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UBE2Z UBE2Z UBE2D4 UBE2D4 UBE2L6 UBE2L6 OTUB1 OTUB1 UBE2E2 UBE2E2 UBE2D3 UBE2D3 UBE2N UBE2N UBE2U UBE2U UBE2K UBE2K UBE2O UBE2O UBE2R2 UBE2R2 UBE2D1 UBE2D1 UBE2D2 UBE2D2 UBE2I UBE2I UBE2B UBE2B UBE2S UBE2S UBE2E1 UBE2E1 CDC34 CDC34 UBE2A UBE2A OTUB2 OTUB2 UBA52 UBA52 UBE2C UBE2C UBE2E3 UBE2E3 STUB1 STUB1 ENSG00000124208 ENSG00000124208 UBE2T UBE2T
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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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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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experimentally determined
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OTUB2Ubiquitin thioesterase OTUB2; Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Mediates deubiquitination of ’Lys-11’-,’Lys-48’- and ’Lys-63’- linked polyubiquitin chains, with a preference for ’Lys-63’-linked polyubiquitin chains; Belongs to the peptidase C65 family (234 aa)
CDC34Ubiquitin-conjugating enzyme E2 R1; 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 monoubiquitin. Cooper [...] (236 aa)
STUB1E3 ubiquitin-protein ligase CHIP; 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 that have no effect on HSPA8 degradation. Me [...] (303 aa)
UBE2D4Ubiquitin-conjugating enzyme E2 D4; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, but may prefer ’Lys-11’ and ’Lys-48’-linked polyubiquitination; Belongs to the ubiquitin-conjugating enzyme family (147 aa)
UBE2KUbiquitin-conjugating enzyme E2 K; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of ’Lys-48’-linked polyubiquitin chains. Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein. Mediates the selective degradation of short-lived and abnormal proteins, such as the endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins. Ubiquitinates huntingtin. May mediate foam [...] (200 aa)
UBE2R2Ubiquitin-conjugating enzyme E2 R2; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes monoubiquitination and ’Lys-48’-linked polyubiquitination. May be involved in degradation of katenin; Ubiquitin conjugating enzymes E2 (238 aa)
UBE2SUbiquitin-conjugating enzyme E2 S; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes ’Lys-11’-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 specifically elongating ’Lys-11’-linked polyubiquitin chains initiated by the E2 enzyme UBE2C/UBCH10 on APC/C substrates, enhancing the degradation of APC/C substrates by the proteasome and promoting mitotic exit. Also acts by elongating ubiqu [...] (222 aa)
UBE2BUbiquitin-conjugating enzyme E2 B; 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’- and ’Lys-63’-linked polyubiquit [...] (152 aa)
UBE2L6Ubiquitin/ISG15-conjugating enzyme E2 L6; 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; Ubiquitin conjugating enzymes E2 (153 aa)
UBE2E1Ubiquitin-conjugating enzyme E2 E1; 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; Belongs to the ubiquitin-conjugating enzyme family (193 aa)
UBE2NUbiquitin-conjugating enzyme E2 N; 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 P [...] (152 aa)
UBE2O(E3-independent) E2 ubiquitin-conjugating enzyme; E2/E3 hybrid ubiquitin-protein ligase that displays both E2 and E3 ligase activities and mediates monoubiquitination of target proteins. Negatively regulates TRAF6-mediated NF-kappa-B activation independently of its E2 activity. Acts as a positive regulator of BMP7 signaling by mediating monoubiquitination of SMAD6, thereby regulating adipogenesis. Mediates monoubiquitination at different sites of the nuclear localization signal (NLS) of BAP1, leading to cytoplasmic retention of BAP1. Also able to monoubiquitinate the NLS of other chrom [...] (1292 aa)
ENSG00000124208TMEM189-UBE2V1 readthrough; Belongs to the ubiquitin-conjugating enzyme family (370 aa)
UBE2ISUMO-conjugating enzyme UBC9; Accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3 and SUMO4 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2, CBX4 and ZNF451. Can catalyze the formation of poly-SUMO chains. Necessary for sumoylation of FOXL2 and KAT5. Essential for nuclear architecture and chromosome segregation. Sumoylates p53/TP53 at ’Lys-386’; Belongs to the ubiquitin-conjugating enzyme family (158 aa)
UBE2CUbiquitin-conjugating enzyme E2 C; 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; Ubiquitin conjugating enzymes E2 (179 aa)
UBE2D3Ubiquitin conjugating enzyme E2 D3; Belongs to the ubiquitin-conjugating enzyme family (149 aa)
UBE2ZUbiquitin-conjugating enzyme E2 Z; Catalyzes the covalent attachment of ubiquitin to other proteins (By similarity). Specific substrate for UBA6, not charged with ubiquitin by UBE1. May be involved in apoptosis regulation; Ubiquitin conjugating enzymes E2 (354 aa)
UBE2TUbiquitin-conjugating enzyme E2 T; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes monoubiquitination. Involved in mitomycin-C (MMC)-induced DNA repair. Acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway. Also mediates monoubiquitination of FANCL and FANCI. May contribute to ubiquitination and degradation of BRCA1. In vitro able to promote polyubiquitination using a [...] (197 aa)
UBE2UUbiquitin-conjugating enzyme E2 U; Catalyzes the covalent attachment of ubiquitin to other proteins; Belongs to the ubiquitin-conjugating enzyme family (226 aa)
UBE2AUbiquitin-conjugating enzyme E2 A; 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. Requir [...] (152 aa)
UBE2D1Ubiquitin-conjugating enzyme E2 D1; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys-48’-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and auto-ubiquitination of STUB1, TRAF6 and TRIM63/MURF1. Ubiquitinates STUB1-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubi [...] (147 aa)
UBE2E2Ubiquitin-conjugating enzyme E2 E2; 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. Catalyzes the ISGylation of influenza A virus NS1 protein; Ubiquitin conjugating enzymes E2 (201 aa)
UBE2D2Ubiquitin-conjugating enzyme E2 D2; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys- 48’-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP- induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and autoubiquitination of STUB1 and TRAF6. Involved in the signal-induced conjugation and subsequent degradation of NFKBIA, FBXW2-mediated GCM1 ubiquitination and degradation, MDM2-dependent degradation of p53/TP53 and the activation of [...] (147 aa)
UBE2E3Ubiquitin-conjugating enzyme E2 E3; 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; Ubiquitin conjugating enzymes E2 (207 aa)
UBA52Ubiquitin-60S ribosomal protein L40; Ubiquitin- Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked- Lys-6-linked may be invo [...] (128 aa)
OTUB1Ubiquitin thioesterase OTUB1; Hydrolase that can specifically remove ’Lys-48’-linked conjugated ubiquitin from proteins and plays an important regulatory role at the level of protein turnover by preventing degradation. Regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered unresponsive to antigen rechallenge and no longer respond to their cognate antigen. Acts via its interaction with RNF128/GRAIL, a crucial inductor of CD4 T-cell anergy. Isoform 1 destabilizes RNF128, leading to prevent anergy. In contrast, isoform 2 stabilizes RNF128 and promotes anergy. Surpr [...] (271 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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