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p(HGNC:TTBK1)

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Entity

Name
TTBK1
Namespace
hgnc
Namespace Version
20180906
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/hgnc-names.belns

Appears in Networks 1

Tau Modifications v1.9.5

Tau Modifications Sections of NESTOR

In-Edges 4

a(HBP:pretangles) association p(HGNC:TTBK1) View Subject | View Object

These data suggest a role for TTBK1 in pre-tangle formation prior to the formation of fibrillar tau and strengthen the idea that tau is phosphorylated at Ser422 at an early intermediate stage in NFT formation. PubMed:18239272

Appears in Networks:

act(p(ECCODE:"3.4.22.52")) positiveCorrelation p(HGNC:TTBK1) View Subject | View Object

TTBK1-Tg mice show significant age-dependent memory impairment as determined by radial arm water maze test, which is associated with enhancement of tau and neurofilament phosphorylation, increased levels of p25 and p35, both activators of cyclin-dependent protein kinase 5 (CDK5), enhanced calpain I activity, and reduced levels of hippocampal NMDA receptor types 2B (NR2B) and D. Enhanced CDK5/p35 complex formation is strongly correlated with dissociation of F-actin from p35, suggesting the inhibitory mechanism of CDK5/p35 complex formation by F-actin. PubMed:21548880

Appears in Networks:

p(HGNC:GRIN2B) negativeCorrelation p(HGNC:TTBK1) View Subject | View Object

TTBK1-Tg mice show significant age-dependent memory impairment as determined by radial arm water maze test, which is associated with enhancement of tau and neurofilament phosphorylation, increased levels of p25 and p35, both activators of cyclin-dependent protein kinase 5 (CDK5), enhanced calpain I activity, and reduced levels of hippocampal NMDA receptor types 2B (NR2B) and D. Enhanced CDK5/p35 complex formation is strongly correlated with dissociation of F-actin from p35, suggesting the inhibitory mechanism of CDK5/p35 complex formation by F-actin. PubMed:21548880

Appears in Networks:

p(HGNC:GRIN2D) negativeCorrelation p(HGNC:TTBK1) View Subject | View Object

TTBK1-Tg mice show significant age-dependent memory impairment as determined by radial arm water maze test, which is associated with enhancement of tau and neurofilament phosphorylation, increased levels of p25 and p35, both activators of cyclin-dependent protein kinase 5 (CDK5), enhanced calpain I activity, and reduced levels of hippocampal NMDA receptor types 2B (NR2B) and D. Enhanced CDK5/p35 complex formation is strongly correlated with dissociation of F-actin from p35, suggesting the inhibitory mechanism of CDK5/p35 complex formation by F-actin. PubMed:21548880

Appears in Networks:

Out-Edges 22

p(HGNC:TTBK1) increases p(HGNC:MAPT, pmod(Ph, Thr, 205)) View Subject | View Object

Epitopes S198, S199, S202, T205, S422 (Lund 2013) PubMed:18239272

Appears in Networks:

p(HGNC:TTBK1) increases p(HGNC:MAPT, pmod(Ph, Ser, 422)) View Subject | View Object

Epitopes S198, S199, S202, T205, S422 (Lund 2013) PubMed:18239272

Appears in Networks:

p(HGNC:TTBK1) increases p(HGNC:MAPT, pmod(Ph, Ser, 198)) View Subject | View Object

Epitopes S198, S199, S202, T205, S422 (Lund 2013) PubMed:18239272

Appears in Networks:

p(HGNC:TTBK1) increases p(HGNC:MAPT, pmod(Ph, Ser, 199)) View Subject | View Object

Epitopes S198, S199, S202, T205, S422 (Lund 2013) PubMed:18239272

Appears in Networks:

p(HGNC:TTBK1) increases p(HGNC:MAPT, pmod(Ph, Ser, 202)) View Subject | View Object

Epitopes S198, S199, S202, T205, S422 (Lund 2013) PubMed:18239272

Appears in Networks:

p(HGNC:TTBK1) association a(HBP:pretangles) View Subject | View Object

These data suggest a role for TTBK1 in pre-tangle formation prior to the formation of fibrillar tau and strengthen the idea that tau is phosphorylated at Ser422 at an early intermediate stage in NFT formation. PubMed:18239272

