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a(HBP:"proline-rich domain")

Equivalencies: 1 | Classes: 0 | Children: 0 | Explore

Entity

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

Appears in Networks 2

Tau Biochemistry v1.2.5

Tau Biochemistry Section of NESTOR

Tau Modifications v1.9.5

Tau Modifications Sections of NESTOR

In-Edges 8

a(HBP:"proline-rich region 1") partOf a(HBP:"proline-rich domain") View Subject | View Object

Appears in Networks:

a(HBP:"proline-rich region 2") partOf a(HBP:"proline-rich domain") View Subject | View Object

Appears in Networks:

p(INTERPRO:"PSP, proline-rich") equivalentTo a(HBP:"proline-rich domain") View Subject | View Object

Appears in Networks:

act(p(FPLX:Actin)) association a(HBP:"proline-rich domain") View Subject | View Object

However, robust monomethylation was identified at seven sites distributed throughout the tau sequence (Table 1). Three of the sites (K163, K174, and K180) reside within the proline-rich region of the tau N-terminal projection domain, which mediates interactions with microtubule-associated proteins such as actin [27] and the Src homology three domain of plasma membrane-associated proteins including Src family kinases [37] and phospholipase Cc [54]. In contrast, K254, K267, and K290 are part of the first and second repeats of the microtubule binding domain. Although no Lys acetylation was detected at these sites in our datasets, it was possible to quantify relative methylation and ubiquitylation of K254. PubMed:22033876

Appears in Networks:
Annotations
Uberon
hippocampal formation
Disease Ontology (DO)
Alzheimer's disease

p(HGNC:MAPT, pmod(Me, Lys, 163)) partOf a(HBP:"proline-rich domain") View Subject | View Object

Appears in Networks:

p(HGNC:MAPT, pmod(Me, Lys, 174)) partOf a(HBP:"proline-rich domain") View Subject | View Object

Appears in Networks:

p(HGNC:MAPT, pmod(Me, Lys, 180)) partOf a(HBP:"proline-rich domain") View Subject | View Object

Appears in Networks:

p(INTERPRO:"SH3 domain") association a(HBP:"proline-rich domain") View Subject | View Object

However, robust monomethylation was identified at seven sites distributed throughout the tau sequence (Table 1). Three of the sites (K163, K174, and K180) reside within the proline-rich region of the tau N-terminal projection domain, which mediates interactions with microtubule-associated proteins such as actin [27] and the Src homology three domain of plasma membrane-associated proteins including Src family kinases [37] and phospholipase Cc [54]. In contrast, K254, K267, and K290 are part of the first and second repeats of the microtubule binding domain. Although no Lys acetylation was detected at these sites in our datasets, it was possible to quantify relative methylation and ubiquitylation of K254. PubMed:22033876

Appears in Networks:
Annotations
Uberon
hippocampal formation
Disease Ontology (DO)
Alzheimer's disease

Out-Edges 3

a(HBP:"proline-rich domain") equivalentTo p(INTERPRO:"PSP, proline-rich") View Subject | View Object

Appears in Networks:

a(HBP:"proline-rich domain") association act(p(FPLX:Actin)) View Subject | View Object

However, robust monomethylation was identified at seven sites distributed throughout the tau sequence (Table 1). Three of the sites (K163, K174, and K180) reside within the proline-rich region of the tau N-terminal projection domain, which mediates interactions with microtubule-associated proteins such as actin [27] and the Src homology three domain of plasma membrane-associated proteins including Src family kinases [37] and phospholipase Cc [54]. In contrast, K254, K267, and K290 are part of the first and second repeats of the microtubule binding domain. Although no Lys acetylation was detected at these sites in our datasets, it was possible to quantify relative methylation and ubiquitylation of K254. PubMed:22033876

Appears in Networks:
Annotations
Uberon
hippocampal formation
Disease Ontology (DO)
Alzheimer's disease

a(HBP:"proline-rich domain") association p(INTERPRO:"SH3 domain") View Subject | View Object

However, robust monomethylation was identified at seven sites distributed throughout the tau sequence (Table 1). Three of the sites (K163, K174, and K180) reside within the proline-rich region of the tau N-terminal projection domain, which mediates interactions with microtubule-associated proteins such as actin [27] and the Src homology three domain of plasma membrane-associated proteins including Src family kinases [37] and phospholipase Cc [54]. In contrast, K254, K267, and K290 are part of the first and second repeats of the microtubule binding domain. Although no Lys acetylation was detected at these sites in our datasets, it was possible to quantify relative methylation and ubiquitylation of K254. PubMed:22033876

Appears in Networks:
Annotations
Uberon
hippocampal formation
Disease Ontology (DO)
Alzheimer's disease

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.