Full Link:
  • Version:
  • 10.0 (archived version)
STRINGSTRING
UBE2G2 UBE2G2 FBXO7 FBXO7 VPRBP VPRBP RNF182 RNF182 FBXO2 FBXO2 LTN1 LTN1 TRIM69 TRIM69 FBXL3 FBXL3 TRAIP TRAIP FBXO22 FBXO22 SKP2 SKP2 FBXL18 FBXL18 ZBTB16 ZBTB16 FBXL8 FBXL8 ZNRF2 ZNRF2 UBE2M UBE2M RBBP6 RBBP6 UBR4 UBR4 RCHY1 RCHY1 KCTD6 KCTD6 UBE2Q2 UBE2Q2 LRRC41 LRRC41 UBE2Q1 UBE2Q1 FBXW10 FBXW10 FBXO15 FBXO15 UBE2O UBE2O
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Size
small protein node
small nodes:
protein of unknown 3D structure
large protein node
large nodes:
some 3D structure is known or predicted
Node Color
colored protein node
colored nodes:
query proteins and first shell of interactors
non-colored protein node
white nodes:
second shell of interactors
Edges:
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.
Known Interactions
database edge
from curated databases
experiment edge
experimentally determined
Predicted Interactions
neighborhood edge
gene neighborhood
fusion edge
gene fusions
cooccurrence edge
gene co-occurrence
Others
textmining edge
textmining
coexpression edge
co-expression
homology edge
protein homology
Your Input:
UBE2Mubiquitin-conjugating enzyme E2M; Accepts the ubiquitin-like protein NEDD8 from the UBA3- NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX1, but not RBX2, suggests that the RBX1-UBE2M complex neddylates specific target proteins, such as CUL1, CUL2, CUL3 and CUL4. Involved in cell proliferation (183 aa)
FBXL8F-box and leucine-rich repeat protein 8; Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex (By similarity) (374 aa)
FBXO7F-box protein 7; Substrate recognition component of a (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes BIRC2 and DLGAP5 (522 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)
SKP2S-phase kinase-associated protein 2, 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 involved in cell cycle progression, signal transduction and transcription. Specifically recognizes phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. Degradation of CDKN1B/p27kip also requires CKS1. Recognizes target proteins ORC1, CDT1, RBL2, MLL, CDK9, RAG2, FOXO1, UBP43, and probably MYC, TOB1 and [...] (424 aa)
UBE2Q1ubiquitin-conjugating enzyme E2Q family member 1 (422 aa)
FBXO22F-box protein 22; Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex. Promotes the proteasome-dependent degradation of key sarcomeric proteins, such as alpha-actinin (ACTN2) and filamin-C (FLNC), essential for maintenance of normal contractile function (403 aa)
RBBP6retinoblastoma binding protein 6 (1792 aa)
RCHY1ring finger and CHY zinc finger domain containing 1, E3 ubiquitin protein ligase; Mediates E3-dependent ubiquitination and proteasomal degradation of target proteins, including p53/TP53, P73, HDAC1 and CDKN1B. Preferentially acts on tetrameric p53/TP53. Monoubiquitinates the translesion DNA polymerase POLH. Contributes to the regulation of the cell cycle progression. Increases AR transcription factor activity (261 aa)
UBE2Oubiquitin-conjugating enzyme E2O (1292 aa)
ZNRF2zinc and ring finger 2; May play a role in the establishment and maintenance of neuronal transmission and plasticity via its ubiquitin ligase activity. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates (242 aa)
TRAIPTRAF interacting protein; Inhibits activation of NF-kappa-B mediated by TNF (By similarity) (469 aa)
TRIM69tripartite motif containing 69; May have E3 ubiquitin-protein ligase activity. May play a role in apoptosis (500 aa)
ZBTB16zinc finger and BTB domain containing 16; Probable transcription factor. May play a role in myeloid maturation and in the development and/or maintenance of other differentiated tissues. Probable substrate-recognition component of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (673 aa)
UBE2G2ubiquitin-conjugating enzyme E2G 2; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys- 48’-linked polyubiquitination. Involved in endoplasmic reticulum- associated degradation (ERAD) (165 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)
KCTD6potassium channel tetramerisation domain containing 6 (237 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)
UBR4ubiquitin protein ligase E3 component n-recognin 4 (5183 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)
LTN1listerin E3 ubiquitin protein ligase 1 (1812 aa)
FBXW10F-box and WD repeat domain containing 10; Probable substrate-recognition component of a SCF (SKP1- CUL1-F-box protein)-type E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Overexpression is leading to degradation of CBX5 and CBX1 (1051 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)
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)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
Server load: low (29%)