MBOA5_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MBOA5_MOUSE
• UniProt AC: Q91V01
• Protein Name: Lysophospholipid acyltransferase 5
• Gene Name: Lpcat3
• Organism: Mus musculus (Mouse).
• Sequence Length: 487
• Subcellular Localization: Endoplasmic reticulum membrane ; Multi-pass membrane protein .
• Protein Description: Acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (LPCAT activity). To a lesser extent, also catalyzes the acylation of lysophosphatidylethanolamine (1-acyl-sn-glycero-3-phosphoethanolamine or LPE) into phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine or PE) (LPEAT activity), and the conversion of lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero-3-phospho-L-serine or LPS) into phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine or PS) (LPSAT activity). Favors polyunsaturated fatty acyl-CoAs as acyl donors compared to saturated fatty acyl-CoAs. Seems to be the major enzyme contributing to LPCAT activity in the liver. Lysophospholipid acyltransferases (LPLATs) catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle..
• Protein Sequence: MASTADGDMGETLEQMRGLWPGVEDLSLNKLATSLGASEQALRLIFSIFLGYPLALFYRHYLFYKDSYLIHLFHTFTGLSIAYFNFGHQFYHSLLCVVLQFLILRLMGRTVTAVITTLCFQMAYLLAGYYYTATGDYDIKWTMPHCVLTLKLIGLCIDYYDGGKDGNSLTSEQQKYAIRGVPSLLEVAGFSYFYGAFLVGPQFSMNHYMKLVRGQLTDIPGKMPNSTIPALKRLSLGLVYLVGYTLLSPHITDDYLLTEDYDNRPFWFRCMYMLIWGKFVLYKYVTCWLVTEGVCILSGLGFNGFDENGTVRWDACANMKVWLFETTPRFNGTIASFNINTNAWVARYIFKRLKFLGNKELSQGLSLLFLALWHGLHSGYLICFQMEFLIVIVEKQVSSLIRDSPALSSLASITALQPFYYLVQQTIHWLFMGYSMTAFCLFTWDKWLKVYRSIYFLGHVFFLSLLFILPYIHKAMVPRKEKLKKRE

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	------MASTADGDM ------CCCCCCCCH	18.65	-
3	Phosphorylation	-----MASTADGDMG -----CCCCCCCCHH	23.88	30635358
4	Phosphorylation	----MASTADGDMGE ----CCCCCCCCHHH	21.16	30635358
80	Ubiquitination	FHTFTGLSIAYFNFG HHHCCCCCEEEEECC	13.40	27667366
171	Phosphorylation	KDGNSLTSEQQKYAI CCCCCCCHHHHHHHH	38.41	-
175	Acetylation	SLTSEQQKYAIRGVP CCCHHHHHHHHCCCC	36.02	23954790
175	Malonylation	SLTSEQQKYAIRGVP CCCHHHHHHHHCCCC	36.02	26320211
222	Ubiquitination	QLTDIPGKMPNSTIP CCCCCCCCCCCCHHH	45.92	27667366
225	N-linked_Glycosylation	DIPGKMPNSTIPALK CCCCCCCCCHHHHHH	48.57	-
232	Acetylation	NSTIPALKRLSLGLV CCHHHHHHHHHHHHH	54.09	7744431
308	N-linked_Glycosylation	GFNGFDENGTVRWDA CCCCCCCCCCEEEHH	53.96	-
331	N-linked_Glycosylation	FETTPRFNGTIASFN EECCCCCCCEEEEEE	48.23	-
354	Malonylation	RYIFKRLKFLGNKEL HHHHHHHHHCCCHHH	42.44	26320211

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

Oops, there are no upstream regulatory protein records of MBOA5_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MBOA5_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of MBOA5_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of MBOA5_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.