E, et al. Proc Natl Acad Sci U S A, 2003 Dec 9. PMID 14630953, Free PMC Article
  4. Crystal structure of human tryptophanyl-tRNA synthetase catalytic fragment: insights into substrate recognition, tRNA binding, and angiogenesis activity. Yu Y, et al. J Biol Chem, 2004 Feb 27. PMID 14660560
  5. Two conformations of a crystalline human tRNA synthetase-tRNA complex: implications for protein synthesis. Yang XL, et al. EMBO J, 2006 Jun 21. PMID 16724112, Free PMC Article

See all (144) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Highly secreted tryptophanyl tRNA synthetase 1 as a potential theranostic target for hypercytokinemic severe sepsis.
    Title: Highly secreted tryptophanyl tRNA synthetase 1 as a potential theranostic target for hypercytokinemic severe sepsis.
  2. Tryptophanyl-Transfer RNA Synthetase Is Involved in a Negative Feedback Loop Mitigating Interferon-gamma-Induced Gene Expression.
    Title: Tryptophanyl-Transfer RNA Synthetase Is Involved in a Negative Feedback Loop Mitigating Interferon-γ-Induced Gene Expression.
  3. Tryptophan-Starved Human Cells Overexpressing Tryptophanyl-tRNA Synthetase Enhance High-Affinity Tryptophan Uptake via Enzymatic Production of Tryptophanyl-AMP.
    Title: Tryptophan-Starved Human Cells Overexpressing Tryptophanyl-tRNA Synthetase Enhance High-Affinity Tryptophan Uptake via Enzymatic Production of Tryptophanyl-AMP.
  4. Exploring the role of tryptophanyl-tRNA synthetase and associations with inflammatory markers and clinical outcomes in COVID-19 patients: A case-control study.
    Title: Exploring the role of tryptophanyl-tRNA synthetase and associations with inflammatory markers and clinical outcomes in COVID-19 patients: A case-control study.
  5. Biallelic variants in WARS1 cause a highly variable neurodevelopmental syndrome and implicate a critical exon for normal auditory function.
    Title: Biallelic variants in WARS1 cause a highly variable neurodevelopmental syndrome and implicate a critical exon for normal auditory function.
  6. WARS1 and SARS1: Two tRNA synthetases implicated in autosomal recessive microcephaly.
    Title: WARS1 and SARS1: Two tRNA synthetases implicated in autosomal recessive microcephaly.
  7. Identification of Prognostic RBPs in Osteosarcoma.
    Title: Identification of Prognostic RBPs in Osteosarcoma.
  8. Mini tryptophanyl-tRNA synthetase is required for a synthetic phenotype in vascular smooth muscle cells induced by IFN-gamma-mediated beta2-adrenoceptor signaling.
    Title: Mini tryptophanyl-tRNA synthetase is required for a synthetic phenotype in vascular smooth muscle cells induced by IFN-γ-mediated β2-adrenoceptor signaling.
  9. Tryptophanyl-tRNA Synthetase 1 Signals Activate TREM-1 via TLR2 and TLR4.
    Title: Tryptophanyl-tRNA Synthetase 1 Signals Activate TREM-1 via TLR2 and TLR4.
  10. Expression of Indoleamine 2, 3-dioxygenase 1 (IDO1) and Tryptophanyl-tRNA Synthetase (WARS) in Gastric Cancer Molecular Subtypes.
    Title: Expression of Indoleamine 2, 3-dioxygenase 1 (IDO1) and Tryptophanyl-tRNA Synthetase (WARS) in Gastric Cancer Molecular Subtypes.
Submit: New GeneRIF Correction See all GeneRIFs (40)

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

HIV-1 interactions

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Protein interactions

Protein Gene Interaction Pubs
capsid gag The Capsid domain of HIV-1 Gag is sufficient for the interaction of Gag with tryptophanyl-tRNA synthetase in an in vitro pull-down assay PubMed

Go to the HIV-1, Human Interaction Database

Pathways from PubChem

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Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Markers

Homology

Gene Ontology Provided by GOA

Function Evidence Code Pubs
enables ATP binding IEA
Inferred from Electronic Annotation
more info
  
enables kinase inhibitor activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables protein domain specific binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables protein homodimerization activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables protein kinase binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables tryptophan-tRNA ligase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables tryptophan-tRNA ligase activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables tryptophan-tRNA ligase activity NAS
Non-traceable Author Statement
more info
 PubMed 
Process Evidence Code Pubs
involved_in angiogenesis IEA
Inferred from Electronic Annotation
more info
  
