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Appears in Networks 2

In-Edges 10

p(HGNC:CEP164) association p(HGNC:TTBK2) View Subject | View Object

TTBK2 bound EB1 and Cep164 through its SxIP motifs and a proline-rich motif, respectively. Using TTBK2 variants that contained mutations in the SxIP or proline-rich motifs, we obtained evidence that Cep164, but not EB1, is essential for centriolar localization of TTBK2. Therefore, Cep164 binding is essential for the function of TTBK2 in promoting CP110 removal and ciliogenesis. We also provide evidence that TTBK2 has the potential to effectively phosphorylate Cep164 and Cep97 and inhibits the interaction between Cep164 and its binding partner Dishevelled-3 (an important regulator of ciliogenesis) in a kinase activity-dependent manner. PubMed:26323690

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p(HGNC:CEP164) positiveCorrelation act(p(HGNC:TTBK2)) View Subject | View Object

TTBK2 bound EB1 and Cep164 through its SxIP motifs and a proline-rich motif, respectively. Using TTBK2 variants that contained mutations in the SxIP or proline-rich motifs, we obtained evidence that Cep164, but not EB1, is essential for centriolar localization of TTBK2. Therefore, Cep164 binding is essential for the function of TTBK2 in promoting CP110 removal and ciliogenesis. We also provide evidence that TTBK2 has the potential to effectively phosphorylate Cep164 and Cep97 and inhibits the interaction between Cep164 and its binding partner Dishevelled-3 (an important regulator of ciliogenesis) in a kinase activity-dependent manner. PubMed:26323690

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p(HGNC:MAPRE1) association p(HGNC:TTBK2) View Subject | View Object

TTBK2 bound EB1 and Cep164 through its SxIP motifs and a proline-rich motif, respectively. Using TTBK2 variants that contained mutations in the SxIP or proline-rich motifs, we obtained evidence that Cep164, but not EB1, is essential for centriolar localization of TTBK2. Therefore, Cep164 binding is essential for the function of TTBK2 in promoting CP110 removal and ciliogenesis. We also provide evidence that TTBK2 has the potential to effectively phosphorylate Cep164 and Cep97 and inhibits the interaction between Cep164 and its binding partner Dishevelled-3 (an important regulator of ciliogenesis) in a kinase activity-dependent manner. PubMed:26323690

Appears in Networks:

p(HGNC:TTBK2, var("p.Asp449*")) increases p(HGNC:TTBK2) View Subject | View Object

SCA11 truncating mutations promote TTBK2 protein expression, suppress kinase activity and lead to enhanced nuclear localization. Using a SCA11-mutation-carrying knockin mouse we show that this leads to inhibition of endogenous TTBK2 protein kinase activity. PubMed:21548880

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p(HGNC:TTBK2, var("p.Asp449*")) decreases act(p(HGNC:TTBK2), ma(kin)) View Subject | View Object

SCA11 truncating mutations promote TTBK2 protein expression, suppress kinase activity and lead to enhanced nuclear localization. Using a SCA11-mutation-carrying knockin mouse we show that this leads to inhibition of endogenous TTBK2 protein kinase activity. PubMed:21548880

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p(HGNC:TTBK2, var("p.Glu450*")) increases p(HGNC:TTBK2) View Subject | View Object

SCA11 truncating mutations promote TTBK2 protein expression, suppress kinase activity and lead to enhanced nuclear localization. Using a SCA11-mutation-carrying knockin mouse we show that this leads to inhibition of endogenous TTBK2 protein kinase activity. PubMed:21548880

Appears in Networks:

p(HGNC:TTBK2, var("p.Glu450*")) decreases act(p(HGNC:TTBK2), ma(kin)) View Subject | View Object

SCA11 truncating mutations promote TTBK2 protein expression, suppress kinase activity and lead to enhanced nuclear localization. Using a SCA11-mutation-carrying knockin mouse we show that this leads to inhibition of endogenous TTBK2 protein kinase activity. PubMed:21548880

Appears in Networks:

p(HGNC:TTBK2, var("p.Tyr448*")) increases p(HGNC:TTBK2) View Subject | View Object

SCA11 truncating mutations promote TTBK2 protein expression, suppress kinase activity and lead to enhanced nuclear localization. Using a SCA11-mutation-carrying knockin mouse we show that this leads to inhibition of endogenous TTBK2 protein kinase activity. PubMed:21548880

