dbPTM

SYDC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SYDC_HUMAN
UniProt AC	P14868
Protein Name	Aspartate--tRNA ligase, cytoplasmic
Gene Name	DARS
Organism	Homo sapiens (Human).
Sequence Length	501
Subcellular Localization	Cytoplasm, cytosol .
Protein Description	Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA..
Protein Sequence	MPSASASRKSQEKPREIMDAAEDYAKERYGISSMIQSQEKPDRVLVRVRDLTIQKADEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQMVKFAANINKESIVDVEGVVRKVNQKIGSCTQQDVELHVQKIYVISLAEPRLPLQLDDAVRPEAEGEEEGRATVNQDTRLDNRVIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQLYKQMCICADFEKVFSIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYHEVMEEIADTMVQIFKGLQERFQTEIQTVNKQFPCEPFKFLEPTLRLEYCEALAMLREAGVEMGDEDDLSTPNEKLLGHLVKEKYDTDFYILDKYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MPSASASRKS -----CCCHHCCCCC	33.29	29759185
5	Phosphorylation	---MPSASASRKSQE ---CCCHHCCCCCCC	30.99	23312004
7	Phosphorylation	-MPSASASRKSQEKP -CCCHHCCCCCCCCC	37.43	25106551
10	Phosphorylation	SASASRKSQEKPREI CHHCCCCCCCCCHHH	42.32	28450419
13	Ubiquitination	ASRKSQEKPREIMDA CCCCCCCCCHHHHHH	41.56	-
18	Sulfoxidation	QEKPREIMDAAEDYA CCCCHHHHHHHHHHH	2.16	21406390
24	Phosphorylation	IMDAAEDYAKERYGI HHHHHHHHHHHHHCH	15.86	20071362
26	Acetylation	DAAEDYAKERYGISS HHHHHHHHHHHCHHH	36.17	23236377
26	Malonylation	DAAEDYAKERYGISS HHHHHHHHHHHCHHH	36.17	26320211
26	Ubiquitination	DAAEDYAKERYGISS HHHHHHHHHHHCHHH	36.17	-
29	Phosphorylation	EDYAKERYGISSMIQ HHHHHHHHCHHHHHC	21.65	29449344
32	Phosphorylation	AKERYGISSMIQSQE HHHHHCHHHHHCCCC	14.97	28857561
33	Phosphorylation	KERYGISSMIQSQEK HHHHCHHHHHCCCCC	20.27	28857561
34	Sulfoxidation	ERYGISSMIQSQEKP HHHCHHHHHCCCCCC	2.29	30846556
37	Phosphorylation	GISSMIQSQEKPDRV CHHHHHCCCCCCCCE	29.40	29449344
40	Acetylation	SMIQSQEKPDRVLVR HHHCCCCCCCCEEEE	44.58	23236377
40	Ubiquitination	SMIQSQEKPDRVLVR HHHCCCCCCCCEEEE	44.58	-
43	Methylation	QSQEKPDRVLVRVRD CCCCCCCCEEEEEEE	32.00	-
52	Phosphorylation	LVRVRDLTIQKADEV EEEEEECEECCCCEE	26.17	30266825
55	Acetylation	VRDLTIQKADEVVWV EEECEECCCCEEEEE	54.69	57530815
63	Methylation	ADEVVWVRARVHTSR CCEEEEEEEEEECHH	10.85	-
74	Malonylation	HTSRAKGKQCFLVLR ECHHCCCCEEEEEEE	43.09	26320211
74	Ubiquitination	HTSRAKGKQCFLVLR ECHHCCCCEEEEEEE	43.09	19608861
74	Acetylation	HTSRAKGKQCFLVLR ECHHCCCCEEEEEEE	43.09	19608861
99	Acetylation	AVGDHASKQMVKFAA EECCHHHHHHHHHHH	43.10	25953088
99	Ubiquitination	AVGDHASKQMVKFAA EECCHHHHHHHHHHH	43.10	21890473
99	Ubiquitination	AVGDHASKQMVKFAA EECCHHHHHHHHHHH	43.10	21890473
103	Ubiquitination	HASKQMVKFAANINK HHHHHHHHHHHCCCH	24.76	21890473
103	Acetylation	HASKQMVKFAANINK HHHHHHHHHHHCCCH	24.76	23954790
103	Malonylation	HASKQMVKFAANINK HHHHHHHHHHHCCCH	24.76	26320211
103	Ubiquitination	HASKQMVKFAANINK HHHHHHHHHHHCCCH	24.76	21890473
110	Acetylation	KFAANINKESIVDVE HHHHCCCHHHCCCHH	49.38	19816139
110	Ubiquitination	KFAANINKESIVDVE HHHHCCCHHHCCCHH	49.38	-
112	Phosphorylation	AANINKESIVDVEGV HHCCCHHHCCCHHHH	29.53	21406692
126	2-Hydroxyisobutyrylation	VVRKVNQKIGSCTQQ HHHHHHHHHCCCCHH	43.78	-
