Protein Family Models

CYLD_phos_site is a natively unstructured region on a subset of tumour-suppressor and de-ubiquitinating enzyme CYLD proteins in eukaryotes. It lies between the second pair of CAP_GLY domains, Pfam:PF01302, on these proteins. This region of CYLD, being unstructured, carries a number of serine residues which, in response to cellular stimuli, become phosphorylated. This transient phosphorylation-state induces ubiquitination of TRAF2, a ubiquitin ligase that catalyses both self-ubiquitination and the ubiquitination of specific target molecules involved in signal transduction [1]. [1]. 15870263. Regulation of the deubiquitinating enzyme CYLD by IkappaB kinase. gamma-dependent phosphorylation.. Reiley W, Zhang M, Wu X, Granger E, Sun SC;. Mol Cell Biol. 2005;25:3886-3895. (from Pfam)

Date:

2024-08-14

This is a repeated domain found in de-ubiquitinating proteins. It's exact function is not known although it is likely to be involved in the binding of the Ubps in the complex with Rsp5 and Rup1. [1]. 20838651. A global census of fission yeast deubiquitinating enzyme. localization and interaction networks reveals distinct. compartmentalization profiles and overlapping functions in. endocytosis and polarity.. Kouranti I, McLean JR, Feoktistova A, Liang P, Johnson AE,. Roberts-Galbraith RH, Gould KL;. PLoS Biol. 2010; [Epub ahead of print]. [2]. 17079730. Hse1, a component of the yeast Hrs-STAM ubiquitin-sorting. complex, associates with ubiquitin peptidases and a ligase to. control sorting efficiency into multivesicular bodies.. Ren J, Kee Y, Huibregtse JM, Piper RC;. Mol Biol Cell. 2007;18:324-335. (from Pfam)

Date:

2024-08-14

RPN13_C is a family of all-helical domains that forms the binding-surface for the proteasome-ubiquitn-receptor protein Rpn13 to UCH37, one of the three de-ubiquitinating enzymes of the proteasome [1,2]. [1]. 16906146. Proteasome recruitment and activation of the Uch37. deubiquitinating enzyme by Adrm1.. Yao T, Song L, Xu W, DeMartino GN, Florens L, Swanson SK,. Washburn MP, Conaway RC, Conaway JW, Cohen RE;. Nat Cell Biol. 2006;8:994-1002.. [2]. 20471946. Structure of proteasome ubiquitin receptor hRpn13 and its. activation by the scaffolding protein hRpn2.. Chen X, Lee BH, Finley D, Walters KJ;. Mol Cell. 2010;38:404-415. (from Pfam)

Date:

2024-08-14

This family was thought originally to be involved in cell-adhesion [1,2], but the members are now known to be proteasome subunit Rpn13, a novel ubiquitin receptor. The 26S proteasome is a huge macromolecular protein-degradation machine consisting of a proteolytically active 20S core, in the form of four disc-like proteins, and one or two 19S regulatory particles. The regulatory particle(s) sit on the top and or bottom of the core, de-ubiquitinate the substrate peptides, unfold them and guide them into the narrow channel through the centre of the core. Rpn13 and its homologues dock onto the regulatory particle through the N-terminal region which binds Rpn2. The C-terminal part of the domain binds de-ubiquitinating enzyme Uch37/UCHL5 and enhances its isopeptidase activity. Rpn13 binds ubiquitin via a conserved amino-terminal region called the pleckstrin-like receptor for ubiquitin, termed Pru, domain [4]. The domain forms two contiguous anti-parallel beta-sheets with a configuration similar to the pleckstrin-homology domain (PHD) fold [5]. Rpn13's ability to bind ubiquitin and the proteasome subunit Rpn2/S1 simultaneously supports evidence of its role as a ubiquitin receptor. Finally, when complexed to di-ubiquitin, via the Pru, and Uch37 via the C-terminal part, it frees up the distal ubiquitin for de-ubiquitination by the Uch37 [5]. [1]. 10610020. Xoom: a novel oocyte membrane protein maternally expressed and. involved in the gastrulation movement of Xenopus embryos.. Hasegawa K, Shiraishi T, Kinoshita T;. Int J Dev Biol 1999;43:479-485.. [2]. 10919708. Functional cloning of ARM-1, an adhesion-regulating molecule. upregula. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-08-14