UniProt ID | TM205_HUMAN | |
---|---|---|
UniProt AC | Q6UW68 | |
Protein Name | Transmembrane protein 205 | |
Gene Name | TMEM205 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 189 | |
Subcellular Localization |
Membrane Multi-pass membrane protein . Located on cell surface microvilli. In cancer cells, transition in subcellular location from cell surface to intracellular regions correlates the progression of cisplatin resistance. |
|
Protein Description | In cancer cells, plays a role in resistance to the chemotherapeutic agent cisplatin.. | |
Protein Sequence | MEEGGNLGGLIKMVHLLVLSGAWGMQMWVTFVSGFLLFRSLPRHTFGLVQSKLFPFYFHISMGCAFINLCILASQHAWAQLTFWEASQLYLLFLSLTLATVNARWLEPRTTAAMWALQTVEKERGLGGEVPGSHQGPDPYRQLREKDPKYSALRQNFFRYHGLSSLCNLGCVLSNGLCLAGLALEIRSL | |
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 |
---|---|---|---|---|---|
122 | 2-Hydroxyisobutyrylation | WALQTVEKERGLGGE HHHHHHHHHCCCCCC | 48.66 | - | |
122 | Ubiquitination | WALQTVEKERGLGGE HHHHHHHHHCCCCCC | 48.66 | 21906983 | |
133 | Phosphorylation | LGGEVPGSHQGPDPY CCCCCCCCCCCCCHH | 13.43 | 27174698 | |
140 | Phosphorylation | SHQGPDPYRQLREKD CCCCCCHHHHHHHHC | 20.55 | 27174698 | |
149 | 2-Hydroxyisobutyrylation | QLREKDPKYSALRQN HHHHHCCCHHHHHHH | 63.07 | - | |
149 | Acetylation | QLREKDPKYSALRQN HHHHHCCCHHHHHHH | 63.07 | 19608861 | |
149 | Ubiquitination | QLREKDPKYSALRQN HHHHHCCCHHHHHHH | 63.07 | 19608861 |
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 TM205_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TM205_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 TM205_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
RET4_HUMAN | RBP4 | physical | 28514442 | |
TPM2_HUMAN | TPM2 | physical | 28514442 | |
COR1A_HUMAN | CORO1A | physical | 28514442 |
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. |
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Acetylation | |
Reference | PubMed |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-149, AND MASS SPECTROMETRY. |