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| Functional site class: | S-palmitoylation site |
| Functional site description: | Reversible addition of palmitate or other long chain fatty acids to protein at cysteine residues via a thioester linkage |
|---|---|
| ELMs: | MOD_SPalmitoyl_2 MOD_SPalmitoyl_4 |
| Description: | Class 2 Palmitoylation motif. Proteins that belong to this class: Ras proteins (H-Ras, N-Ras). |
| Pattern: | G(C)M[GS][CL][KP]C (Probability: 0.0000000) |
| Present in taxons: |
Eukaryota
Homo sapiens
|
| Interaction Domain: |
|
See 2 Instances for MOD_SPalmitoyl_2
|
| The post-translational addition of palmitate to many integral and peripheral membrane proteins is the most common modification. Palmitate group promotes stable membrane association. In combination with a myristoyl or farnesyl group, palmitoylated proteins are essentially permanently anchored to the membrane. |
(click table headers for sorting)
| Sequence | Start | End | Subsequence | Logic | PDB | Organism |
|---|---|---|---|---|---|---|
(P01112) RASH_HUMAN |
180 | 186 | KLNPPDESGPGCMSCKCVLS | TP | --- |
Homo sapiens
(Human)
|
(P01111) RASN_HUMAN |
180 | 186 | KLNSSDDGTQGCMGLPCVVM | TP | --- |
Homo sapiens
(Human)
|
Please cite: ELM - the database of eukaryotic linear motifs (PMID:
22110040)
ELM data can be downloaded and distributed for non-commercial use according to the ELM Software License Agreement





