ATD3C_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ATD3C_HUMAN
• UniProt AC: Q5T2N8
• Protein Name: ATPase family AAA domain-containing protein 3C
• Gene Name: ATAD3C
• Organism: Homo sapiens (Human).
• Sequence Length: 411
• Protein Sequence: MSKDALNLAQMQEQTLQLEQQSKLKQLVNEDLRKQEESVQKHHQTFLESIRAAGTLFGEGFRAFVTDRDKVTATVAGLTLLAVGVYSAKNATAVTGRYIEARLGKPSLVRETSRITVLEALRHPIQQVSRRLLSRPQDVLEGVVLSPSLEARVRDIAIMTRNIKKNRGLYRHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAMHKLFDWANTSRRGLLLFVDEADAFLRKRATEKISEDLRATLNAFLYRTGQHSNKFMLILASCHPEQFDWAINACIDVMVHFDLPGQEERARLVRMYLNEYVLKPATEGKRRLKLAQFDYGRKCLEIARLTEGMSCRKIAQLAVSWQATAYASKDGVLTEAMMDACVQDFVQQHQQMMRWLKGERPGPEDEQPSS

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	------MSKDALNLA ------CCHHHHHHH	38.96	24043423
11	Sulfoxidation	DALNLAQMQEQTLQL HHHHHHHHHHHHHHH	3.83	21406390
15	Phosphorylation	LAQMQEQTLQLEQQS HHHHHHHHHHHHHHH	18.73	21406692
22	Phosphorylation	TLQLEQQSKLKQLVN HHHHHHHHHHHHHHH	39.38	21406692
23	Ubiquitination	LQLEQQSKLKQLVNE HHHHHHHHHHHHHHH	56.20	32015554
87	Phosphorylation	LLAVGVYSAKNATAV HEHEEEECCCCCCHH	30.29	-
105	Malonylation	YIEARLGKPSLVRET HHHHHCCCCHHHCCH	35.70	26320211
107	Phosphorylation	EARLGKPSLVRETSR HHHCCCCHHHCCHHH	42.87	21406692
112	Phosphorylation	KPSLVRETSRITVLE CCHHHCCHHHHHHHH	16.85	-
113	Phosphorylation	PSLVRETSRITVLEA CHHHCCHHHHHHHHH	19.55	-
116	Phosphorylation	VRETSRITVLEALRH HCCHHHHHHHHHHHC	20.23	20860994
146	Phosphorylation	VLEGVVLSPSLEARV HHCCCCCCCCHHHHH	10.79	27050516
148	Phosphorylation	EGVVLSPSLEARVRD CCCCCCCCHHHHHHH	35.15	27050516
170	Phosphorylation	IKKNRGLYRHILLYG HHHCCCCCCEEEEEC	11.72	27811184
176	Phosphorylation	LYRHILLYGPPGTGK CCCEEEEECCCCCCH	24.92	27811184
181	Phosphorylation	LLYGPPGTGKTLFAK EEECCCCCCHHHHHH	41.08	27811184
183	Ubiquitination	YGPPGTGKTLFAKKL ECCCCCCHHHHHHHH	41.72	22817900
188	Ubiquitination	TGKTLFAKKLALHSG CCHHHHHHHHHHCCC	40.77	22817900
189	Malonylation	GKTLFAKKLALHSGM CHHHHHHHHHHCCCC	35.25	26320211
198	Phosphorylation	ALHSGMDYAIMTGGD HHCCCCCEEEECCCC	6.80	-
202	Phosphorylation	GMDYAIMTGGDVAPM CCCEEEECCCCCCCC	31.72	23401153
215	Phosphorylation	PMGREGVTAMHKLFD CCCCCCCHHHHHHHH	29.17	23401153
219	Ubiquitination	EGVTAMHKLFDWANT CCCHHHHHHHHHHCC	37.45	21890473
219	Acetylation	EGVTAMHKLFDWANT CCCHHHHHHHHHHCC	37.45	25953088
227	Phosphorylation	LFDWANTSRRGLLLF HHHHHCCCCCCEEEE	21.56	29116813
249	Acetylation	LRKRATEKISEDLRA HHHHHHHHHCHHHHH	47.37	25953088
249	Ubiquitination	LRKRATEKISEDLRA HHHHHHHHHCHHHHH	47.37	24816145
249	Malonylation	LRKRATEKISEDLRA HHHHHHHHHCHHHHH	47.37	26320211
251	Phosphorylation	KRATEKISEDLRATL HHHHHHHCHHHHHHH	35.80	23186163
320	Malonylation	YLNEYVLKPATEGKR HHHHHCCCCCCCCCH	23.67	26320211
320	Acetylation	YLNEYVLKPATEGKR HHHHHCCCCCCCCCH	23.67	19608861
320	Succinylation	YLNEYVLKPATEGKR HHHHHCCCCCCCCCH	23.67	27452117
330	Acetylation	TEGKRRLKLAQFDYG CCCCHHHEEECCHHH	39.71	25953088
330	Ubiquitination	TEGKRRLKLAQFDYG CCCCHHHEEECCHHH	39.71	24816145

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

Oops, there are no upstream regulatory protein records of ATD3C_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ATD3C_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 ATD3C_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of ATD3C_HUMAN !!

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
• There are no disease associations of PTM sites.

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-320, AND MASS SPECTROMETRY.
PubMed: 19608861