PLIN5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PLIN5_HUMAN
• UniProt AC: Q00G26
• Protein Name: Perilipin-5
• Gene Name: PLIN5
• Organism: Homo sapiens (Human).
• Sequence Length: 463
• Subcellular Localization: Lipid droplet . Cytoplasm . Mitochondrion . Lipid droplet surface-associated. Exchanges between lipid droplets and the cytoplasm.
• Protein Description: Lipid droplet-associated protein that maintains the balance between lipogenesis and lipolysis and also regulates fatty acid oxidation in oxidative tissues. Recruits mitochondria to the surface of lipid droplets and is involved in lipid droplet homeostasis by regulating both the storage of fatty acids in the form of triglycerides and the release of fatty acids for mitochondrial fatty acid oxidation. In lipid droplet triacylglycerol hydrolysis, plays a role as a scaffolding protein for three major key lipolytic players: ABHD5, PNPLA2 and LIPE. Reduces the triacylglycerol hydrolase activity of PNPLA2 by recruiting and sequestering PNPLA2 to lipid droplets. Phosphorylation by PKA enables lipolysis probably by promoting release of ABHD5 from the perilipin scaffold and by facilitating interaction of ABHD5 with PNPLA2. Also increases lipolysis through interaction with LIPE and upon PKA-mediated phosphorylation of LIPE (By similarity)..
• Protein Sequence: MSEEEAAQIPRSSVWEQDQQNVVQRVVALPLVRATCTAVCDVYSAAKDRHPLLGSACRLAENCVCGLTTRALDHAQPLLEHLQPQLATMNSLACRGLDKLEEKLPFLQQPSETVVTSAKDVVASSVTGVVDLARRGRRWSVELKRSVSHAVDVVLEKSEELVDHFLPMTEEELAALAAEAEGPEVGSVEDQRRQQGYFVRLGSLSARIRHLAYEHSVGKLRQSKHRAQDTLAQLQETLELIDHMQCGVTPTAPACPGKVHELWGEWGQRPPESRRRSQAELETLVLSRSLTQELQGTVEALESSVRGLPAGAQEKVAEVRRSVDALQTAFADARCFRDVPAAALAEGRGRVAHAHACVDELLELVVQAVPLPWLVGPFAPILVERPEPLPDLADLVDEVIGGPDPRWAHLDWPAQQRAWEAEHRDGSGNGDGDRMGVAGDICEQEPETPSCPVKHTLMPELDF

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	Phosphorylation	------MSEEEAAQI ------CCHHHHHCC	54.43	22673903
55	Phosphorylation	DRHPLLGSACRLAEN CCCCCCHHHHHHHHH	24.94	24275569
127	O-linked_Glycosylation	DVVASSVTGVVDLAR HHHHHHHHCHHHHHH	26.63	30620550
140	Phosphorylation	ARRGRRWSVELKRSV HHCCCCCEEEHHHHH	12.14	28857561
144	Acetylation	RRWSVELKRSVSHAV CCCEEEHHHHHHHHH	29.17	12433537
146	Phosphorylation	WSVELKRSVSHAVDV CEEEHHHHHHHHHHH	26.78	28857561
148	Phosphorylation	VELKRSVSHAVDVVL EEHHHHHHHHHHHHH	13.63	28857561
203	Phosphorylation	GYFVRLGSLSARIRH CCEEEHHHHHHHHHH	24.60	23401153
205	Phosphorylation	FVRLGSLSARIRHLA EEEHHHHHHHHHHHH	19.73	30266825
273	Phosphorylation	WGQRPPESRRRSQAE CCCCCCHHHHHCHHH	36.54	26437602
277	Phosphorylation	PPESRRRSQAELETL CCHHHHHCHHHHHHH	31.75	30278072
287	Phosphorylation	ELETLVLSRSLTQEL HHHHHHHHHHHHHHH	16.61	24719451
289	Phosphorylation	ETLVLSRSLTQELQG HHHHHHHHHHHHHHH	32.18	28348404
291	Phosphorylation	LVLSRSLTQELQGTV HHHHHHHHHHHHHHH	22.65	28348404
322	Phosphorylation	KVAEVRRSVDALQTA HHHHHHHHHHHHHHH	17.49	28258704

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

Oops, there are no upstream regulatory protein records of PLIN5_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PLIN5_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 PLIN5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MAP2_HUMAN	METAP2	physical	26186194
SHIP2_HUMAN	INPPL1	physical	26186194
SAPC2_HUMAN	SAPCD2	physical	26186194
SAPC2_HUMAN	SAPCD2	physical	28514442
MAP2_HUMAN	METAP2	physical	28514442
SHIP2_HUMAN	INPPL1	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.