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Group by :Switch typeMotif classProteinEnzymePathway            Group Index    Colouring Info              Filtered: PFAM:PF00595 (51 hits) x


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  Domain hiding  Altered binding specificity  Motif hiding  Composite binding site formation
  Uncategorised  Rheostatic  Allostery  Avidity-sensing
  Physicochemical compatibility  Pre-translational  Competition

x  Index
Type: Binary Subtype: AllosteryType: Binary Subtype: Physicochemical compatibilityType: Binary Subtype: Pre‑translational
Type: Specificity Subtype: CompetitionType: Specificity Subtype: Domain hidingType: Specificity Subtype: Motif hiding


ProteinMotifStartEndSwitch descriptionInformation

Type: Specificity Subtype: Domain hiding
A domain can be sterically masked by binding of an effector when there is a large difference in intrinsic affinity of the domain for different binding partners, or a large difference in the local abundance of these partners, thereby precluding further interactions of the domain. Binding of the masking molecule can be PTM-dependent or -independent.
APBA1_HUMANLIG_PDZ_Class_2832837An intramolecular interaction of the C-terminal PDZ binding motif of Amyloid beta A4 precursor protein-binding family A member 1 (APBA1) (also known as X11alpha/Mint1) with the PDZ domain tandem of APBA1 results in an auto-inhibited conformation of APBA1, where binding of ligands containing a PDZ binding motif such as Presenilin-1 (PSEN1) is blocked. Binding of these ligands might be regulated by phosphorylation of Y836 in the APBA1 PDZ-binding motif, as its mutation to glutamate releases autoinhibition and enhances the interaction of the APBA1 PDZ tandem with presenilin.
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PSN1_HUMANLIG_PDZ_Class_2462467An intramolecular interaction of the C-terminal PDZ binding motif of Amyloid beta A4 precursor protein-binding family A member 1 (APBA1) (also known as X11alpha/Mint1) with the PDZ domain tandem of APBA1 results in an auto-inhibited conformation of APBA1, where binding of ligands containing a PDZ binding motif such as Presenilin-1 (PSEN1) is blocked. Binding of these ligands might be regulated by phosphorylation of Y836 in the APBA1 PDZ-binding motif, as its mutation to glutamate releases autoinhibition and enhances the interaction of the APBA1 PDZ tandem with presenilin.
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NHRF1_HUMANLIG_PDZ_Class_1353358Binding of Ezrin via its FERM domain to the EB domain of Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1) results in allosteric coupling to the second PDZ domain of SLC9A3R1. This relieves the intramolecular interaction with the SLC9A3R1 PDZ-binding ligand and increases the affinity of the PDZ domain for other ligands including Catenin beta-1 (CTNNB1).
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CTNB1_HUMANLIG_PDZ_Class_1776781Binding of Ezrin via its FERM domain to the EB domain of Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1) results in allosteric coupling to the second PDZ domain of SLC9A3R1. This relieves the intramolecular interaction with the SLC9A3R1 PDZ-binding ligand and increases the affinity of the PDZ domain for other ligands including Catenin beta-1 (CTNNB1).
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GRM5_RATLIG_PDZ_Class_111981203Binding of the PDZ-binding motif of General receptor for phosphoinositides 1-associated scaffold protein (Grasp) (Tamalin) to the Tamalin (Grasp) PDZ domain locks this protein in an auto-inhibited conformation. Binding of the PDZ-binding motif of Metabotropic glutamate receptor 5 (Grm5) to the Tamalin (Grasp) PDZ domain results in disruption of the weaker intramolecular Tamalin (Grasp) interactions. The PDZ-binding motif of Tamalin (Grasp) becomes available to interact with the PDZ domain of Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2 (Magi2) (S-SCAM), which functions as a receptor for kinesin motor proteins. See also switch details.
