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UBE2J1 UBE2J1 SH3RF1 SH3RF1 UBE2E3 UBE2E3 RBCK1 RBCK1 FBXW9 FBXW9 UBA7 UBA7 UBE2N UBE2N TRIP12 TRIP12 RNF111 RNF111 TRIM36 TRIM36 HECTD3 HECTD3 RBBP6 RBBP6 UBE2E1 UBE2E1 DZIP3 DZIP3 ANAPC4 ANAPC4 FBXL13 FBXL13 CDC20 CDC20 ANAPC13 ANAPC13 FBXO2 FBXO2 BTRC BTRC LRRC41 LRRC41 RNF217 RNF217 FBXO6 FBXO6 RNF182 RNF182 SPSB2 SPSB2 RNF19B RNF19B
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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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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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fusion edge
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co-expression
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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)
TRIP12thyroid hormone receptor interactor 12; E3 ubiquitin-protein ligase involved in ubiquitin fusion degradation (UFD) pathway and regulation of DNA repair. Part of the ubiquitin fusion degradation (UFD) pathway, a process that mediates ubiquitination of protein at their N-terminus, regardeless of the presence of lysine residues in target proteins. In normal cells, mediates ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A, a lysine-less tumor suppressor required for p53/TP53 activation under oncogenic stress. In cancer cells, however, isoform p19ARF/ARF and TRIP12 are located [...] (1992 aa)
SH3RF1SH3 domain containing ring finger 1; Acts as a scaffold protein, contributes to Rac-induced signal transduction such as JNKs (MAPK8 and MAPK9) activation and induces apoptosis. Within a signaling complex, it probably recruits protein kinases such as MAP3K10 or MAP3K11 which are in turn activated leading to the sequential activation of MAP2K4, MAP2K7 and JNKs (MAPK8 and MAPK9) (By similarity). May be involved in targeting of HIV-1 GAG and GAG-POL polyproteins to the plasma membrane (888 aa)
RNF111ring finger protein 111 (986 aa)
UBE2E1ubiquitin-conjugating enzyme E2E 1; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes the covalent attachment of ISG15 to other proteins. Mediates the selective degradation of short-lived and abnormal proteins. In vitro also catalyzes ’Lys-48’-linked polyubiquitination (193 aa)
CDC20cell division cycle 20 homolog (S. cerevisiae); Required for full ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C) and may confer substrate specificity upon the complex. Is regulated by MAD2L1- in metaphase the MAD2L1-CDC20-APC/C ternary complex is inactive and in anaphase the CDC20-APC/C binary complex is active in degrading substrates. The CDC20-APC/C complex positively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. CDC20-APC/C-induced degradation of NEUROD2 induces presynaptic dif [...] (499 aa)
UBE2Nubiquitin-conjugating enzyme E2N; The UBE2V1-UBE2N and UBE2V2-UBE2N heterodimers catalyze the synthesis of non-canonical ’Lys-63’-linked polyubiquitin chains. This type of polyubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Acts together with the E3 ligases, HLTF and SHPRH, in the ’Lys-63’-linked poly-ubiquitination of PC [...] (152 aa)
RBBP6retinoblastoma binding protein 6 (1792 aa)
ANAPC4anaphase promoting complex subunit 4; 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 (808 aa)
FBXL13F-box and leucine-rich repeat protein 13 (735 aa)
UBA7ubiquitin-like modifier activating enzyme 7; Activates ubiquitin by first adenylating with ATP its C- terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin- E1 thioester and free AMP (1012 aa)
LRRC41leucine rich repeat containing 41; Probable substrate recognition component of an ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (812 aa)
FBXO2F-box protein 2; Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Involved in the endoplasmic reticulum-associated degradation pathway (ERAD) for misfolded lumenal proteins by recognizing and binding sugar chains on unfolded glycoproteins that are retrotranslocated into the cytosol and promoting their ubiquitination and subsequent degradation. Prevents formation of cytosolic aggregates of unfolded glycoproteins that have been retrotranslocat [...] (296 aa)
ANAPC13anaphase promoting complex subunit 13; 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 (74 aa)
RBCK1RanBP-type and C3HC4-type zinc finger containing 1; E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2L3/UBCM4, and then transfers it to substrates. Functions as an E3 ligase for oxidized IREB2 and both heme and oxygen are necessary for IREB2 ubiquitination. Promotes ubiquitination of TAB2 and IRF3 and their degradation by the proteasome. Component of the LUBAC complex which conjugates linear (’M-1’-linked) polyubiquitin chains to substrates and plays a key role in NF- kappa-B activation and regulation of inflammation. LUBA [...] (510 aa)
RNF217ring finger protein 217; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (By similarity) (275 aa)
DZIP3DAZ interacting protein 3, zinc finger (1208 aa)
BTRCbeta-transducin repeat containing E3 ubiquitin protein ligase; 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 target proteins. Recognizes and binds to phosphorylated target proteins. SCF(BTRC) mediates the ubiquitination of CTNNB1 and participates in Wnt signaling. SCF(BTRC) mediates the ubiquitination of NFKBIA, NFKBIB and NFKBIE; the degradation frees the associated NFKB1 to translocate into the nucleus and to activate transcription. Ubiquitination of N [...] (605 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)
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)
FBXO6F-box protein 6; Substrate-recognition component of some SCF (SKP1-CUL1- F-box protein)-type E3 ubiquitin ligase complexes. Involved in endoplasmic reticulum-associated degradation pathway (ERAD) for misfolded lumenal proteins by recognizing and binding sugar chains on unfolded glycoproteins that are retrotranlocated into the cytosol and promoting their ubiquitination and subsequent degradation. Able to recognize and bind denatured glycoproteins, which are modified with not only high-mannose but also complex- type oligosaccharides. Also recognizes sulfated glycans. Also involved in DNA [...] (293 aa)
UBE2E3ubiquitin-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)
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)
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)
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)
UBE2J1ubiquitin-conjugating enzyme E2, J1 (318 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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