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P23381

- SYWC_HUMAN

UniProt

P23381 - SYWC_HUMAN

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Protein
Tryptophan--tRNA ligase, cytoplasmic
Gene
WARS, IFI53, WRS
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Isoform 1, isoform 2 and T1-TrpRS have aminoacylation activity while T2-TrpRS lacks it. Isoform 2, T1-TrpRS and T2-TrpRS possess angiostatic activity whereas isoform 1 lacks it. T2-TrpRS inhibits fluid shear stress-activated responses of endothelial cells. Regulates ERK, Akt, and eNOS activation pathways that are associated with angiogenesis, cytoskeletal reorganization and shear stress-responsive gene expression.4 Publications

Catalytic activityi

ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp).

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein binding Source: UniProtKB
  3. tryptophan-tRNA ligase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. gene expression Source: Reactome
  3. negative regulation of cell proliferation Source: ProtInc
  4. regulation of angiogenesis Source: UniProtKB
  5. tRNA aminoacylation for protein translation Source: Reactome
  6. translation Source: ProtInc
  7. tryptophanyl-tRNA aminoacylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Angiogenesis, Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_15306. Cytosolic tRNA aminoacylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Tryptophan--tRNA ligase, cytoplasmic (EC:6.1.1.2)
Alternative name(s):
Interferon-induced protein 53
Short name:
IFP53
Tryptophanyl-tRNA synthetase
Short name:
TrpRS
Short name:
hWRS
Cleaved into the following 2 chains:
Gene namesi
Name:WARS
Synonyms:IFI53, WRS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:12729. WARS.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
  4. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37340.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 471470Tryptophan--tRNA ligase, cytoplasmic
PRO_0000136738Add
BLAST
Chaini71 – 471401T1-TrpRS
PRO_0000386461Add
BLAST
Chaini94 – 471378T2-TrpRS
PRO_0000386462Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei154 – 1541N6-succinyllysine By similarity

Post-translational modificationi

Proteolytic cleavage generates 2 forms; T1-TrpRS and T2-TrpRS.

Proteomic databases

MaxQBiP23381.
PaxDbiP23381.
PeptideAtlasiP23381.
PRIDEiP23381.

2D gel databases

OGPiP23381.

PTM databases

PhosphoSiteiP23381.

Expressioni

Inductioni

By IFNG/IFN-gamma.1 Publication

Gene expression databases

ArrayExpressiP23381.
BgeeiP23381.
CleanExiHS_WARS.
GenevestigatoriP23381.

Organism-specific databases

HPAiHPA018944.

Interactioni

Subunit structurei

Homodimer. Isoform 1 and isoform 2 interact with an oxidized form of GAPDH. GAPDH stimulates the aminoacylation activity of isoform 2.

Protein-protein interaction databases

BioGridi113292. 34 interactions.
DIPiDIP-29493N.
IntActiP23381. 5 interactions.
MINTiMINT-1408962.
STRINGi9606.ENSP00000347495.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 2821
Helixi33 – 5321
Beta strandi54 – 563
Beta strandi84 – 863
Beta strandi89 – 913
Turni100 – 1023
Helixi103 – 1064
Helixi114 – 12411
Helixi130 – 1334
Beta strandi136 – 1427
Helixi143 – 1508
Turni151 – 1533
Beta strandi156 – 1627
Helixi171 – 18717
Beta strandi191 – 1955
Helixi197 – 2037
Helixi208 – 22316
Turni224 – 2263
Helixi229 – 2313
Beta strandi232 – 2365
Helixi237 – 2404
Helixi241 – 2433
Helixi247 – 25610
Helixi260 – 2678
Beta strandi271 – 2744
Helixi275 – 28511
Helixi286 – 2883
Helixi290 – 2923
Helixi294 – 2974
Beta strandi304 – 3107
Helixi311 – 3133
Helixi314 – 32310
Helixi324 – 3274
Beta strandi333 – 3375
Beta strandi345 – 3495
Beta strandi354 – 3574
Beta strandi360 – 3623
Helixi365 – 37410
Helixi384 – 3907
Turni394 – 3963
Helixi398 – 4069
Helixi410 – 42213
Beta strandi423 – 4253
Helixi430 – 45021
Helixi454 – 4607