Appears in Networks:

p(HGNC:TTBK2, var("p.Tyr448*")) decreases act(p(HGNC:TTBK2), ma(kin)) View Subject | View Object

SCA11 truncating mutations promote TTBK2 protein expression, suppress kinase activity and lead to enhanced nuclear localization. Using a SCA11-mutation-carrying knockin mouse we show that this leads to inhibition of endogenous TTBK2 protein kinase activity. PubMed:21548880

Appears in Networks:

path(MESH:Tauopathies) association p(HGNC:TTBK2) View Subject | View Object

Some of these enhancer genes are specific only to the tau-induced disease phenotype and include genes encoding proteins like WNT2 (111), TTBK2 (112), GSK-3b (113), TAOK1 (114, 115), CTSE (116) and CHRNA7 (117), have been implicated in tau-mediated pathology. PubMed:29191965

Out-Edges 25

p(HGNC:TTBK2) increases p(HGNC:MAPT, pmod(Ph, Ser, 210)) View Subject | View Object

Tau-tubulin kinase 2 (TTBK2) is a Ser/Thr kinase that putatively phosphorylates residues Ser208 and Ser210 (numbered according to a 441-residue human tau isoform) in tau protein. PubMed:17620722

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p(HGNC:TTBK2) increases p(HGNC:MAPT, pmod(Ph, Ser, 208)) View Subject | View Object

Tau-tubulin kinase 2 (TTBK2) is a Ser/Thr kinase that putatively phosphorylates residues Ser208 and Ser210 (numbered according to a 441-residue human tau isoform) in tau protein. PubMed:17620722

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p(HGNC:TTBK2) increases p(HGNC:SV2A, pmod(Ph, Ser, 42)) View Subject | View Object

We demonstrate that Casein kinase 1 family members, including isoforms of Tau-tubulin protein kinases (TTBK1 and TTBK2), phosphorylate human SV2A at two constellations of residues, namely Cluster-1 (Ser42, Ser45, and Ser47) and Cluster-2 (Ser80, Ser81, and Thr84). These residues are also phosphorylated in vivo, and the phosphorylation of Thr84 within Cluster-2 is essential for triggering binding to the C2B domain of human synaptotagmin-1 PubMed:25673844

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p(HGNC:TTBK2) increases p(HGNC:SV2A, pmod(Ph, Ser, 45)) View Subject | View Object

We demonstrate that Casein kinase 1 family members, including isoforms of Tau-tubulin protein kinases (TTBK1 and TTBK2), phosphorylate human SV2A at two constellations of residues, namely Cluster-1 (Ser42, Ser45, and Ser47) and Cluster-2 (Ser80, Ser81, and Thr84). These residues are also phosphorylated in vivo, and the phosphorylation of Thr84 within Cluster-2 is essential for triggering binding to the C2B domain of human synaptotagmin-1 PubMed:25673844

Appears in Networks:

p(HGNC:TTBK2) increases p(HGNC:SV2A, pmod(Ph, Ser, 47)) View Subject | View Object

We demonstrate that Casein kinase 1 family members, including isoforms of Tau-tubulin protein kinases (TTBK1 and TTBK2), phosphorylate human SV2A at two constellations of residues, namely Cluster-1 (Ser42, Ser45, and Ser47) and Cluster-2 (Ser80, Ser81, and Thr84). These residues are also phosphorylated in vivo, and the phosphorylation of Thr84 within Cluster-2 is essential for triggering binding to the C2B domain of human synaptotagmin-1 PubMed:25673844

Appears in Networks:

p(HGNC:TTBK2) increases p(HGNC:SV2A, pmod(Ph, Ser, 80)) View Subject | View Object

We demonstrate that Casein kinase 1 family members, including isoforms of Tau-tubulin protein kinases (TTBK1 and TTBK2), phosphorylate human SV2A at two constellations of residues, namely Cluster-1 (Ser42, Ser45, and Ser47) and Cluster-2 (Ser80, Ser81, and Thr84). These residues are also phosphorylated in vivo, and the phosphorylation of Thr84 within Cluster-2 is essential for triggering binding to the C2B domain of human synaptotagmin-1 PubMed:25673844

