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LONRF1 LONRF1 MEX3C MEX3C UNKL UNKL CDC26 CDC26 BTBD1 BTBD1 FBXL18 FBXL18 UBR4 UBR4 RNF7 RNF7 HECTD1 HECTD1 KBTBD13 KBTBD13 FBXL14 FBXL14 VPRBP VPRBP SKP1 SKP1 KBTBD6 KBTBD6 CUL1 CUL1 UBE2Q2 UBE2Q2 MKRN1 MKRN1 FBXL3 FBXL3 TRIM36 TRIM36 FBXO44 FBXO44 STUB1 STUB1 FBXO17 FBXO17 UBE2J2 UBE2J2 RNF6 RNF6 HECTD2 HECTD2 LNX1 LNX1
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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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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)
SKP1S-phase kinase-associated protein 1; Essential component of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as an adapter that links the F-box protein to CUL1. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11) directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC [...] (163 aa)
FBXO44F-box protein 44; Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex (255 aa)
MKRN1makorin ring finger protein 1 (482 aa)
BTBD1BTB (POZ) domain containing 1; Probable substrate-specific adapter of an E3 ubiquitin- protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (482 aa)
LNX1ligand 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)
UBE2Q2ubiquitin-conjugating enzyme E2Q family member 2; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys- 48’-linked polyubiquitination (375 aa)
RNF7ring finger protein 7; Probable component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription. Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme to the complex and brings it into close proximity to the substrate. Promotes the neddylation of CUL5 via its interaction with UBE2F. May play a role in protecting cells from apoptosis induced by redox agents (113 aa)
TRIM36tripartite motif containing 36; E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins. Involved in chromosome segregation and cell cycle regulation. May play a role in the acrosome reaction and fertilization (By similarity) (728 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)
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)
CUL1cullin 1; Core component of multiple cullin-RING-based SCF (SKP1- CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. May contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and exchange of the substrate [...] (776 aa)
RNF6ring finger protein (C3H2C3 type) 6; E3 ubiquitin-protein ligase mediating ’Lys-48’-linked polyubiquitination of LIMK1 and its subsequent targeting to the proteasome for degradation. Negatively regulates axonal outgrowth through regulation of the LIMK1 turnover. Mediates ’Lys-6’ and ’Lys-27’-linked polyubiquitination of AR/androgen receptor thereby modulating its transcriptional activity. May also bind DNA and function as a transcriptional regulator (685 aa)
FBXL14F-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)
FBXL3F-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)
CDC26cell division cycle 26 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. May recruit the E2 ubiquitin-conjugating enzymes to the complex (85 aa)
UBR4ubiquitin protein ligase E3 component n-recognin 4 (5183 aa)
KBTBD6kelch repeat and BTB (POZ) domain containing 6 (674 aa)
FBXL18F-box and leucine-rich repeat protein 18; Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex (By similarity) (718 aa)
UNKLunkempt 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)
LONRF1LON peptidase N-terminal domain and ring finger 1 (773 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)
UBE2J2ubiquitin-conjugating enzyme E2, J2; Catalyzes the covalent attachment of ubiquitin to other proteins. Seems to function in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD) (By similarity) (275 aa)
MEX3Cmex-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)
KBTBD13kelch repeat and BTB (POZ) domain containing 13; Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex (458 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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