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CDC16 CDC16 ANAPC10 ANAPC10 VPRBP VPRBP TRIM71 TRIM71 TRIM69 TRIM69 HECTD1 HECTD1 LRSAM1 LRSAM1 SOCS1 SOCS1 UBE2A UBE2A SOCS3 SOCS3 TRIM41 TRIM41 KLHDC5 KLHDC5 TRIM4 TRIM4 UBA6 UBA6 ITCH ITCH HECTD2 HECTD2 RCHY1 RCHY1 HECW2 HECW2 RNF19A RNF19A UBE2L6 UBE2L6 FBXO7 FBXO7 ZNF645 ZNF645 ZNRF1 ZNRF1 FBXO31 FBXO31 RNF34 RNF34 FBXL5 FBXL5
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Size
small protein node
small nodes:
protein of unknown 3D structure
large protein node
large nodes:
some 3D structure is known or predicted
Node Color
colored protein node
colored nodes:
query proteins and first shell of interactors
non-colored protein node
white nodes:
second shell of interactors
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.
Known Interactions
database edge
from curated databases
experiment edge
experimentally determined
Predicted Interactions
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gene neighborhood
fusion edge
gene fusions
cooccurrence edge
gene co-occurrence
Others
textmining edge
textmining
coexpression edge
co-expression
homology edge
protein homology
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HECW2HECT, C2 and WW domain containing E3 ubiquitin protein ligase 2; E3 ubiquitin-protein ligase that mediates ubiquitination of TP73. Acts to stabilize TP73 and enhance activation of transcription by TP73 (1572 aa)
FBXO7F-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)
UBE2L6ubiquitin-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)
HECTD2HECT domain containing E3 ubiquitin protein ligase 2; Probable E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (By similarity) (776 aa)
LRSAM1leucine rich repeat and sterile alpha motif containing 1; E3 ubiquitin-protein ligase that mediates monoubiquitination of TSG101 at multiple sites, leading to inactivate the ability of TSG101 to sort endocytic (EGF receptors) and exocytic (HIV-1 viral proteins) cargos (723 aa)
ANAPC10anaphase promoting complex subunit 10; 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 (185 aa)
FBXO31F-box protein 31; Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in G1 arrest following DNA damage. Specifically recognizes phosphorylated cyclin-D1 (CCND1), promoting its ubiquitination and degradation by the proteasome, resulting in G1 arrest. May act as a tumor suppressor (539 aa)
UBA6ubiquitin-like modifier activating enzyme 6 (1052 aa)
TRIM41tripartite motif containing 41; Functions as an E3 ligase that catalyzes the ubiquitin- mediated degradation of protein kinase C (630 aa)
RCHY1ring finger and CHY zinc finger domain containing 1, E3 ubiquitin protein ligase; Mediates E3-dependent ubiquitination and proteasomal degradation of target proteins, including p53/TP53, P73, HDAC1 and CDKN1B. Preferentially acts on tetrameric p53/TP53. Monoubiquitinates the translesion DNA polymerase POLH. Contributes to the regulation of the cell cycle progression. Increases AR transcription factor activity (261 aa)
ZNF645zinc finger protein 645; E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. May operate on tyrosine-phosphorylated SRC substrates (425 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)
SOCS3suppressor 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)
TRIM69tripartite motif containing 69; May have E3 ubiquitin-protein ligase activity. May play a role in apoptosis (500 aa)
ZNRF1zinc and ring finger 1, E3 ubiquitin protein ligase; E3 ubiquitin-protein ligase that mediates the ubiquitination of AKT1 and GLUL, thereby playing a role in neuron cells differentiation. Plays a role in the establishment and maintenance of neuronal transmission and plasticity. Regulates Schwann cells differentiation by mediating ubiquitination of GLUL. Promotes neurodegeneration by mediating ’Lys-48’-linked polyubiquitination and subsequent degradation of AKT1 in axons- degradation of AKT1 prevents AKT1-mediated phosphorylation of GSK3B, leading to GSK3B activation and phosphorylation [...] (227 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)
FBXL5F-box and leucine-rich repeat protein 5 (691 aa)
TRIM4tripartite motif containing 4 (500 aa)
CDC16cell division cycle 16 homolog (S. cerevisiae); 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 (620 aa)
UBE2Aubiquitin-conjugating enzyme E2A; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In association with the E3 enzyme BRE1 (RNF20 and/or RNF40), it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B at ’Lys-120’ to form H2BK120ub1. H2BK120ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. In vitro catalyzes ’Lys-11’, as well as ’Lys-48’-linked polyubiquitination. Require [...] (152 aa)
ITCHitchy E3 ubiquitin protein ligase (862 aa)
KLHDC5kelch domain containing 5; Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for mitotic progression and cytokinesis. The BCR(KLHL42) E3 ubiquitin ligase complex mediates the ubiquitination and subsequent degradation of KATNA1. Involved in microtubule dynamics throughout mitosis (505 aa)
TRIM71tripartite motif containing 71, E3 ubiquitin protein ligase; E3 ubiquitin-protein ligase that cooperates with the microRNAs (miRNAs) machinery and promotes embryonic stem cells proliferation and maintenance. Binds to miRNAs and associates with AGO2, participating to post-transcriptional repression of transcripts such as CDKN1A. Facilitates the G1-S transition to promote rapid embryonic stem cell self-renewal by repressing CDKN1A expression. Required to maintain proliferation and prevent premature differentiation of neural progenitor cells during early neural development- positively reg [...] (868 aa)
RNF34ring finger protein 34, E3 ubiquitin protein ligase; Has E3 ubiquitin-protein ligase activity. Regulates the levels of CASP8 and CASP10 by targeting them for proteasomal degradation. Protects cells against apoptosis induced by TNF. Binds phosphatidylinositol 5-phosphate and phosphatidylinositol 3- phosphate (373 aa)
HECTD1HECT domain containing E3 ubiquitin protein ligase 1; Probable E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. May be required for development of the head mesenchyme and neural tube closure (By similarity) (2610 aa)
VPRBPVpr (HIV-1) binding protein; Component of the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex, VprBP/DCAF1 may function as the substrate recognition module within this complex. For example, VprBP/DCAF1 targets NF2 to the E3 ubiquitin-ligase complex for ubiquitination and subsequent proteasome-dependent degradation. In case of infection by HIV-1 virus, it is recruited by HIV-1 Vpr in order to hijack the CUL4A-RBX1-DDB1 function leading to arrest the cell cycle in G2 phase, and also to protect the viral protein from proteasomal degradation by another E3 ubiquitin ligase. [...] (1078 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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