Q9C0B5 · ZDHC5_HUMAN
- ProteinPalmitoyltransferase ZDHHC5
- GeneZDHHC5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids715 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays an important role in the regulation of synapse efficacy by mediating palmitoylation of delta-catenin/CTNND2, thereby increasing synaptic delivery and surface stabilization of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors (AMPARs) (PubMed:26334723).
Under basal conditions, remains at the synaptic membrane through FYN-mediated phosphorylation that prevents association with endocytic proteins (PubMed:26334723).
Neuronal activity enhances the internalization and trafficking of DHHC5 from spines to dendritic shafts where it palmitoylates delta-catenin/CTNND2 (PubMed:26334723).
Regulates cell adhesion at the plasma membrane by palmitoylating GOLGA7B and DSG2 (PubMed:31402609).
Plays a role in innate immune response by mediating the palmitoylation of NOD1 and NOD2 and their proper recruitment to the bacterial entry site and phagosomes (PubMed:31649195, PubMed:34293401).
Participates also in fatty acid uptake by palmitoylating CD36 and thereby targeting it to the plasma membrane (PubMed:32958780).
Upon binding of fatty acids to CD36, gets phosphorylated by LYN leading to inactivation and subsequent CD36 caveolar endocytosis (PubMed:32958780).
Controls oligodendrocyte development by catalyzing STAT3 palmitoylation (By similarity).
Acts as a regulator of inflammatory response by mediating palmitoylation of NLRP3 and GSDMD (PubMed:38092000, PubMed:38599239, PubMed:38530158).
Palmitoylates NLRP3 to promote inflammasome assembly and activation (PubMed:38092000).
Activates pyroptosis by catalyzing palmitoylation of gasdermin-D (GSDMD), thereby promoting membrane translocation and pore formation of GSDMD (PubMed:38599239, PubMed:38530158).
Catalytic activity
- hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]This reaction proceeds in the forward direction.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 134 | S-palmitoyl cysteine intermediate | ||||
Sequence: C |
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Has protein S-acyltransferase activity. Palmitoylates GOLGA7B and DSG2. Interacts with GOLGA7B. ZDHHC5/GOLGA7B complex is involved in the regulation of cell adhesion.
Names & Taxonomy
Protein names
- Recommended namePalmitoyltransferase ZDHHC5
- EC number
- Alternative names
Gene names
- Community suggested namesDHHC5
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9C0B5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-13 | Cytoplasmic | ||||
Sequence: MPAESGKRFKPSK | ||||||
Transmembrane | 14-34 | Helical | ||||
Sequence: YVPVSAAAIFLVGATTLFFAF | ||||||
Topological domain | 35-38 | Extracellular | ||||
Sequence: TCPG | ||||||
Transmembrane | 39-59 | Helical | ||||
Sequence: LSLYVSPAVPIYNAIMFLFVL | ||||||
Topological domain | 60-148 | Cytoplasmic | ||||
Sequence: ANFSMATFMDPGIFPRAEEDEDKEDDFRAPLYKTVEIKGIQVRMKWCATCRFYRPPRCSHCSVCDNCVEEFDHHCPWVNNCIGRRNYRY | ||||||
Transmembrane | 149-169 | Helical | ||||
Sequence: FFLFLLSLTAHIMGVFGFGLL | ||||||
Topological domain | 170-191 | Extracellular | ||||
Sequence: YVLYHIEELSGVRTAVTMAVMC | ||||||
Transmembrane | 192-212 | Helical | ||||
Sequence: VAGLFFIPVAGLTGFHVVLVA | ||||||
Topological domain | 213-715 | Cytoplasmic | ||||
Sequence: RGRTTNEQVTGKFRGGVNPFTNGCCNNVSRVLCSSPAPRYLGRPKKEKTIVIRPPFLRPEVSDGQITVKIMDNGIQGELRRTKSKGSLEITESQSADAEPPPPPKPDLSRYTGLRTHLGLATNEDSSLLAKDSPPTPTMYKYRPGYSSSSTSAAMPHSSSAKLSRGDSLKEPTSIAESSRHPSYRSEPSLEPESFRSPTFGKSFHFDPLSSGSRSSSLKSAQGTGFELGQLQSIRSEGTTSTSYKSLANQTRNGSLSYDSLLTPSDSPDFESVQAGPEPDPPLGYTSPFLSARLAQQREAERHPRLVPTGPTHREPSPVRYDNLSRHIVASLQEREKLLRQSPPLPGREEEPGLGDSGIQSTPGSGHAPRTSSSSDDSKRSPLGKTPLGRPAVPRFGKPDGLRGRGVGSPEPGPTAPYLGRSMSYSSQKAQPGVSETEEVALQPLLTPKDEVQLKTTYSKSNGQPKSLGSASPGPGQPPLSSPTRGGVKKVSGVGGTTYEISV |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 91 | More than 50% loss of activity. | ||||
Sequence: Y → E | ||||||
Mutagenesis | 533 | More than 50% loss of FYN-mediated phosphorylation. | ||||
Sequence: Y → E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 692 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
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_0000212868 | 1-715 | UniProt | Palmitoyltransferase ZDHHC5 | |||
Sequence: MPAESGKRFKPSKYVPVSAAAIFLVGATTLFFAFTCPGLSLYVSPAVPIYNAIMFLFVLANFSMATFMDPGIFPRAEEDEDKEDDFRAPLYKTVEIKGIQVRMKWCATCRFYRPPRCSHCSVCDNCVEEFDHHCPWVNNCIGRRNYRYFFLFLLSLTAHIMGVFGFGLLYVLYHIEELSGVRTAVTMAVMCVAGLFFIPVAGLTGFHVVLVARGRTTNEQVTGKFRGGVNPFTNGCCNNVSRVLCSSPAPRYLGRPKKEKTIVIRPPFLRPEVSDGQITVKIMDNGIQGELRRTKSKGSLEITESQSADAEPPPPPKPDLSRYTGLRTHLGLATNEDSSLLAKDSPPTPTMYKYRPGYSSSSTSAAMPHSSSAKLSRGDSLKEPTSIAESSRHPSYRSEPSLEPESFRSPTFGKSFHFDPLSSGSRSSSLKSAQGTGFELGQLQSIRSEGTTSTSYKSLANQTRNGSLSYDSLLTPSDSPDFESVQAGPEPDPPLGYTSPFLSARLAQQREAERHPRLVPTGPTHREPSPVRYDNLSRHIVASLQEREKLLRQSPPLPGREEEPGLGDSGIQSTPGSGHAPRTSSSSDDSKRSPLGKTPLGRPAVPRFGKPDGLRGRGVGSPEPGPTAPYLGRSMSYSSQKAQPGVSETEEVALQPLLTPKDEVQLKTTYSKSNGQPKSLGSASPGPGQPPLSSPTRGGVKKVSGVGGTTYEISV | |||||||
Modified residue | 91 | UniProt | Phosphotyrosine; by LYN | ||||
Sequence: Y | |||||||
Modified residue | 247 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 247 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 274 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 294 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 296 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 296 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 299 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 299 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 303 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 303 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 339 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 345 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 345 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 348 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 348 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 350 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 352 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 362 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 370 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 376 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 380 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 380 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 385 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 395 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 396 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 398 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 398 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 406 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 406 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 409 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 409 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 411 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 411 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 415 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 415 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 422 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 423 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 425 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 425 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 427 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 428 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 429 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 429 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 432 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 432 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 436 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 436 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 455 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 458 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 521 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 524 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 529 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 529 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 533 | UniProt | Phosphotyrosine; by FYN | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 533 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 537 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 554 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 554 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 569 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 573 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 574 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 577 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 590 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 593 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 617 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 621 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 621 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 630 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 636 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 659 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 659 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 679 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 682 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 684 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 684 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 693 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 694 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 694 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 696 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 697 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 704 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 711 | PRIDE | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Phosphorylation by LYN during fatty acid uptake leads to inactivation of the activity (PubMed:32958780).