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GRASP_RATLIG_PDZ_Class_1389394Binding of the PDZ-binding motif of General receptor for phosphoinositides 1-associated scaffold protein (Grasp) (Tamalin) to the Tamalin (Grasp) PDZ domain locks this protein in an auto-inhibited conformation. Binding of the PDZ-binding motif of Metabotropic glutamate receptor 5 (Grm5) to the Tamalin (Grasp) PDZ domain results in disruption of the weaker intramolecular Tamalin (Grasp) interactions. The PDZ-binding motif of Tamalin (Grasp) becomes available to interact with the PDZ domain of Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2 (Magi2) (S-SCAM), which functions as a receptor for kinesin motor proteins. See also switch details.
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Type: Specificity Subtype: Competition
Competitive binding of multiple binding partners to overlapping or adjacent, mutually exclusive interaction interfaces depends on local target protein abundance, which can be regulated by changing the expression level or subcellular localisation of the competitors, or by scaffolding.
CFTR_HUMANLIG_PDZ_Class_114751480The PDZ domains of Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1) and SH3 and multiple ankyrin repeat domains protein 2 (SHANK2) compete for the PDZ-binding motif of Cystic fibrosis transmembrane conductance regulator (CFTR). SLC9A3R1 positively regulates CFTR activity by recruiting a PKA-containing complex, while SH3 and multiple ankyrin repeat domains protein 2 (SHANK2) negatively affects CFTR activity by recruiting PDE4D.
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CFTR_HUMANLIG_PDZ_Class_114751480The PDZ domains of Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1) and SH3 and multiple ankyrin repeat domains protein 2 (SHANK2) compete for the PDZ-binding motif of Cystic fibrosis transmembrane conductance regulator (CFTR). SLC9A3R1 positively regulates CFTR activity by recruiting a PKA-containing complex, while SH3 and multiple ankyrin repeat domains protein 2 (SHANK2) negatively affects CFTR activity by recruiting PDE4D.
details

Type: Specificity Subtype: Motif hiding
Motif hiding occurs when there is a large difference in intrinsic affinity of overlapping or adjacent motifs for their respective binding partners, or a large difference in the local abundance of these partners. Binding of an effector to one motif sterically masks the overlapping or adjacent motif, thereby precluding it from binding. Binding of the masking molecule can be PTM-dependent or -independent.
GRASP_RATLIG_PDZ_Class_1389394Binding of the PDZ-binding motif of General receptor for phosphoinositides 1-associated scaffold protein (Grasp) (Tamalin) to the Tamalin Grasp PDZ domain locks this protein in an auto-inhibited conformation. Binding of the PDZ-binding motif of Metabotropic glutamate receptor 5 (Grm5) to the Tamalin GraspPDZ domain results in disruption of the weaker intramolecular Tamalin (Grasp) interactions. The PDZ-binding motif of Tamalin (General receptor for phosphoinositides 1-associated scaffold protein (Grasp)) becomes available to interact with the PDZ domain of Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2 (Magi2) (S-SCAM), which functions as a receptor for kinesin motor proteins. See also switch details.
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GRASP_RATLIG_PDZ_Class_1389394Binding of the PDZ-binding motif of General receptor for phosphoinositides 1-associated scaffold protein (Grasp) (Tamalin) to the Tamalin Grasp PDZ domain locks this protein in an auto-inhibited conformation. Binding of the PDZ-binding motif of Metabotropic glutamate receptor 5 (Grm5) to the Tamalin GraspPDZ domain results in disruption of the weaker intramolecular Tamalin (Grasp) interactions. The PDZ-binding motif of Tamalin (General receptor for phosphoinositides 1-associated scaffold protein (Grasp)) becomes available to interact with the PDZ domain of Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2 (Magi2) (S-SCAM), which functions as a receptor for kinesin motor proteins. See also switch details.
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NMDZ1_HUMANLIG_PDZ_Class_1917922Binding of the PDZ domain of Disks large homolog 4 (DLG4) suppresses the ER-retention motif of Isoform 4 of Glutamate receptor subunit zeta-1 (GRIN1) in a splice variant-specific manner, thereby promoting cell surface expression of this particular isoform. This supports the hypothesis that local regulation of receptor exit from neuronal ER plays a role in modifying discrete synaptic receptor number.
