dbPTM

SYWC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SYWC_HUMAN
UniProt AC	P23381
Protein Name	Tryptophan--tRNA ligase, cytoplasmic
Gene Name	WARS
Organism	Homo sapiens (Human).
Sequence Length	471
Subcellular Localization	Cytoplasm.
Protein 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..
Protein Sequence	MPNSEPASLLELFNSIATQGELVRSLKAGNASKDEIDSAVKMLVSLKMSYKAAAGEDYKADCPPGNPAPTSNHGPDATEAEEDFVDPWTVQTSSAKGIDYDKLIVRFGSSKIDKELINRIERATGQRPHHFLRRGIFFSHRDMNQVLDAYENKKPFYLYTGRGPSSEAMHVGHLIPFIFTKWLQDVFNVPLVIQMTDDEKYLWKDLTLDQAYSYAVENAKDIIACGFDINKTFIFSDLDYMGMSSGFYKNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAIQAAPSFSNSFPQIFRDRTDIQCLIPCAIDQDPYFRMTRDVAPRIGYPKPALLHSTFFPALQGAQTKMSASDPNSSIFLTDTAKQIKTKVNKHAFSGGRDTIEEHRQFGGNCDVDVSFMYLTFFLEDDDKLEQIRKDYTSGAMLTGELKKALIEVLQPLIAEHQARRKEVTDEIVKEFMTPRKLSFDFQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MPNSEPASLLE ----CCCCCCHHHHH	38.80	25159151
8	Phosphorylation	MPNSEPASLLELFNS CCCCCCHHHHHHHHH	44.17	28464451
15	Phosphorylation	SLLELFNSIATQGEL HHHHHHHHHCHHHHH	13.28	29632367
18	Phosphorylation	ELFNSIATQGELVRS HHHHHHCHHHHHHHH	35.12	29632367
27	Ubiquitination	GELVRSLKAGNASKD HHHHHHHHCCCCCHH	56.33	21906983
27	Malonylation	GELVRSLKAGNASKD HHHHHHHHCCCCCHH	56.33	26320211
27	Acetylation	GELVRSLKAGNASKD HHHHHHHHCCCCCHH	56.33	25953088
31	Ubiquitination	RSLKAGNASKDEIDS HHHHCCCCCHHHHHH	19.62	21890473
32	Phosphorylation	SLKAGNASKDEIDSA HHHCCCCCHHHHHHH	44.64	25849741
33	Acetylation	LKAGNASKDEIDSAV HHCCCCCHHHHHHHH	57.90	23749302
33	Ubiquitination	LKAGNASKDEIDSAV HHCCCCCHHHHHHHH	57.90	-
33	Malonylation	LKAGNASKDEIDSAV HHCCCCCHHHHHHHH	57.90	26320211
38	Phosphorylation	ASKDEIDSAVKMLVS CCHHHHHHHHHHHHH	40.39	25849741
41	Ubiquitination	DEIDSAVKMLVSLKM HHHHHHHHHHHHHHH	26.66	-
41	2-Hydroxyisobutyrylation	DEIDSAVKMLVSLKM HHHHHHHHHHHHHHH	26.66	-
45	Phosphorylation	SAVKMLVSLKMSYKA HHHHHHHHHHHHHHH	20.50	27251275
47	Ubiquitination	VKMLVSLKMSYKAAA HHHHHHHHHHHHHHC	20.49	21906983
47	Malonylation	VKMLVSLKMSYKAAA HHHHHHHHHHHHHHC	20.49	26320211
49	Phosphorylation	MLVSLKMSYKAAAGE HHHHHHHHHHHHCCC	23.15	30576142
50	Phosphorylation	LVSLKMSYKAAAGED HHHHHHHHHHHCCCC	10.93	30576142
51	Ubiquitination	VSLKMSYKAAAGEDY HHHHHHHHHHCCCCC	25.00	-
51	2-Hydroxyisobutyrylation	VSLKMSYKAAAGEDY HHHHHHHHHHCCCCC	25.00	-
51	Succinylation	VSLKMSYKAAAGEDY HHHHHHHHHHCCCCC	25.00	23954790