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O5TX-ray2.50A94-471[»]
1R6TX-ray2.10A/B1-466[»]
1R6UX-ray2.00A/B48-471[»]
1ULHX-ray2.31A/B82-471[»]
2AKEX-ray3.10A94-471[»]
2AZXX-ray2.80A/B1-471[»]
2DR2X-ray3.00A94-471[»]
2QUHX-ray2.40A/B1-471[»]
2QUIX-ray2.40A/B1-471[»]
2QUJX-ray2.42A/B1-471[»]
2QUKX-ray2.80A1-471[»]
ProteinModelPortaliP23381.
SMRiP23381. Positions 82-471.

Miscellaneous databases

EvolutionaryTraceiP23381.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 6457WHEP-TRS
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi164 – 17310"HIGH" region
Motifi349 – 3535"KMSKS" region

Sequence similaritiesi

Contains 1 WHEP-TRS domain.

Phylogenomic databases

eggNOGiCOG0180.
HOVERGENiHBG002325.
InParanoidiP23381.
KOiK01867.
OMAiKTFIFNN.
OrthoDBiEOG7T4MK3.
PhylomeDBiP23381.
TreeFamiTF105669.

Family and domain databases

Gene3Di1.10.287.10. 1 hit.
3.40.50.620. 1 hit.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009068. S15_NS1_RNA-bd.
IPR002306. Trp-tRNA-ligase.
IPR000738. WHEP-TRS.
[Graphical view]
PANTHERiPTHR10055. PTHR10055. 1 hit.
PfamiPF00579. tRNA-synt_1b. 1 hit.
PF00458. WHEP-TRS. 1 hit.
[Graphical view]
PRINTSiPR01039. TRNASYNTHTRP.
SMARTiSM00991. WHEP-TRS. 1 hit.
[Graphical view]
SUPFAMiSSF47060. SSF47060. 1 hit.
TIGRFAMsiTIGR00233. trpS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
PS00762. WHEP_TRS_1. 1 hit.
PS51185. WHEP_TRS_2. 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 1 (identifier: P23381-1) [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

MPNSEPASLL ELFNSIATQG ELVRSLKAGN ASKDEIDSAV KMLVSLKMSY    50
KAAAGEDYKA DCPPGNPAPT SNHGPDATEA EEDFVDPWTV QTSSAKGIDY 100
DKLIVRFGSS KIDKELINRI ERATGQRPHH FLRRGIFFSH RDMNQVLDAY 150
ENKKPFYLYT GRGPSSEAMH VGHLIPFIFT KWLQDVFNVP LVIQMTDDEK 200
YLWKDLTLDQ AYSYAVENAK DIIACGFDIN KTFIFSDLDY MGMSSGFYKN 250
VVKIQKHVTF NQVKGIFGFT DSDCIGKISF PAIQAAPSFS NSFPQIFRDR 300
TDIQCLIPCA IDQDPYFRMT RDVAPRIGYP KPALLHSTFF PALQGAQTKM 350
SASDPNSSIF LTDTAKQIKT KVNKHAFSGG RDTIEEHRQF GGNCDVDVSF 400
MYLTFFLEDD DKLEQIRKDY TSGAMLTGEL KKALIEVLQP LIAEHQARRK 450
EVTDEIVKEF MTPRKLSFDF Q 471
Length:471
Mass (Da):53,165
Last modified:December 1, 1992 - v2
Checksum:iE96344449053A0D0
GO
Isoform 2 (identifier: P23381-2) [UniParc]FASTAAdd to Basket

Also known as: mini TrpRS

The sequence of this isoform differs from the canonical sequence as follows:
     1-41: Missing.