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NMDZ1_HUMANLIG_PDZ_Class_1917922Binding of the PDZ domain of Disks large homolog 4 (DLG4) suppresses the ER-retention motif of Isoform 4 of Glutamate receptor subunit zeta-1 (GRIN1) in a splice variant-specific manner, thereby promoting cell surface expression of this particular isoform. This supports the hypothesis that local regulation of receptor exit from neuronal ER plays a role in modifying discrete synaptic receptor number.
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NMDZ1_HUMANLIG_PDZ_Class_1917922Binding of the PDZ domain of Disks large homolog 4 (DLG4) suppresses the ER-retention motif of Isoform 4 of Glutamate receptor subunit zeta-1 (GRIN1) in a splice variant-specific manner, thereby promoting cell surface expression of this particular isoform. This supports the hypothesis that local regulation of receptor exit from neuronal ER plays a role in modifying discrete synaptic receptor number.
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Type: Binary Subtype: Physicochemical compatibility
PTM of a residue in a motif or in its flanking regions alters the physicochemical and/or structural compatibility of the motif with its binding partner. This can either induce or enhance an interaction, or result in inhibition or even abrogation of an interaction.
SDC1_HUMANLIG_PDZ_Class_2305310Phosphorylation of Y309 in the PDZ-binding motif of Syndecan-1 (SDC1) prevents binding to the PDZ domain of Syntenin-1 (SDCBP), an interaction involved in the formation of cellular protrusions.
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CCG2_MOUSELIG_PDZ_Class_1318323Phosphorylation of T321 in the PDZ-binding motif of Voltage-dependent calcium channel gamma-2 subunit (Cacng2) by cAMP subfamily prevents binding to the PDZ domain of Disks large homolog 4 (Dlg4), an interaction involved in regulating synaptic targeting of AMPA-selective glutamate receptors.
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IRK4_HUMANLIG_PDZ_Class_1440445Phosphorylation of S443 in the PDZ-binding motif of Inward rectifier potassium channel 4 (KCNJ4) by inhibits its interaction with the Disks large homolog 4 (DLG4) protein.
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ADRB2_HUMANLIG_PDZ_Class_1408413Phosphorylation of S411 in the PDZ-binding motif of Beta-2 adrenergic receptor (ADRB2) by inhibits its interaction with the Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1) protein.
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BCR_HUMANLIG_PDZ_Class_112661271Phosphorylation of T1269 in the PDZ-binding motif of Breakpoint cluster region protein (BCR) inhibits its interaction with the Afadin (MLLT4) protein.
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PGFRB_HUMANLIG_PDZ_Class_111011106Phosphorylation of S1104 in the PDZ-binding motif of Platelet-derived growth factor receptor beta (PDGFRB) by Beta-adrenergic receptor kinase 1 (ADRBK1) inhibits binding to Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1). Binding of Platelet-derived growth factor receptor beta (PDGFRB) to Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1) potentiates dimerisation and signalling of the receptor, while phosphorylation at S1104 desensitises the receptor.
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Type: Binary Subtype: Pre‑translational
Pre-translational mechanisms such as alternative splicing, alternative promoter-usage and/or RNA editing result in inclusion or removal of exons that contain an entire or partial motif.
ADA22_HUMANLIG_PDZ_Class_1901906Alternative splicing removes the PDZ-binding motif of Disintegrin and metalloproteinase domain-containing protein 22 (ADAM22), abrogating binding to Disks large homolog 4 (DLG4). The motif-containing Isoform Epsilon of Disintegrin and metalloproteinase domain-containing protein 22 (ADAM22) forms part of a complex containing Leucine-rich glioma-inactivated protein 1 (LGI1), AMPA-R (e.g. Glutamate receptor 1 (GRIA1)) and AMPA-R regulatory proteins (e.g. Voltage-dependent calcium channel gamma-2 subunit (CACNG2)), and is closely associated with epilepsy.
