UniProt ID | SAMD8_HUMAN | |
---|---|---|
UniProt AC | Q96LT4 | |
Protein Name | Sphingomyelin synthase-related protein 1 | |
Gene Name | SAMD8 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 415 | |
Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . |
|
Protein Description | Sphingomyelin synthases synthesize sphingolipids through transfer of a phosphatidyl head group on to the primary hydroxyl of ceramide. SAMD8 is an endoplasmic reticulum (ER) transferase that has no sphingomyelin synthase activity but can convert phosphatidylethanolamine (PE) and ceramide to ceramide phosphoethanolamine (CPE) albeit with low product yield. Appears to operate as a ceramide sensor to control ceramide homeostasis in the endoplasmic reticulum rather than a converter of ceramides. Seems to be critical for the integrity of the early secretory pathway.. | |
Protein Sequence | MAGPNQLCIRRWTTKHVAVWLKDEGFFEYVDILCNKHRLDGITLLTLTEYDLRSPPLEIKVLGDIKRLMLSVRKLQKIHIDVLEEMGYNSDSPMGSMTPFISALQSTDWLCNGELSHDCDGPITDLNSDQYQYMNGKNKHSVRRLDPEYWKTILSCIYVFIVFGFTSFIMVIVHERVPDMQTYPPLPDIFLDSVPRIPWAFAMTEVCGMILCYIWLLVLLLHKHRSILLRRLCSLMGTVFLLRCFTMFVTSLSVPGQHLQCTGKIYGSVWEKLHRAFAIWSGFGMTLTGVHTCGDYMFSGHTVVLTMLNFFVTEYTPRSWNFLHTLSWVLNLFGIFFILAAHEHYSIDVFIAFYITTRLFLYYHTLANTRAYQQSRRARIWFPMFSFFECNVNGTVPNEYCWPFSKPAIMKRLIG | |
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 |
---|---|---|---|---|---|
13 | Phosphorylation | QLCIRRWTTKHVAVW CEEEECCCCCEEEEE | 24.93 | 22798277 | |
60 | Ubiquitination | RSPPLEIKVLGDIKR CCCCEEEEEHHHHHH | 23.25 | 2190698 | |
66 | Ubiquitination | IKVLGDIKRLMLSVR EEEHHHHHHHHHHHH | 44.19 | - | |
123 | Ubiquitination | SHDCDGPITDLNSDQ CCCCCCCCCCCCCHH | 5.98 | 21906983 | |
183 | Phosphorylation | RVPDMQTYPPLPDIF CCCCCCCCCCCCCCC | 5.98 | - | |
193 | Phosphorylation | LPDIFLDSVPRIPWA CCCCCCCCCCCCCHH | 35.85 | 21815630 | |
234 | Phosphorylation | ILLRRLCSLMGTVFL HHHHHHHHHHHHHHH | 26.44 | - | |
238 | Phosphorylation | RLCSLMGTVFLLRCF HHHHHHHHHHHHHHH | 8.30 | - | |
246 | Phosphorylation | VFLLRCFTMFVTSLS HHHHHHHHHHHHHCC | 17.21 | 29083192 | |
250 | Phosphorylation | RCFTMFVTSLSVPGQ HHHHHHHHHCCCCCC | 16.82 | 29083192 | |
251 | Phosphorylation | CFTMFVTSLSVPGQH HHHHHHHHCCCCCCC | 17.22 | 29083192 | |
253 | Phosphorylation | TMFVTSLSVPGQHLQ HHHHHHCCCCCCCEE | 26.49 | 29083192 | |
262 | Phosphorylation | PGQHLQCTGKIYGSV CCCCEEECCEEEHHH | 28.66 | 29083192 | |
362 | Phosphorylation | ITTRLFLYYHTLANT HHHHHHHHHHHHHCC | 5.95 | 29759185 | |
363 | Phosphorylation | TTRLFLYYHTLANTR HHHHHHHHHHHHCCH | 7.17 | 24260401 | |
365 | Phosphorylation | RLFLYYHTLANTRAY HHHHHHHHHHCCHHH | 16.08 | 29759185 | |
369 | Phosphorylation | YYHTLANTRAYQQSR HHHHHHCCHHHHHHH | 15.86 | 24260401 |
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 SAMD8_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SAMD8_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 SAMD8_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of SAMD8_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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