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Article

Structural and functional studies of mutations affecting the UBA domain of SQSTM1 (p62) which cause Paget's disease of bone.

Biochemical Society transactions - 1 Nov 2004

Layfield R, Ciani B, Ralston S H, Hocking L J, Sheppard P W, Searle M S, Cavey J R

Abstract excerpt

Mutations affecting the UBA (ubiquitin-associated) domain of SQSTM1 (Sequestosome 1) (p62) are a common cause of Paget's disease of bone. The missense mutations resolve into those which retain [P392L (Pro(392)-->Leu), G411S] or abolish (M404V, G425R) the ability of the isolated UBA domain to bind Lys-48-linked polyubiquitin. These effects can be rationalized with reference to the solution structure of the UBA...

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Identifiers

PMID: 15493999
DOI: 10.1042/BST0320728

Genes

SQSTM1

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Structural and functional studies of mutations affecting the UBA domain of SQSTM1 (p62) which cause Paget's disease of bone.PMID 15493999Read ↗

Structure of the ubiquitin-associated domain of p62 (SQSTM1) and implications for mutations that cause Paget's disease of bone.Semantic proximity Read ↗

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Novel UBA domain mutations of SQSTM1 in Paget's disease of bone: genotype phenotype correlation, functional analysis, and structural consequences.Semantic proximity Read ↗

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Dimerisation of the UBA domain of p62 inhibits ubiquitin binding and regulates NF-kappaB signalling.Semantic proximity Read ↗

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