palmitoyltransferase ZDHHC12 isoform 3 [Homo sapiens]
Protein Classification
DHHC palmitoyltransferase family protein( domain architecture ID 139791)
DHHC palmitoyltransferase family protein may catalyze the post-translational modification that involves the attachment of palmitic acid to Cys residues through a thioester linkage
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| DHHC super family | cl19890 | DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ... |
123-165 | 1.80e-11 | ||
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which are palmitoyltransferases. Palmitoylation or, more specifically S-acylation, plays important roles in the regulation of protein localization, stability, and activity. It is a post-translational protein modification that involves the attachment of palmitic acid to Cys residues through a thioester linkage. Protein acyltransferases (PATs), also known as palmitoyltransferases, catalyze this reaction by transferring the palmitoyl group from palmitoyl-CoA to the thiol group of Cys residues. They are characterized by the presence of a 50-residue-long domain called the DHHC domain, which in most but not all cases is also cysteine-rich and gets its name from a highly conserved DHHC signature tetrapeptide (Asp-His-His-Cys). The Cys residue within the DHHC domain forms a stable acyl intermediate and transfers the acyl chain to the Cys residues of a target protein. Some proteins containing a DHHC domain include Drosophila DNZ1 protein, Mouse Abl-philin 2 (Aph2) protein, Mammalian ZDHHC9, Yeast ankyrin repeat-containing protein AKR1, Yeast Erf2 protein, and Arabidopsis thaliana tip growth defective 1. The actual alignment was detected with superfamily member pfam01529: Pssm-ID: 418707 Cd Length: 132 Bit Score: 59.69 E-value: 1.80e-11
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| Name | Accession | Description | Interval | E-value | ||
| DHHC | pfam01529 | DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ... |
123-165 | 1.80e-11 | ||
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which are palmitoyltransferases. Palmitoylation or, more specifically S-acylation, plays important roles in the regulation of protein localization, stability, and activity. It is a post-translational protein modification that involves the attachment of palmitic acid to Cys residues through a thioester linkage. Protein acyltransferases (PATs), also known as palmitoyltransferases, catalyze this reaction by transferring the palmitoyl group from palmitoyl-CoA to the thiol group of Cys residues. They are characterized by the presence of a 50-residue-long domain called the DHHC domain, which in most but not all cases is also cysteine-rich and gets its name from a highly conserved DHHC signature tetrapeptide (Asp-His-His-Cys). The Cys residue within the DHHC domain forms a stable acyl intermediate and transfers the acyl chain to the Cys residues of a target protein. Some proteins containing a DHHC domain include Drosophila DNZ1 protein, Mouse Abl-philin 2 (Aph2) protein, Mammalian ZDHHC9, Yeast ankyrin repeat-containing protein AKR1, Yeast Erf2 protein, and Arabidopsis thaliana tip growth defective 1. Pssm-ID: 396215 Cd Length: 132 Bit Score: 59.69 E-value: 1.80e-11
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| COG5273 | COG5273 | Uncharacterized protein containing DHHC-type Zn finger [General function prediction only]; |
123-161 | 6.76e-08 | ||
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only]; Pssm-ID: 227598 [Multi-domain] Cd Length: 309 Bit Score: 52.06 E-value: 6.76e-08
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| Name | Accession | Description | Interval | E-value | ||
| DHHC | pfam01529 | DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ... |
123-165 | 1.80e-11 | ||
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which are palmitoyltransferases. Palmitoylation or, more specifically S-acylation, plays important roles in the regulation of protein localization, stability, and activity. It is a post-translational protein modification that involves the attachment of palmitic acid to Cys residues through a thioester linkage. Protein acyltransferases (PATs), also known as palmitoyltransferases, catalyze this reaction by transferring the palmitoyl group from palmitoyl-CoA to the thiol group of Cys residues. They are characterized by the presence of a 50-residue-long domain called the DHHC domain, which in most but not all cases is also cysteine-rich and gets its name from a highly conserved DHHC signature tetrapeptide (Asp-His-His-Cys). The Cys residue within the DHHC domain forms a stable acyl intermediate and transfers the acyl chain to the Cys residues of a target protein. Some proteins containing a DHHC domain include Drosophila DNZ1 protein, Mouse Abl-philin 2 (Aph2) protein, Mammalian ZDHHC9, Yeast ankyrin repeat-containing protein AKR1, Yeast Erf2 protein, and Arabidopsis thaliana tip growth defective 1. Pssm-ID: 396215 Cd Length: 132 Bit Score: 59.69 E-value: 1.80e-11
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| COG5273 | COG5273 | Uncharacterized protein containing DHHC-type Zn finger [General function prediction only]; |
123-161 | 6.76e-08 | ||
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only]; Pssm-ID: 227598 [Multi-domain] Cd Length: 309 Bit Score: 52.06 E-value: 6.76e-08
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