UniProt ID | CIDEC_HUMAN | |
---|---|---|
UniProt AC | Q96AQ7 | |
Protein Name | Cell death activator CIDE-3 | |
Gene Name | CIDEC | |
Organism | Homo sapiens (Human). | |
Sequence Length | 238 | |
Subcellular Localization | Nucleus. Endoplasmic reticulum. Lipid droplet. Diffuses quickly on lipid droplet surface, but becomes trapped and clustered at lipid droplet contact sites, thereby enabling its rapid enrichment at lipid droplet contact sites. | |
Protein Description | 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. Its role in neutral lipid transfer and lipid droplet enlargement is activated by the interaction with PLIN1. May act as a CEBPB coactivator in the white adipose tissue to control the expression of a subset of CEBPB downstream target genes, including SOCS1, SOCS3, TGFB1, TGFBR1, ID2 and XDH. When overexpressed in preadipocytes, induces apoptosis or increases cell susceptibility to apoptosis induced by serum deprivation or TGFB treatment. As mature adipocytes, that express high CIDEC levels, are quite resistant to apoptotic stimuli, the physiological significance of its role in apoptosis is unclear. May play a role in the modulation of the response to osmotic stress by preventing NFAT5 to translocate into the nucleus and activate its target genes expression.. | |
Protein Sequence | MEYAMKSLSLLYPKSLSRHVSVRTSVVTQQLLSEPSPKAPRARPCRVSTADRSVRKGIMAYSLEDLLLKVRDTLMLADKPFFLVLEEDGTTVETEEYFQALAGDTVFMVLQKGQKWQPPSEQGTRHPLSLSHKPAKKIDVARVTFDLYKLNPQDFIGCLNVKATFYDTYSLSYDLHCCGAKRIMKEAFRWALFSMQATGHVLLGTSCYLQQLLDATEEGQPPKGKASSLIPTCLKILQ | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
3 | Phosphorylation | -----MEYAMKSLSL -----CCHHHHHHHH | 15.65 | 24043423 | |
7 | Phosphorylation | -MEYAMKSLSLLYPK -CCHHHHHHHHHCCH | 15.31 | 24043423 | |
9 | Phosphorylation | EYAMKSLSLLYPKSL CHHHHHHHHHCCHHH | 24.34 | 24043423 | |
12 | Phosphorylation | MKSLSLLYPKSLSRH HHHHHHHCCHHHCCC | 17.57 | 24043423 | |
21 | Phosphorylation | KSLSRHVSVRTSVVT HHHCCCCCCCHHHHH | 10.35 | 24719451 | |
34 | Phosphorylation | VTQQLLSEPSPKAPR HHHHHHCCCCCCCCC | 50.17 | 24719451 | |
56 | Acetylation | TADRSVRKGIMAYSL HCCHHHHHHHHHCCH | 51.11 | 19817445 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of CIDEC_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CIDEC_HUMAN !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of CIDEC_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
CIDEC_HUMAN | CIDEC | physical | 19843876 | |
EGR1_HUMAN | EGR1 | physical | 24742676 | |
TRY2_HUMAN | PRSS2 | physical | 28514442 | |
TOP1_HUMAN | TOP1 | physical | 28514442 | |
AMFR_HUMAN | AMFR | physical | 28656280 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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