UniProt ID | CERS6_HUMAN | |
---|---|---|
UniProt AC | Q6ZMG9 | |
Protein Name | Ceramide synthase 6 | |
Gene Name | CERS6 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 384 | |
Subcellular Localization |
Nucleus membrane Multi-pass membrane protein . Endoplasmic reticulum membrane Multi-pass membrane protein. |
|
Protein Description | May be involved in sphingolipid synthesis or its regulation.. | |
Protein Sequence | MAGILAWFWNERFWLPHNVTWADLKNTEEATFPQAEDLYLAFPLAFCIFMVRLIFERFVAKPCAIALNIQANGPQIAPPNAILEKVFTAITKHPDEKRLEGLSKQLDWDVRSIQRWFRQRRNQEKPSTLTRFCESMWRFSFYLYVFTYGVRFLKKTPWLWNTRHCWYNYPYQPLTTDLHYYYILELSFYWSLMFSQFTDIKRKDFGIMFLHHLVSIFLITFSYVNNMARVGTLVLCLHDSADALLEAAKMANYAKFQKMCDLLFVMFAVVFITTRLGIFPLWVLNTTLFESWEIVGPYPSWWVFNLLLLLVQGLNCFWSYLIVKIACKAVSRGKVSKDDRSDIESSSDEEDSEPPGKNPHTATTTNGTSGTNGYLLTGSCSMDD | |
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 |
---|---|---|---|---|---|
18 | N-linked_Glycosylation | ERFWLPHNVTWADLK CCCCCCCCCCHHHHC | 30.86 | 19159218 | |
91 | Phosphorylation | EKVFTAITKHPDEKR HHHHHHHHHCCCHHH | 22.34 | - | |
92 | Ubiquitination | KVFTAITKHPDEKRL HHHHHHHHCCCHHHH | 47.21 | 29967540 | |
97 | Ubiquitination | ITKHPDEKRLEGLSK HHHCCCHHHHHHHHH | 70.44 | - | |
104 | Ubiquitination | KRLEGLSKQLDWDVR HHHHHHHHHCCHHHH | 60.98 | 21906983 | |
104 | Ubiquitination | KRLEGLSKQLDWDVR HHHHHHHHHCCHHHH | 60.98 | 21890473 | |
111 | Methylation | KQLDWDVRSIQRWFR HHCCHHHHHHHHHHH | 26.10 | 115481863 | |
112 | Phosphorylation | QLDWDVRSIQRWFRQ HCCHHHHHHHHHHHH | 23.95 | 23898821 | |
125 | Ubiquitination | RQRRNQEKPSTLTRF HHHHCCCCCCHHHHH | 34.21 | 24816145 | |
155 | Ubiquitination | YGVRFLKKTPWLWNT HHCHHHHCCCCCEEC | 63.06 | - | |
255 | Ubiquitination | AKMANYAKFQKMCDL HHHHCHHHHHHHHHH | 37.66 | - | |
336 | Phosphorylation | AVSRGKVSKDDRSDI HHHCCCCCCCCHHHH | 33.58 | 29449344 | |
341 | Phosphorylation | KVSKDDRSDIESSSD CCCCCCHHHHCCCCC | 50.35 | 25849741 | |
345 | Phosphorylation | DDRSDIESSSDEEDS CCHHHHCCCCCCCCC | 35.16 | 20363803 | |
346 | Phosphorylation | DRSDIESSSDEEDSE CHHHHCCCCCCCCCC | 29.08 | 20363803 | |
347 | Phosphorylation | RSDIESSSDEEDSEP HHHHCCCCCCCCCCC | 59.32 | 20363803 | |
352 | Phosphorylation | SSSDEEDSEPPGKNP CCCCCCCCCCCCCCC | 56.11 | 27732954 | |
377 | Phosphorylation | GTNGYLLTGSCSMDD CCCCEEEEEECCCCC | 25.18 | 26471730 | |
379 | Phosphorylation | NGYLLTGSCSMDD-- CCEEEEEECCCCC-- | 9.59 | 26471730 | |
381 | Phosphorylation | YLLTGSCSMDD---- EEEEEECCCCC---- | 27.26 | 26471730 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
341 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
345 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
346 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
347 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CERS6_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 CERS6_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of CERS6_HUMAN !! |
Kegg Disease | ||||||
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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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N-linked Glycosylation | |
Reference | PubMed |
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-18, AND MASS SPECTROMETRY. |