Q9BWD1 · THIC_HUMAN
- ProteinAcetyl-CoA acetyltransferase, cytosolic
- GeneACAT2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids397 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the biosynthetic pathway of cholesterol.
Catalytic activity
- 2 acetyl-CoA = acetoacetyl-CoA + CoAThis reaction proceeds in the backward direction.
Pathway
Lipid metabolism; fatty acid metabolism.
Features
Showing features for active site, binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 92 | Acyl-thioester intermediate | ||||
Sequence: C | ||||||
Binding site | 223 | CoA (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 226 | CoA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 252 | CoA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Site | 353 | Increases nucleophilicity of active site Cys | ||||
Sequence: H | ||||||
Active site | 383 | Proton donor/acceptor | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | extracellular exosome | |
Cellular Component | mitochondrion | |
Molecular Function | acetyl-CoA C-acetyltransferase activity | |
Biological Process | fatty acid beta-oxidation | |
Biological Process | lipid metabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameAcetyl-CoA acetyltransferase, cytosolic
- 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 accessionQ9BWD1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_019686 | 211 | in dbSNP:rs25683 | |||
Sequence: K → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 427 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 modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000206409 | 1-397 | Acetyl-CoA acetyltransferase, cytosolic | |||
Sequence: MNAGSDPVVIVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWSCQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHLAYLRTGVKIGEMPLTDSILCDGLTDAFHNCHMGITAENVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGLIEVKTDEFPRHGSNIEAMSKLKPYFLTDGTGTVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQRE | ||||||
Modified residue | 200 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 233 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 235 | N6-acetyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Interaction
Subunit
Homotetramer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9BWD1 | LNX1 Q8TBB1 | 3 | EBI-1047273, EBI-739832 | |
BINARY | Q9BWD1 | TERF1 P54274 | 2 | EBI-1047273, EBI-710997 | |
BINARY | Q9BWD1 | WWOX Q9NZC7-5 | 3 | EBI-1047273, EBI-12040603 | |
BINARY | Q9BWD1 | ZNF76 P36508 | 3 | EBI-1047273, EBI-7254550 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9BWD1-1
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
- Length397
- Mass (Da)41,351
- Last updated2004-09-13 v2
- ChecksumE3A8DAFB6F341B18
Q9BWD1-2
- Name2
- Differences from canonical
- 1-19: MNAGSDPVVIVSAARTIIG → MGSHPVLRIWGNRRATAASLGRSGGRLSSPRLLRVVAPTLTFAQTSRC
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_056217 | 1-19 | in isoform 2 | |||
Sequence: MNAGSDPVVIVSAARTIIG → MGSHPVLRIWGNRRATAASLGRSGGRLSSPRLLRVVAPTLTFAQTSRC | ||||||
Sequence conflict | 169 | in Ref. 1; AAB30856 | ||||
Sequence: K → T | ||||||
Sequence conflict | 262 | in Ref. 1; AAB30856 | ||||
Sequence: V → A | ||||||
Sequence conflict | 375 | in Ref. 2; AAM00223 | ||||
Sequence: R → G |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
S70154 EMBL· GenBank· DDBJ | AAB30856.1 EMBL· GenBank· DDBJ | mRNA | ||
AF356877 EMBL· GenBank· DDBJ | AAM00223.1 EMBL· GenBank· DDBJ | mRNA | ||
AK294273 EMBL· GenBank· DDBJ | BAH11719.1 EMBL· GenBank· DDBJ | mRNA | ||
AL135914 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471051 EMBL· GenBank· DDBJ | EAW47619.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471051 EMBL· GenBank· DDBJ | EAW47620.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC000408 EMBL· GenBank· DDBJ | AAH00408.1 EMBL· GenBank· DDBJ | mRNA |