SYDM_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SYDM_HUMAN
• UniProt AC: Q6PI48
• Protein Name: Aspartate--tRNA ligase, mitochondrial
• Gene Name: DARS2
• Organism: Homo sapiens (Human).
• Sequence Length: 645
• Subcellular Localization: Mitochondrion matrix .
• Protein Sequence: MYFPSWLSQLYRGLSRPIRRTTQPIWGSLYRSLLQSSQRRIPEFSSFVVRTNTCGELRSSHLGQEVTLCGWIQYRRQNTFLVLRDFDGLVQVIIPQDESAASVKKILCEAPVESVVQVSGTVISRPAGQENPKMPTGEIEIKVKTAELLNACKKLPFEIKNFVKKTEALRLQYRYLDLRSFQMQYNLRLRSQMVMKMREYLCNLHGFVDIETPTLFKRTPGGAKEFLVPSREPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFTQIDIEMSFVDQTGIQSLIEGLLQYSWPNDKDPVVVPFPTMTFAEVLATYGTDKPDTRFGMKIIDISDVFRNTEIGFLQDALSKPHGTVKAICIPEGAKYLKRKDIESIRNFAADHFNQEILPVFLNANRNWNSPVANFIMESQRLELIRLMETQEEDVVLLTAGEHNKACSLLGKLRLECADLLETRGVVLRDPTLFSFLWVVDFPLFLPKEENPRELESAHHPFTAPHPSDIHLLYTEPKKARSQHYDLVLNGNEIGGGSIRIHNAELQRYILATLLKEDVKMLSHLLQALDYGAPPHGGIALGLDRLICLVTGSPSIRDVIAFPKSFRGHDLMSNTPDSVPPEELKPYHIRVSKPTDSKAERAH

