signal-induced proliferation-associated protein 1 [Mus musculus]
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
Rap_GAP | pfam02145 | Rap/ran-GAP; |
347-528 | 1.51e-78 | ||||
Rap/ran-GAP; : Pssm-ID: 460463 Cd Length: 179 Bit Score: 254.36 E-value: 1.51e-78
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PDZ_SIPA1-like | cd06745 | PDZ domain of signal-induced proliferation-associated protein 1 (SIPA1), and related domains; ... |
683-755 | 1.98e-31 | ||||
PDZ domain of signal-induced proliferation-associated protein 1 (SIPA1), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SIPA1, and related domains. The Rap-GTPase activating protein SIPA1 (also known as GTPase-activating protein Spa-1, p130 SPA1) is a metastasis promoter; a polymorphism in a region of the Sipa1 gene encoding the PDZ domain is associated with metastasis. The SIPA1 PDZ domain binds ribosomal RNA processing 1 homolog B (Rrp1b). SIPA1 also forms a complex with water channel aquaporin-2 (AQP2) and plays a role in trafficking of AQP2, targeted positioning of which strictly regulates body water homeostasis; the SIPA1 PDZ domain binds AQP2. Rrp1b or AQP2 binding inhibits the RapGAP activity of SIPA1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SIPA1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F. : Pssm-ID: 467227 [Multi-domain] Cd Length: 73 Bit Score: 117.38 E-value: 1.98e-31
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ZapB | pfam06005 | Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ... |
970-1026 | 7.57e-04 | ||||
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation. : Pssm-ID: 428718 [Multi-domain] Cd Length: 71 Bit Score: 39.17 E-value: 7.57e-04
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PHA03378 super family | cl33729 | EBNA-3B; Provisional |
29-112 | 1.09e-03 | ||||
EBNA-3B; Provisional The actual alignment was detected with superfamily member PHA03378: Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 43.13 E-value: 1.09e-03
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Name | Accession | Description | Interval | E-value | ||||
Rap_GAP | pfam02145 | Rap/ran-GAP; |
347-528 | 1.51e-78 | ||||
Rap/ran-GAP; Pssm-ID: 460463 Cd Length: 179 Bit Score: 254.36 E-value: 1.51e-78
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PDZ_SIPA1-like | cd06745 | PDZ domain of signal-induced proliferation-associated protein 1 (SIPA1), and related domains; ... |
683-755 | 1.98e-31 | ||||
PDZ domain of signal-induced proliferation-associated protein 1 (SIPA1), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SIPA1, and related domains. The Rap-GTPase activating protein SIPA1 (also known as GTPase-activating protein Spa-1, p130 SPA1) is a metastasis promoter; a polymorphism in a region of the Sipa1 gene encoding the PDZ domain is associated with metastasis. The SIPA1 PDZ domain binds ribosomal RNA processing 1 homolog B (Rrp1b). SIPA1 also forms a complex with water channel aquaporin-2 (AQP2) and plays a role in trafficking of AQP2, targeted positioning of which strictly regulates body water homeostasis; the SIPA1 PDZ domain binds AQP2. Rrp1b or AQP2 binding inhibits the RapGAP activity of SIPA1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SIPA1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F. Pssm-ID: 467227 [Multi-domain] Cd Length: 73 Bit Score: 117.38 E-value: 1.98e-31
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PDZ | pfam00595 | PDZ domain; PDZ domains are found in diverse signaling proteins. |
683-755 | 2.95e-12 | ||||
PDZ domain; PDZ domains are found in diverse signaling proteins. Pssm-ID: 395476 [Multi-domain] Cd Length: 81 Bit Score: 63.07 E-value: 2.95e-12
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PDZ | smart00228 | Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ... |
680-758 | 4.30e-08 | ||||
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities. Pssm-ID: 214570 [Multi-domain] Cd Length: 85 Bit Score: 51.61 E-value: 4.30e-08
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ZapB | pfam06005 | Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ... |
970-1026 | 7.57e-04 | ||||
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation. Pssm-ID: 428718 [Multi-domain] Cd Length: 71 Bit Score: 39.17 E-value: 7.57e-04
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PHA03378 | PHA03378 | EBNA-3B; Provisional |
29-112 | 1.09e-03 | ||||
EBNA-3B; Provisional Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 43.13 E-value: 1.09e-03
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Name | Accession | Description | Interval | E-value | ||||
Rap_GAP | pfam02145 | Rap/ran-GAP; |
347-528 | 1.51e-78 | ||||
Rap/ran-GAP; Pssm-ID: 460463 Cd Length: 179 Bit Score: 254.36 E-value: 1.51e-78
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PDZ_SIPA1-like | cd06745 | PDZ domain of signal-induced proliferation-associated protein 1 (SIPA1), and related domains; ... |