Appears in Networks:

p(HGNC:TTBK2) increases p(HGNC:SV2A, pmod(Ph, Ser, 81)) View Subject | View Object

We demonstrate that Casein kinase 1 family members, including isoforms of Tau-tubulin protein kinases (TTBK1 and TTBK2), phosphorylate human SV2A at two constellations of residues, namely Cluster-1 (Ser42, Ser45, and Ser47) and Cluster-2 (Ser80, Ser81, and Thr84). These residues are also phosphorylated in vivo, and the phosphorylation of Thr84 within Cluster-2 is essential for triggering binding to the C2B domain of human synaptotagmin-1 PubMed:25673844

Appears in Networks:

p(HGNC:TTBK2) increases p(HGNC:SV2A, pmod(Ph, Thr, 84)) View Subject | View Object

We demonstrate that Casein kinase 1 family members, including isoforms of Tau-tubulin protein kinases (TTBK1 and TTBK2), phosphorylate human SV2A at two constellations of residues, namely Cluster-1 (Ser42, Ser45, and Ser47) and Cluster-2 (Ser80, Ser81, and Thr84). These residues are also phosphorylated in vivo, and the phosphorylation of Thr84 within Cluster-2 is essential for triggering binding to the C2B domain of human synaptotagmin-1 PubMed:25673844

Appears in Networks:

p(HGNC:TTBK2) directlyIncreases p(HGNC:TARDBP, pmod(Ph)) View Subject | View Object

Using refined methodology, we demonstrate TTBK1 and TTBK2 directly phosphorylate TDP-43 in vitro and promote TDP-43 phosphorylation in mammalian cultured cells. TTBK1/2 overexpression drives phosphorylation and relocalization of TDP-43 from the nucleus to cytoplasmic inclusions reminiscent of neuropathologic changes in disease states. PubMed:25473830

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p(HGNC:TTBK2) increases tloc(p(HGNC:TARDBP, pmod(Ph)), fromLoc(GO:nucleus), toLoc(GO:cytoplasm)) View Subject | View Object

Using refined methodology, we demonstrate TTBK1 and TTBK2 directly phosphorylate TDP-43 in vitro and promote TDP-43 phosphorylation in mammalian cultured cells. TTBK1/2 overexpression drives phosphorylation and relocalization of TDP-43 from the nucleus to cytoplasmic inclusions reminiscent of neuropathologic changes in disease states. PubMed:25473830

Appears in Networks:

p(HGNC:TTBK2) decreases surf(p(HGNC:GRIK2)) View Subject | View Object

TTBK2 down-regulates GluK2 activity by decreasing the receptor protein abundance in the cell membrane via RAB5-dependent endocytosis, an effect that may protect against neuroexcitotoxicity. PubMed:27607061

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p(HGNC:TTBK2) increases p(HGNC:KIF2A, pmod(Ph)) View Subject | View Object

These findings indicate that TTBK2 with EB1/3 phosphorylates KIF2A and antagonizes KIF2A-induced depolymerization at MT plus ends for cell migration. PubMed:26323690

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p(HGNC:TTBK2) increases act(p(HGNC:SLC6A12)) View Subject | View Object

Upregulation of Na+Cl- coupled betaine/GABA transporter BGT1 for organic osmolytes PubMed:26323690

Appears in Networks:

p(HGNC:TTBK2) increases act(p(HGNC:SLC5A1)) View Subject | View Object

Upregulation of SLC5A1 Na-copled Glucose transport PubMed:26323690

Appears in Networks:

p(HGNC:TTBK2) association p(HGNC:CEP164) View Subject | View Object

TTBK2 bound EB1 and Cep164 through its SxIP motifs and a proline-rich motif, respectively. Using TTBK2 variants that contained mutations in the SxIP or proline-rich motifs, we obtained evidence that Cep164, but not EB1, is essential for centriolar localization of TTBK2. Therefore, Cep164 binding is essential for the function of TTBK2 in promoting CP110 removal and ciliogenesis. We also provide evidence that TTBK2 has the potential to effectively phosphorylate Cep164 and Cep97 and inhibits the interaction between Cep164 and its binding partner Dishevelled-3 (an important regulator of ciliogenesis) in a kinase activity-dependent manner. PubMed:26323690

