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HECTD3 HECTD3 RNF19B RNF19B RNF19A RNF19A SPSB4 SPSB4 ASB6 ASB6 FBXW9 FBXW9 HERC2 HERC2 ANAPC5 ANAPC5 UBR2 UBR2 FBXL12 FBXL12 FBXO15 FBXO15 UBE3C UBE3C HERC6 HERC6 CDC34 CDC34 NEDD4 NEDD4 RNF144B RNF144B SOCS1 SOCS1 TRIM56 TRIM56 TRIM32 TRIM32 KBTBD10 KBTBD10 KLHL21 KLHL21 TRIM50 TRIM50 STUB1 STUB1 MYLIP MYLIP RNF182 RNF182 KLHL5 KLHL5
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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protein of unknown 3D structure
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query proteins and first shell of interactors
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second shell of interactors
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CDC34cell division cycle 34 homolog (S. cerevisiae); Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys- 48’-linked polyubiquitination. Cooperates with the E2 UBCH5C and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Performs ubiquitin chain elongation building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. UBE2D3 acts as an initiator E2, priming the phosphorylated NFKBIA target at positions ’Lys-21’ and/or ’Lys-22’ with a monoubiqu [...] (236 aa)
STUB1STIP1 homology and U-box containing protein 1, E3 ubiquitin protein ligase; E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates- ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 th [...] (303 aa)
FBXL12F-box and leucine-rich repeat protein 12; Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex (By similarity) (326 aa)
RNF144Bring finger protein 144B; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates such as LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin-dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se (303 aa)
HERC2HECT and RLD domain containing E3 ubiquitin protein ligase 2 (4834 aa)
ANAPC5anaphase promoting complex subunit 5; 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 (755 aa)
HERC6HECT and RLD domain containing E3 ubiquitin protein ligase family member 6 (1022 aa)
ASB6ankyrin repeat and SOCS box containing 6; Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (421 aa)
KBTBD10kelch repeat and BTB (POZ) domain containing 10; Involved in skeletal muscle development and differentiation. Regulates proliferation and differentiation of myoblasts and plays a role in myofibril assembly by promoting lateral fusion of adjacent thin fibrils into mature, wide myofibrils. Required for pseudopod elongation in transformed cells (By similarity) (606 aa)
TRIM56tripartite motif containing 56; E3 ubiquitin-protein ligase that mediates ’Lys-63’- linked polyubiquitination of TMEM173/STING, thereby playing a key role in innate immunity. TMEM173/STING ’Lys-63’-linked ubiquitination activates the production of type I interferon IFN- beta following detection of pathogen- and host-derived double- stranded DNA (By similarity) (755 aa)
UBE3Cubiquitin protein ligase E3C; E3 ubiquitin-protein ligase that accepts ubiquitin from the E2 ubiquitin-conjugating enzyme UBE2D1 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Can assemble unanchored poly-ubiquitin chains in either ’Lys-29’- or ’Lys-48’-linked polyubiquitin chains. Has preference for ’Lys-48’ linkages. It can target itself for ubiquitination in vitro and may promote its own degradation in vivo (1083 aa)
SPSB4splA/ryanodine receptor domain and SOCS box containing 4; 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)
TRIM50tripartite motif containing 50; E3 ubiquitin-protein ligase (487 aa)
SOCS1suppressor of cytokine signaling 1; SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS1 is involved in negative regulation of cytokines that signal through the JAK/STAT3 pathway. Through binding to JAKs, inhibits their kinase activity. In vitro, also suppresses Tec protein- tyrosine activity. Appears to be a major regulator of signaling by interleukin 6 (IL6) and leukemia inhibitory factor (LIF). Regulates interferon-gamma mediated sensory neuron survival (By similarity). Probable substrate recognition component of a [...] (211 aa)
RNF19Aring finger protein 19A, E3 ubiquitin protein ligase; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as SNCAIP or CASR. Specifically ubiquitinates pathogenic SOD1 variants, which leads to their proteasomal degradation and to neuronal protection (838 aa)
NEDD4neural precursor cell expressed, developmentally down-regulated 4, E3 ubiquitin protein ligase (1247 aa)
MYLIPmyosin regulatory light chain interacting protein; E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of myosin regulatory light chain (MRLC), LDLR, VLDLR and LRP8. Activity depends on E2 enzymes of the UBE2D family. Proteasomal degradation of MRLC leads to inhibit neurite outgrowth in presence of NGF by counteracting the stabilization of MRLC by saposin-like protein (CNPY2/MSAP) and reducing CNPY2-stimulated neurite outgrowth. Acts as a sterol- dependent inhibitor of cellular cholesterol uptake by mediating ubiquitination and subsequent deg [...] (445 aa)
HECTD3HECT domain containing E3 ubiquitin protein ligase 3; E3 ubiquitin ligases accepts 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 TRIOBP and its subsequent proteasomal degradation, thus faciliting cell cycle progression by regulating the turn-over of TRIOBP. Mediates also ubiquitination of STX8 (By similarity) (861 aa)
UBR2ubiquitin protein ligase E3 component n-recognin 2; E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Plays a critical role in chromatin inactivation and chromosome-wide transcriptional silencing during meiosis via ubiquitination of histone H2A. Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth (1755 aa)
RNF19Bring finger protein 19B; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as UCKL1. Involved in the cytolytic activity of natural killer cells and cytotoxic T-cells (732 aa)
TRIM32tripartite motif containing 32; Has an E3 ubiquitin ligase activity. Ubiquitinates DTNBP1 (dysbindin) and promotes its degradation. May play a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo. Binds specifically to the activation domain of HIV-1 Tat and can also interact with the HIV-2 and EIAV Tat proteins in vivo (653 aa)
KLHL21kelch-like 21 (Drosophila); Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for efficient chromosome alignment and cytokinesis. The BCR(KLHL21) E3 ubiquitin ligase complex regulates localization of the chromosomal passenger complex (CPC) from chromosomes to the spindle midzone in anaphase and mediates the ubiquitination of AURKB. Ubiquitination of AURKB by BCR(KLHL21) E3 ubiquitin ligase complex may not lead to its degradation by the proteasome (597 aa)
FBXW9F-box and WD repeat domain containing 9; Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex (By similarity) (458 aa)
FBXO15F-box protein 15; Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex (By similarity) (510 aa)
RNF182ring finger protein 182; E3 ubiquitin-protein ligase that mediates the ubiquitination of ATP6V0C and targets it to degradation via the ubiquitin-proteasome pathway (247 aa)
KLHL5kelch-like 5 (Drosophila) (755 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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