MBOA5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MBOA5_HUMAN
• UniProt AC: Q6P1A2
• Protein Name: Lysophospholipid acyltransferase 5
• Gene Name: LPCAT3
• Organism: Homo sapiens (Human).
• 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). Catalyzes also 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). Has also weak lysophosphatidylethanolamine acyltransferase activity (LPEAT 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: MASSAEGDEGTVVALAGVLQSGFQELSLNKLATSLGASEQALRLIISIFLGYPFALFYRHYLFYKETYLIHLFHTFTGLSIAYFNFGNQLYHSLLCIVLQFLILRLMGRTITAVLTTFCFQMAYLLAGYYYTATGNYDIKWTMPHCVLTLKLIGLAVDYFDGGKDQNSLSSEQQKYAIRGVPSLLEVAGFSYFYGAFLVGPQFSMNHYMKLVQGELIDIPGKIPNSIIPALKRLSLGLFYLVGYTLLSPHITEDYLLTEDYDNHPFWFRCMYMLIWGKFVLYKYVTCWLVTEGVCILTGLGFNGFEEKGKAKWDACANMKVWLFETNPRFTGTIASFNINTNAWVARYIFKRLKFLGNKELSQGLSLLFLALWHGLHSGYLVCFQMEFLIVIVERQAARLIQESPTLSKLAAITVLQPFYYLVQQTIHWLFMGYSMTAFCLFTWDKWLKVYKSIYFLGHIFFLSLLFILPYIHKAMVPRKEKLKKME

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	------MASSAEGDE ------CCCCCCCCH	16.52	25944712
3	Phosphorylation	-----MASSAEGDEG -----CCCCCCCCHH	28.87	20068231
4	Phosphorylation	----MASSAEGDEGT ----CCCCCCCCHHH	22.32	20068231
11	Phosphorylation	SAEGDEGTVVALAGV CCCCCHHHHHHHHHH	15.12	20068231
21	Phosphorylation	ALAGVLQSGFQELSL HHHHHHHHHCHHHCH	37.10	20068231
27	Phosphorylation	QSGFQELSLNKLATS HHHCHHHCHHHHHHH	29.19	20068231
47	Phosphorylation	QALRLIISIFLGYPF HHHHHHHHHHHHCHH	10.57	27251275
159	Phosphorylation	LIGLAVDYFDGGKDQ HHHHHHHHCCCCCCC	9.29	-
164	Ubiquitination	VDYFDGGKDQNSLSS HHHCCCCCCCCCCCH	62.76	22817900
175	Ubiquitination	SLSSEQQKYAIRGVP CCCHHHHHHHHCCHH	36.02	21890473
175	Ubiquitination	SLSSEQQKYAIRGVP CCCHHHHHHHHCCHH	36.02	21906983
222	Ubiquitination	ELIDIPGKIPNSIIP CEECCCCCCCCCHHH	50.03	21906983
232	Ubiquitination	NSIIPALKRLSLGLF CCHHHHHHHHHHHHH	54.09	27667366
232	2-Hydroxyisobutyrylation	NSIIPALKRLSLGLF CCHHHHHHHHHHHHH	54.09	-
333	Phosphorylation	TNPRFTGTIASFNIN CCCCCCCEEEEEECC	15.43	-
348	Phosphorylation	TNAWVARYIFKRLKF CCHHHHHHHHHHHHH	10.85	-
354	Ubiquitination	RYIFKRLKFLGNKEL HHHHHHHHHCCCCHH	42.44	33845483
485	Ubiquitination	PRKEKLKKME----- CCHHHHHCCC-----	59.71	24816145

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

Oops, there are no upstream regulatory protein records of MBOA5_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MBOA5_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 MBOA5_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of MBOA5_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.