Appears in Networks:

p(HGNC:TTBK1) increases act(p(HGNC:CDK5)) View Subject | View Object

Activates cdk5 and GSK3; genetic variation protects against AD in Spanish cohort PubMed:20096481

Appears in Networks:

p(HGNC:TTBK1) increases act(p(HGNC:GSK3B), ma(kin)) View Subject | View Object

Activates cdk5 and GSK3; genetic variation protects against AD in Spanish cohort PubMed:20096481

Appears in Networks:

p(HGNC:TTBK1) increases p(HGNC:CDK5R1) View Subject | View Object

TTBK1-Tg mice show significant age-dependent memory impairment as determined by radial arm water maze test, which is associated with enhancement of tau and neurofilament phosphorylation, increased levels of p25 and p35, both activators of cyclin-dependent protein kinase 5 (CDK5), enhanced calpain I activity, and reduced levels of hippocampal NMDA receptor types 2B (NR2B) and D. Enhanced CDK5/p35 complex formation is strongly correlated with dissociation of F-actin from p35, suggesting the inhibitory mechanism of CDK5/p35 complex formation by F-actin. PubMed:21548880

Appears in Networks:

p(HGNC:TTBK1) positiveCorrelation act(p(ECCODE:"3.4.22.52")) View Subject | View Object

TTBK1-Tg mice show significant age-dependent memory impairment as determined by radial arm water maze test, which is associated with enhancement of tau and neurofilament phosphorylation, increased levels of p25 and p35, both activators of cyclin-dependent protein kinase 5 (CDK5), enhanced calpain I activity, and reduced levels of hippocampal NMDA receptor types 2B (NR2B) and D. Enhanced CDK5/p35 complex formation is strongly correlated with dissociation of F-actin from p35, suggesting the inhibitory mechanism of CDK5/p35 complex formation by F-actin. PubMed:21548880

Appears in Networks:

p(HGNC:TTBK1) negativeCorrelation p(HGNC:GRIN2B) View Subject | View Object

TTBK1-Tg mice show significant age-dependent memory impairment as determined by radial arm water maze test, which is associated with enhancement of tau and neurofilament phosphorylation, increased levels of p25 and p35, both activators of cyclin-dependent protein kinase 5 (CDK5), enhanced calpain I activity, and reduced levels of hippocampal NMDA receptor types 2B (NR2B) and D. Enhanced CDK5/p35 complex formation is strongly correlated with dissociation of F-actin from p35, suggesting the inhibitory mechanism of CDK5/p35 complex formation by F-actin. PubMed:21548880

Appears in Networks:

p(HGNC:TTBK1) negativeCorrelation p(HGNC:GRIN2D) View Subject | View Object

TTBK1-Tg mice show significant age-dependent memory impairment as determined by radial arm water maze test, which is associated with enhancement of tau and neurofilament phosphorylation, increased levels of p25 and p35, both activators of cyclin-dependent protein kinase 5 (CDK5), enhanced calpain I activity, and reduced levels of hippocampal NMDA receptor types 2B (NR2B) and D. Enhanced CDK5/p35 complex formation is strongly correlated with dissociation of F-actin from p35, suggesting the inhibitory mechanism of CDK5/p35 complex formation by F-actin. PubMed:21548880

Appears in Networks:

p(HGNC:TTBK1) isA p(HBP:"CK1 superfamily") View Subject | View Object

Appears in Networks:

p(HGNC:TTBK1) 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

Appears in Networks:

p(HGNC:TTBK1) 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:TTBK1) 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:TTBK1) 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:TTBK1) 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:TTBK1) 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:TTBK1) 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

Appears in Networks:

p(HGNC:TTBK1) 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:

act(p(HGNC:TTBK1), ma(kin)) directlyIncreases p(HGNC:MAPT, pmod(Ph, Tyr, 197)) View Subject | View Object

The single kinase and sequential kinase-catalyzed Fc-phosphorylations points to dramatic changes around the Fc group in the Fc-phosphorylated tau films. Additional surface characterization of the Fc-tau films by time-of-flight secondary ion-mass spectrometry and X-ray photoelectron spectroscopy revealed that Fc-phosphorylations influence the tau orientation and conformation on surfaces. PubMed:23687953

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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.