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UBE2L3 UBE2L3 UBE2L6 UBE2L6 UBE2E2 UBE2E2 ABHD16A ABHD16A UBE2N UBE2N UBE2E1 UBE2E1 FHOD1 FHOD1 UBE2D2 UBE2D2 CDC34 CDC34 UBE2D1 UBE2D1 UBE2D3 UBE2D3 MPDZ MPDZ RNF5 RNF5 UBE2U UBE2U UBE2K UBE2K UBE2V1 UBE2V1 UBE2E3 UBE2E3 PXN PXN UBE2Q1 UBE2Q1 UBE2Z UBE2Z UBE2D4 UBE2D4 DERL1 DERL1 CFTR CFTR UBE2J1 UBE2J1 UBE2W UBE2W UBE2S UBE2S
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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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large nodes:
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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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.
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from curated databases
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experimentally determined
Predicted Interactions
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textmining
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co-expression
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CFTRcystic fibrosis transmembrane conductance regulator (ATP-binding cassette sub-family C, member 7); Involved in the transport of chloride ions. May regulate bicarbonate secretion and salvage in epithelial cells by regulating the SLC4A7 transporter. Can inhibit the chloride channel activity of ANO1 (1480 aa)
CDC34cell division cycle 34 homolog (S. cerevisiae); 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 monoubiqu [...] (236 aa)
UBE2D4ubiquitin-conjugating enzyme E2D 4 (putative); 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 (147 aa)
PXNpaxillin; Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion) (591 aa)
FHOD1formin homology 2 domain containing 1; Required for the assembly of F-actin structures, such as stress fibers. Depends on the Rho-ROCK cascade for its activity. Contributes to the coordination of microtubules with actin fibers and plays a role in cell elongation. Acts synergistically with ROCK1 to promote SRC-dependent non-apoptotic plasma membrane blebbing (1164 aa)
DERL1derlin 1; Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by forming a channel that allows the retrotranslocation of misfolded proteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the degradation substrate. In case of infection by cytomegaloviruses, it plays a central role in the export from the ER and subsequent degradation of MHC class I heavy chains via its interaction with US11 viral protein, which recognizes and associates with MHC class [...] (251 aa)
UBE2Kubiquitin-conjugating enzyme E2K (200 aa)
UBE2Subiquitin-conjugating enzyme E2S; 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 ubiquit [...] (222 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)
UBE2Q1ubiquitin-conjugating enzyme E2Q family member 1 (422 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)
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)
UBE2V1ubiquitin-conjugating enzyme E2 variant 1 (170 aa)
UBE2L3ubiquitin-conjugating enzyme E2L 3; Ubiquitin-conjugating enzyme E2 that specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. Does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine- in contrast, it has activity with the RBR family E3 enzymes, such as PARK2 and ARIH1, that function like function like RING-HECT hybrids. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys-11’-linked polyubiquitination. Involved in th [...] (154 aa)
UBE2D3ubiquitin-conjugating enzyme E2D 3; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys- 11’-, as well as ’Lys-48’-linked polyubiquitination. Cooperates with the E2 CDC34 and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Acts as an initiator E2, priming the phosphorylated NFKBIA target at positions ’Lys-21’ and/or ’Lys-22’ with a monoubiquitin. Ubiquitin chain elongation is then performed by CDC34, building ubiquitin chains from the UBE2D3-prime [...] (149 aa)
UBE2Zubiquitin-conjugating enzyme E2Z; 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 (354 aa)
UBE2Uubiquitin-conjugating enzyme E2U (putative); Catalyzes the covalent attachment of ubiquitin to other proteins (By similarity) (226 aa)
UBE2D1ubiquitin-conjugating enzyme E2D 1; 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 polyu [...] (147 aa)
RNF5ring finger protein 5, E3 ubiquitin protein ligase; Has E2-dependent E3 ubiquitin-protein ligase activity. May function together with E2 ubiquitin-conjugating enzymes UBE2D1/UBCH5A and UBE2D2/UBC4. Mediates ubiquitination of PXN/paxillin and Salmonella type III secreted protein sopA. May be involved in regulation of cell motility and localization of PXN/paxillin. Mediates the ’Lys-63’-linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD; the ubiquitination appears to involve E2 ubiquitin-conjugatin [...] (180 aa)
MPDZmultiple PDZ domain protein (2041 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)
ABHD16Aabhydrolase domain containing 16A (558 aa)
UBE2E2ubiquitin-conjugating enzyme E2E 2; 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 (201 aa)
UBE2D2ubiquitin-conjugating enzyme E2D 2; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys- 11’-, as well as ’Lys-48’-linked polyubiquitination. Cooperates with the E2 CDC34 and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Acts as an initiator E2, priming the phosphorylated NFKBIA target at positions ’Lys-21’ and/or ’Lys-22’ with a monoubiquitin. Ubiquitin chain elongation is then performed by CDC34, building ubiquitin chains from the UBE2D3-prime [...] (147 aa)
UBE2Wubiquitin-conjugating enzyme E2W (putative); Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes monoubiquitination. Involved in degradation of misfolded chaperone substrates by mediating monoubiquitination of STUB1/CHIP, leading to recruitment of ATXN3 to monoubiquitinated STUB1/CHIP, and restriction of the length of ubiquitin chain attached to STUB1/CHIP substrates by ATXN3. After UV irradiation, but not after mitomycin-C (MMC) treatment, acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associati [...] (162 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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