involved_in negative regulation of cell population proliferation TAS
Traceable Author Statement
more info
 PubMed 
involved_in negative regulation of protein kinase activity IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in positive regulation of gene expression IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in positive regulation of protein-containing complex assembly IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in regulation of angiogenesis IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in translation TAS
Traceable Author Statement
more info
 PubMed 
involved_in tryptophanyl-tRNA aminoacylation IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in tryptophanyl-tRNA aminoacylation NAS
Non-traceable Author Statement
more info
 PubMed 
Component Evidence Code Pubs
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytoplasm TAS
Traceable Author Statement
more info
 PubMed 
located_in cytosol IDA
Inferred from Direct Assay
more info
  
located_in cytosol TAS
Traceable Author Statement
more info
  
located_in extracellular exosome HDA PubMed 
located_in nucleus HDA PubMed 
located_in nucleus IDA
Inferred from Direct Assay
more info
 PubMed 
part_of protein-containing complex IMP
Inferred from Mutant Phenotype
more info
 PubMed 

General protein information

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Preferred Names
tryptophan--tRNA ligase, cytoplasmic
Names
epididymis secretory sperm binding protein
hWRS
interferon-induced protein 53
trpRS
tryptophan tRNA ligase 1, cytoplasmic
NP_004175.2
NP_776049.1
NP_998810.1
NP_998811.1
XP_011535438.1
XP_016877116.1
XP_024305475.1
XP_047287713.1
XP_047287714.1
XP_047287715.1
XP_047287716.1
XP_047287717.1
XP_047287718.1
XP_047287719.1
XP_047287720.1
XP_047287721.1
XP_054232671.1
XP_054232672.1
XP_054232673.1
XP_054232674.1
XP_054232675.1
XP_054232676.1
XP_054232677.1
XP_054232678.1
XP_054232679.1
XP_054232680.1

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

Genomic

  1. NG_029914.1 RefSeqGene

    Range
    5997..47554
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_004184.4 → NP_004175.2  tryptophan--tRNA ligase, cytoplasmic isoform a

    See identical proteins and their annotated locations for NP_004175.2

    Status: REVIEWED

    Description
    Transcript Variant: This variant (1) represents the longest transcript. Variants 1 and 2 both encode isoform a.
    Source sequence(s)
    AV710027, BC017489
    Consensus CDS
    CCDS9960.1
    UniProtKB/Swiss-Prot
    A6NGN1, A6NID3, P23381, P78535, Q502Y0, Q53XB6, Q9UDI5, Q9UDL3
    UniProtKB/TrEMBL
    A0A024R6K8
    Related
    ENSP00000376620.2, ENST00000392882.7
    Conserved Domains (2) summary
    PLN02486
    Location:85 → 466
    PLN02486; aminoacyl-tRNA ligase
    cd00936
    Location:12 → 61
    WEPRS_RNA; WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates ...

  2. NM_173701.2 → NP_776049.1  tryptophan--tRNA ligase, cytoplasmic isoform a

    See identical proteins and their annotated locations for NP_776049.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (2) differs in the 5' UTR compared to variant 1. Variants 1 and 2 both encode isoform a.
    Source sequence(s)
    AK056100, BC017489
    Consensus CDS
    CCDS9960.1
    UniProtKB/Swiss-Prot
    A6NGN1, A6NID3, P23381, P78535, Q502Y0, Q53XB6, Q9UDI5, Q9UDL3
    UniProtKB/TrEMBL
    A0A024R6K8
    Related
    ENSP00000347495.2, ENST00000355338.6
    Conserved Domains (2) summary
    PLN02486
    Location:85 → 466
    PLN02486; aminoacyl-tRNA ligase
    cd00936
    Location:12 → 61
    WEPRS_RNA; WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates ...

  3. NM_213645.2 → NP_998810.1  tryptophan--tRNA ligase, cytoplasmic isoform b

    See identical proteins and their annotated locations for NP_998810.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (3) lacks an alternate exon compared to variant 1. The resulting isoform (b) uses a downstream start codon but has the same C-terminus compared to isoform a. Variants 3 and 4 both encode isoform b.
    Source sequence(s)
    BC017489, BG717903
    Consensus CDS
    CCDS9961.1
    UniProtKB/Swiss-Prot
    P23381
    Related
    ENSP00000351481.4, ENST00000358655.8
    Conserved Domains (2) summary
    PLN02486
    Location:44 → 425
    PLN02486; aminoacyl-tRNA ligase
    cl00349
    Location:2 → 23
    S15_NS1_EPRS_RNA-bind; S15/NS1/EPRS_RNA-binding domain. This short domain consists of a helix-turn-helix structure, which can bind to several types of RNA. It is found in the ribosomal protein S15, the influenza A viral nonstructural protein (NSA) and in several eukaryotic ...