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MYFPSWLSQ ------CCCHHHHHH	24.97	24043423
5	Phosphorylation	---MYFPSWLSQLYR ---CCCHHHHHHHHH	30.65	24043423
8	Phosphorylation	MYFPSWLSQLYRGLS CCCHHHHHHHHHHCC	16.33	24043423
11	Phosphorylation	PSWLSQLYRGLSRPI HHHHHHHHHHCCCCC	8.59	24043423
15	Phosphorylation	SQLYRGLSRPIRRTT HHHHHHCCCCCHHHC	38.54	24043423
45	Phosphorylation	QRRIPEFSSFVVRTN HCCCCCCCCEEEECC	22.62	22210691
104	Ubiquitination	DESAASVKKILCEAP CCCCCHHHHHHHCCC	31.44	-
108	Glutathionylation	ASVKKILCEAPVESV CHHHHHHHCCCCCCE	4.83	22555962
142	Acetylation	PTGEIEIKVKTAELL CCCEEEEEEEHHHHH	25.53	20167786
152	Glutathionylation	TAELLNACKKLPFEI HHHHHHHHHCCCCCH	3.77	22555962
153	Acetylation	AELLNACKKLPFEIK HHHHHHHHCCCCCHH	55.74	30587985
153	Ubiquitination	AELLNACKKLPFEIK HHHHHHHHCCCCCHH	55.74	-
154	Malonylation	ELLNACKKLPFEIKN HHHHHHHCCCCCHHH	62.37	26320211
154	Acetylation	ELLNACKKLPFEIKN HHHHHHHCCCCCHHH	62.37	7672383
160	Ubiquitination	KKLPFEIKNFVKKTE HCCCCCHHHHHHHHH	36.82	-
212	Phosphorylation	HGFVDIETPTLFKRT HCCCCCCCCCCEECC	23.16	24719451
219	Phosphorylation	TPTLFKRTPGGAKEF CCCCEECCCCCCCCC	27.20	-
224	Ubiquitination	KRTPGGAKEFLVPSR ECCCCCCCCCEECCC	52.88	21890473
235	Ubiquitination	VPSREPGKFYSLPQS ECCCCCCCCCCCCCC	52.42	21890473
235	Acetylation	VPSREPGKFYSLPQS ECCCCCCCCCCCCCC	52.42	19608861
237	Phosphorylation	SREPGKFYSLPQSPQ CCCCCCCCCCCCCHH	16.88	29396449
238	Phosphorylation	REPGKFYSLPQSPQQ CCCCCCCCCCCCHHH	36.38	30108239
242	Phosphorylation	KFYSLPQSPQQFKQL CCCCCCCCHHHHHHH	23.80	25159151
340	Ubiquitination	PDTRFGMKIIDISDV CCCCCEEEEEEHHHH	36.57	-
362	Ubiquitination	FLQDALSKPHGTVKA HHHHHHHCCCCCEEE	41.71	-
368	Ubiquitination	SKPHGTVKAICIPEG HCCCCCEEEEECCCH	31.69	-
371	Glutathionylation	HGTVKAICIPEGAKY CCCEEEEECCCHHHH	5.19	22555962
377	Acetylation	ICIPEGAKYLKRKDI EECCCHHHHCCCCCH	63.07	25825284
382	Succinylation	GAKYLKRKDIESIRN HHHHCCCCCHHHHHH	62.56	27452117
382	Acetylation	GAKYLKRKDIESIRN HHHHCCCCCHHHHHH	62.56	19608861
421	Phosphorylation	VANFIMESQRLELIR HHHHHHHHHHHHHHH	11.83	26552605
432	Phosphorylation	ELIRLMETQEEDVVL HHHHHHHCCCCCEEE	27.58	26552605
441	Phosphorylation	EEDVVLLTAGEHNKA CCCEEEEEECCHHHH	28.58	26552605
454	Acetylation	KACSLLGKLRLECAD HHHHHHHHHHHHHHH	30.33	25953088
454	Ubiquitination	KACSLLGKLRLECAD HHHHHHHHHHHHHHH	30.33	-
454	2-Hydroxyisobutyrylation	KACSLLGKLRLECAD HHHHHHHHHHHHHHH	30.33	-
459	Glutathionylation	LGKLRLECADLLETR HHHHHHHHHHHHHHC	4.17	22555962
520	Acetylation	HLLYTEPKKARSQHY EEEECCCCCHHHCCC	53.48	30587991
524	Phosphorylation	TEPKKARSQHYDLVL CCCCCHHHCCCEEEE	26.60	25278378
527	Phosphorylation	KKARSQHYDLVLNGN CCHHHCCCEEEECCC	11.88	25278378
540	Phosphorylation	GNEIGGGSIRIHNAE CCEECCCCEEECHHH	16.39	25278378
551	Phosphorylation	HNAELQRYILATLLK CHHHHHHHHHHHHHH	6.32	20068231
555	Phosphorylation	LQRYILATLLKEDVK HHHHHHHHHHHHHHH	29.22	25278378
573	Phosphorylation	HLLQALDYGAPPHGG HHHHHHHHCCCCCCC	18.94	-
606	Ubiquitination	RDVIAFPKSFRGHDL HHHHCCCHHHCCCCC	56.63	21890473
627	Acetylation	SVPPEELKPYHIRVS CCCHHHCCCCEEEEC	46.97	19608861
635	Acetylation	PYHIRVSKPTDSKAE CCEEEECCCCCCHHH	49.43	26210075
635	Succinylation	PYHIRVSKPTDSKAE CCEEEECCCCCCHHH	49.43	27452117

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

Oops, there are no upstream regulatory protein records of SYDM_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SYDM_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of SYDM_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SYK_HUMAN	KARS	physical	9878398
EPHA8_HUMAN	EPHA8	physical	21988832
DPYL5_HUMAN	DPYSL5	physical	21988832
FNTA_HUMAN	FNTA	physical	26344197
NCPR_HUMAN	POR	physical	26344197
RFA2_HUMAN	RPA2	physical	26344197
G3PT_HUMAN	GAPDHS	physical	28514442
BBS1_HUMAN	BBS1	physical	27173435

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 611105: Leukoencephalopathy with brainstem and spinal cord involvement and lactate elevation (LBSL)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• DB00128: L-Aspartic Acid

Related Literatures of Post-Translational Modification

Acetylation

"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-235; LYS-382 AND LYS-627,AND MASS SPECTROMETRY.
PubMed: 19608861