Show »
Length:430
Mass (Da):48,852
Checksum:i5FE1254E781221DD
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti54 – 541A → S.
Corresponds to variant rs2234521 [ dbSNP | Ensembl ].
VAR_052406
Natural varianti455 – 4551E → D in a breast cancer sample; somatic mutation. 1 Publication
VAR_036466

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4141Missing in isoform 2.
VSP_038221Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti213 – 2142SY → GD in AAA61298. 1 Publication
Sequence conflicti310 – 3101A → V in AAH95453. 1 Publication
Sequence conflicti424 – 4241A → R in CAA44450. 1 Publication
Sequence conflicti439 – 4391Q → L in AAH95453. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M77804 mRNA. Translation: AAA67324.1.
X59892 mRNA. Translation: CAA42545.1.
M61715 mRNA. Translation: AAA61298.1.
X62570 mRNA. Translation: CAA44450.1.
BX248006 mRNA. Translation: CAD62335.1.
AK056100 mRNA. Translation: BAG51626.1.
AK291141 mRNA. Translation: BAF83830.1.
AL157871 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW81700.1.
BC017489 mRNA. Translation: AAH17489.1.
BC095453 mRNA. Translation: AAH95453.1.
S82905 Genomic DNA. Translation: AAB39381.1.
X67920, X67921, X67922 Genomic DNA. Translation: CAB94198.1.
X67923
, X67924, X67925, X67926, X67927, X67928 Genomic DNA. Translation: CAB94199.1.
CCDSiCCDS9960.1. [P23381-1]
PIRiA41633. A41706.
RefSeqiNP_004175.2. NM_004184.3. [P23381-1]
NP_776049.1. NM_173701.1. [P23381-1]
NP_998810.1. NM_213645.1.
NP_998811.1. NM_213646.1.
XP_005268101.1. XM_005268044.1. [P23381-1]
XP_006720311.1. XM_006720248.1. [P23381-1]
XP_006720312.1. XM_006720249.1. [P23381-1]
UniGeneiHs.497599.

Genome annotation databases

EnsembliENST00000344102; ENSP00000339485; ENSG00000140105.
ENST00000355338; ENSP00000347495; ENSG00000140105. [P23381-1]
ENST00000358655; ENSP00000351481; ENSG00000140105.
ENST00000392882; ENSP00000376620; ENSG00000140105. [P23381-1]
ENST00000556645; ENSP00000451887; ENSG00000140105.
ENST00000557135; ENSP00000451460; ENSG00000140105. [P23381-1]
GeneIDi7453.
KEGGihsa:7453.
UCSCiuc001yhg.2. human. [P23381-1]

Polymorphism databases

DMDMi135191.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M77804 mRNA. Translation: AAA67324.1 .
X59892 mRNA. Translation: CAA42545.1 .
M61715 mRNA. Translation: AAA61298.1 .
X62570 mRNA. Translation: CAA44450.1 .
BX248006 mRNA. Translation: CAD62335.1 .
AK056100 mRNA. Translation: BAG51626.1 .
AK291141 mRNA. Translation: BAF83830.1 .
AL157871 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW81700.1 .
BC017489 mRNA. Translation: AAH17489.1 .
BC095453 mRNA. Translation: AAH95453.1 .
S82905 Genomic DNA. Translation: AAB39381.1 .
X67920 , X67921 , X67922 Genomic DNA. Translation: CAB94198.1 .
X67923
, X67924 , X67925 , X67926 , X67927 , X67928 Genomic DNA. Translation: CAB94199.1 .
CCDSi CCDS9960.1. [P23381-1 ]
PIRi A41633. A41706.
RefSeqi NP_004175.2. NM_004184.3. [P23381-1 ]
NP_776049.1. NM_173701.1. [P23381-1 ]
NP_998810.1. NM_213645.1.
NP_998811.1. NM_213646.1.
XP_005268101.1. XM_005268044.1. [P23381-1 ]
XP_006720311.1. XM_006720248.1. [P23381-1 ]
XP_006720312.1. XM_006720249.1. [P23381-1 ]
UniGenei Hs.497599.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1O5T X-ray 2.50 A 94-471 [» ]
1R6T X-ray 2.10 A/B 1-466 [» ]
1R6U X-ray 2.00 A/B 48-471 [» ]
1ULH X-ray 2.31 A/B 82-471 [» ]
2AKE X-ray 3.10 A 94-471 [» ]
2AZX X-ray 2.80 A/B 1-471 [» ]
2DR2 X-ray 3.00 A 94-471 [» ]
2QUH X-ray 2.40 A/B 1-471 [» ]
2QUI X-ray 2.40 A/B 1-471 [» ]
2QUJ X-ray 2.42 A/B 1-471 [» ]
2QUK X-ray 2.80 A 1-471 [» ]
ProteinModelPortali P23381.
SMRi P23381. Positions 82-471.
ModBasei Search...

