Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
CPF00595e3rl7C1 A: beta barrelsX: PDZ domain (From Topology)H: PDZ domain (From Topology)T: PDZ domainF: PF00595ECOD (1.6)
DPF00595e3rl7D1 A: beta barrelsX: PDZ domain (From Topology)H: PDZ domain (From Topology)T: PDZ domainF: PF00595ECOD (1.6)
A [auth B]PF00595e3rl7B1 A: beta barrelsX: PDZ domain (From Topology)H: PDZ domain (From Topology)T: PDZ domainF: PF00595ECOD (1.6)
B [auth A]PF00595e3rl7A1 A: beta barrelsX: PDZ domain (From Topology)H: PDZ domain (From Topology)T: PDZ domainF: PF00595ECOD (1.6)
EPF00595e3rl7E1 A: beta barrelsX: PDZ domain (From Topology)H: PDZ domain (From Topology)T: PDZ domainF: PF00595ECOD (1.6)
FPF00595e3rl7F1 A: beta barrelsX: PDZ domain (From Topology)H: PDZ domain (From Topology)T: PDZ domainF: PF00595ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
C2.30.42.10 Mainly Beta Roll Pdz3 Domain PDZ domainCATH (4.3.0)
D2.30.42.10 Mainly Beta Roll Pdz3 Domain PDZ domainCATH (4.3.0)
A [auth B]2.30.42.10 Mainly Beta Roll Pdz3 Domain PDZ domainCATH (4.3.0)
B [auth A]2.30.42.10 Mainly Beta Roll Pdz3 Domain PDZ domainCATH (4.3.0)
E2.30.42.10 Mainly Beta Roll Pdz3 Domain PDZ domainCATH (4.3.0)
F2.30.42.10 Mainly Beta Roll Pdz3 Domain PDZ domainCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
G, H, I, J, K
PF05937EB-1 Binding Domain (EB1_binding)EB-1 Binding Domain- Family
PF10608Polyubiquitination (PEST) N-terminal domain of MAGUK (MAGUK_N_PEST)Polyubiquitination (PEST) N-terminal domain of MAGUKThe residues upstream of this domain are the probable palmitoylation sites, particularly two cysteines. The domain has a putative PEST site at the very start that seems to be responsible for poly-ubiquitination [1]. PEST domains are polypeptide seque ...The residues upstream of this domain are the probable palmitoylation sites, particularly two cysteines. The domain has a putative PEST site at the very start that seems to be responsible for poly-ubiquitination [1]. PEST domains are polypeptide sequences enriched in proline (P), glutamic acid (E), serine (S) and threonine (T) that target proteins for rapid destruction. The whole domain, in conjunction with a C-terminal domain of the longer protein, is necessary for dimerisation of the whole protein [2].
Domain
PF00595PDZ domain (PDZ)PDZ domainPDZ domains are found in diverse signaling proteins.Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
G, H, I, J, K
11-mer peptide from Adenomatous polyposis coli protein
Disks large homolog 1

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
G, H, I, J, K
IPR016024Armadillo-type foldHomologous Superfamily
G, H, I, J, K
IPR009240Adenomatous polyposis coli protein, 15 residue repeatRepeat
G, H, I, J, K
IPR009232EB-1 bindingDomain
G, H, I, J, K
IPR000225ArmadilloRepeat
G, H, I, J, K
IPR009223Adenomatous polyposis coli protein repeatRepeat
G, H, I, J, K
IPR026818Adenomatous polyposis coli (APC) familyFamily
G, H, I, J, K
IPR036149APC, N-terminal coiled-coil domain superfamilyHomologous Superfamily
G, H, I, J, K
IPR009224SAMPRepeat
G, H, I, J, K
IPR011989Armadillo-like helicalHomologous Superfamily
G, H, I, J, K
IPR041257Adenomatous polyposis coli (APC) repeatRepeat
G, H, I, J, K
IPR026831Adenomatous polyposis coli proteinHomologous Superfamily
G, H, I, J, K
IPR009234Adenomatous polyposis coli protein basic domainDomain
G, H, I, J, K
IPR032038Adenomatous polyposis coli, N-terminal dimerisation domainDomain
IPR015143L27-1Domain
IPR016313Disks large 1-likeFamily
IPR019590Disks large homologue 1, N-terminal PEST domainDomain
IPR008144Guanylate kinase-like domainDomain
IPR008145Guanylate kinase/L-type calcium channel beta subunitDomain
IPR001478PDZ domainDomain
IPR036028SH3-like domain superfamilyHomologous Superfamily
IPR020590Guanylate kinase, conserved siteConserved Site
IPR019583Disks large homolog 1-4, PDZ-associated domainDomain
IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
IPR001452SH3 domainDomain
IPR004172L27 domainDomain
IPR036034PDZ superfamilyHomologous Superfamily
IPR036892L27 domain superfamilyHomologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
G, H, I, J, K
PharosP25054
PharosQ12959