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KBTBD8 KBTBD8 FBXO15 FBXO15 FBXL16 FBXL16 UBE2C UBE2C CUL7 CUL7 MKRN1 MKRN1 KLHL2 KLHL2 STUB1 STUB1 DET1 DET1 KLHL13 KLHL13 PARK2 PARK2 KEAP1 KEAP1 TRIM41 TRIM41 KLHDC5 KLHDC5 VHL VHL RLIM RLIM RNF123 RNF123 UBAC1 UBAC1 VPRBP VPRBP FBXO17 FBXO17 FBXW12 FBXW12 CCNF CCNF KLHL11 KLHL11 ZNF645 ZNF645 KIAA0317 KIAA0317 SPSB2 SPSB2
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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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small nodes:
protein of unknown 3D structure
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some 3D structure is known or predicted
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query proteins and first shell of interactors
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white nodes:
second shell of interactors
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experimentally determined
Predicted Interactions
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textmining
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co-expression
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KEAP1kelch-like ECH-associated protein 1; Acts as a substrate adapter protein for the E3 ubiquitin ligase complex formed by CUL3 and RBX1 and targets NFE2L2/NRF2 for ubiquitination and degradation by the proteasome, thus resulting in the suppression of its transcriptional activity and the repression of antioxidant response element-mediated detoxifying enzyme gene expression. Retains NFE2L2/NRF2 and may also retain BPTF in the cytosol. Targets PGAM5 for ubiquitination and degradation by the proteasome (624 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)
RLIMring finger protein, LIM domain interacting; E3 ubiquitin-protein ligase. Acts as a negative coregulator for LIM homeodomain transcription factors by mediating the ubiquitination and subsequent degradation of LIM cofactors LDB1 and LDB2 and by mediating the recruitment the SIN3a/histone deacetylase corepressor complex. Ubiquitination and degradation of LIM cofactors LDB1 and LDB2 allows DNA-bound LIM homeodomain transcription factors to interact with other protein partners such as RLIM. Plays a role in telomere length-mediated growth suppression by mediating the ubiquitination and degr [...] (624 aa)
MKRN1makorin ring finger protein 1 (482 aa)
VHLvon Hippel-Lindau tumor suppressor, E3 ubiquitin protein ligase; Involved in the ubiquitination and subsequent proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Seems to act as target recruitment subunit in the E3 ubiquitin ligase complex and recruits hydroxylated hypoxia- inducible factor (HIF) under normoxic conditions. Involved in transcriptional repression through interaction with HIF1A, HIF1AN and histone deacetylases. Ubiquitinates, in an oxygen-responsive manner, ADRB2 (213 aa)
FBXO17F-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)
FBXW12F-box and WD repeat domain containing 12; Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex (By similarity) (464 aa)
KLHL11kelch-like 11 (Drosophila); Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, leading most often to their proteasomal degradation (By similarity) (708 aa)
FBXL16F-box and leucine-rich repeat protein 16; Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex (By similarity) (479 aa)
TRIM41tripartite motif containing 41; Functions as an E3 ligase that catalyzes the ubiquitin- mediated degradation of protein kinase C (630 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)
RNF123ring finger protein 123 (1314 aa)
KIAA0317KIAA0317 (823 aa)
UBE2Cubiquitin-conjugating enzyme E2C; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys- 11’- and ’Lys-48’-linked polyubiquitination. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by initiating ’Lys-11’-linked polyubiquitin chains on APC/C substrates, leading to the degradation of APC/C substrates by the proteasome and promoting mitotic exit (179 aa)
PARK2parkinson protein 2, E3 ubiquitin protein ligase (parkin) (465 aa)
UBAC1UBA domain containing 1; Non-catalytic subunit of the KPC complex that acts as E3 ubiquitin-protein ligase. Required for poly-ubiquitination and proteasome-mediated degradation of CDKN1B during G1 phase of the cell cycle (405 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)
CCNFcyclin F; Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of CP110 during G2 phase, thereby acting as an inhibitor of centrosome reduplication (786 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)
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)
KBTBD8kelch repeat and BTB (POZ) domain containing 8 (601 aa)
DET1de-etiolated homolog 1 (Arabidopsis); Component of the E3 ubiquitin ligase DCX DET1-COP1 complex, which is required for ubiquitination and subsequent degradation of target proteins. The complex is involved in JUN ubiquitination and degradation (561 aa)
KLHL2kelch-like 2, Mayven (Drosophila); Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, such as NPTXR, leading most often to their proteasomal degradation (By similarity). Plays a role in the reorganization of the actin cytoskeleton. Promotes growth of cell projections in oligodendrocyte precursors (597 aa)
SPSB2splA/ryanodine receptor domain and SOCS box containing 2; 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 (263 aa)
CUL7cullin 7; Component of a probable SCF-like E3 ubiquitin-protein ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably plays a role in the degradation of proteins involved in endothelial proliferation and/or differentiation (By similarity). Seems not to promote polyubiquitination and proteasomal degradation of TP53. In vitro, complexes of CUL7 with either CUL9 or FBXW8 or TP53 contain E3 ubiquitin-protein ligase activity. In complex with FBXW8, mediates ubiquitination and consequent degradation of GORASP1, acting as a compo [...] (1782 aa)
KLHL13kelch-like 13 (Drosophila) (658 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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