ATG3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ATG3_HUMAN
• UniProt AC: Q9NT62
• Protein Name: Ubiquitin-like-conjugating enzyme ATG3
• Gene Name: ATG3
• Organism: Homo sapiens (Human).
• Sequence Length: 314
• Subcellular Localization: Cytoplasm .
• Protein Description: E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A). The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8-like proteins from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8-like proteins. The formation of the ATG8-phosphatidylethanolamine conjugates is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). Preferred substrate is MAP1LC3A. Also acts as an autocatalytic E2-like enzyme, catalyzing the conjugation of ATG12 to itself, ATG12 conjugation to ATG3 playing a role in mitochondrial homeostasis but not in autophagy. ATG7 (E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with ATG3. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway..
• Protein Sequence: MQNVINTVKGKALEVAEYLTPVLKESKFKETGVITPEEFVAAGDHLVHHCPTWQWATGEELKVKAYLPTGKQFLVTKNVPCYKRCKQMEYSDELEAIIEEDDGDGGWVDTYHNTGITGITEAVKEITLENKDNIRLQDCSALCEEEEDEDEGEAADMEEYEESGLLETDEATLDTRKIVEACKAKTDAGGEDAILQTRTYDLYITYDKYYQTPRLWLFGYDEQRQPLTVEHMYEDISQDHVKKTVTIENHPHLPPPPMCSVHPCRHAEVMKKIIETVAEGGGELGVHMYLLIFLKFVQAVIPTIEYDYTRHFTM

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
1	Acetylation	-------MQNVINTV -------CCCHHHHH	6.20	22223895
7	Phosphorylation	-MQNVINTVKGKALE -CCCHHHHHHHHHHH	16.69	28857561
9	Acetylation	QNVINTVKGKALEVA CCHHHHHHHHHHHHH	53.29	25953088
9	Ubiquitination	QNVINTVKGKALEVA CCHHHHHHHHHHHHH	53.29	-
11	Ubiquitination	VINTVKGKALEVAEY HHHHHHHHHHHHHHH	44.04	32015554
18	Phosphorylation	KALEVAEYLTPVLKE HHHHHHHHHHHHHCH	13.21	21945579
20	Phosphorylation	LEVAEYLTPVLKESK HHHHHHHHHHHCHHH	15.50	21945579
24	Ubiquitination	EYLTPVLKESKFKET HHHHHHHCHHHCCCC	61.24	32015554
26	Phosphorylation	LTPVLKESKFKETGV HHHHHCHHHCCCCCC	41.63	29083192
44	Ubiquitination	EEFVAAGDHLVHHCP HHHHCCCCCHHHCCC	27.50	22053931
66	Phosphorylation	EELKVKAYLPTGKQF CCEEEEEECCCCCEE	13.90	28152594
69	Phosphorylation	KVKAYLPTGKQFLVT EEEEECCCCCEEEEE	55.18	28152594
71	Ubiquitination	KAYLPTGKQFLVTKN EEECCCCCEEEEECC	40.11	29967540
76	Phosphorylation	TGKQFLVTKNVPCYK CCCEEEEECCCCHHH	21.03	30576142
77	Acetylation	GKQFLVTKNVPCYKR CCEEEEECCCCHHHH	48.76	26051181
96	Ubiquitination	EYSDELEAIIEEDDG CCCHHHHHHEEECCC	22.23	22817900
98	Ubiquitination	SDELEAIIEEDDGDG CHHHHHHEEECCCCC	6.46	22817900
111	Phosphorylation	DGGWVDTYHNTGITG CCCEEEECCCCCCCC	6.65	22817900
117	Phosphorylation	TYHNTGITGITEAVK ECCCCCCCCHHHHHH	24.71	-
127	Phosphorylation	TEAVKEITLENKDNI HHHHHHHCCCCCCCE	29.16	21815630
131 (in isoform 1)	Ubiquitination	-	42.66	22053931
131	Ubiquitination	KEITLENKDNIRLQD HHHCCCCCCCEEEEH	42.66	22053931
131	2-Hydroxyisobutyrylation	KEITLENKDNIRLQD HHHCCCCCCCEEEEH	42.66	-
177	Ubiquitination	EATLDTRKIVEACKA HHHCCHHHHHHHHHH	53.87	29967540
183	Ubiquitination	RKIVEACKAKTDAGG HHHHHHHHHCCCCCC	61.02	22817900
185 (in isoform 2)	Ubiquitination	-	32.22	21906983
185 (in isoform 1)	Ubiquitination	-	32.22	22053931
185	Ubiquitination	IVEACKAKTDAGGED HHHHHHHCCCCCCCC	32.22	22817900
186	Phosphorylation	VEACKAKTDAGGEDA HHHHHHCCCCCCCCC	35.62	26503514
205	Phosphorylation	RTYDLYITYDKYYQT CEEEEEEEECCCCCC	16.47	28152594
206	Phosphorylation	TYDLYITYDKYYQTP EEEEEEEECCCCCCC	10.81	28152594
208	Ubiquitination	DLYITYDKYYQTPRL EEEEEECCCCCCCEE	35.13	-
209	Phosphorylation	LYITYDKYYQTPRLW EEEEECCCCCCCEEE	9.63	28152594
210	Phosphorylation	YITYDKYYQTPRLWL EEEECCCCCCCEEEE	16.20	28152594
212	Phosphorylation	TYDKYYQTPRLWLFG EECCCCCCCEEEEEE	8.34	28152594
233	Phosphorylation	PLTVEHMYEDISQDH CCCHHHHCHHCCHHH	16.62	28796482
243	Ubiquitination	ISQDHVKKTVTIENH CCHHHCCCEEEECCC	47.33	29967540
271	2-Hydroxyisobutyrylation	CRHAEVMKKIIETVA CCCHHHHHHHHHHHH	46.10	-
303	Phosphorylation	FVQAVIPTIEYDYTR HHHHHCCCCCCCCCC	18.47	21406692
306	Phosphorylation	AVIPTIEYDYTRHFT HHCCCCCCCCCCCCC	15.48	21406692
308	Phosphorylation	IPTIEYDYTRHFTM- CCCCCCCCCCCCCC-	12.55	21406692
309	Phosphorylation	PTIEYDYTRHFTM-- CCCCCCCCCCCCC--	18.12	21406692
310	Methylation	TIEYDYTRHFTM--- CCCCCCCCCCCC---	19.38	-
313	Phosphorylation	YDYTRHFTM------ CCCCCCCCC------	18.82	-

