| UniProt ID | PMEL_HUMAN | |
|---|---|---|
| UniProt AC | P40967 | |
| Protein Name | Melanocyte protein PMEL | |
| Gene Name | PMEL | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 661 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Single-pass type I membrane protein. Golgi apparatus. Melanosome. Endosome, multivesicular body. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Localizes predominantly to intralumenal |
|
| Protein Description | Plays a central role in the biogenesis of melanosomes. Involved in the maturation of melanosomes from stage I to II. The transition from stage I melanosomes to stage II melanosomes involves an elongation of the vesicle, and the appearance within of distinct fibrillar structures. Release of the soluble form, ME20-S, could protect tumor cells from antibody mediated immunity.. | |
| Protein Sequence | MDLVLKRCLLHLAVIGALLAVGATKVPRNQDWLGVSRQLRTKAWNRQLYPEWTEAQRLDCWRGGQVSLKVSNDGPTLIGANASFSIALNFPGSQKVLPDGQVIWVNNTIINGSQVWGGQPVYPQETDDACIFPDGGPCPSGSWSQKRSFVYVWKTWGQYWQVLGGPVSGLSIGTGRAMLGTHTMEVTVYHRRGSRSYVPLAHSSSAFTITDQVPFSVSVSQLRALDGGNKHFLRNQPLTFALQLHDPSGYLAEADLSYTWDFGDSSGTLISRALVVTHTYLEPGPVTAQVVLQAAIPLTSCGSSPVPGTTDGHRPTAEAPNTTAGQVPTTEVVGTTPGQAPTAEPSGTTSVQVPTTEVISTAPVQMPTAESTGMTPEKVPVSEVMGTTLAEMSTPEATGMTPAEVSIVVLSGTTAAQVTTTEWVETTARELPIPEPEGPDASSIMSTESITGSLGPLLDGTATLRLVKRQVPLDCVLYRYGSFSVTLDIVQGIESAEILQAVPSGEGDAFELTVSCQGGLPKEACMEISSPGCQPPAQRLCQPVLPSPACQLVLHQILKGGSGTYCLNVSLADTNSLAVVSTQLIMPGQEAGLGQVPLIVGILLVLMAVVLASLIYRRRLMKQDFSVPQLPHSSSHWLRLPRIFCSCPIGENSPLLSGQQV | |
| 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 |
|---|---|---|---|---|---|
| 81 | N-linked_Glycosylation | GPTLIGANASFSIAL CCCEEEEEEEEEEEE | 30.79 | UniProtKB CARBOHYD | |
| 106 | N-linked_Glycosylation | DGQVIWVNNTIINGS CCCEEEECCEEECCC | 25.57 | UniProtKB CARBOHYD | |
| 111 | N-linked_Glycosylation | WVNNTIINGSQVWGG EECCEEECCCCCCCC | 39.97 | UniProtKB CARBOHYD | |
| 203 | Phosphorylation | SYVPLAHSSSAFTIT CEEEEEECCCCEEEC | 22.00 | - | |
| 204 | Phosphorylation | YVPLAHSSSAFTITD EEEEEECCCCEEECC | 18.80 | - | |
| 321 | N-linked_Glycosylation | RPTAEAPNTTAGQVP CCCCCCCCCCCCCCC | 58.05 | UniProtKB CARBOHYD | |
| 346 | Phosphorylation | QAPTAEPSGTTSVQV CCCCCCCCCCEEEEC | 40.03 | 29759185 | |
| 482 | Phosphorylation | CVLYRYGSFSVTLDI EEEEEECCEEEEEEE | 12.86 | - | |
| 568 | N-linked_Glycosylation | GSGTYCLNVSLADTN CCCEEEEEEEECCCC | 20.12 | UniProtKB CARBOHYD | |
| 653 | Phosphorylation | SCPIGENSPLLSGQQ ECCCCCCCCCCCCCC | 16.78 | 29507054 |
| 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 PMEL_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PMEL_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 PMEL_HUMAN !! | ||||||
| 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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