Appears in Networks:

act(p(HGNC:TTBK2)) positiveCorrelation p(HGNC:CEP164) View Subject | View Object

TTBK2 bound EB1 and Cep164 through its SxIP motifs and a proline-rich motif, respectively. Using TTBK2 variants that contained mutations in the SxIP or proline-rich motifs, we obtained evidence that Cep164, but not EB1, is essential for centriolar localization of TTBK2. Therefore, Cep164 binding is essential for the function of TTBK2 in promoting CP110 removal and ciliogenesis. We also provide evidence that TTBK2 has the potential to effectively phosphorylate Cep164 and Cep97 and inhibits the interaction between Cep164 and its binding partner Dishevelled-3 (an important regulator of ciliogenesis) in a kinase activity-dependent manner. PubMed:26323690

Appears in Networks:

p(HGNC:TTBK2) association p(HGNC:MAPRE1) View Subject | View Object

TTBK2 bound EB1 and Cep164 through its SxIP motifs and a proline-rich motif, respectively. Using TTBK2 variants that contained mutations in the SxIP or proline-rich motifs, we obtained evidence that Cep164, but not EB1, is essential for centriolar localization of TTBK2. Therefore, Cep164 binding is essential for the function of TTBK2 in promoting CP110 removal and ciliogenesis. We also provide evidence that TTBK2 has the potential to effectively phosphorylate Cep164 and Cep97 and inhibits the interaction between Cep164 and its binding partner Dishevelled-3 (an important regulator of ciliogenesis) in a kinase activity-dependent manner. PubMed:26323690

Appears in Networks:

act(p(HGNC:TTBK2)) decreases p(HGNC:CCP110) View Subject | View Object

TTBK2 bound EB1 and Cep164 through its SxIP motifs and a proline-rich motif, respectively. Using TTBK2 variants that contained mutations in the SxIP or proline-rich motifs, we obtained evidence that Cep164, but not EB1, is essential for centriolar localization of TTBK2. Therefore, Cep164 binding is essential for the function of TTBK2 in promoting CP110 removal and ciliogenesis. We also provide evidence that TTBK2 has the potential to effectively phosphorylate Cep164 and Cep97 and inhibits the interaction between Cep164 and its binding partner Dishevelled-3 (an important regulator of ciliogenesis) in a kinase activity-dependent manner. PubMed:26323690

Appears in Networks:

act(p(HGNC:TTBK2)) increases p(HGNC:CEP164, pmod(Ph)) View Subject | View Object

TTBK2 bound EB1 and Cep164 through its SxIP motifs and a proline-rich motif, respectively. Using TTBK2 variants that contained mutations in the SxIP or proline-rich motifs, we obtained evidence that Cep164, but not EB1, is essential for centriolar localization of TTBK2. Therefore, Cep164 binding is essential for the function of TTBK2 in promoting CP110 removal and ciliogenesis. We also provide evidence that TTBK2 has the potential to effectively phosphorylate Cep164 and Cep97 and inhibits the interaction between Cep164 and its binding partner Dishevelled-3 (an important regulator of ciliogenesis) in a kinase activity-dependent manner. PubMed:26323690

Appears in Networks:

act(p(HGNC:TTBK2)) increases p(HGNC:CEP97, pmod(Ph)) View Subject | View Object

TTBK2 bound EB1 and Cep164 through its SxIP motifs and a proline-rich motif, respectively. Using TTBK2 variants that contained mutations in the SxIP or proline-rich motifs, we obtained evidence that Cep164, but not EB1, is essential for centriolar localization of TTBK2. Therefore, Cep164 binding is essential for the function of TTBK2 in promoting CP110 removal and ciliogenesis. We also provide evidence that TTBK2 has the potential to effectively phosphorylate Cep164 and Cep97 and inhibits the interaction between Cep164 and its binding partner Dishevelled-3 (an important regulator of ciliogenesis) in a kinase activity-dependent manner. PubMed:26323690

Appears in Networks:

p(HGNC:TTBK2) association path(MESH:Tauopathies) View Subject | View Object

Some of these enhancer genes are specific only to the tau-induced disease phenotype and include genes encoding proteins like WNT2 (111), TTBK2 (112), GSK-3b (113), TAOK1 (114, 115), CTSE (116) and CHRNA7 (117), have been implicated in tau-mediated pathology. PubMed:29191965

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BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.

If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.