  4. NM_213646.2 → NP_998811.1  tryptophan--tRNA ligase, cytoplasmic isoform b

    See identical proteins and their annotated locations for NP_998811.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (4) differs in the 5' UTR and coding region compared to variant 1. The resulting isoform (b) uses a downstream start codon but has the same C-terminus compared to isoform a. Variants 3 and 4 both encode isoform b.
    Source sequence(s)
    BC017489, BM561448
    Consensus CDS
    CCDS9961.1
    UniProtKB/Swiss-Prot
    P23381
    Related
    ENSP00000339485.5, ENST00000344102.9
    Conserved Domains (2) summary
    PLN02486
    Location:44 → 425
    PLN02486; aminoacyl-tRNA ligase
    cl00349
    Location:2 → 23
    S15_NS1_EPRS_RNA-bind; S15/NS1/EPRS_RNA-binding domain. This short domain consists of a helix-turn-helix structure, which can bind to several types of RNA. It is found in the ribosomal protein S15, the influenza A viral nonstructural protein (NSA) and in several eukaryotic ...

RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2024_08

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p14 Primary Assembly

Genomic

  1. NC_000014.9 Reference GRCh38.p14 Primary Assembly

    Range
    100333790..100376327 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_024449707.2 → XP_024305475.1  tryptophan--tRNA ligase, cytoplasmic isoform X1

    UniProtKB/Swiss-Prot
    A6NGN1, A6NID3, P23381, P78535, Q502Y0, Q53XB6, Q9UDI5, Q9UDL3
    UniProtKB/TrEMBL
    A0A024R6K8
    Conserved Domains (2) summary
    PLN02486
    Location:85 → 466
    PLN02486; aminoacyl-tRNA ligase
    cd00936
    Location:12 → 61
    WEPRS_RNA; WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates ...

  2. XM_047431762.1 → XP_047287718.1  tryptophan--tRNA ligase, cytoplasmic isoform X1

    UniProtKB/Swiss-Prot
    A6NGN1, A6NID3, P23381, P78535, Q502Y0, Q53XB6, Q9UDI5, Q9UDL3
    UniProtKB/TrEMBL
    A0A024R6K8

  3. XM_047431763.1 → XP_047287719.1  tryptophan--tRNA ligase, cytoplasmic isoform X1

    UniProtKB/Swiss-Prot
    A6NGN1, A6NID3, P23381, P78535, Q502Y0, Q53XB6, Q9UDI5, Q9UDL3
    UniProtKB/TrEMBL
    A0A024R6K8

  4. XM_017021627.3 → XP_016877116.1  tryptophan--tRNA ligase, cytoplasmic isoform X1

    UniProtKB/Swiss-Prot
    A6NGN1, A6NID3, P23381, P78535, Q502Y0, Q53XB6, Q9UDI5, Q9UDL3
    UniProtKB/TrEMBL
    A0A024R6K8
    Conserved Domains (2) summary
    PLN02486
    Location:85 → 466
    PLN02486; aminoacyl-tRNA ligase
    cd00936
    Location:12 → 61
    WEPRS_RNA; WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates ...

  5. XM_047431759.1 → XP_047287715.1  tryptophan--tRNA ligase, cytoplasmic isoform X1

    UniProtKB/Swiss-Prot
    A6NGN1, A6NID3, P23381, P78535, Q502Y0, Q53XB6, Q9UDI5, Q9UDL3
    UniProtKB/TrEMBL
    A0A024R6K8

  6. XM_047431758.1 → XP_047287714.1  tryptophan--tRNA ligase, cytoplasmic isoform X1

    UniProtKB/Swiss-Prot
    A6NGN1, A6NID3, P23381, P78535, Q502Y0, Q53XB6, Q9UDI5, Q9UDL3
    UniProtKB/TrEMBL
    A0A024R6K8

  7. XM_047431757.1 → XP_047287713.1  tryptophan--tRNA ligase, cytoplasmic isoform X1

    UniProtKB/Swiss-Prot
    A6NGN1, A6NID3, P23381, P78535, Q502Y0, Q53XB6, Q9UDI5, Q9UDL3
    UniProtKB/TrEMBL
    A0A024R6K8

  8. XM_047431765.1 → XP_047287721.1  tryptophan--tRNA ligase, cytoplasmic isoform X2

  9. XM_047431764.1 → XP_047287720.1  tryptophan--tRNA ligase, cytoplasmic isoform X1

    UniProtKB/Swiss-Prot
    A6NGN1, A6NID3, P23381, P78535, Q502Y0, Q53XB6, Q9UDI5, Q9UDL3
    UniProtKB/TrEMBL
    A0A024R6K8

  10. XM_011537136.4 → XP_011535438.1  tryptophan--tRNA ligase, cytoplasmic isoform X3

    See identical proteins and their annotated locations for XP_011535438.1

    UniProtKB/Swiss-Prot
    P23381
    Conserved Domains (2) summary
    PLN02486
    Location:44 → 425
    PLN02486; aminoacyl-tRNA ligase
    cl00349
    Location:2 → 23
    S15_NS1_EPRS_RNA-bind; S15/NS1/EPRS_RNA-binding domain. This short domain consists of a helix-turn-helix structure, which can bind to several types of RNA. It is found in the ribosomal protein S15, the influenza A viral nonstructural protein (NSA) and in several eukaryotic ...

