Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyBromodomain 8084259 3001843 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
ABromodomaine5lkuA4 A: alpha bundlesX: Bromodomain-likeH: Bromodomain (From Topology)T: BromodomainF: BromodomainECOD (1.6)
AHAT_KAT11e5lkuA3 A: a+b three layersX: Nat/IvyH: Acyl-CoA N-acyltransferases (Nat) (From Topology)T: Acyl-CoA N-acyltransferases (Nat)F: HAT_KAT11ECOD (1.6)
ADUF902e5lkuA2 A: few secondary structure elementsX: RING/U-box-likeH: RING/U-box-likeT: RING/U-boxF: DUF902ECOD (1.6)
APHD_CBPe5lkuA1 A: few secondary structure elementsX: RING/U-box-likeH: RING/U-box-likeT: FYVE/PHD zinc fingerF: PHD_CBPECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A1.20.920.10 Mainly Alpha Up-down Bundle Histone Acetyltransferase Chain ACATH (4.3.0)
A2.10.110.40 Mainly Beta Ribbon Cysteine Rich Protein CREB-binding protein/p300 RING domainCATH (4.3.0)
A3.30.40.10 Alpha Beta 2-Layer Sandwich Herpes Virus-1 Zinc/RING finger domain, C3HC4 (zinc finger)CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF08214Histone acetylation protein (HAT_KAT11)Histone acetylation proteinHistone acetylation is required in many cellular processes including transcription, DNA repair, and chromatin assembly. This family contains the fungal KAT11 protein (previously known as RTT109) which is required for H3K56 acetylation. Loss of KAT11 ...Histone acetylation is required in many cellular processes including transcription, DNA repair, and chromatin assembly. This family contains the fungal KAT11 protein (previously known as RTT109) which is required for H3K56 acetylation. Loss of KAT11 results in the loss of H3K56 acetylation, both on bulk histone and on chromatin [1]. KAT11 and H3K56 acetylation appear to correlate with actively transcribed genes and associate with the elongating form of Pol II in yeast [1]. This family also incorporates the p300/CBP histone acetyltransferase domain which has different catalytic properties and cofactor regulation to KAT11 [3].
Domain
PF00439Bromodomain (Bromodomain)BromodomainBromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine [3].Domain
PF06001CREB-binding protein/p300, atypical RING domain (RING_CBP-p300)CREB-binding protein/p300, atypical RING domainCBP (CREB-binding protein) and p300 (also known as CREBBP or KAT3A and EP300 or KAT3B, respectively) are two histone acetyltransferases (HATs) that associate with and acetylate transcriptional regulators and chromatin. The catalytic core of animal CB ...CBP (CREB-binding protein) and p300 (also known as CREBBP or KAT3A and EP300 or KAT3B, respectively) are two histone acetyltransferases (HATs) that associate with and acetylate transcriptional regulators and chromatin. The catalytic core of animal CBP-p300 contains a bromodomain, a CH2 region containing a discontinuous PHD domain interrupted by this RING domain, and a HAT domain. Bromodomain-RING-PHD forms a compact module in which the RING domain is juxtaposed with the HAT substrate-binding site. This RING domain contains only a single zinc ion-binding cluster instead of two; instead of a second zinc atom, a network of hydrophobic interactions stabilizes the domain. The RING domain has an inhibitory role. Disease mutations that disrupt RING attachment lead to upregulation of HAT activity. HAT regulation may require repositioning of the RING domain to facilitate access to an otherwise partially occluded HAT active site. Plant CBP-p300 type HATs lack a bromodomain whose role in the animal animal CBP-p300's is to bind acetylated histones; it has been suggested that these plant proteins may utilise a different domain or another bromodomain protein to perform this function [1]. This RING domain has also been referred to as DUF902.
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
Histone acetyltransferase p300,Histone acetyltransferase p300

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
PharosQ09472