| UniProt ID | TM127_HUMAN | |
|---|---|---|
| UniProt AC | O75204 | |
| Protein Name | Transmembrane protein 127 | |
| Gene Name | TMEM127 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 238 | |
| Subcellular Localization |
Cell membrane Multi-pass membrane protein . Cytoplasm . Association of TMEM127 with the cell membrane is enhanced by inhibition of endocytosis. In the cytoplasm, it colocalizes with markers of early endosomal structures, Golgi apparatus and lysosom |
|
| Protein Description | Controls cell proliferation acting as a negative regulator of TOR signaling pathway mediated by mTORC1. May act as a tumor suppressor.. | |
| Protein Sequence | MYAPGGAGLPGGRRRRSPGGSALPKQPERSLASALPGALSITALCTALAEPAWLHIHGGTCSRQELGVSDVLGYVHPDLLKDFCMNPQTVLLLRVIAAFCFLGILCSLSAFLLDVFGPKHPALKITRRYAFAHILTVLQCATVIGFSYWASELILAQQQQHKKYHGSQVYVTFAVSFYLVAGAGGASILATAANLLRHYPTEEEEQALELLSEMEENEPYPAEYEVINQFQPPPAYTP | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MYAPGGAG -------CCCCCCCC | 6.09 | 25732826 | |
| 2 | Phosphorylation | ------MYAPGGAGL ------CCCCCCCCC | 22.85 | 24173317 | |
| 17 | Phosphorylation | PGGRRRRSPGGSALP CCCCCCCCCCCCCCC | 26.53 | 28348404 | |
| 21 | Phosphorylation | RRRSPGGSALPKQPE CCCCCCCCCCCCCCC | 32.33 | - | |
| 25 | Ubiquitination | PGGSALPKQPERSLA CCCCCCCCCCCHHHH | 78.36 | 2113904 | |
| 224 | Phosphorylation | NEPYPAEYEVINQFQ CCCCCCCHHHHHCCC | 20.01 | - |
| 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 TM127_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TM127_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 TM127_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of TM127_HUMAN !! | ||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 171300 | Pheochromocytoma (PCC) | |||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND MASSSPECTROMETRY. | |