59	Ubiquitination	AAAGEDYKADCPPGN HHCCCCCCCCCCCCC	50.50	-
59	Acetylation	AAAGEDYKADCPPGN HHCCCCCCCCCCCCC	50.50	26051181
61 (in isoform 2)	Ubiquitination	-	41.10	21890473
96	Ubiquitination	TVQTSSAKGIDYDKL CEECCCCCCCCCCCE	59.35	-
102	Ubiquitination	AKGIDYDKLIVRFGS CCCCCCCCEEEECCC	33.61	21890473
102	2-Hydroxyisobutyrylation	AKGIDYDKLIVRFGS CCCCCCCCEEEECCC	33.61	-
102	Acetylation	AKGIDYDKLIVRFGS CCCCCCCCEEEECCC	33.61	26822725
102 (in isoform 1)	Ubiquitination	-	33.61	21890473
111	Ubiquitination	IVRFGSSKIDKELIN EEECCCCHHCHHHHH	57.53	-
111	Malonylation	IVRFGSSKIDKELIN EEECCCCHHCHHHHH	57.53	26320211
111	Succinylation	IVRFGSSKIDKELIN EEECCCCHHCHHHHH	57.53	23954790
113 (in isoform 2)	Ubiquitination	-	41.96	21890473
114	Ubiquitination	FGSSKIDKELINRIE CCCCHHCHHHHHHHH	58.87	-
114	2-Hydroxyisobutyrylation	FGSSKIDKELINRIE CCCCHHCHHHHHHHH	58.87	-
114	Malonylation	FGSSKIDKELINRIE CCCCHHCHHHHHHHH	58.87	26320211
114	Acetylation	FGSSKIDKELINRIE CCCCHHCHHHHHHHH	58.87	26822725
139	Phosphorylation	LRRGIFFSHRDMNQV HHCCCEECCCCHHHH	13.58	20068231
143	Sulfoxidation	IFFSHRDMNQVLDAY CEECCCCHHHHHHHH	3.68	30846556
153	Ubiquitination	VLDAYENKKPFYLYT HHHHHHCCCCEEEEE	50.30	-
153	Succinylation	VLDAYENKKPFYLYT HHHHHHCCCCEEEEE	50.30	23954790
154	Succinylation	LDAYENKKPFYLYTG HHHHHCCCCEEEEEC	52.52	-
154	Ubiquitination	LDAYENKKPFYLYTG HHHHHCCCCEEEEEC	52.52	21890473
154	Succinylation	LDAYENKKPFYLYTG HHHHHCCCCEEEEEC	52.52	21890473
154	Acetylation	LDAYENKKPFYLYTG HHHHHCCCCEEEEEC	52.52	26051181
154 (in isoform 1)	Ubiquitination	-	52.52	21890473
169	Sulfoxidation	RGPSSEAMHVGHLIP CCCCHHHHCHHHHHH	2.00	30846556
200	Acetylation	IQMTDDEKYLWKDLT EEECCCCCCEEEECC	53.27	30593399
204	Acetylation	DDEKYLWKDLTLDQA CCCCCEEEECCHHHH	40.02	23954790
204	Ubiquitination	DDEKYLWKDLTLDQA CCCCCEEEECCHHHH	40.02	-
204	Succinylation	DDEKYLWKDLTLDQA CCCCCEEEECCHHHH	40.02	23954790
212	Phosphorylation	DLTLDQAYSYAVENA ECCHHHHHHHHHHCH	9.15	28152594
213	Phosphorylation	LTLDQAYSYAVENAK CCHHHHHHHHHHCHH	15.05	28152594
214	Phosphorylation	TLDQAYSYAVENAKD CHHHHHHHHHHCHHH	11.29	28152594
220	Ubiquitination	SYAVENAKDIIACGF HHHHHCHHHHEEECC	62.13	-
240	Phosphorylation	FIFSDLDYMGMSSGF EECCCCCCCCCCCCC	11.67	25954137
241	Sulfoxidation	IFSDLDYMGMSSGFY ECCCCCCCCCCCCCH	3.47	30846556