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AT2B2_HUMANLIG_PDZ_Class_112381243Alternative splicing removes the PDZ-binding motif of Plasma membrane calcium-transporting ATPase 2 (ATP2B2), abrogating binding to Na(+)/H(+) exchange regulatory cofactor NHE-RF2 (SLC9A3R2), altering the location of this Ca2+ pump. Despite the similarity in C-terminal between the 'b' splice variants of Plasma membrane calcium-transporting ATPase 4 (ATP2B4) (-ETSV) and Plasma membrane calcium-transporting ATPase 2 (ATP2B2) (-ETSL), 'b' splice variants of ATP2B4 did not interact with either of the NHERFs whereas PMCA2b selectively preferred Na(+)/H(+) exchange regulatory cofactor NHE-RF2 (SLC9A3R2) over Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1). NHERFs have been previously implicated in the targeting, retention and regulation of membrane proteins including the β2-adrenergic receptor, cystic fibrosis transmembrane conductance regulator, and Trp4 Ca2+channel. This study suggests Plasma membrane calcium-transporting ATPase 2 (ATP2B2) may be under similar regulation.
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AT2B4_HUMANLIG_PDZ_Class_112361241Alternative splicing removes the PDZ-binding motif of Plasma membrane calcium-transporting ATPase 4 (ATP2B4), abrogating binding to Nitric oxide synthase, brain (NOS1). PMCA4b acts as a negative regulator of Nitric oxide synthase, brain (NOS1), reducing production of nitric oxide in heart tissue. This negative regulation was not dependent on a conformational change due to binding of the PDZ ligand, but on Ca2+ depletion in close proximity of the enzyme. Nitric oxide production by NOS1 is known to be important in the regulation of excitation-contraction (EC) coupling and subsequently contractility.
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AT2B4_HUMANLIG_PDZ_Class_112361241Alternative splicing removes the PDZ-binding motif of Plasma membrane calcium-transporting ATPase 4 (ATP2B4), abrogating binding to Disks large homolog 3 (DLG3). Disks large homolog 3 (DLG3) did not bind to 'b' isoform of PMCA2. There is therefore an interaction selectivity between 'b' isoforms of ATP2B4 and DLG3 as opposed to the promiscuity of 'b' isoforms of ATP2B2 and ATP2B4 in interacting with other SAPs. Same study DLG4, DLG2 and DLG1 shown to bind to PDZ-binding motifs in 'b' isoforms of ATP2B4 and ATP2B2.
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AT2B4_HUMANLIG_PDZ_Class_112361241Alternative splicing removes the PDZ-binding motif of Plasma membrane calcium-transporting ATPase 4 (ATP2B4), abrogating binding to Disks large homolog 1 (DLG1). A much lower affinity was recorded for the third PDZ domain of DLG1 (in in the micromolar range (KD = 1.2 microM) compared to nanomolar affinity (KD = 1.6 nM)). PMCA4b and DLG1 are co-expressed in kidney and intestinal epithelial cells as well as in several areas of the brain. Should be noted that the 'b' isoforms of Plasma membrane calcium-transporting ATPase 2 (ATP2B2) bind much more weakly to all PDZ domains of DLG1
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AT2B4_HUMANLIG_PDZ_Class_112361241Alternative splicing removes the PDZ-binding motif of Plasma membrane calcium-transporting ATPase 4 (ATP2B4), abrogating binding to Peripheral plasma membrane protein CASK (CASK). The PDZ domain-containing protein CASK and PMCA4b co-precipitate in kidney and brain. Similar to NOS1, binding to PMCA4b allows Ca2+ dependent regulation. Depletion of local Ca2+ by PMCA4b in close proximity to CASK may inhibit Ca2+/calmodulin binding. This can subsequently inhibit binding to T-box brain protein 1 (TBR1) and/or translocation of CASK or the CASK/TBR1 complex to the nucleus.
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5HT4R_MOUSELIG_PDZ_Class_1382387Alternative splicing removes the PDZ-binding motif of Isoform 5-HT4(A) of 5-hydroxytryptamine receptor 4 (Htr4), abrogating binding to Sorting nexin-27 (Snx27). Snx27 is responsible for targeting of the Isoform 5-HT4(A) of 5-hydroxytryptamine receptor 4 (Htr4) to early endosomes.
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5HT4R_MOUSELIG_PDZ_Class_1382387Alternative splicing removes the PDZ-binding motif of Isoform 5-HT4(A) of 5-hydroxytryptamine receptor 4 (Htr4), abrogating binding to Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (Slc9a3r1). Isoform 5-HT4(A) of 5-hydroxytryptamine receptor 4 (Htr4) interacts specifically with a protein complex including Slc9a3r1 and Ezrin (Ezr) that might participate in its targeting to specialised subcellular regions, such as microvilli.