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

Oops, there are no upstream regulatory protein records of ATG3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ATG3_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 ATG3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ATG7_HUMAN	ATG7	physical	11825910
ATG12_HUMAN	ATG12	physical	11825910
A16L1_HUMAN	ATG16L1	physical	20562859
ATG7_HUMAN	ATG7	physical	20562859
ATG12_HUMAN	ATG12	physical	20562859
TCPR1_HUMAN	TECPR1	physical	20562859
ATG5_HUMAN	ATG5	physical	20562859
KRT85_HUMAN	KRT85	physical	20562859
GBRL2_HUMAN	GABARAPL2	physical	20562859
GBRAP_HUMAN	GABARAP	physical	20562859
MAP1B_HUMAN	MAP1B	physical	20562859
ATG4B_HUMAN	ATG4B	physical	20562859
OBSL1_HUMAN	OBSL1	physical	20562859
CFLAR_HUMAN	CFLAR	physical	19838173
MLP3A_HUMAN	MAP1LC3A	physical	19838173
GBRL1_HUMAN	GABARAPL1	physical	16704426
BAG3_HUMAN	BAG3	physical	23824909
ASSY_HUMAN	ASS1	physical	22863883
DFFA_HUMAN	DFFA	physical	22863883
GRP75_HUMAN	HSPA9	physical	22863883
SIAS_HUMAN	NANS	physical	22863883
NHLC2_HUMAN	NHLRC2	physical	22863883
RL23_HUMAN	RPL23	physical	22863883
TFIP8_HUMAN	TNFAIP8	physical	22863883
MLP3B_HUMAN	MAP1LC3B	physical	15355958
ATG7_HUMAN	ATG7	physical	24186333
ATG5_HUMAN	ATG5	physical	24186333
ATG12_HUMAN	ATG12	physical	24186333
BECN1_HUMAN	BECN1	physical	24186333
MLP3A_HUMAN	MAP1LC3A	physical	16303767
GBRL2_HUMAN	GABARAPL2	physical	16303767
GBRAP_HUMAN	GABARAP	physical	16303767
MLP3A_HUMAN	MAP1LC3A	physical	25503391
CLUS_HUMAN	CLU	physical	25503391
ATG5_HUMAN	ATG5	physical	28514442
A16L1_HUMAN	ATG16L1	physical	28514442
ATG12_HUMAN	ATG12	physical	28514442
GBRAP_HUMAN	GABARAP	physical	28514442
MP3B2_HUMAN	MAP1LC3B2	physical	28514442
GNAQ_HUMAN	GNAQ	physical	28514442
RASH_HUMAN	HRAS	physical	28514442
ACTBL_HUMAN	ACTBL2	physical	28514442
MAP1S_HUMAN	MAP1S	physical	28514442
EFR3A_HUMAN	EFR3A	physical	28514442

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

"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
PubMed: 19413330

Phosphorylation

"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-18, AND MASSSPECTROMETRY.
PubMed: 15592455