UniProt ID | PLLP_HUMAN | |
---|---|---|
UniProt AC | Q9Y342 | |
Protein Name | Plasmolipin | |
Gene Name | PLLP | |
Organism | Homo sapiens (Human). | |
Sequence Length | 182 | |
Subcellular Localization |
Membrane Multi-pass membrane protein. |
|
Protein Description | Appears to be involved in myelination. Could also participate in ion transport events as addition of plasmolipin to lipid bilayers induces the formation of ion channels, which are voltage-dependent and K(+)-selective (By similarity).. | |
Protein Sequence | MAEFPSKVSTRTSSPAQGAEASVSALRPDLGFVRSRLGALMLLQLVLGLLVWALIADTPYHLYPAYGWVMFVAVFLWLVTIVLFNLYLFQLHMKLYMVPWPLVLMIFNISATVLYITAFIACSAAVDLTSLRGTRPYNQRAAASFFACLVMIAYGVSAFFSYQAWRGVGSNAATSQMAGGYA | |
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 |
---|---|---|---|---|---|
6 | Phosphorylation | --MAEFPSKVSTRTS --CCCCCCCCCCCCC | 51.51 | 28857561 | |
7 | Ubiquitination | -MAEFPSKVSTRTSS -CCCCCCCCCCCCCC | 40.20 | - | |
9 | Phosphorylation | AEFPSKVSTRTSSPA CCCCCCCCCCCCCHH | 18.86 | 28355574 | |
10 | Phosphorylation | EFPSKVSTRTSSPAQ CCCCCCCCCCCCHHC | 40.74 | 23186163 | |
12 | Phosphorylation | PSKVSTRTSSPAQGA CCCCCCCCCCHHCCC | 33.38 | 25850435 | |
13 | Phosphorylation | SKVSTRTSSPAQGAE CCCCCCCCCHHCCCC | 30.91 | 26657352 | |
14 | Phosphorylation | KVSTRTSSPAQGAEA CCCCCCCCHHCCCCH | 24.52 | 21082442 | |
22 | Phosphorylation | PAQGAEASVSALRPD HHCCCCHHHHHHCCC | 14.22 | 23322592 | |
24 | Phosphorylation | QGAEASVSALRPDLG CCCCHHHHHHCCCHH | 21.06 | 24719451 | |
170 | Phosphorylation | QAWRGVGSNAATSQM HHHCCCCCCHHHHHH | 22.38 | 22461510 | |
181 | Phosphorylation | TSQMAGGYA------ HHHHCCCCC------ | 14.28 | 27642862 |
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 PLLP_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PLLP_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 PLLP_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
M4A12_HUMAN | MS4A12 | physical | 25416956 |
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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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-14, AND MASSSPECTROMETRY. |