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5HT4R_MOUSELIG_PDZ_Class_2368371Alternative splicing removes the PDZ-binding motif of Isoform 5-HT4(E) of 5-hydroxytryptamine receptor 4 (Htr4), abrogating binding to InaD-like protein (Inadl).
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IRK6_MOUSELIG_PDZ_Class_1420425Alternative splicing removes the PDZ-binding motif of G protein-activated inward rectifier potassium channel 2 (Kcnj6), abrogating binding to Sorting nexin-27 (Snx27).
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KIF1B_MOUSELIG_PDZ_Class_111451150Alternative splicing removes the PDZ-binding motif of Isoform 3 of Kinesin-like protein KIF1B (Kif1b), abrogating binding to PDZ domain-containing protein GIPC1 (Gipc1).
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GRIK1_RATLIG_PDZ_Class_1900905Alternative splicing removes the PDZ-binding motif of Isoform Glur5-2 of Glutamate receptor ionotropic, kainate 1 (Grik1), abrogating binding to PRKCA-binding protein (Pick1). The ER-retention motif of Grik1 splice variants can be inhibited by PKC phosphorylation and association with a PDZ protein. It has also been shown that the PDZ domain-containing proteins Disks large homolog 4 (Dlg4) and Syntenin-1 (Sdcbp) are able to bind.
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GRIK1_RATLIG_PDZ_Class_1900905Alternative splicing removes the PDZ-binding motif of Glutamate receptor, ionotropic kainate 1 (Grik1), abrogating binding to Glutamate receptor-interacting protein 1 (Grip1). The ER retention of Grik1 splice variants can be inhibited by PKC phosphorylation and association with a PDZ domain-containing protein. Also shown that the PDZ-binding containing proteins PSD95 and syntenin are able to bind.
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GUAD_HUMANLIG_PDZ_Class_1449454Alternative splicing removes the PDZ-binding motif of Guanine deaminase (GDA) (Nedasin), abrogating binding to Disks large homolog 3 (DLG3). Isoform 1 of Guanine deaminase (GDA) (Nedasin S) is predominately expressed in neuronal tissues and binds PDZ domains. Isoform 3 of Guanine deaminase (GDA) (Nedasin V1), which is predominately expressed in non-neuronal tissues, does not bind PDZ domains. The presence of Nedasin S inhibits binding of NMDA receptors and K+ channels to PDZ domain-containing proteins such as members of the MAGUK family. This suggests that GDA might modulate the receptor clustering function of the PDZ domains of MAGUK family members, and this modulation is regulated by alternative splicing of GDA transcripts.
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NMDZ1_HUMANLIG_PDZ_Class_1917922Alternative splicing removes the PDZ-binding motif of Isoform 4 of Glutamate [NMDA] receptor subunit zeta-1 (GRIN1), abrogating binding to Disks large homolog 4 (DLG4). Binding of the PDZ domain of DLG4 suppresses an ER-retention motif in GRIN1, promoting its cell surface expression in a splice variant-specific manner.
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SYNJ2_RATLIG_PDZ_Class_112881293Alternative splicing removes the PDZ-binding motif of Isoform 7.5kb of Synaptojanin-2 (Synj2), abrogating binding to Synaptojanin-2-binding protein (Synj2bp). Isoform 7.5kb of Synaptojanin-2 (Synj2) (Synaptojanin 2A) is recruited to mitochondria through the interaction with the PDZ domain of the mitochondrial outer membrane protein Synj2bp.
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CLCN3_HUMANLIG_PDZ_Class_1861866Alternative splicing removes the PDZ-binding motif of Isoform ClC-3B of H(+)/Cl(-) exchange transporter 3 (CLCN3), abrogating binding to Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1). Isoform ClC-3B of H(+)/Cl(-) exchange transporter 3 (CLCN3) is expressed at the leading edge of membrane ruffles. The interaction of CLCN3 with SLC9A3R1 is important for localising outwardly rectifying chloride channels at the leading edge.
