MOD_SPalmitoyl_4
| Accession: | |
|---|---|
| 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 with same func. site: | MOD_SPalmitoyl_2 MOD_SPalmitoyl_4 |
| ELM Description: | Class 4 palmitoylation motif. Proteins that belong to this class: Src-family kinases (all except src itself) and G-protein alpha subunits. |
| Pattern: | ^M{0,1}G(C)..S[AKS] |
| Pattern Probability: | 3.261e-08 |
| Present in taxons: | Canis lupus familiaris Eukaryota Gallus gallus Homo sapiens Mus musculus Rattus norvegicus |
| Interaction Domain: |
zf-DHHC (PF01529)
DHHC zinc finger domain
(Stochiometry: 1 : 1)
|
 Abstract |
The post-translational addition of palmitate to many integral and peripheral membrane proteins is the most common modification. The palmitate group promotes stable membrane association. In combination with a myristoyl or farnesyl group, palmitoylation essentially permanently anchors a protein to the membrane. The target proteins of Palmitoyl acyltransferase (PAT) can be divided in four classes: (1) transmembrane proteins, (2) prenylated proteins, (3) exclusively palmitoylated proteins, and (4) myristoylated proteins. |
4 selected references:
-
Signalling functions of protein palmitoylation.
Dunphy JT, Linder ME
Biochim Biophys Acta 1998 Dec 8; 1436 (1), 245-61
PMID: 9838145
-
Fatty acylation of proteins: new insights into membrane targeting of
myristoylated and palmitoylated proteins.
Resh MD
Biochim Biophys Acta 1999 Aug 12; 1451 (1), 1-16
PMID: 10446384
-
Regulation of G proteins by covalent modification.
Chen CA, Manning DR
Oncogene 2001 Mar 26; 20 (13), 1643-52
PMID: 11313912
-
The on-off story of protein palmitoylation.
Bijlmakers MJ, Marsh M
Trends Cell Biol 2003 Jan; 13 (1), 32-42
PMID: 12480338
3 GO-Terms:
6 Instances for MOD_SPalmitoyl_4
(click table headers for sorting; Notes column: =Number of Switches, =Number of Interactions)
| Acc., Gene-, Name | Start | End | Subsequence | Logic | #Ev. | Organism | Notes |
|---|---|---|---|---|---|---|---|
| P06240 Lck LCK_MOUSE |
1 | 7 | MGCVCSSNPEDDWMENIDVC | TP | 2 | Mus musculus (House mouse) | |
| P07948 LYN LYN_HUMAN |
1 | 7 | MGCIKSKGKDSLSDDGVDLK | U | 0 | Homo sapiens (Human) | |
| P07947 YES1 YES_HUMAN |
1 | 7 | MGCIKSKENKSPAIKYRPEN | U | 0 | Homo sapiens (Human) | |
| P09471 GNAO1 GNAO_HUMAN |
1 | 7 | MGCTLSAEERAALERSKAIE | TP | 0 | Homo sapiens (Human) | |
| P06239 LCK LCK_HUMAN |
1 | 7 | MGCGCSSHPEDDWMENIDVC | TP | 0 | Homo sapiens (Human) | |
| P19086 GNAZ GNAZ_HUMAN |
1 | 7 | MGCRQSSEEKEAARRSRRID | TP | 0 | Homo sapiens (Human) |
Please cite:
ELM-the Eukaryotic Linear Motif resource-2024 update.
(PMID:37962385)
ELM data can be downloaded & distributed for non-commercial use according to the ELM Software License Agreement
ELM data can be downloaded & distributed for non-commercial use according to the ELM Software License Agreement