NMR structure of the p62 PB1 domainNMR structure of the p62 PB1 domain
Structural highlights
2kkc is a 1 chain structure with sequence from Rattus norvegicus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
SQSTM_RAT Required both for the formation and autophagic degradation of polyubiquitin-containing bodies, called ALIS (aggresome-like induced structures). Links ALIS to the autophagic machinery via direct interaction with MAP1 LC3 family members (By similarity). May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1. Adapter that mediates the interaction between TRAF6 and CYLD (By similarity). May play a role in titin/TTN downstream signaling in muscle cells. May regulate signaling cascades through ubiquitination. May be involved in cell differentiation, apoptosis, immune response and regulation of K(+) channels. Isoform 1 is more potent than isoform 2 to stimulate PRKCZ-dependent phosphorylation of KCNAB2.[1][2][3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
↑Gong J, Xu J, Bezanilla M, van Huizen R, Derin R, Li M. Differential stimulation of PKC phosphorylation of potassium channels by ZIP1 and ZIP2. Science. 1999 Sep 3;285(5433):1565-9. PMID:10477520
↑Wooten MW, Seibenhener ML, Mamidipudi V, Diaz-Meco MT, Barker PA, Moscat J. The atypical protein kinase C-interacting protein p62 is a scaffold for NF-kappaB activation by nerve growth factor. J Biol Chem. 2001 Mar 16;276(11):7709-12. Epub 2001 Jan 22. PMID:11244088 doi:10.1074/jbc.C000869200
↑Samuels IS, Seibenhener ML, Neidigh KB, Wooten MW. Nerve growth factor stimulates the interaction of ZIP/p62 with atypical protein kinase C and targets endosomal localization: evidence for regulation of nerve growth factor-induced differentiation. J Cell Biochem. 2001;82(3):452-66. PMID:11500922
