Q5W0Z9 · ZDH20_HUMAN
- ProteinPalmitoyltransferase ZDHHC20
- GeneZDHHC20
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids365 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes palmitoylation of Cys residues in the cytoplasmic C-terminus of EGFR, and modulates the duration of EGFR signaling by modulating palmitoylation-dependent EGFR internalization and degradation (PubMed:27153536).
Has a preference for acyl-CoA with C16 fatty acid chains (PubMed:29326245).
Can also utilize acyl-CoA with C14 and C18 fatty acid chains (PubMed:29326245).
May palmitoylate CALHM1 subunit of gustatory voltage-gated ion channels and modulate channel gating and kinetics
Catalytic activity
- hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]This reaction proceeds in the forward direction.
- L-cysteinyl-[protein] + tetradecanoyl-CoA = CoA + S-tetradecanoyl-L-cysteinyl-[protein]This reaction proceeds in the forward direction.
- L-cysteinyl-[protein] + octadecanoyl-CoA = CoA + S-octadecanoyl-L-cysteinyl-[protein]This reaction proceeds in the forward direction.
Features
Showing features for site, binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 29 | Important for selectivity toward medium-length fatty acids | ||||
Sequence: S | ||||||
Binding site | 128 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 131 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 135 | substrate | ||||
Sequence: K | ||||||
Binding site | 140-143 | substrate | ||||
Sequence: HHCS | ||||||
Binding site | 141 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 142 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 145 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 148 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 155 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 156 | S-palmitoyl cysteine intermediate | ||||
Sequence: C | ||||||
Binding site | 162 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Site | 181 | Important for selectivity toward medium-length fatty acids | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | endoplasmic reticulum-Golgi intermediate compartment membrane | |
Cellular Component | Golgi apparatus | |
Cellular Component | Golgi membrane | |
Cellular Component | intracellular membrane-bounded organelle | |
Cellular Component | membrane | |
Cellular Component | perinuclear region of cytoplasm | |
Cellular Component | plasma membrane | |
Molecular Function | palmitoyltransferase activity | |
Molecular Function | protein-cysteine S-myristoyltransferase activity | |
Molecular Function | protein-cysteine S-palmitoyltransferase activity | |
Molecular Function | protein-cysteine S-stearoyltransferase activity | |
Molecular Function | zinc ion binding | |
Biological Process | peptidyl-L-cysteine S-palmitoylation | |
Biological Process | positive regulation by host of viral process | |
Biological Process | protein palmitoylation | |
Biological Process | protein targeting to membrane | |
Biological Process | synaptic vesicle maturation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePalmitoyltransferase ZDHHC20
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ5W0Z9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-14 | Cytoplasmic | ||||
Sequence: MAPWTLWRCCQRVV | ||||||
Transmembrane | 15-35 | Helical | ||||
Sequence: GWVPVLFITFVVVWSYYAYVV | ||||||
Topological domain | 36-53 | Lumenal | ||||
Sequence: ELCVFTIFGNEENGKTVV | ||||||
Transmembrane | 54-74 | Helical | ||||
Sequence: YLVAFHLFFVMFVWSYWMTIF | ||||||
Topological domain | 75-169 | Cytoplasmic | ||||
Sequence: TSPASPSKEFYLSNSEKERYEKEFSQERQQEILRRAARALPIYTTSASKTIRYCEKCQLIKPDRAHHCSACDSCILKMDHHCPWVNNCVGFSNYK | ||||||
Transmembrane | 170-190 | Helical | ||||
Sequence: FFLLFLLYSLLYCLFVAATVL | ||||||
Topological domain | 191-207 | Lumenal | ||||
Sequence: EYFIKFWTNELTDTRAK | ||||||
Transmembrane | 208-231 | Helical | ||||
Sequence: FHVLFLFFVSAMFFISVLSLFSYH | ||||||
Topological domain | 232-365 | Cytoplasmic | ||||
Sequence: CWLVGKNRTTIESFRAPTFSYGPDGNGFSLGCSKNWRQVFGDEKKYWLLPIFSSLGDGCSFPTRLVGMDPEQASVTNQNEYARSSGSNQPFPIKPLSESKNRLLDSESQWLENGAEEGIVKSGTNNHVTVAIEN |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 22 | Strongly reduced catalytic activity. | ||||
Sequence: I → W | ||||||
Mutagenesis | 29 | Strongly reduced catalytic activity. Enhances activity with acyl-CoA with C12 and C14 fatty acid chains. | ||||
