Entry Database : PDB / ID : 2vhf Structure visualization Downloads & linksTitle Structure of the CYLD USP domain ComponentsUBIQUITIN CARBOXYL-TERMINAL HYDROLASE CYLD Details Keywords HYDROLASE / CYTOKINE SIGNALLING / LINKAGE SPECIFICITY / DEUBIQUITINATING ENZYME / LYS63- LINKED / ANTI-ONCOGENE / THIOL PROTEASE / CELL SIGNALLING / PHOSPHORYLATION / ZN-BINDING DOMAIN / UBIQUITIN / CELL CYCLE / USP DOMAIN / CROSS-BRACE / NF-KB / B-BOX / PROTEASE / CYTOPLASM / ALTERNATIVE SPLICING / UBL CONJUGATION PATHWAYFunction / homology Function and homology informationFunction Domain/homology Component
negative regulation of interleukin-18-mediated signaling pathway / Met1-linked polyubiquitin deubiquitinase activity / protein linear deubiquitination / ripoptosome assembly involved in necroptotic process / regulation of intrinsic apoptotic signaling pathway / regulation of B cell differentiation / nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway / regulation of cilium assembly / negative regulation of p38MAPK cascade / ciliary tip ... negative regulation of interleukin-18-mediated signaling pathway / Met1-linked polyubiquitin deubiquitinase activity / protein linear deubiquitination / ripoptosome assembly involved in necroptotic process / regulation of intrinsic apoptotic signaling pathway / regulation of B cell differentiation / nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway / regulation of cilium assembly / negative regulation of p38MAPK cascade / ciliary tip / regulation of necroptotic process / CD4-positive or CD8-positive, alpha-beta T cell lineage commitment / negative regulation of JNK cascade / regulation of tumor necrosis factor-mediated signaling pathway / positive regulation of extrinsic apoptotic signaling pathway / proline-rich region binding / K48-linked deubiquitinase activity / negative regulation of non-canonical NF-kappaB signal transduction / TNFR1-induced proapoptotic signaling / positive regulation of T cell differentiation / negative regulation of type I interferon production / K63-linked deubiquitinase activity / positive regulation of protein localization / negative regulation of NF-kappaB transcription factor activity / positive regulation of T cell receptor signaling pathway / protein deubiquitination / necroptotic process / homeostasis of number of cells / regulation of microtubule cytoskeleton organization / regulation of mitotic cell cycle / ciliary basal body / TNFR1-induced NF-kappa-B signaling pathway / Negative regulators of DDX58/IFIH1 signaling / Regulation of TNFR1 signaling / NOD1/2 Signaling Pathway / negative regulation of canonical Wnt signaling pathway / Wnt signaling pathway / negative regulation of inflammatory response / spindle / regulation of inflammatory response / microtubule / ubiquitinyl hydrolase 1 / cysteine-type deubiquitinase activity / Ub-specific processing proteases / cell cycle / innate immune response / centrosome / protein kinase binding / perinuclear region of cytoplasm / proteolysis / zinc ion binding / plasma membrane / cytosol Similarity search - Function Phosphorylation region of CYLD, unstructured / CAP-Gly domain signature. / CAP Gly-rich domain / CAP Gly-rich domain superfamily / CAP-Gly domain / CAP-Gly domain profile. / CAP_GLY / Ubiquitin specific protease (USP) domain signature 1. / Ubiquitin specific protease, conserved site / Peptidase C19, ubiquitin carboxyl-terminal hydrolase ... Phosphorylation region of CYLD, unstructured / CAP-Gly domain signature. / CAP Gly-rich domain / CAP Gly-rich domain superfamily / CAP-Gly domain / CAP-Gly domain profile. / CAP_GLY / Ubiquitin specific protease (USP) domain signature 1. / Ubiquitin specific protease, conserved site / Peptidase C19, ubiquitin carboxyl-terminal hydrolase / Ubiquitin carboxyl-terminal hydrolase / Ubiquitin specific protease domain / Ubiquitin specific protease (USP) domain profile. / Cysteine proteinases / Cathepsin B; Chain A / Papain-like cysteine peptidase superfamily / Alpha-Beta Complex / Alpha Beta Similarity search - Domain/homologyBiological species HOMO SAPIENS (human)Method X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution : 2.8 Å DetailsAuthors Komander, D. / Lord, C.J. / Scheel, H. / Swift, S. / Hofmann, K. / Ashworth, A. / Barford, D. CitationJournal : Mol.Cell.Biol. / Year : 2008Title : The Structure of the Cyld Usp Domain Explains its Specificity for Lys63-Linked Polyubiquitin and Reveals a B-Box ModuleAuthors : Komander, D. / Lord, C.J. / Scheel, H. / Swift, S. / Hofmann, K. / Ashworth, A. / Barford, D. History Deposition Nov 21, 2007 Deposition site : PDBE / Processing site : PDBERevision 1.0 Mar 11, 2008 Provider : repository / Type : Initial releaseRevision 1.1 May 8, 2011 Group : Version format complianceRevision 1.2 Jul 13, 2011 Group : Version format complianceRevision 1.3 May 8, 2024 Group : Data collection / Database references ... Data collection / Database references / Derived calculations / Other / Refinement description Category : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_struct_conn_angle / software / struct_conn Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _software.name / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id
Show all Show less Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.