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GRIA2_RATLIG_PDZ_Class_2878883Alternative splicing removes the PDZ-binding motif of Glutamate receptor 2 (Gria2), abrogating binding to PRKCA-binding protein (Pick1). The presence of PDZ-binding motifs is also seen in the short isoforms of Gria3 (Isoform Flop of Glutamate receptor 3 (Gria3)) and Gria4 (Isoform 4C flop of Glutamate receptor 4 (Gria4)). PRKCA-binding protein (Pick1) recruits both Protein kinase C alpha type (Prkca) and Gria2 simultaneously, possibly allowing Pick1 to play a role in the selective targeting to and possible anchoring of GluRshort-containing AMPA receptors to intracellular membrane-associated Prkca.
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PKHG5_MOUSELIG_PDZ_Class_110681073Alternative splicing removes the PDZ-binding motif of Pleckstrin homology domain-containing family G member 5 (Plekhg5), abrogating binding to PDZ domain-containing protein GIPC1 (Gipc1). The PDZ adaptor protein Gipc1 (Synectin) bound the longer splice variant, Isoform SYX1 of Pleckstrin homology domain-containing family G member 5 (Plekhg5) (Syx1), which was targeted to the plasma membrane in a Synectin-dependent manner. The shorter variant, Isoform SYX2 of Pleckstrin homology domain-containing family G member 5 (Plekhg5) (Syx2), was diffusely distributed in the cytoplasm. Expression of Syx1 augmented endothelial cell migration and tube formation, whereas Syx2 expression did not. Significant expression of Syx2 was only seen in brain tumour cells, which also exhibited high basal Transforming protein RhoA (Rhoa) activity.
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KALRN_RATLIG_PDZ_Class_116491654Alternative splicing removes the PDZ-binding motif of Isoform Kalirin-7 of Kalirin (Kalrn), abrogating binding to Disks large homolog 4 (Dlg4). Isoform Kalirin-7 of Kalirin (Kalrn) is the most prevalent isoform in the adult rat hippocampus where it locates to the postsynaptic density via an interaction with Dlg4 and regulates dendritic morphogenesis.
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PLCB1_HUMANLIG_PDZ_Class_112111216Alternative splicing removes the PDZ-binding motif of 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 (PLCB1), abrogating binding to Partitioning defective 3 homolog (PARD3). The G protein-activated PLCB1 can directly interact with cell polarity proteins Partitioning defective 3 homolog (PARD3) and Partitioning defective 6 homolog alpha (PARD6A) to form protein complexes in the cell, which potentially modulate G protein-activated PLCB1 activity in cell polarity formation and asymmetric cell division.
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PLCB1_MOUSELIG_PDZ_Class_112111216Alternative splicing removes the PDZ-binding motif of 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 (Plcb1), abrogating binding to Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (Slc9a3r1). Plcb1 does not bind to Slc9a3r2.
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BAIP2_HUMANLIG_PDZ_Class_1516521Alternative splicing removes the PDZ-binding motif of Isoform BAIAP2-alpha of Brain-specific angiogenesis inhibitor 1-associated protein 2 (BAIAP2), abrogating binding to Disks large homolog 3 (DLG3). The SH3 domain of Isoform BAIAP2-alpha of Brain-specific angiogenesis inhibitor 1-associated protein 2 (BAIAP2) also binds to SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), meaning it can link two prominent proteins of the postsynaptic NMDA-receptor complex, namely SHANK1 and DLG3.
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AT2B4_HUMANLIG_PDZ_Class_112361241Alternative splicing removes the PDZ-binding motif of Plasma membrane calcium-transporting ATPase 4 (ATP2B4), abrogating binding to Disks large homolog 1 (DLG1). A much lower affinity was recorded for the third PDZ domain of DLG1 (in in the micromolar range (KD = 1.2 microM) compared to nanomolar affinity (KD = 1.6 nM)). PMCA4b and DLG1 are co-expressed in kidney and intestinal epithelial cells as well as in several areas of the brain.
