ubiquitin carboxyl-terminal esterase L1 (ubiquitin thiolesterase); Ubiquitin-protein hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. Also binds to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer may have ATP-independent ubiquitin ligase activity (223 aa)

annexin A10 (324 aa)

mesogenin 1; Involved in specifying the paraxial, but not dorsal, mesoderm. May regulate the expression of T-box transcription factors required for mesoderm formation and differentiation (By similarity) (193 aa)

visinin-like 1; Regulates (in vitro) the inhibition of rhodopsin phosphorylation in a calcium-dependent manner (By similarity) (191 aa)

sparc/osteonectin, cwcv and kazal-like domains proteoglycan (testican) 3 (436 aa)

ankyrin repeat domain 46 (228 aa)

serine/threonine/tyrosine interacting protein; Probable pseudophosphatase. Contains a Gly residue instead of a conserved Cys residue in the dsPTPase catalytic loop which renders it catalytically inactive as a phosphatase. The binding pocket is however sufficiently preserved to bind phosphorylated substrates, and maybe protect them from phosphatases. Seems to play a role in spermiogenesis (By similarity) (223 aa)

ring finger protein 31; E3 ubiquitin-protein ligase component of the LUBAC complex which conjugates linear (’M-1’-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF- induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) followi [...] (1072 aa)