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p(HBP:"VQIINK motif")

Equivalencies: 2 | Classes: 0 | Children: 0 | Explore

Entity

Name
VQIINK motif
Namespace
HBP
Namespace Version
20181119
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/90e1cb9e5e882703380c9db8d4915ac6f3cba137/export/hbp-names.belns

Appears in Networks 3

Tau Biochemistry v1.2.5

Tau Biochemistry Section of NESTOR

Tau Modifications v1.9.5

Tau Modifications Sections of NESTOR

Tau in physiology and pathology v1.0.0

In-Edges 6

p(HGNC:MAPT, pmod(Ac, Lys, 280)) partOf p(HBP:"VQIINK motif") View Subject | View Object

Appears in Networks:

p(HGNC:MAPT, pmod(Ac, Lys, 281)) partOf p(HBP:"VQIINK motif") View Subject | View Object

Appears in Networks:

p(HGNC:MAP4, frag("1023_1030")) equivalentTo p(HBP:"VQIINK motif") View Subject | View Object

Appears in Networks:

p(HGNC:MAP4, frag("992_999")) equivalentTo p(HBP:"VQIINK motif") View Subject | View Object

Appears in Networks:

p(HGNC:MAPT, var("p.Lys280del")) positiveCorrelation p(HBP:"VQIINK motif") View Subject | View Object

We also show that two of the tau mutations found in hereditary frontotemporal dementias, DeltaK280 and P301L, have a much stronger tendency for PHF aggregation which correlates with their high propensity for beta-structure around the hexapeptide motifs. PubMed:11606569

Appears in Networks:

p(HGNC:MAPT, var("p.Pro301Leu")) positiveCorrelation p(HBP:"VQIINK motif") View Subject | View Object

We also show that two of the tau mutations found in hereditary frontotemporal dementias, DeltaK280 and P301L, have a much stronger tendency for PHF aggregation which correlates with their high propensity for beta-structure around the hexapeptide motifs. PubMed:11606569

Appears in Networks:

Out-Edges 9

p(HBP:"VQIINK motif") partOf p(HBP:"tubulin-binding repeat 2") View Subject | View Object

Appears in Networks:

p(HBP:"VQIINK motif") increases bp(GO:"neurofibrillary tangle assembly") View Subject | View Object

Two hexapeptide motifs at the beginning of R2 and R3 promote paired helical filament (PHF) aggregation by inducing β-structure. PubMed:17493042

Appears in Networks:
Annotations
Uberon
brain

p(HBP:"VQIINK motif") equivalentTo p(HGNC:MAP4, frag("992_999")) View Subject | View Object

Appears in Networks:

p(HBP:"VQIINK motif") equivalentTo p(HGNC:MAP4, frag("1023_1030")) View Subject | View Object

Appears in Networks:

p(HBP:"VQIINK motif") positiveCorrelation p(HGNC:MAPT, var("p.Lys280del")) View Subject | View Object

We also show that two of the tau mutations found in hereditary frontotemporal dementias, DeltaK280 and P301L, have a much stronger tendency for PHF aggregation which correlates with their high propensity for beta-structure around the hexapeptide motifs. PubMed:11606569

Appears in Networks:

p(HBP:"VQIINK motif") positiveCorrelation p(HGNC:MAPT, var("p.Pro301Leu")) View Subject | View Object

We also show that two of the tau mutations found in hereditary frontotemporal dementias, DeltaK280 and P301L, have a much stronger tendency for PHF aggregation which correlates with their high propensity for beta-structure around the hexapeptide motifs. PubMed:11606569

Appears in Networks:

p(HBP:"VQIINK motif") increases p(HBP:"Tau aggregates") View Subject | View Object

We also show that two of the tau mutations found in hereditary frontotemporal dementias, DeltaK280 and P301L, have a much stronger tendency for PHF aggregation which correlates with their high propensity for beta-structure around the hexapeptide motifs. PubMed:11606569

Appears in Networks:

p(HBP:"VQIINK motif") increases a(HBP:"Tau aggregates") View Subject | View Object

The two short hexapeptide motifs VQIINK and VQIVYK at the beginning of R2 and R3, respectively, show propensity for forming β‑sheet structures and are essential for tau aggregation, even though they comprise only a tiny fraction of the sequence PubMed:26631930

Appears in Networks:

p(HBP:"VQIINK motif") increases a(HBP:"Tau aggregates") View Subject | View Object

Disruption of these motifs (for example, by Pro mutations) abrogates the tendency for tau to aggregate; by contrast, strengthening the β‑structure with certain mutations (for instance, ΔK280 or P301L) accelerates tau aggregation both in vitro and in vivo PubMed:26631930

Appears in Networks:

About

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.