243	Sulfoxidation	SDLDYMGMSSGFYKN CCCCCCCCCCCCHHC	1.32	30846556
245	Phosphorylation	LDYMGMSSGFYKNVV CCCCCCCCCCHHCCE	24.83	25954137
248	Phosphorylation	MGMSSGFYKNVVKIQ CCCCCCCHHCCEEEE	12.74	25954137
253	Ubiquitination	GFYKNVVKIQKHVTF CCHHCCEEEEECCCH	34.83	-
256	Ubiquitination	KNVVKIQKHVTFNQV HCCEEEEECCCHHHC	43.44	-
256	Acetylation	KNVVKIQKHVTFNQV HCCEEEEECCCHHHC	43.44	26051181
259	Phosphorylation	VKIQKHVTFNQVKGI EEEEECCCHHHCCEE	19.31	20068231
264	Ubiquitination	HVTFNQVKGIFGFTD CCCHHHCCEECCCCC	36.20	-
272	Phosphorylation	GIFGFTDSDCIGKIS EECCCCCHHHCEEEC	31.18	21712546
288	Phosphorylation	PAIQAAPSFSNSFPQ HHHHCCCCCCCCCHH	36.26	25693802
290	Phosphorylation	IQAAPSFSNSFPQIF HHCCCCCCCCCHHHH	35.58	25693802
292	Phosphorylation	AAPSFSNSFPQIFRD CCCCCCCCCHHHHCC	36.79	25693802
301	Phosphorylation	PQIFRDRTDIQCLIP HHHHCCCCCCEEEEE	41.57	-
316	Phosphorylation	CAIDQDPYFRMTRDV ECCCCCCCCCCCCCC	16.47	20090780
319 (in isoform 2)	Ubiquitination	-	2.30	-
320	Phosphorylation	QDPYFRMTRDVAPRI CCCCCCCCCCCHHHC	21.33	28555341
325	Acetylation	RMTRDVAPRIGYPKP CCCCCCHHHCCCCCC	28.42	19608861
325	Ubiquitination	RMTRDVAPRIGYPKP CCCCCCHHHCCCCCC	28.42	19608861
329	Phosphorylation	DVAPRIGYPKPALLH CCHHHCCCCCCCHHH	13.00	28152594
337	Phosphorylation	PKPALLHSTFFPALQ CCCCHHHHCHHHHHC	27.21	28152594
349	Ubiquitination	ALQGAQTKMSASDPN HHCCCCCCCCCCCCC	20.83	-
350	Sulfoxidation	LQGAQTKMSASDPNS HCCCCCCCCCCCCCC	4.61	21406390
351	Phosphorylation	QGAQTKMSASDPNSS CCCCCCCCCCCCCCC	26.61	29255136
353	Phosphorylation	AQTKMSASDPNSSIF CCCCCCCCCCCCCEE	46.42	29255136
357	Phosphorylation	MSASDPNSSIFLTDT CCCCCCCCCEEEECH	30.14	29255136
358	Phosphorylation	SASDPNSSIFLTDTA CCCCCCCCEEEECHH	24.81	29255136
366	Acetylation	IFLTDTAKQIKTKVN EEEECHHHHHHHHHH	55.43	19608861
366	Ubiquitination	IFLTDTAKQIKTKVN EEEECHHHHHHHHHH	55.43	19608861
366	2-Hydroxyisobutyrylation	IFLTDTAKQIKTKVN EEEECHHHHHHHHHH	55.43	-
366	Malonylation	IFLTDTAKQIKTKVN EEEECHHHHHHHHHH	55.43	26320211
369	Ubiquitination	TDTAKQIKTKVNKHA ECHHHHHHHHHHHHH	39.54	-
374	Acetylation	QIKTKVNKHAFSGGR HHHHHHHHHHCCCCC	39.02	25953088
378	Phosphorylation	KVNKHAFSGGRDTIE HHHHHHCCCCCCHHH	40.91	24275569
381	Methylation	KHAFSGGRDTIEEHR HHHCCCCCCHHHHHH	41.23	115919881
383	Phosphorylation	AFSGGRDTIEEHRQF HCCCCCCHHHHHHHH	29.00	24275569
403 (in isoform 2)	Ubiquitination	-	1.95	-
418	Malonylation	DKLEQIRKDYTSGAM HHHHHHHHHCCCCCH	57.63	26320211