683-755 | 1.98e-31 | ||||
PDZ domain of signal-induced proliferation-associated protein 1 (SIPA1), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SIPA1, and related domains. The Rap-GTPase activating protein SIPA1 (also known as GTPase-activating protein Spa-1, p130 SPA1) is a metastasis promoter; a polymorphism in a region of the Sipa1 gene encoding the PDZ domain is associated with metastasis. The SIPA1 PDZ domain binds ribosomal RNA processing 1 homolog B (Rrp1b). SIPA1 also forms a complex with water channel aquaporin-2 (AQP2) and plays a role in trafficking of AQP2, targeted positioning of which strictly regulates body water homeostasis; the SIPA1 PDZ domain binds AQP2. Rrp1b or AQP2 binding inhibits the RapGAP activity of SIPA1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SIPA1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F. Pssm-ID: 467227 [Multi-domain] Cd Length: 73 Bit Score: 117.38 E-value: 1.98e-31
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PDZ | pfam00595 | PDZ domain; PDZ domains are found in diverse signaling proteins. |
683-755 | 2.95e-12 | ||||
PDZ domain; PDZ domains are found in diverse signaling proteins. Pssm-ID: 395476 [Multi-domain] Cd Length: 81 Bit Score: 63.07 E-value: 2.95e-12
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PDZ | smart00228 | Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ... |
680-758 | 4.30e-08 | ||||
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities. Pssm-ID: 214570 [Multi-domain] Cd Length: 85 Bit Score: 51.61 E-value: 4.30e-08
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PDZ_canonical | cd00136 | canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ... |
683-750 | 5.38e-04 | ||||
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain. PDZ domains usually bind to short specific peptide sequences located at the C-terminal end of their partner proteins known as PDZ binding motifs. These domains can also interact with internal peptide motifs and certain lipids, and can take part in a head-to-tail oligomerization with other PDZ domains. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. Pssm-ID: 467153 [Multi-domain] Cd Length: 81 Bit Score: 39.83 E-value: 5.38e-04
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ZapB | pfam06005 | Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ... |
970-1026 | 7.57e-04 | ||||
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation. Pssm-ID: 428718 [Multi-domain] Cd Length: 71 Bit Score: 39.17 E-value: 7.57e-04
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PHA03378 | PHA03378 | EBNA-3B; Provisional |
29-112 | 1.09e-03 | ||||
EBNA-3B; Provisional Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 43.13 E-value: 1.09e-03
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PDZ_RapGEF2_RapGEF6-like | cd06755 | PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange ... |
703-754 | 2.07e-03 | ||||
PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange factor 6, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Rap guanine nucleotide exchange factor 2 (RapGEF2, also named RA-GEF-1, PDZ-GEF1, CNrasGEF and nRapGEP) and Rap guanine nucleotide exchange factor 6 (RapGEF6, also named RA-GEF-2 and PDZ-GEF2). RapGEF2 and RapGEF6 constitute a subfamily of guanine nucleotide exchange factors (GEFs) for RAP small GTPases that is characterized by the possession of the PDZ and Ras/Rap-associating domains. They activate Rap small GTPases, by catalyzing the release of GDP from the inactive GDP-bound forms, thereby accelerating GTP loading to yield the active GTP-bound forms. The PDZ domain of RapGEF6 (also known as PDZ-GEF2) binds junctional adhesion molecule A (JAM-A). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RapGEF2 and RapGEF6 family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. Pssm-ID: 467237 [Multi-domain] Cd Length: 83 Bit Score: 38.01 E-value: 2.07e-03
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PDZ3_Dlg1-2-4-like | cd06795 | PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ... |
680-762 | 4.83e-03 | ||||