Protein-protein interaction databases

BioGridi 113292. 34 interactions.
DIPi DIP-29493N.
IntActi P23381. 5 interactions.
MINTi MINT-1408962.
STRINGi 9606.ENSP00000347495.

Chemistry

DrugBanki DB00150. L-Tryptophan.

PTM databases

PhosphoSitei P23381.

Polymorphism databases

DMDMi 135191.

2D gel databases

OGPi P23381.

Proteomic databases

MaxQBi P23381.
PaxDbi P23381.
PeptideAtlasi P23381.
PRIDEi P23381.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000344102 ; ENSP00000339485 ; ENSG00000140105 .
ENST00000355338 ; ENSP00000347495 ; ENSG00000140105 . [P23381-1 ]
ENST00000358655 ; ENSP00000351481 ; ENSG00000140105 .
ENST00000392882 ; ENSP00000376620 ; ENSG00000140105 . [P23381-1 ]
ENST00000556645 ; ENSP00000451887 ; ENSG00000140105 .
ENST00000557135 ; ENSP00000451460 ; ENSG00000140105 . [P23381-1 ]
GeneIDi 7453.
KEGGi hsa:7453.
UCSCi uc001yhg.2. human. [P23381-1 ]

Organism-specific databases

CTDi 7453.
GeneCardsi GC14M100800.
HGNCi HGNC:12729. WARS.
HPAi HPA018944.
MIMi 191050. gene.
neXtProti NX_P23381.
PharmGKBi PA37340.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0180.
HOVERGENi HBG002325.
InParanoidi P23381.
KOi K01867.
OMAi KTFIFNN.
OrthoDBi EOG7T4MK3.
PhylomeDBi P23381.
TreeFami TF105669.

Enzyme and pathway databases

Reactomei REACT_15306. Cytosolic tRNA aminoacylation.

Miscellaneous databases

ChiTaRSi WARS. human.
EvolutionaryTracei P23381.
GeneWikii WARS_(gene).
GenomeRNAii 7453.
NextBioi 29178.
PROi P23381.
SOURCEi Search...

Gene expression databases

ArrayExpressi P23381.
Bgeei P23381.
CleanExi HS_WARS.
Genevestigatori P23381.

