UniProt ID | DLK2_HUMAN | |
---|---|---|
UniProt AC | Q6UY11 | |
Protein Name | Protein delta homolog 2 | |
Gene Name | DLK2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 383 | |
Subcellular Localization |
Membrane Single-pass type I membrane protein . |
|
Protein Description | Regulates adipogenesis.. | |
Protein Sequence | MPSGCRCLHLVCLLCILGAPGQPVRADDCSSHCDLAHGCCAPDGSCRCDPGWEGLHCERCVRMPGCQHGTCHQPWQCICHSGWAGKFCDKDEHICTTQSPCQNGGQCMYDGGGEYHCVCLPGFHGRDCERKAGPCEQAGSPCRNGGQCQDDQGFALNFTCRCLVGFVGARCEVNVDDCLMRPCANGATCLDGINRFSCLCPEGFAGRFCTINLDDCASRPCQRGARCRDRVHDFDCLCPSGYGGKTCELVLPVPDPPTTVDTPLGPTSAVVVPATGPAPHSAGAGLLRISVKEVVRRQEAGLGEPSLVALVVFGALTAALVLATVLLTLRAWRRGVCPPGPCCYPAPHYAPACQDQECQVSMLPAGLPLPRDLPPEPGKTTAL | |
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 |
---|---|---|---|---|---|
157 | N-linked_Glycosylation | DDQGFALNFTCRCLV CCCCCCCEEEEHHHH | 27.10 | UniProtKB CARBOHYD | |
275 | O-linked_Glycosylation | SAVVVPATGPAPHSA EEEEEECCCCCCCCC | 37.31 | OGP | |
281 | O-linked_Glycosylation | ATGPAPHSAGAGLLR CCCCCCCCCCCCEEE | 27.60 | OGP |
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 DLK2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DLK2_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 DLK2_HUMAN !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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