  11. XM_047431760.1 → XP_047287716.1  tryptophan--tRNA ligase, cytoplasmic isoform X1

    UniProtKB/Swiss-Prot
    A6NGN1, A6NID3, P23381, P78535, Q502Y0, Q53XB6, Q9UDI5, Q9UDL3
    UniProtKB/TrEMBL
    A0A024R6K8

  12. XM_047431761.1 → XP_047287717.1  tryptophan--tRNA ligase, cytoplasmic isoform X1

    UniProtKB/Swiss-Prot
    A6NGN1, A6NID3, P23381, P78535, Q502Y0, Q53XB6, Q9UDI5, Q9UDL3
    UniProtKB/TrEMBL
    A0A024R6K8
    Related
    ENSP00000451460.1, ENST00000557135.5

Alternate T2T-CHM13v2.0

Genomic

  1. NC_060938.1 Alternate T2T-CHM13v2.0

    Range
    94566811..94609425 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_054376700.1 → XP_054232675.1  tryptophan--tRNA ligase, cytoplasmic isoform X1

    UniProtKB/Swiss-Prot
    A6NGN1, A6NID3, P23381, P78535, Q502Y0, Q53XB6, Q9UDI5, Q9UDL3
    UniProtKB/TrEMBL
    A0A024R6K8

  2. XM_054376703.1 → XP_054232678.1  tryptophan--tRNA ligase, cytoplasmic isoform X1

    UniProtKB/Swiss-Prot
    A6NGN1, A6NID3, P23381, P78535, Q502Y0, Q53XB6, Q9UDI5, Q9UDL3
    UniProtKB/TrEMBL
    A0A024R6K8

  3. XM_054376704.1 → XP_054232679.1  tryptophan--tRNA ligase, cytoplasmic isoform X1

    UniProtKB/Swiss-Prot
    A6NGN1, A6NID3, P23381, P78535, Q502Y0, Q53XB6, Q9UDI5, Q9UDL3
    UniProtKB/TrEMBL
    A0A024R6K8

  4. XM_054376696.1 → XP_054232671.1  tryptophan--tRNA ligase, cytoplasmic isoform X1

    UniProtKB/Swiss-Prot
    A6NGN1, A6NID3, P23381, P78535, Q502Y0, Q53XB6, Q9UDI5, Q9UDL3
    UniProtKB/TrEMBL
    A0A024R6K8

  5. XM_054376699.1 → XP_054232674.1  tryptophan--tRNA ligase, cytoplasmic isoform X1

    UniProtKB/Swiss-Prot
    A6NGN1, A6NID3, P23381, P78535, Q502Y0, Q53XB6, Q9UDI5, Q9UDL3
    UniProtKB/TrEMBL
    A0A024R6K8

  6. XM_054376698.1 → XP_054232673.1  tryptophan--tRNA ligase, cytoplasmic isoform X1

    UniProtKB/Swiss-Prot
    A6NGN1, A6NID3, P23381, P78535, Q502Y0, Q53XB6, Q9UDI5, Q9UDL3
    UniProtKB/TrEMBL
    A0A024R6K8

  7. XM_054376697.1 → XP_054232672.1  tryptophan--tRNA ligase, cytoplasmic isoform X1

    UniProtKB/Swiss-Prot
    A6NGN1, A6NID3, P23381, P78535, Q502Y0, Q53XB6, Q9UDI5, Q9UDL3
    UniProtKB/TrEMBL
    A0A024R6K8

  8. XM_054376705.1 → XP_054232680.1  tryptophan--tRNA ligase, cytoplasmic isoform X3

  9. XM_054376701.1 → XP_054232676.1  tryptophan--tRNA ligase, cytoplasmic isoform X1

    UniProtKB/Swiss-Prot
    A6NGN1, A6NID3, P23381, P78535, Q502Y0, Q53XB6, Q9UDI5, Q9UDL3
    UniProtKB/TrEMBL
    A0A024R6K8

  10. XM_054376702.1 → XP_054232677.1  tryptophan--tRNA ligase, cytoplasmic isoform X1

    UniProtKB/Swiss-Prot
    A6NGN1, A6NID3, P23381, P78535, Q502Y0, Q53XB6, Q9UDI5, Q9UDL3
    UniProtKB/TrEMBL
    A0A024R6K8
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P23381.2 GenPept UniProtKB/Swiss-Prot:P23381

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