dbPTM

SYVC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SYVC_HUMAN
UniProt AC	P26640
Protein Name	Valine--tRNA ligase
Gene Name	VARS
Organism	Homo sapiens (Human).
Sequence Length	1264
Subcellular Localization
Protein Description
Protein Sequence	MSTLYVSPHPDAFPSLRALIAARYGEAGEGPGWGGAHPRICLQPPPTSRTPFPPPRLPALEQGPGGLWVWGATAVAQLLWPAGLGGPGGSRAAVLVQQWVSYADTELIPAACGATLPALGLRSSAQDPQAVLGALGRALSPLEEWLRLHTYLAGEAPTLADLAAVTALLLPFRYVLDPPARRIWNNVTRWFVTCVRQPEFRAVLGEVVLYSGARPLSHQPGPEAPALPKTAAQLKKEAKKREKLEKFQQKQKIQQQQPPPGEKKPKPEKREKRDPGVITYDLPTPPGEKKDVSGPMPDSYSPRYVEAAWYPWWEQQGFFKPEYGRPNVSAANPRGVFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIATQVVVEKKLWREQGLSRHQLGREAFLQEVWKWKEEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSAAVTEAFVRLHEEGIIYRSTRLVNWSCTLNSAISDIEVDKKELTGRTLLSVPGYKEKVEFGVLVSFAYKVQGSDSDEEVVVATTRIETMLGDVAVAVHPKDTRYQHLKGKNVIHPFLSRSLPIVFDEFVDMDFGTGAVKITPAHDQNDYEVGQRHGLEAISIMDSRGALINVPPPFLGLPRFEARKAVLVALKERGLFRGIEDNPMVVPLCNRSKDVVEPLLRPQWYVRCGEMAQAASAAVTRGDLRILPEAHQRTWHAWMDNIREWCISRQLWWGHRIPAYFVTVSDPAVPPGEDPDGRYWVSGRNEAEAREKAAKEFGVSPDKISLQQDEDVLDTWFSSGLFPLSILGWPNQSEDLSVFYPGTLLETGHDILFFWVARMVMLGLKLTGRLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVIYGISLQGLHNQLLNSNLDPSEVEKAKEGQKADFPAGIPECGTDALRFGLCAYMSQGRDINLDVNRILGYRHFCNKLWNATKFALRGLGKGFVPSPTSQPGGHESLVDRWIRSRLTEAVRLSNQGFQAYDFPAVTTAQYSFWLYELCDVYLECLKPVLNGVDQVAAECARQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRRMPQAPPSLCVTPYPEPSECSWKDPEAEAALELALSITRAVRSLRADYNLTRIRPDCFLEVADEATGALASAVSGYVQALASAGVVAVLALGAPAPQGCAVALASDRCSIHLQLQGLVDPARELGKLQAKRVEAQRQAQRLRERRAASGYPVKVPLEVQEADEAKLQQTEAELRKVDEAIALFQKML

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSTLYVSPH ------CCCEECCCC	38.12	22223895
2	Phosphorylation	------MSTLYVSPH ------CCCEECCCC	38.12	25693802
3	Phosphorylation	-----MSTLYVSPHP -----CCCEECCCCC	33.69	25002506
5	Phosphorylation	---MSTLYVSPHPDA ---CCCEECCCCCCC	10.04	25693802
7	Phosphorylation	-MSTLYVSPHPDAFP -CCCEECCCCCCCCH	12.16	27050516
15	Phosphorylation	PHPDAFPSLRALIAA CCCCCCHHHHHHHHH	24.84	25693802
24	Phosphorylation	RALIAARYGEAGEGP HHHHHHHHCCCCCCC	18.00	28152594
25	Ubiquitination	ALIAARYGEAGEGPG HHHHHHHCCCCCCCC	16.84	21890473
123	Phosphorylation	LPALGLRSSAQDPQA HHHHCCCCCCCCHHH	34.76	28857561
123	Ubiquitination	LPALGLRSSAQDPQA HHHHCCCCCCCCHHH	34.76	21890473
124	Phosphorylation	PALGLRSSAQDPQAV HHHCCCCCCCCHHHH	24.42	28857561
137	Ubiquitination	AVLGALGRALSPLEE HHHHHHHHHHCHHHH	32.95	21890473
138	Ubiquitination	VLGALGRALSPLEEW HHHHHHHHHCHHHHH	15.59	21890473
140	Phosphorylation	GALGRALSPLEEWLR HHHHHHHCHHHHHHH	26.84	30087585