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AT2B4_HUMANLIG_PDZ_Class_112361241Alternative splicing removes the PDZ-binding motif of Plasma membrane calcium-transporting ATPase 4 (ATP2B4), abrogating binding to Disks large homolog 3 (DLG3). Disks large homolog 3 (DLG3) did not bind to 'b' isoform of PMCA2. There is therefore an interaction selectivity between 'b' isoforms of ATP2B4 and DLG3 as opposed to the promiscuity of 'b' isoforms of ATP2B2 and ATP2B4 in interacting with other SAPs. Same study DLG4, DLG2 and DLG1 shown to bind to PDZ-binding motifs in 'b' isoforms of ATP2B4 and ATP2B2.
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KALRN_RATLIG_PDZ_Class_116491654Alternative splicing removes the PDZ-binding motif of Isoform Kalirin-7 of Kalirin (Kalrn), abrogating binding to Disks large homolog 4 (Dlg4). Isoform Kalirin-7 of Kalirin (Kalrn) is the most prevalent isoform in the adult rat hippocampus where it locates to the postsynaptic density via an interaction with Dlg4 and regulates dendritic morphogenesis.
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KALRN_RATLIG_PDZ_Class_116491654Alternative splicing removes the PDZ-binding motif of Isoform Kalirin-7 of Kalirin (Kalrn), abrogating binding to Disks large homolog 4 (Dlg4). Isoform Kalirin-7 of Kalirin (Kalrn) is the most prevalent isoform in the adult rat hippocampus where it locates to the postsynaptic density via an interaction with Dlg4 and regulates dendritic morphogenesis.
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NMDZ1_HUMANLIG_PDZ_Class_1917922Alternative splicing removes the PDZ-binding motif of Isoform 4 of Glutamate [NMDA] receptor subunit zeta-1 (GRIN1), abrogating binding to Disks large homolog 4 (DLG4). Binding of the PDZ domain of DLG4 suppresses an ER-retention motif in GRIN1, promoting its cell surface expression in a splice variant-specific manner.
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NMDZ1_HUMANLIG_PDZ_Class_1917922Alternative splicing removes the PDZ-binding motif of Isoform 4 of Glutamate [NMDA] receptor subunit zeta-1 (GRIN1), abrogating binding to Disks large homolog 4 (DLG4). Binding of the PDZ domain of DLG4 suppresses an ER-retention motif in GRIN1, promoting its cell surface expression in a splice variant-specific manner.
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GUAD_HUMANLIG_PDZ_Class_1449454Alternative splicing removes the PDZ-binding motif of Guanine deaminase (GDA) (Nedasin), abrogating binding to Disks large homolog 3 (DLG3). Isoform 1 of Guanine deaminase (GDA) (Nedasin S) is predominately expressed in neuronal tissues and binds PDZ domains. Isoform 3 of Guanine deaminase (GDA) (Nedasin V1), which is predominately expressed in non-neuronal tissues, does not bind PDZ domains. The presence of Nedasin S inhibits binding of NMDA receptors and K+ channels to PDZ domain-containing proteins such as members of the MAGUK family. This suggests that GDA might modulate the receptor clustering function of the PDZ domains of MAGUK family members, and this modulation is regulated by alternative splicing of GDA transcripts.
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5HT4R_MOUSELIG_PDZ_Class_1382387Alternative splicing removes the PDZ-binding motif of Isoform 5-HT4(A) of 5-hydroxytryptamine receptor 4 (Htr4), abrogating binding to Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (Slc9a3r1). Isoform 5-HT4(A) of 5-hydroxytryptamine receptor 4 (Htr4) interacts specifically with a protein complex including Slc9a3r1 and Ezrin (Ezr) that might participate in its targeting to specialised subcellular regions, such as microvilli.
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Type: Binary Subtype: Allostery
The binding properties of a motif or a motif-binding domain are modulated indirectly by allosteric effects resulting from PTM or effector binding at a site that is distinct from the actual interaction interface.
CTNB1_HUMANLIG_PDZ_Class_1776781Binding of Ezrin (EZR) via its FERM domain to the EB domain of Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1) results in allosteric coupling to the second PDZ domain of Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1), which results in relief of the intramolecular interaction with the PDZ binding ligand, thereby increasing the affinity of the PDZ domain for other ligands, including Catenin beta-1 (CTNNB1).
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