126	Acetylation	VVRKVNQKIGSCTQQ HHHHHHHHHCCCCHH	43.78	25953088
126	Ubiquitination	VVRKVNQKIGSCTQQ HHHHHHHHHCCCCHH	43.78	-
130	Glutathionylation	VNQKIGSCTQQDVEL HHHHHCCCCHHHHHH	3.16	22555962
143	Phosphorylation	ELHVQKIYVISLAEP HHEEEEEEEEECCCC	9.96	28152594
146	Phosphorylation	VQKIYVISLAEPRLP EEEEEEEECCCCCCC	16.10	20068231
188	Methylation	DNRVIDLRTSTSQAV CCEEEEECCCCHHHH	23.92	-
200	Phosphorylation	QAVFRLQSGICHLFR HHHHHHHHHHHHHHH	34.42	21210654
213	2-Hydroxyisobutyrylation	FRETLINKGFVEIQT HHHHHHHCCCEEECC	46.89	-
213	Acetylation	FRETLINKGFVEIQT HHHHHHHCCCEEECC	46.89	57530807
220	Phosphorylation	KGFVEIQTPKIISAA CCCEEECCCCEEEEC	32.01	24702127
225	Phosphorylation	IQTPKIISAASEGGA ECCCCEEEECCCCCC	22.66	20068231
228	Phosphorylation	PKIISAASEGGANVF CCEEEECCCCCCCEE	36.17	21406692
236	Phosphorylation	EGGANVFTVSYFKNN CCCCCEEEEEEECCC	12.31	28152594
238	Phosphorylation	GANVFTVSYFKNNAY CCCEEEEEEECCCEE	23.07	28152594
239	Phosphorylation	ANVFTVSYFKNNAYL CCEEEEEEECCCEEE	17.78	28152594
241	Acetylation	VFTVSYFKNNAYLAQ EEEEEEECCCEEECC	40.85	57530811
241	Ubiquitination	VFTVSYFKNNAYLAQ EEEEEEECCCEEECC	40.85	-
245	Phosphorylation	SYFKNNAYLAQSPQL EEECCCEEECCCHHH	12.51	28152594
249	Phosphorylation	NNAYLAQSPQLYKQM CCEEECCCHHHHHHH	14.70	19664994
253	Phosphorylation	LAQSPQLYKQMCICA ECCCHHHHHHHHHHC	8.23	23403867
254	Acetylation	AQSPQLYKQMCICAD CCCHHHHHHHHHHCC	39.90	26051181
274	Acetylation	SIGPVFRAEDSNTHR EECCEEECCCCCCCC	17.30	19608861
274	Ubiquitination	SIGPVFRAEDSNTHR EECCEEECCCCCCCC	17.30	19608861
323	Phosphorylation	GLQERFQTEIQTVNK HHHHHHHHHHHHHHH	32.13	20068231
327	Phosphorylation	RFQTEIQTVNKQFPC HHHHHHHHHHHCCCC	31.54	20068231
330	Ubiquitination	TEIQTVNKQFPCEPF HHHHHHHHCCCCCCC	49.32	21890473
330	Acetylation	TEIQTVNKQFPCEPF HHHHHHHHCCCCCCC	49.32	25953088
330	Ubiquitination	TEIQTVNKQFPCEPF HHHHHHHHCCCCCCC	49.32	21890473
338	Ubiquitination	QFPCEPFKFLEPTLR CCCCCCCCCCCCCHH	60.81	-
343	Phosphorylation	PFKFLEPTLRLEYCE CCCCCCCCHHHHHHH	18.35	21712546
362	Sulfoxidation	LREAGVEMGDEDDLS HHHHCCCCCCCCCCC	8.34	28183972
369	Phosphorylation	MGDEDDLSTPNEKLL CCCCCCCCCCCHHHH	49.14	-
370	Phosphorylation	GDEDDLSTPNEKLLG CCCCCCCCCCHHHHH	37.11	28985074
374	Acetylation	DLSTPNEKLLGHLVK CCCCCCHHHHHHHHH	56.50	19608861
374	Ubiquitination	DLSTPNEKLLGHLVK CCCCCCHHHHHHHHH	56.50	21906983
381	Ubiquitination	KLLGHLVKEKYDTDF HHHHHHHHHHCCCCE	55.65	-
383	Ubiquitination	LGHLVKEKYDTDFYI HHHHHHHHCCCCEEE	42.58	-
383	2-Hydroxyisobutyrylation	LGHLVKEKYDTDFYI HHHHHHHHCCCCEEE	42.58	-
383	Acetylation	LGHLVKEKYDTDFYI HHHHHHHHCCCCEEE	42.58	27452117
384	Phosphorylation	GHLVKEKYDTDFYIL HHHHHHHCCCCEEEE	25.76	25884760
386	Phosphorylation	LVKEKYDTDFYILDK HHHHHCCCCEEEEEC	25.56	-
389	Phosphorylation	EKYDTDFYILDKYPL HHCCCCEEEEECCCC	11.91	25884760
393	Ubiquitination	TDFYILDKYPLAVRP CCEEEEECCCCEEEC	45.37	-
394	Phosphorylation	DFYILDKYPLAVRPF CEEEEECCCCEEECC	11.80	24719451
402	Phosphorylation	PLAVRPFYTMPDPRN CCEEECCCCCCCCCC	12.57	25884760
403	Phosphorylation	LAVRPFYTMPDPRNP CEEECCCCCCCCCCC	23.70	24719451
