CPLM-005169

CPLM 1.0 - Compendium of Protein Lysine Modification

Tag

Content

CPLM ID

CPLM-005169

UniProt Accession

SYWC_HUMAN; P23381; A6NGN1; A6NID3; P78535; Q502Y0; Q53XB6; Q9UDI5; Q9UDL3

Genbank Protein ID

M77804; X59892; M61715; X62570; BX248006; AK056100; AK291141; AL157871; CH471061; BC017489; BC095453; S82905; X67920; X67921; X67922; X67923; X67924; X67925; X67926; X67927; X67928

Genbank Nucleotide ID

AAA67324.1; CAA42545.1; AAA61298.1; CAA44450.1; CAD62335.1; BAG51626.1; BAF83830.1; EAW81700.1; AAH17489.1; AAH95453.1; AAB39381.1; CAB94198.1; CAB94198.1; CAB94198.1; CAB94199.1; CAB94199.1; CAB94199.1; CAB94199.1; CAB94199.1; CAB94199.1

Protein Name

Tryptophan--tRNA ligase, cytoplasmic

Protein Synonyms/Alias

Interferon-induced protein 53; IFP53; Tryptophanyl-tRNA synthetase; TrpRS; hWRS; T1-TrpRS; T2-TrpRS

Gene Name

WARS

Gene Synonyms/Alias

IFI53; WRS

Created Date

July 27, 2013

Organism

Homo sapiens (Human)

NCBI Taxa ID

9606

Lysine Modification

Position	Peptide	Type	References
319	IFLTDTAKQIKTKVN	ubiquitination	[1]
403	AEHQARRKEVTDEIV	ubiquitination	[1]

Reference

[1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]

Functional Description

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.

Sequence Annotation

DOMAIN 8 64 WHEP-TRS.
MOTIF 164 173 "HIGH" region.
MOTIF 349 353 "KMSKS" region.

Keyword

3D-structure; Alternative splicing; Aminoacyl-tRNA synthetase; Angiogenesis; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Ligase; Nucleotide-binding; Polymorphism; Protein biosynthesis; Reference proteome.

Sequence Source

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

Protein Length

471 AA

Protein Sequence

MSYKAAAGED YKADCPPGNP APTSNHGPDA TEAEEDFVDP WTVQTSSAKG IDYDKLIVRF 60
GSSKIDKELI NRIERATGQR PHHFLRRGIF FSHRDMNQVL DAYENKKPFY LYTGRGPSSE 120
AMHVGHLIPF IFTKWLQDVF NVPLVIQMTD DEKYLWKDLT LDQAYSYAVE NAKDIIACGF 180
DINKTFIFSD LDYMGMSSGF YKNVVKIQKH VTFNQVKGIF GFTDSDCIGK ISFPAIQAAP 240
SFSNSFPQIF RDRTDIQCLI PCAIDQDPYF RMTRDVAPRI GYPKPALLHS TFFPALQGAQ 300
TKMSASDPNS SIFLTDTAKQ IKTKVNKHAF SGGRDTIEEH RQFGGNCDVD VSFMYLTFFL 360
EDDDKLEQIR KDYTSGAMLT GELKKALIEV LQPLIAEHQA RRKEVTDEIV KEFMTPRKLS 420
FDFQ 424

Gene Ontology

GO:0005829; C:cytosol; TAS:Reactome.
GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO:0004830; F:tryptophan-tRNA ligase activity; NAS:UniProtKB.
GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
GO:0045765; P:regulation of angiogenesis; IDA:UniProtKB.
GO:0006436; P:tryptophanyl-tRNA aminoacylation; NAS:UniProtKB.

Interpro

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.

Pfam

PF00579; tRNA-synt_1b
PF00458; WHEP-TRS

SMART

SM00991; WHEP-TRS

PROSITE

PS00178; AA_TRNA_LIGASE_I
PS00762; WHEP_TRS_1
PS51185; WHEP_TRS_2

PRINTS

PR01039; TRNASYNTHTRP.