Target intelligence / Profile preview

Ankyrin repeat and SOCS box protein 5 (ASB5)

Target
ASB5
Molecular classification
E3 ubiquitin ligase adaptor/substrate recognition protein, Ankyrin repeat-containing protein, SOCS box-containing protein, Other (SCF-like Cullin–RING E3 ligase component)
01

Overview

Ankyrin repeat and SOCS box protein 5 (ASB5) is a human protein that belongs to the ankyrin repeat and SOCS box-containing (ASB) family. These proteins contain an N-terminal ankyrin repeat domain for substrate recognition and a C-terminal SOCS box for assembly with Elongin B/C, Cul5, and Rbx2, forming part of Cullin–RING E3 ubiquitin ligase complexes. ASB proteins act as substrate-adaptor components, mediating the ubiquitination and subsequent proteasomal degradation of specific targets, thereby influencing diverse cellular processes such as protein turnover, signal transduction, and possibly vascular development. The specific substrates and physiological roles of ASB5 remain under investigation, but it is categorized structurally and functionally with other ASB family proteins that regulate key pathways in cell biology and disease.

Other names
ASB5Ankyrin repeat and SOCS box-containing protein 5Ankyrin repeat and SOCS box protein 5
02

Mechanism of action

Inhibition or modulation of substrate recognition and ubiquitination activity (disrupts recruitment of ubiquitin E2 enzymes and substrate interaction)

03

Biological functions

Substrate recognition for Cullin–RING E3 ligase complexesProtein ubiquitination (targets substrates for proteasomal degradation)Possibly initiation of arteriogenesis (formation of arteries), suggested by pathway similarity
04

Disease associations

Roles in disease remain incompletely characterized, but as a member of E3 ubiquitin ligase complexes, ASB family proteins have been implicated in:Cancer (protein degradation involvement)Inflammatory processes (by analogy to other SOCS box proteins)Cardiovascular disease (initiation of arteriogenesis/vascular remodeling)
05

Safety considerations

No notable safety issues reported specific to ASB5 as a direct therapeutic target. General challenges for E3 ligase targeting include potential off-target effects and proteostasis disruption.
06

Interacting drugs

None directly identified in current databases; therapeutic modulation of ASB5 would likely be via inhibitors or modulators of the Cullin–RING E3 ligase pathway. No approved drugs currently target ASB5 specifically.
07

Biomarkers

None currently validated for patient selection or efficacy monitoring; possible future biomarker utility if specific disease involvement is revealed.

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