420	Phosphorylation	LEQIRKDYTSGAMLT HHHHHHHCCCCCHHC	13.07	21406692
421	Phosphorylation	EQIRKDYTSGAMLTG HHHHHHCCCCCHHCH	30.71	21406692
422	Phosphorylation	QIRKDYTSGAMLTGE HHHHHCCCCCHHCHH	20.51	21406692
425	Sulfoxidation	KDYTSGAMLTGELKK HHCCCCCHHCHHHHH	3.82	30846556
427	Phosphorylation	YTSGAMLTGELKKAL CCCCCHHCHHHHHHH	18.61	21406692
431	Acetylation	AMLTGELKKALIEVL CHHCHHHHHHHHHHH	31.53	25953088
431	Ubiquitination	AMLTGELKKALIEVL CHHCHHHHHHHHHHH	31.53	-
431	Succinylation	AMLTGELKKALIEVL CHHCHHHHHHHHHHH	31.53	23954790
432	Ubiquitination	MLTGELKKALIEVLQ HHCHHHHHHHHHHHH	62.14	-
450	Ubiquitination	AEHQARRKEVTDEIV HHHHHHHHHCHHHHH	51.49	-
453	Phosphorylation	QARRKEVTDEIVKEF HHHHHHCHHHHHHHH	29.07	-
458	Ubiquitination	EVTDEIVKEFMTPRK HCHHHHHHHHCCCCC	51.39	-
458	Acetylation	EVTDEIVKEFMTPRK HCHHHHHHHHCCCCC	51.39	25038526
458	Succinylation	EVTDEIVKEFMTPRK HCHHHHHHHHCCCCC	51.39	23954790
461	Sulfoxidation	DEIVKEFMTPRKLSF HHHHHHHCCCCCCCC	5.45	30846556
462	Phosphorylation	EIVKEFMTPRKLSFD HHHHHHCCCCCCCCC	25.84	29514088
465	Ubiquitination	KEFMTPRKLSFDFQ- HHHCCCCCCCCCCC-	50.08	-
467	Phosphorylation	FMTPRKLSFDFQ--- HCCCCCCCCCCC---	26.29	29255136

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of SYWC_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SYWC_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of SYWC_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DCA13_HUMAN	DCAF13	physical	21900206
DNM3B_HUMAN	DNMT3B	physical	21900206
A4_HUMAN	APP	physical	21832049
TRI25_HUMAN	TRIM25	physical	22939629
CALU_HUMAN	CALU	physical	22863883
UB2R1_HUMAN	CDC34	physical	22863883
PYRG2_HUMAN	CTPS2	physical	22863883
GNPI1_HUMAN	GNPDA1	physical	22863883
GTF2I_HUMAN	GTF2I	physical	22863883
HERC4_HUMAN	HERC4	physical	22863883
PCNA_HUMAN	PCNA	physical	22863883
TCPG_HUMAN	CCT3	physical	26344197
CATD_HUMAN	CTSD	physical	26344197
DHB12_HUMAN	HSD17B12	physical	26344197
IMA1_HUMAN	KPNA2	physical	26344197
MB12A_HUMAN	MVB12A	physical	26344197
PUR4_HUMAN	PFAS	physical	26344197
PSMG1_HUMAN	PSMG1	physical	26344197
MSS4_HUMAN	RABIF	physical	26344197
TATD1_HUMAN	TATDN1	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00150	L-Tryptophan

Regulatory Network of SYWC_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467, AND MASSSPECTROMETRY.	16083285 [Abstract]