Palmitoylation of the C-terminal tail regulates stimulation-dependent plasma membrane motility (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9C0B5 | GOLGA7B Q2TAP0 | 4 | EBI-2799626, EBI-13310443 | |
XENO | Q9C0B5 | S P0DTC2 | 8 | EBI-2799626, EBI-25474821 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 104-154 | DHHC | ||||
Sequence: KWCATCRFYRPPRCSHCSVCDNCVEEFDHHCPWVNNCIGRRNYRYFFLFLL | ||||||
Region | 289-715 | Disordered | ||||
Sequence: GELRRTKSKGSLEITESQSADAEPPPPPKPDLSRYTGLRTHLGLATNEDSSLLAKDSPPTPTMYKYRPGYSSSSTSAAMPHSSSAKLSRGDSLKEPTSIAESSRHPSYRSEPSLEPESFRSPTFGKSFHFDPLSSGSRSSSLKSAQGTGFELGQLQSIRSEGTTSTSYKSLANQTRNGSLSYDSLLTPSDSPDFESVQAGPEPDPPLGYTSPFLSARLAQQREAERHPRLVPTGPTHREPSPVRYDNLSRHIVASLQEREKLLRQSPPLPGREEEPGLGDSGIQSTPGSGHAPRTSSSSDDSKRSPLGKTPLGRPAVPRFGKPDGLRGRGVGSPEPGPTAPYLGRSMSYSSQKAQPGVSETEEVALQPLLTPKDEVQLKTTYSKSNGQPKSLGSASPGPGQPPLSSPTRGGVKKVSGVGGTTYEISV | ||||||
Compositional bias | 331-345 | Polar residues | ||||
Sequence: GLATNEDSSLLAKDS | ||||||
Compositional bias | 354-405 | Polar residues | ||||
Sequence: YRPGYSSSSTSAAMPHSSSAKLSRGDSLKEPTSIAESSRHPSYRSEPSLEPE | ||||||
Compositional bias | 416-482 | Polar residues | ||||
Sequence: FHFDPLSSGSRSSSLKSAQGTGFELGQLQSIRSEGTTSTSYKSLANQTRNGSLSYDSLLTPSDSPDF | ||||||
Compositional bias | 570-593 | Polar residues | ||||
Sequence: GIQSTPGSGHAPRTSSSSDDSKRS | ||||||
Compositional bias | 632-646 | Polar residues | ||||
Sequence: GRSMSYSSQKAQPGV | ||||||
Compositional bias | 662-687 | Polar residues | ||||
Sequence: DEVQLKTTYSKSNGQPKSLGSASPGP |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9C0B5-1
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
- Length715
- Mass (Da)77,545
- Last updated2003-02-01 v2
- Checksum9E4FB0C9AC8EFE28
Q9C0B5-2
- Name2
- Differences from canonical
- 1-53: Missing
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_006935 | 1-53 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 331-345 | Polar residues | ||||
Sequence: GLATNEDSSLLAKDS | ||||||
Compositional bias | 354-405 | Polar residues | ||||
Sequence: YRPGYSSSSTSAAMPHSSSAKLSRGDSLKEPTSIAESSRHPSYRSEPSLEPE | ||||||
Compositional bias | 416-482 | Polar residues | ||||
Sequence: FHFDPLSSGSRSSSLKSAQGTGFELGQLQSIRSEGTTSTSYKSLANQTRNGSLSYDSLLTPSDSPDF | ||||||
Sequence conflict | 508-509 | in Ref. 6; CAB56033 | ||||
Sequence: QQ → TR | ||||||
Compositional bias | 570-593 | Polar residues | ||||
Sequence: GIQSTPGSGHAPRTSSSSDDSKRS | ||||||
Compositional bias | 632-646 | Polar residues | ||||
Sequence: GRSMSYSSQKAQPGV | ||||||
Compositional bias | 662-687 | Polar residues | ||||
Sequence: DEVQLKTTYSKSNGQPKSLGSASPGP |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB051535 EMBL· GenBank· DDBJ | BAB21839.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AY894889 EMBL· GenBank· DDBJ | AAX73368.1 EMBL· GenBank· DDBJ | mRNA | ||
AK023130 EMBL· GenBank· DDBJ | BAB14420.1 EMBL· GenBank· DDBJ | mRNA | ||
AK172807 EMBL· GenBank· DDBJ | BAD18778.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
CH471076 EMBL· GenBank· DDBJ | EAW73771.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC026967 EMBL· GenBank· DDBJ | AAH26967.1 EMBL· GenBank· DDBJ | mRNA | ||
AL117662 EMBL· GenBank· DDBJ | CAB56033.1 EMBL· GenBank· DDBJ | mRNA |