Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyBromodomain 8084259 3001843 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyBromodomain 8084259 3001843 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
ABromodomaine6gytA2 A: alpha bundlesX: Bromodomain-likeH: Bromodomain (From Topology)T: BromodomainF: BromodomainECOD (1.6)
APHD_CBPe6gytA1 A: few secondary structure elementsX: RING/U-box-likeH: RING/U-box-likeT: FYVE/PHD zinc fingerF: PHD_CBPECOD (1.6)
BBromodomaine6gytB1 A: alpha bundlesX: Bromodomain-likeH: Bromodomain (From Topology)T: BromodomainF: BromodomainECOD (1.6)
BPHD_CBPe6gytB2 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

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
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
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
Histone H4

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
IPR043145Zinc finger, ZZ-type superfamilyHomologous Superfamily
IPR018359Bromodomain, conserved siteConserved Site
IPR036529Coactivator CBP, KIX domain superfamilyHomologous Superfamily
IPR009110Nuclear receptor coactivator, interlockingHomologous Superfamily
IPR000433Zinc finger, ZZ-typeDomain
IPR013178Histone acetyltransferase Rtt109/CBPFamily
IPR013083Zinc finger, RING/FYVE/PHD-typeHomologous Superfamily
IPR010303CREB-binding protein/p300, atypical RING domainDomain
IPR037073Nuclear receptor coactivator, CREB-bp-like, interlocking domain superfamilyHomologous Superfamily
IPR014744Nuclear receptor coactivator, CREB-bp-like, interlockingDomain
IPR038547CBP/p300, atypical RING domain superfamilyHomologous Superfamily
IPR000197Zinc finger, TAZ-typeDomain
IPR003101Coactivator CBP, KIX domainDomain
IPR036427Bromodomain-like superfamilyHomologous Superfamily
IPR001487BromodomainDomain
IPR035898TAZ domain superfamilyHomologous Superfamily
IPR031162CBP/p300-type histone acetyltransferase domainDomain
IPR043145Zinc finger, ZZ-type superfamilyHomologous Superfamily
IPR018359Bromodomain, conserved siteConserved Site
IPR036529Coactivator CBP, KIX domain superfamilyHomologous Superfamily
IPR009110Nuclear receptor coactivator, interlockingHomologous Superfamily
IPR000433Zinc finger, ZZ-typeDomain
IPR013178Histone acetyltransferase Rtt109/CBPFamily
IPR013083Zinc finger, RING/FYVE/PHD-typeHomologous Superfamily
IPR010303CREB-binding protein/p300, atypical RING domainDomain
IPR037073Nuclear receptor coactivator, CREB-bp-like, interlocking domain superfamilyHomologous Superfamily
IPR014744Nuclear receptor coactivator, CREB-bp-like, interlockingDomain
IPR038547CBP/p300, atypical RING domain superfamilyHomologous Superfamily
IPR000197Zinc finger, TAZ-typeDomain
IPR003101Coactivator CBP, KIX domainDomain
IPR036427Bromodomain-like superfamilyHomologous Superfamily
IPR001487BromodomainDomain
IPR035898TAZ domain superfamilyHomologous Superfamily
IPR031162CBP/p300-type histone acetyltransferase domainDomain
IPR009072Histone-foldHomologous Superfamily
IPR001951Histone H4Family
IPR035425CENP-T/Histone H4, histone foldDomain
IPR019809Histone H4, conserved siteConserved Site
IPR004823TATA box binding protein associated factor (TAF), histone-like fold domainDomain

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
PharosQ09472
PharosQ09472

Protein Modification Annotation

Modified Residue(s)
ChainResidue(s)Description
ALY Parent Component: LYS

RESIDAA0055

PSI-MOD :  N6-acetyl-L-lysine MOD:00064