CIDEA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CIDEA_HUMAN
• UniProt AC: O60543
• Protein Name: Cell death activator CIDE-A
• Gene Name: CIDEA
• Organism: Homo sapiens (Human).
• Sequence Length: 219
• Subcellular Localization: Lipid droplet . Nucleus. Enriched at lipid droplet contact sites. Has been shown to localize to mitonchondria, where it could interact with UCP1 and hence inhibit UCP1 uncoupling activity (By similarity). These data could not be confirmed (PubMed:185
• Protein Description: Acts as a CEBPB coactivator in mammary epithelial cells to control the expression of a subset of CEBPB downstream target genes, including ID2, IGF1, PRLR, SOCS1, SOCS3, XDH, but not casein. By interacting with CEBPB, strengthens the association of CEBPB with the XDH promoter, increases histone acetylation and dissociates HDAC1 from the promoter (By similarity). Binds to lipid droplets and regulates their enlargement, thereby restricting lipolysis and favoring storage. At focal contact sites between lipid droplets, promotes directional net neutral lipid transfer from the smaller to larger lipid droplets. The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair and occurs at a lower rate than that promoted by CIDEC. When overexpressed, induces apoptosis. The physiological significance of its role in apoptosis is unclear..
• Protein Sequence: MEAARDYAGALIRPLTFMGSQTKRVLFTPLMHPARPFRVSNHDRSSRRGVMASSLQELISKTLDALVIATGLVTLVLEEDGTVVDTEEFFQTLGDNTHFMILEKGQKWMPGSQHVPTCSPPKRSGIARVTFDLYRLNPKDFIGCLNVKATMYEMYSVSYDIRCTGLKGLLRSLLRFLSYSAQVTGQFLIYLGTYMLRVLDDKEERPSLRSQAKGRFTCG

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
16	Phosphorylation	GALIRPLTFMGSQTK HHHHHCEEECCCCCC	17.79	-
22	Phosphorylation	LTFMGSQTKRVLFTP EEECCCCCCEEEEEC	23.63	-
28	Phosphorylation	QTKRVLFTPLMHPAR CCCEEEEECCCCCCC	16.02	29449344
45	Phosphorylation	RVSNHDRSSRRGVMA CCCCCCHHHCHHCHH	33.96	24260401
53	Phosphorylation	SRRGVMASSLQELIS HCHHCHHHHHHHHHH	17.31	20873877
54	Phosphorylation	RRGVMASSLQELISK CHHCHHHHHHHHHHH	25.24	20873877
112	Phosphorylation	GQKWMPGSQHVPTCS CCCCCCCCCCCCCCC	15.96	25954137
117	Phosphorylation	PGSQHVPTCSPPKRS CCCCCCCCCCCCCCC	25.24	25954137
119	Phosphorylation	SQHVPTCSPPKRSGI CCCCCCCCCCCCCCC	46.87	25954137
134	Phosphorylation	ARVTFDLYRLNPKDF EEEEEEEEECCHHHE	18.20	18083107
155	Phosphorylation	KATMYEMYSVSYDIR EEEEEEEECCCEECC	8.25	18083107
159	Phosphorylation	YEMYSVSYDIRCTGL EEEECCCEECCCCCH	17.15	18083107

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CIDEA_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 CIDEA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ZBT16_HUMAN	ZBTB16	physical	16169070
CIDEB_HUMAN	CIDEB	physical	10837461
AAKB1_HUMAN	PRKAB1	physical	18480843
PKP1_HUMAN	PKP1	physical	26186194
S10AE_HUMAN	S100A14	physical	26186194
SPA12_HUMAN	SERPINA12	physical	26186194
PKP3_HUMAN	PKP3	physical	26186194
CIDEC_HUMAN	CIDEC	physical	19843876
ICAM1_HUMAN	ICAM1	physical	28514442
SPA12_HUMAN	SERPINA12	physical	28514442
KPRP_HUMAN	KPRP	physical	28514442
PKP1_HUMAN	PKP1	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.