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of Drosophila Dlg1, human Dlg1, 2, and 4 and related domains. Dlg1 (also known as synapse-associated protein Dlg197; SAP-97), Dlg2 (also known as channel-associated protein of synapse-110; postsynaptic density protein 93, PSD-93), Dlg4 (also known as postsynaptic density protein 95, PSD-95; synapse-associated protein 90, SAP-90) each have 3 PDZ domains and belong to the membrane-associated guanylate kinase family. Dlg1 regulates antigen receptor signaling and cell polarity in lymphocytes, B-cell proliferation and antibody production, and TGFalpha bioavailability; its PDZ3 domain binds pro-TGFalpha, and its PDZ2 domain binds the TACE metalloprotease responsible for cleaving pro-TGFalpha to a soluble form. Dlg2 is involved in N-methyl-D-aspartate (NMDA) receptor signaling, regulating surface expression of NMDA receptors in dorsal horn neurons of the spinal cord; it interacts with NMDA receptor subunits and with Shaker-type K+ channel subunits to cluster into a channel complex. The Dlg4 PDZ1 domain binds NMDA receptors, and its PDZ2 domain binds neuronal nitric oxide synthase (nNOS), forming a complex in neurons. The Drosophila Scribble complex (Scribble, Dlg, and lethal giant larvae) plays a role in apico-basal cell polarity, and in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development; postsynaptic targeting of Drosophila DLG requires interactions mediated by the first two PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. Pssm-ID: 467257 [Multi-domain] Cd Length: 91 Bit Score: 37.33 E-value: 4.83e-03
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HAUS-augmin3 | pfam14932 | HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found ... |
940-1032 | 5.66e-03 | ||||
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found from Drosophila to humans. The HAUS-augmin complex is made up of eight subunits. The augmin complex interacts with gamma-TuRC, and attenuation of this interaction severely impairs spindle MT generation. Furthermore, we provide evidence that human augmin plays critical and non-redundant roles in the kinetochore-MT attachment and also central spindle formation during anaphase in human cells.The HAUS complex is required for mitotic spindle assembly and for maintenance of centrosome integrity. Pssm-ID: 464384 [Multi-domain] Cd Length: 261 Bit Score: 39.99 E-value: 5.66e-03
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PDZ1_FL-whirlin | cd06740 | PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ... |
703-754 | 5.81e-03 | ||||
PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of the full-length isoform of whirlin and related domains. Whirlin is an essential protein for developmental pathways in photoreceptor cells of the retina and hair cells of the inner ear. The full-length whirlin isoform has two harmonin N-like domains, three PDZ domains, a proline-rich region, and a PDZ-binding motif. Whirlin isoforms may form different complexes at the periciliary membrane complex (PMC) in photoreceptors, and the stereociliary tip and base in inner ear hair cells. It interacts with ADGRV1 and usherin at the PMC; with SANS and RpgrORF15 at the connecting cilium in photoreceptors; with EPS8, MYO15A, p55, and CASK proteins at the stereociliary tip of inner ear hair cells; and with ADGRV1, usherin, and PDZD7 at the stereociliary base in inner ear hair cells. Mutations in the gene encoding whirlin (WHRN; also known as USH2D and DFNB31), have been found to cause either USH2 subtype (USH2D) or autosomal recessive non-syndromic deafness type 31 (DFNB31). Whirlin is the key protein in the USH2 complex (whirlin, usherin and GPR98) which recruits other USH2 causative proteins at the periciliary membrane in photoreceptors and the ankle link of the stereocilia in hair cells. Whirlin's interaction with espin, another stereociliary protein, may be important for the architecture of the USH2 complex. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This whirlin family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. Pssm-ID: 467222 [Multi-domain] Cd Length: 82 Bit Score: 36.96 E-value: 5.81e-03
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PDZ1_harmonin | cd06737 | PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ... |
682-754 | 9.19e-03 | ||||
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of harmonin isoforms a, b, and c, and related domains. Harmonin (also known as Usher Type 1C, PDZ-73 and AIE-75) is a key organizer of the Usher (USH) protein interactome. USH syndrome is the leading cause of hereditary sensory deaf-blindness in humans; three clinically distinct types of USH have been identified, type 1 to 3. The gene encoding harmonin (USH1C) is the causative gene for the USH type 1C phenotype. There are at least 10 alternatively spliced isoforms of harmonin, which are divided into three subclasses (a, b, and c). All isoforms contain the first two PDZ domains and the first coiled-coil domain. The a and b isoforms all have a third PDZ domain. The different PDZ domains are responsible for interactions with all known Usher syndrome type 1 proteins, and most Usher syndrome type 2 proteins. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This harmonin family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. Pssm-ID: 467219 [Multi-domain] Cd Length: 85 Bit Score: 36.47 E-value: 9.19e-03
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Blast search parameters | ||||
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