174	Phosphorylation	ALLLPFRYVLDPPAR HHHHHHHHHCCCCHH	13.02	22817900
211	Phosphorylation	LGEVVLYSGARPLSH HCEEEEECCCCCCCC	23.09	28348404
212	Ubiquitination	GEVVLYSGARPLSHQ CEEEEECCCCCCCCC	16.43	21890473
217	Phosphorylation	YSGARPLSHQPGPEA ECCCCCCCCCCCCCC	23.82	28857561
230	Phosphorylation	EAPALPKTAAQLKKE CCCCCCHHHHHHHHH	25.86	20363803
246	Ubiquitination	KKREKLEKFQQKQKI HHHHHHHHHHHHHHH	59.93	-
252	Ubiquitination	EKFQQKQKIQQQQPP HHHHHHHHHHHCCCC	49.90	-
264	Acetylation	QPPPGEKKPKPEKRE CCCCCCCCCCCCCCC	54.71	30593327
269	Acetylation	EKKPKPEKREKRDPG CCCCCCCCCCCCCCC	74.51	30593333
272	Malonylation	PKPEKREKRDPGVIT CCCCCCCCCCCCCEE	67.16	26320211
279	Phosphorylation	KRDPGVITYDLPTPP CCCCCCEEEECCCCC	14.47	21945579
280	Phosphorylation	RDPGVITYDLPTPPG CCCCCEEEECCCCCC	12.35	21945579
284	Phosphorylation	VITYDLPTPPGEKKD CEEEECCCCCCCCCC	49.79	21945579
289	Ubiquitination	LPTPPGEKKDVSGPM CCCCCCCCCCCCCCC	61.25	21906983
293	Phosphorylation	PGEKKDVSGPMPDSY CCCCCCCCCCCCCCC	47.51	23186163
296	Sulfoxidation	KKDVSGPMPDSYSPR CCCCCCCCCCCCCCH	7.03	30846556
299	Phosphorylation	VSGPMPDSYSPRYVE CCCCCCCCCCCHHHH	22.95	25850435
300	Phosphorylation	SGPMPDSYSPRYVEA CCCCCCCCCCHHHHH	30.03	21082442
301	Phosphorylation	GPMPDSYSPRYVEAA CCCCCCCCCHHHHHE	13.57	22617229
320	Ubiquitination	WEQQGFFKPEYGRPN HHHCCCCCCCCCCCC	34.38	21906983
320	Acetylation	WEQQGFFKPEYGRPN HHHCCCCCCCCCCCC	34.38	21466224
394	2-Hydroxyisobutyrylation	ATQVVVEKKLWREQG EHHHHHHHHHHHHHC	41.37	-
394	Acetylation	ATQVVVEKKLWREQG EHHHHHHHHHHHHHC	41.37	26051181
418	Ubiquitination	AFLQEVWKWKEEKGD HHHHHHHHHHHHHCH	54.27	21906983
420	Acetylation	LQEVWKWKEEKGDRI HHHHHHHHHHHCHHH	52.87	19608861
423	Acetylation	VWKWKEEKGDRIYHQ HHHHHHHHCHHHHHH	68.17	19608861
423	Ubiquitination	VWKWKEEKGDRIYHQ HHHHHHHHCHHHHHH	68.17	-
428	Phosphorylation	EEKGDRIYHQLKKLG HHHCHHHHHHHHHHC	5.61	28152594
432	Ubiquitination	DRIYHQLKKLGSSLD HHHHHHHHHHCCCCC	39.11	21906983
432	2-Hydroxyisobutyrylation	DRIYHQLKKLGSSLD HHHHHHHHHHCCCCC	39.11	-
432	Acetylation	DRIYHQLKKLGSSLD HHHHHHHHHHCCCCC	39.11	25953088
433	Ubiquitination	RIYHQLKKLGSSLDW HHHHHHHHHCCCCCC	67.67	-
433	Malonylation	RIYHQLKKLGSSLDW HHHHHHHHHCCCCCC	67.67	26320211
433	Acetylation	RIYHQLKKLGSSLDW HHHHHHHHHCCCCCC	67.67	25953088
436	Phosphorylation	HQLKKLGSSLDWDRA HHHHHHCCCCCCCHH	37.86	23186163
437	Phosphorylation	QLKKLGSSLDWDRAC HHHHHCCCCCCCHHH	28.66	23917254
447	Sulfoxidation	WDRACFTMDPKLSAA CCHHHHCCCHHHHHH	4.10	30846556
450	Ubiquitination	ACFTMDPKLSAAVTE HHHCCCHHHHHHHHH	51.30	-
450	Acetylation	ACFTMDPKLSAAVTE HHHCCCHHHHHHHHH	51.30	26051181