Family and domain databases

Gene3Di 1.10.287.10. 1 hit.
3.40.50.620. 1 hit.
InterProi IPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009068. S15_NS1_RNA-bd.
IPR002306. Trp-tRNA-ligase.
IPR000738. WHEP-TRS.
[Graphical view ]
PANTHERi PTHR10055. PTHR10055. 1 hit.
Pfami PF00579. tRNA-synt_1b. 1 hit.
PF00458. WHEP-TRS. 1 hit.
[Graphical view ]
PRINTSi PR01039. TRNASYNTHTRP.
SMARTi SM00991. WHEP-TRS. 1 hit.
[Graphical view ]
SUPFAMi SSF47060. SSF47060. 1 hit.
TIGRFAMsi TIGR00233. trpS. 1 hit.
PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
PS00762. WHEP_TRS_1. 1 hit.
PS51185. WHEP_TRS_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Interferon induces tryptophanyl-tRNA synthetase expression in human fibroblasts."
    Rubin B.Y., Anderson S.L., Xing L., Powell R.J., Tate W.P.
    J. Biol. Chem. 266:24245-24248(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Human interferon gamma potently induces the synthesis of a 55-kDa protein (gamma 2) highly homologous to rabbit peptide chain release factor and bovine tryptophanyl-tRNA synthetase."
    Fleckner J., Rasmussen H.H., Justesen J.
    Proc. Natl. Acad. Sci. U.S.A. 88:11520-11524(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Cloning and nucleotide sequence of the structural gene encoding for human tryptophanyl-tRNA synthetase."
    Frolova L.Y., Sudomoina M.A., Grigorieva A.Y., Zinovieva O.L., Kisselev L.L.
    Gene 109:291-296(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Molecular cloning and characterization of an interferon induced human cDNA with sequence homology to a mammalian peptide chain release factor."
    Buwitt U., Flohr T., Boettger E.C.
    EMBO J. 11:489-496(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  5. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Fetal liver.
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Teratocarcinoma.
  7. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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 1).
    Tissue: Blood and Lymph.
  10. "Alternative splicing of 5'-terminal exons of the human tryptophanyl-tRNA synthetase gene."
    Sokolova I.V., Narovlianskii A.N., Amchenkova A.M., Turpaev K.T.
    Mol. Biol. (Mosk.) 30:319-329(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
  11. "The human gene encoding tryptophanyl-tRNA synthetase: interferon-response elements and exon-intron organization."
    Frolova L.Y., Grigorieva A.Y., Sudomoina M.A., Kisselev L.L.
    Gene 128:237-245(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-141 AND 182-471.
    Tissue: Sperm.
  12. "Gamma interferon potently induces tryptophanyl-tRNA synthetase expression in human keratinocytes."
    Reano A., Richard M.H., Denoroy L., Viac J., Benedetto J.P., Schmitt D.
    J. Invest. Dermatol. 100:775-779(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-19; 142-162; 205-220; 278-298; 350-366 AND 433-448, INDUCTION.
    Tissue: Keratinocyte.
  13. Bienvenut W.V., Heiserich L., Gottlieb E.
    Submitted (MAR-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-24; 97-106; 433-448 AND 465-471, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon carcinoma.
  14. Cited for: PROTEIN SEQUENCE OF 71-75 AND 91-98, PROTEOLYTIC CLEAVAGE, FUNCTION.
  15. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
    Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
    Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 265-276; 278-296; 299-317 AND 350-365.
    Tissue: Keratinocyte.
  16. "An interferon-induced protein with release factor activity is a tryptophanyl-tRNA synthetase."
    Bange F.-C., Flohr T., Buwitt U., Boettger E.C.
    FEBS Lett. 300:162-166(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "Transcriptional regulation of the interferon-gamma-inducible tryptophanyl-tRNA synthetase includes alternative splicing."
    Tolstrup A.B., Bejder A., Fleckner J., Justesen J.
    J. Biol. Chem. 270:397-403(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  18. Cited for: FUNCTION.
  19. "Biologically active fragment of a human tRNA synthetase inhibits fluid shear stress-activated responses of endothelial cells."
    Tzima E., Reader J.S., Irani-Tehrani M., Ewalt K.L., Schwartz M.A., Schimmel P.
    Proc. Natl. Acad. Sci. U.S.A. 100:14903-14907(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  20. "Oxidative stress-responsive intracellular regulation specific for the angiostatic form of human tryptophanyl-tRNA synthetase."
    Wakasugi K., Nakano T., Morishima I.
    Biochemistry 44:225-232(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GAPDH.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains."
    Yang X.-L., Otero F.J., Skene R.J., McRee D.E., Schimmel P., Ribas de Pouplana L.
    Proc. Natl. Acad. Sci. U.S.A. 100:15376-15380(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-466.
  27. "Crystal structure of human tryptophanyl-tRNA synthetase catalytic fragment: insights into substrate recognition, tRNA binding, and angiogenesis activity."
    Yu Y., Liu Y., Shen N., Xu X., Xu F., Jia J., Jin Y., Arnold E., Ding J.
    J. Biol. Chem. 279:8378-8388(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 94-471.
  28. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-455.

Entry informationi

Entry nameiSYWC_HUMAN
AccessioniPrimary (citable) accession number: P23381
Secondary accession number(s): A6NGN1
, A6NID3, P78535, Q502Y0, Q53XB6, Q9UDI5, Q9UDL3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: December 1, 1992
Last modified: September 3, 2014
This is version 150 of the entry and version 2 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

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 14
    Human chromosome 14: 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

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