Your Input:
|
||||
FBXL15 | F-box and leucine-rich repeat protein 15 (300 aa) | |||
MKRN1 | makorin ring finger protein 1 (482 aa) | |||
UBE2R2 | ubiquitin-conjugating enzyme E2R 2; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes monoubiquitination and ’Lys-48’-linked polyubiquitination. May be involved in degradation of katenin (238 aa) | |||
LNX1 | ligand of numb-protein X 1, E3 ubiquitin protein ligase; E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of NUMB. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ubiquitination of isoform p66 and isoform p72 of NUMB, but not that of isoform p71 or isoform p65 (By similarity) (728 aa) | |||
FBXO7 | F-box protein 7; Substrate recognition component of a (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes BIRC2 and DLGAP5 (522 aa) | |||
UBE2L6 | ubiquitin-conjugating enzyme E2L 6; Catalyzes the covalent attachment of ubiquitin or ISG15 to other proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Promotes ubiquitination and subsequent proteasomal degradation of FLT3 (153 aa) | |||
FBXO17 | F-box protein 17; Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. Able to recognize and bind denatured glycoproteins, which are modified with complex- type oligosaccharides. Also recognizes sulfated glycans. Does not bind high-mannose glycoproteins (278 aa) | |||
TRIM9 | tripartite motif containing 9; E3 ubiquitin-protein ligase which ubiquitinates itself in cooperation with an E2 enzyme UBE2D2/UBC4 and serves as a targeting signal for proteasomal degradation. May play a role in regulation of neuronal functions and may also participate in the formation or breakdown of abnormal inclusions in neurodegenerative disorders. May act as a regulator of synaptic vesicle exocytosis by controlling the availability of SNAP25 for the SNARE complex formation (710 aa) | |||
FBXO22 | F-box protein 22; Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. Promotes the proteasome-dependent degradation of key sarcomeric proteins, such as alpha-actinin (ACTN2) and filamin-C (FLNC), essential for maintenance of normal contractile function (403 aa) | |||
FBXW8 | F-box and WD repeat domain containing 8; Substrate-recognition component of a SCF-like E3 ubiquitin-protein ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. In complex with CUL7, mediates ubiquitination and consequent degradation of GORASP1, acting as a component of the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain (598 aa) | |||
TRAF7 | TNF receptor-associated factor 7, E3 ubiquitin protein ligase; E3 ubiquitin ligase capable of auto-ubiquitination, following phosphorylation by MAP3K3. Potentiates MEKK3-mediated activation of the NF-kappa-B, JUN/AP1 and DDIT3 transcriptional regulators. Induces apoptosis when overexpressed (670 aa) | |||
FBXO21 | F-box protein 21; Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex (By similarity) (628 aa) | |||
SPSB1 | splA/ryanodine receptor domain and SOCS box containing 1; Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (273 aa) | |||
SOCS3 | suppressor of cytokine signaling 3; SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS3 is involved in negative regulation of cytokines that signal through the JAK/STAT pathway. Inhibits cytokine signal transduction by binding to tyrosine kinase receptors including gp130, LIF, erythropoietin, insulin, IL12, GCSF and leptin receptors. Binding to JAK2 inhibits its kinase activity. Suppresses fetal liver erythropoiesis. Regulates onset and maintenance of allergic responses mediated by T-helper type 2 cells. Regulates IL [...] (225 aa) | |||
TRIM69 | tripartite motif containing 69; May have E3 ubiquitin-protein ligase activity. May play a role in apoptosis (500 aa) | |||
FBXO40 | F-box protein 40; Probable substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex that may function in myogenesis (By similarity) (709 aa) | |||
FBXL14 | F-box and leucine-rich repeat protein 14; Substrate-recognition component of some SCF (SKP1-CUL1- F-box protein)-type E3 ubiquitin-protein ligase complexes. The SCF(FBXL14) complex acts by mediating ubiquitination and subsequent degradation of SNAI1 (418 aa) | |||
FBXL3 | F-box and leucine-rich repeat protein 3; Substrate-recognition component of the SCF(FBXL3) E3 ubiquitin ligase complex involved in circadian rhythm function. Plays a key role in the maintenance of both the speed and the robustness of the circadian clock oscillation. The SCF(FBXL3) complex mainly acts in the nucleus and mediates ubiquitination and subsequent degradation of CRY1 and CRY2. Activity of the SCF(FBXL3) complex is counteracted by the SCF(FBXL21) complex. FBXL3 probably recognizes and binds phosphorylated CRY1 and CRY2 (428 aa) | |||
FBXW2 | F-box and WD repeat domain containing 2; Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex (454 aa) | |||
UNKL | unkempt homolog (Drosophila)-like; May participate in a protein complex showing an E3 ligase activity regulated by RAC1. Ubiquitination is directed towards itself and possibly other substrates, such as SMARCD2/BAF60b. Intrinsic E3 ligase activity has not been proven (680 aa) | |||
UBE2E3 | ubiquitin-conjugating enzyme E2E 3; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys- 11’- and ’Lys-48’-, as well as ’Lys-63’-linked polyubiquitination. Participates in the regulation of transepithelial sodium transport in renal cells. May be involved in cell growth arrest (207 aa) | |||
BTBD6 | BTB (POZ) domain containing 6; Adapter protein for the CUL3 E3 ubiquitin-protein ligase complex. Involved in late neuronal development and muscle formation (By similarity) (485 aa) | |||
LONRF1 | LON peptidase N-terminal domain and ring finger 1 (773 aa) | |||
MEX3C | mex-3 homolog C (C. elegans); E3 ubiquitin ligase responsible for the post- transcriptional regulation of common HLA-A allotypes. Binds to the 3’ UTR of HLA-A2 mRNA, and regulates its levels by promoting mRNA decay. RNA binding is sufficient to prevent translation, but ubiquitin ligase activity is required for mRNA degradation (659 aa) | |||
ANAPC7 | anaphase promoting complex subunit 7; Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins- it mainly mediates the formation of ’Lys-11’-linked polyubiquitin chains and, to a lower extent, the formation of ’Lys-48’- and ’Lys-63’-linked polyubiquitin chains (599 aa) | |||
KCTD7 | potassium channel tetramerisation domain containing 7; Rab effector protein acting as linker between gamma- adaptin, RAB4A or RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Stimulates nucleotide exchange on RAB5A. Can act as a ubiquitin ligase (By similarity) (491 aa) |