469	Phosphorylation	LHEEGIIYRSTRLVN HHHCCCEEEEEEECE	9.15	27155012
478	Phosphorylation	STRLVNWSCTLNSAI EEEECEEEEECCHHH	7.63	25693802
479	Glutathionylation	TRLVNWSCTLNSAIS EEECEEEEECCHHHC	3.66	22555962
480	Phosphorylation	RLVNWSCTLNSAISD EECEEEEECCHHHCC	24.37	28348404
483	Phosphorylation	NWSCTLNSAISDIEV EEEEECCHHHCCEEE	30.05	28348404
486	Phosphorylation	CTLNSAISDIEVDKK EECCHHHCCEEECHH	32.05	20068231
492	Acetylation	ISDIEVDKKELTGRT HCCEEECHHHHCCCE	54.01	26051181
493	Ubiquitination	SDIEVDKKELTGRTL CCEEECHHHHCCCEE	54.19	-
502	Phosphorylation	LTGRTLLSVPGYKEK HCCCEEECCCCCHHE	29.40	23312004
507	Ubiquitination	LLSVPGYKEKVEFGV EECCCCCHHEEEEEE	57.90	21906983
525	Phosphorylation	FAYKVQGSDSDEEVV EEEEECCCCCCCEEE	19.49	29255136
527	Phosphorylation	YKVQGSDSDEEVVVA EEECCCCCCCEEEEE	48.93	29255136
552	Ubiquitination	VAVAVHPKDTRYQHL EEEEECCCCCCCHHH	57.78	-
552	Malonylation	VAVAVHPKDTRYQHL EEEEECCCCCCCHHH	57.78	26320211
552	Acetylation	VAVAVHPKDTRYQHL EEEEECCCCCCCHHH	57.78	26051181
562	Ubiquitination	RYQHLKGKNVIHPFL CCHHHCCCCCCCHHH	46.59	-
570	Phosphorylation	NVIHPFLSRSLPIVF CCCCHHHCCCCCEEE	21.87	24670416
572	Phosphorylation	IHPFLSRSLPIVFDE CCHHHCCCCCEEEEE	34.81	27732954
601	Phosphorylation	PAHDQNDYEVGQRHG CCCCCCCHHHHHHCC	21.77	28152594
613	Phosphorylation	RHGLEAISIMDSRGA HCCCEEEEEEECCCC	20.93	28857561
617	Phosphorylation	EAISIMDSRGALINV EEEEEEECCCCCCCC	18.42	28348404
638	Ubiquitination	LPRFEARKAVLVALK CCHHHHHHHHHHHHH	50.31	-
645	Acetylation	KAVLVALKERGLFRG HHHHHHHHHCCCCCC	35.31	19608861
645	Ubiquitination	KAVLVALKERGLFRG HHHHHHHHHCCCCCC	35.31	-
645	2-Hydroxyisobutyrylation	KAVLVALKERGLFRG HHHHHHHHHCCCCCC	35.31	-
645	Malonylation	KAVLVALKERGLFRG HHHHHHHHHCCCCCC	35.31	26320211
658	Sulfoxidation	RGIEDNPMVVPLCNR CCCCCCCEEEECCCC	6.26	21406390
663	Glutathionylation	NPMVVPLCNRSKDVV CCEEEECCCCCCCCH	3.05	22555962
667	Ubiquitination	VPLCNRSKDVVEPLL EECCCCCCCCHHHHC	51.83	-
667	Malonylation	VPLCNRSKDVVEPLL EECCCCCCCCHHHHC	51.83	26320211
667	Acetylation	VPLCNRSKDVVEPLL EECCCCCCCCHHHHC	51.83	26051181
679	Phosphorylation	PLLRPQWYVRCGEMA HHCCCCEEHHHHHHH	3.47	28152594
682	Glutathionylation	RPQWYVRCGEMAQAA CCCEEHHHHHHHHHH	3.74	22555962
699	Methylation	AVTRGDLRILPEAHQ HHHHCCEECCCHHHH	32.89	115919757
734	Phosphorylation	WGHRIPAYFVTVSDP CCCCCCEEEEEECCC	8.01	-
737	Phosphorylation	RIPAYFVTVSDPAVP CCCEEEEEECCCCCC	12.37	-
769	Ubiquitination	EAREKAAKEFGVSPD HHHHHHHHHHCCCCC	59.44	21906983
769	2-Hydroxyisobutyrylation	EAREKAAKEFGVSPD HHHHHHHHHHCCCCC	59.44	-
774	Phosphorylation	AAKEFGVSPDKISLQ HHHHHCCCCCCCCCC	27.97	21815630
866	Phosphorylation	HGRKMSKSLGNVIDP CCCCCHHHHCCCCCH	33.91	27251275
