VATG1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: VATG1_HUMAN
• UniProt AC: O75348
• Protein Name: V-type proton ATPase subunit G 1
• Gene Name: ATP6V1G1
• Organism: Homo sapiens (Human).
• Sequence Length: 118
• Protein Description: Catalytic subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation. [PubMed: 28296633]
• Protein Sequence: MASQSQGIQQLLQAEKRAAEKVSEARKRKNRRLKQAKEEAQAEIEQYRLQREKEFKAKEAAALGSRGSCSTEVEKETQEKMTILQTYFRQNRDEVLDNLLAFVCDIRPEIHENYRING

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	Acetylation	------MASQSQGIQ ------CCHHHHHHH	19.10	-
3	Phosphorylation	-----MASQSQGIQQ -----CCHHHHHHHH	29.12	25159151
5	Phosphorylation	---MASQSQGIQQLL ---CCHHHHHHHHHH	28.07	29507054
16	Ubiquitination	QQLLQAEKRAAEKVS HHHHHHHHHHHHHHH	50.80	21139048
16	Acetylation	QQLLQAEKRAAEKVS HHHHHHHHHHHHHHH	50.80	25953088
21	Acetylation	AEKRAAEKVSEARKR HHHHHHHHHHHHHHH	46.46	25953088
37	Malonylation	NRRLKQAKEEAQAEI HHHHHHHHHHHHHHH	54.30	26320211
37	Ubiquitination	NRRLKQAKEEAQAEI HHHHHHHHHHHHHHH	54.30	-
47	Phosphorylation	AQAEIEQYRLQREKE HHHHHHHHHHHHHHH	10.66	-
53	Ubiquitination	QYRLQREKEFKAKEA HHHHHHHHHHHHHHH	71.31	-
58	Ubiquitination	REKEFKAKEAAALGS HHHHHHHHHHHHHCC	48.77	-
65	Phosphorylation	KEAAALGSRGSCSTE HHHHHHCCCCCCCHH	34.03	28450419
68	Phosphorylation	AALGSRGSCSTEVEK HHHCCCCCCCHHHHH	12.09	26657352
70	Phosphorylation	LGSRGSCSTEVEKET HCCCCCCCHHHHHHH	29.33	30108239
71	Phosphorylation	GSRGSCSTEVEKETQ CCCCCCCHHHHHHHH	48.67	28450419
75	Ubiquitination	SCSTEVEKETQEKMT CCCHHHHHHHHHHHH	71.84	-
75	Acetylation	SCSTEVEKETQEKMT CCCHHHHHHHHHHHH	71.84	26822725
77	Phosphorylation	STEVEKETQEKMTIL CHHHHHHHHHHHHHH	53.77	27486199
80	Ubiquitination	VEKETQEKMTILQTY HHHHHHHHHHHHHHH	31.37	-
82	Phosphorylation	KETQEKMTILQTYFR HHHHHHHHHHHHHHH	29.60	22210691
86	Phosphorylation	EKMTILQTYFRQNRD HHHHHHHHHHHCCHH	22.60	22210691
87	Phosphorylation	KMTILQTYFRQNRDE HHHHHHHHHHCCHHH	5.47	27642862

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

Oops, there are no upstream regulatory protein records of VATG1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of VATG1_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 VATG1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
B2L11_HUMAN	BCL2L11	physical	21988832
VATE1_HUMAN	ATP6V1E1	physical	22863883
LDOC1_HUMAN	LDOC1	physical	25416956
VATE2_HUMAN	ATP6V1E2	physical	25416956
VATD_HUMAN	ATP6V1D	physical	26344197
KLH18_HUMAN	KLHL18	physical	28514442
LACC1_HUMAN	LACC1	physical	28514442
BTBD9_HUMAN	BTBD9	physical	28514442
CARM1_HUMAN	CARM1	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 ALA-2, AND MASS SPECTROMETRY.
PubMed: 19413330