411	Acetylation	MPDPRNPKQSNSYDM CCCCCCCCCCCCCCC	70.66	25953088
411	Ubiquitination	MPDPRNPKQSNSYDM CCCCCCCCCCCCCCC	70.66	-
413	Phosphorylation	DPRNPKQSNSYDMFM CCCCCCCCCCCCCHH	33.59	21406692
415	Phosphorylation	RNPKQSNSYDMFMRG CCCCCCCCCCCHHCH	27.97	21406692
416	Phosphorylation	NPKQSNSYDMFMRGE CCCCCCCCCCHHCHH	18.71	21406692
427	Phosphorylation	MRGEEILSGAQRIHD HCHHHHHHHHCCCCC	37.43	21406692
451	Acetylation	HHGIDLEKIKAYIDS HCCCCHHHHHHHHHH	57.72	23954790
451	2-Hydroxyisobutyrylation	HHGIDLEKIKAYIDS HCCCCHHHHHHHHHH	57.72	-
451	Ubiquitination	HHGIDLEKIKAYIDS HCCCCHHHHHHHHHH	57.72	-
453	2-Hydroxyisobutyrylation	GIDLEKIKAYIDSFR CCCHHHHHHHHHHHC	46.32	-
453	Acetylation	GIDLEKIKAYIDSFR CCCHHHHHHHHHHHC	46.32	57530803
453	Ubiquitination	GIDLEKIKAYIDSFR CCCHHHHHHHHHHHC	46.32	-
478	Sulfoxidation	IGLERVTMLFLGLHN CCHHHHHHHHHCCCC	1.97	28183972
490	Phosphorylation	LHNVRQTSMFPRDPK CCCCCCCCCCCCCCC	15.30	28857561
500	Phosphorylation	PRDPKRLTP------ CCCCCCCCC------	30.87	24719451

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
500	T	Phosphorylation	Kinase	PKA	-	Uniprot

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AIMP2_HUMAN	AIMP2	physical	16189514
EF1A1_HUMAN	EEF1A1	physical	7806521
SYIC_HUMAN	IARS	physical	22939629
SYMC_HUMAN	MARS	physical	22939629
SYEP_HUMAN	EPRS	physical	22939629
SYRC_HUMAN	RARS	physical	22939629
SYQ_HUMAN	QARS	physical	22939629
SYLC_HUMAN	LARS	physical	22939629
SYK_HUMAN	KARS	physical	22939629
GARS_HUMAN	GARS	physical	22939629
VATB2_HUMAN	ATP6V1B2	physical	22939629
XPO2_HUMAN	CSE1L	physical	22939629
TRM1_HUMAN	TRMT1	physical	22939629
TLN1_HUMAN	TLN1	physical	22939629
XPP1_HUMAN	XPNPEP1	physical	22939629
VATA_HUMAN	ATP6V1A	physical	22939629
AIMP1_HUMAN	AIMP1	physical	22863883
AIMP2_HUMAN	AIMP2	physical	22863883
SYIC_HUMAN	IARS	physical	22863883
SYMC_HUMAN	MARS	physical	22863883
PSA5_HUMAN	PSMA5	physical	22863883
SYQ_HUMAN	QARS	physical	22863883
RL23A_HUMAN	RPL23A	physical	22863883
RL26_HUMAN	RPL26	physical	22863883
RL36_HUMAN	RPL36	physical	22863883
AIMP2_HUMAN	AIMP2	physical	25416956
AIMP1_HUMAN	AIMP1	physical	26344197
AIMP2_HUMAN	AIMP2	physical	26344197
PYR1_HUMAN	CAD	physical	26344197
CALX_HUMAN	CANX	physical	26344197
MCA3_HUMAN	EEF1E1	physical	26344197
SYEP_HUMAN	EPRS	physical	26344197
GFPT1_HUMAN	GFPT1	physical	26344197
SYIC_HUMAN	IARS	physical	26344197
SYLC_HUMAN	LARS	physical	26344197
SYMC_HUMAN	MARS	physical	26344197
OTU6A_HUMAN	OTUD6A	physical	26344197
SYQ_HUMAN	QARS	physical	26344197
RFA2_HUMAN	RPA2	physical	26344197
TIAM1_HUMAN	TIAM1	physical	26344197
ZN598_HUMAN	ZNF598	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615281	Hypomyelination with brainstem and spinal cord involvement and leg spasticity (HBSL)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00128	L-Aspartic Acid

Regulatory Network of SYDC_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-74 AND LYS-374, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, AND MASSSPECTROMETRY.	19413330 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND MASSSPECTROMETRY.	18187866 [Abstract]