Sequence: S → F | ||||||
Mutagenesis | 153 | Loss of catalytic activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 154 | Loss of catalytic activity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 156 | Loss of catalytic activity. | ||||
Sequence: C → S | ||||||
Mutagenesis | 158 | Strongly reduced catalytic activity. | ||||
Sequence: W → A | ||||||
Mutagenesis | 171 | Loss of catalytic activity. | ||||
Sequence: F → A | ||||||
Mutagenesis | 174 | Strongly reduced catalytic activity. | ||||
Sequence: F → A | ||||||
Mutagenesis | 181 | Moderately reduced catalytic activity. Enhances activity with acyl-CoA with C18 and C20 fatty acid chains. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 227 | Loss of catalytic activity. | ||||
Sequence: L → W | ||||||
Mutagenesis | 240-241 | Loss of catalytic activity. | ||||
Sequence: TT → AA | ||||||
Mutagenesis | 243 | Mildly reduced catalytic activity. | ||||
Sequence: E → A | ||||||
Mutagenesis | 266 | Strongly reduced catalytic activity. | ||||
Sequence: N → A | ||||||
Mutagenesis | 267 | Loss of catalytic activity. | ||||
Sequence: Missing | ||||||
Mutagenesis | 271 | Mildly reduced catalytic activity. | ||||
Sequence: F → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 412 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000212906 | 1-365 | UniProt | Palmitoyltransferase ZDHHC20 | |||
Sequence: MAPWTLWRCCQRVVGWVPVLFITFVVVWSYYAYVVELCVFTIFGNEENGKTVVYLVAFHLFFVMFVWSYWMTIFTSPASPSKEFYLSNSEKERYEKEFSQERQQEILRRAARALPIYTTSASKTIRYCEKCQLIKPDRAHHCSACDSCILKMDHHCPWVNNCVGFSNYKFFLLFLLYSLLYCLFVAATVLEYFIKFWTNELTDTRAKFHVLFLFFVSAMFFISVLSLFSYHCWLVGKNRTTIESFRAPTFSYGPDGNGFSLGCSKNWRQVFGDEKKYWLLPIFSSLGDGCSFPTRLVGMDPEQASVTNQNEYARSSGSNQPFPIKPLSESKNRLLDSESQWLENGAEEGIVKSGTNNHVTVAIEN | |||||||
Modified residue | 305 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 305 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 307 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 312 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 315 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 316 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 318 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 328 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 330 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 330 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 339 | UniProt | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q5W0Z9-4 | CTSD P07339 | 3 | EBI-25840130, EBI-2115097 | |
BINARY | Q5W0Z9-4 | RNF11 Q9Y3C5 | 3 | EBI-25840130, EBI-396669 | |
BINARY | Q5W0Z9-4 | WFS1 O76024 | 3 | EBI-25840130, EBI-720609 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 126-176 | DHHC | ||||
Sequence: RYCEKCQLIKPDRAHHCSACDSCILKMDHHCPWVNNCVGFSNYKFFLLFLL |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q5W0Z9-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length365
- Mass (Da)42,278
- Last updated2004-12-07 v1
- Checksum179D8882138E4F53
Q5W0Z9-2
- Name2
Q5W0Z9-3
- Name3
Q5W0Z9-4
- Name4
- Differences from canonical
- 315-365: SSGSNQPFPIKPLSESKNRLLDSESQWLENGAEEGIVKSGTNNHVTVAIEN → RSKLQR
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
B4DRN8 | B4DRN8_HUMAN | ZDHHC20 | 292 | ||
A0A0D9SEN4 | A0A0D9SEN4_HUMAN | ZDHHC20 | 19 | ||
A0A8V8TR49 | A0A8V8TR49_HUMAN | ZDHHC20 | 138 |
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_016276 | 124-130 | in isoform 2 | |||
Sequence: TIRYCEK → SLMQSTK | ||||||
Alternative sequence | VSP_016277 | 131-365 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_040481 | 315 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_056002 | 315-365 | in isoform 4 | |||
Sequence: SSGSNQPFPIKPLSESKNRLLDSESQWLENGAEEGIVKSGTNNHVTVAIEN → RSKLQR | ||||||
Alternative sequence | VSP_040482 | 355-365 | in isoform 3 | |||
Sequence: TNNHVTVAIEN → V |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL136219 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471075 EMBL· GenBank· DDBJ | EAX08309.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC034944 EMBL· GenBank· DDBJ | AAH34944.1 EMBL· GenBank· DDBJ | mRNA | ||
BC050367 EMBL· GenBank· DDBJ | AAH50367.2 EMBL· GenBank· DDBJ | mRNA | ||
BC067898 EMBL· GenBank· DDBJ | AAH67898.1 EMBL· GenBank· DDBJ | mRNA | ||
BC110517 EMBL· GenBank· DDBJ | AAI10518.1 EMBL· GenBank· DDBJ | mRNA |