PLS3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PLS3_HUMAN
• UniProt AC: Q9NRY6
• Protein Name: Phospholipid scramblase 3
• Gene Name: PLSCR3
• Organism: Homo sapiens (Human).
• Sequence Length: 295
• Subcellular Localization: Mitochondrion membrane ; Single-pass type II membrane protein .
• Protein Description: May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system. Seems to play a role in apoptosis, through translocation of cardiolipin from the inner to the outer mitochondrial membrane which promotes BID recruitment and enhances tBid-induced mitochondrial damages..
• Protein Sequence: MAGYLPPKGYAPSPPPPYPVTPGYPEPALHPGPGQAPVPAQVPAPAPGFALFPSPGPVALGSAAPFLPLPGVPSGLEFLVQIDQILIHQKAERVETFLGWETCNRYELRSGAGQPLGQAAEESNCCARLCCGARRPLRVRLADPGDREVLRLLRPLHCGCSCCPCGLQEMEVQAPPGTTIGHVLQTWHPFLPKFSIQDADRQTVLRVVGPCWTCGCGTDTNFEVKTRDESRSVGRISKQWGGLVREALTDADDFGLQFPLDLDVRVKAVLLGATFLIDYMFFEKRGGAGPSAVTS

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
4	Phosphorylation	----MAGYLPPKGYA ----CCCCCCCCCCC	13.39	27642862
21	Phosphorylation	PPPPYPVTPGYPEPA CCCCCCCCCCCCCCC	13.39	16267027
125	S-palmitoylation	QAAEESNCCARLCCG HHHHHCCHHHHHHCC	2.40	29575903
126	S-palmitoylation	AAEESNCCARLCCGA HHHHCCHHHHHHCCC	2.63	29575903
158	S-palmitoylation	RLLRPLHCGCSCCPC HHHCCCCCCCCCCCC	8.50	-
160	S-palmitoylation	LRPLHCGCSCCPCGL HCCCCCCCCCCCCCC	3.24	-
162	S-palmitoylation	PLHCGCSCCPCGLQE CCCCCCCCCCCCCEE	3.32	-
163	S-palmitoylation	LHCGCSCCPCGLQEM CCCCCCCCCCCCEEE	1.47	-
165	S-palmitoylation	CGCSCCPCGLQEMEV CCCCCCCCCCEEEEE	5.47	-
203	Phosphorylation	IQDADRQTVLRVVGP CCCCCCCCEEEEEEE	23.54	17081983
211	S-palmitoylation	VLRVVGPCWTCGCGT EEEEEEECCCCCCCC	3.75	19801377
214	S-palmitoylation	VVGPCWTCGCGTDTN EEEECCCCCCCCCCC	1.51	19801377
216	S-palmitoylation	GPCWTCGCGTDTNFE EECCCCCCCCCCCCE	6.04	19801377
230	Phosphorylation	EVKTRDESRSVGRIS EEEECCCCCCHHHHH	33.86	20363803
232	Phosphorylation	KTRDESRSVGRISKQ EECCCCCCHHHHHHH	37.90	20363803
238	Ubiquitination	RSVGRISKQWGGLVR CCHHHHHHHHHHHHH	47.93	21906983

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
21	T	Phosphorylation	Kinase	PKCD	Q05655	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
21	T	Phosphorylation	Phosphorylation at Thr-21 by PKC/PRKCD upon apoptotic stimuli enhances phospholipid scramblase activity.	17226776

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of PLS3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ALG2_HUMAN	ALG2	physical	18256029
CTSR1_HUMAN	CATSPER1	physical	25416956

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.