878	Phosphorylation	IDPLDVIYGISLQGL CCHHHHHHHEEHHHH	14.30	22817900
881	Phosphorylation	LDVIYGISLQGLHNQ HHHHHHEEHHHHHHH	15.41	-
907	Ubiquitination	EKAKEGQKADFPAGI HHHHCCCCCCCCCCC	61.86	-
929	Phosphorylation	LRFGLCAYMSQGRDI HHHHHHHHHHCCCCC	9.05	-
952	Acetylation	GYRHFCNKLWNATKF CHHHHHHHHHHHHHH	56.94	25953088
952	Ubiquitination	GYRHFCNKLWNATKF CHHHHHHHHHHHHHH	56.94	21906983
958	Ubiquitination	NKLWNATKFALRGLG HHHHHHHHHHHCCCC	26.65	-
958	Malonylation	NKLWNATKFALRGLG HHHHHHHHHHHCCCC	26.65	26320211
958	Acetylation	NKLWNATKFALRGLG HHHHHHHHHHHCCCC	26.65	23236377
966	Ubiquitination	FALRGLGKGFVPSPT HHHCCCCCCCCCCCC	54.97	-
966	Malonylation	FALRGLGKGFVPSPT HHHCCCCCCCCCCCC	54.97	26320211
966	Acetylation	FALRGLGKGFVPSPT HHHCCCCCCCCCCCC	54.97	26051181
971	Phosphorylation	LGKGFVPSPTSQPGG CCCCCCCCCCCCCCC	35.19	-
1061	Phosphorylation	DVGLRLLSPFMPFVT HHHHHHHCCCCHHCC	22.23	-
1064	Sulfoxidation	LRLLSPFMPFVTEEL HHHHCCCCHHCCHHH	2.60	28183972
1120	Phosphorylation	SITRAVRSLRADYNL HHHHHHHHHHHCCCC	18.66	-
1125	Phosphorylation	VRSLRADYNLTRIRP HHHHHHCCCCCEECC	15.87	-
1128	Phosphorylation	LRADYNLTRIRPDCF HHHCCCCCEECCCCH	22.03	-
1225	Phosphorylation	LRERRAASGYPVKVP HHHHHHHCCCCCEEE	37.56	28152594
1227	Phosphorylation	ERRAASGYPVKVPLE HHHHHCCCCCEEEEE	11.45	28152594
1230	Ubiquitination	AASGYPVKVPLEVQE HHCCCCCEEEEEECC	33.36	21906983
1230	Acetylation	AASGYPVKVPLEVQE HHCCCCCEEEEEECC	33.36	23236377
1242	Ubiquitination	VQEADEAKLQQTEAE ECCHHHHHHHHHHHH	44.79	21906983
1242	2-Hydroxyisobutyrylation	VQEADEAKLQQTEAE ECCHHHHHHHHHHHH	44.79	-
1242	Acetylation	VQEADEAKLQQTEAE ECCHHHHHHHHHHHH	44.79	26051181
1252	Ubiquitination	QTEAELRKVDEAIAL HHHHHHHHHHHHHHH	67.66	-
1262	Ubiquitination	EAIALFQKML----- HHHHHHHHHC-----	34.53	21906983

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 SYVC_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EF1A1_HUMAN	EEF1A1	physical	3169261
EF1G_HUMAN	EEF1G	physical	3169261
EF1D_HUMAN	EEF1D	physical	3169261
EF1B_HUMAN	EEF1B2	physical	3169261
AIMP1_HUMAN	AIMP1	physical	22863883
TCPG_HUMAN	CCT3	physical	22863883
EF1D_HUMAN	EEF1D	physical	22863883
KNTC1_HUMAN	KNTC1	physical	22863883
CACO2_HUMAN	CALCOCO2	physical	25416956
EF1G_HUMAN	EEF1G	physical	26344197
FA98B_HUMAN	FAM98B	physical	26344197
PRPK_HUMAN	TP53RK	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
DB00161	L-Valine

Regulatory Network of SYVC_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-420; LYS-423 AND LYS-645,AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-300, AND MASSSPECTROMETRY.	18083107 [Abstract]