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 nodes:
protein of unknown 3D structure
protein of unknown 3D structure
large nodes:
some 3D structure is known or predicted
some 3D structure is known or predicted
Node Color
colored nodes:
query proteins and first shell of interactors
query proteins and first shell of interactors
white nodes:
second shell of interactors
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
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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 | RBX1 | ring-box 1, E3 ubiquitin protein ligase; E3 ubiquitin ligase component of multiple cullin-RING- based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupled nucleotide excision repair. The functional specificity of the E3 ubiquitin-protein ligase complexes depends on the variable substrate recognition components. As a component of the CSA complex promotes the ubiquitination of ERCC6 resulting in pr [...] (108 aa) | ||
 | MKRN1 | makorin ring finger protein 1 (482 aa) | ||
 | MGRN1 | mahogunin ring finger 1, E3 ubiquitin protein ligase; E3 ubiquitin-protein ligase. Mediates monoubiquitination at multiple sites of TSG101 in the presence of UBE2D1, but not of UBE2G1, nor UBE2H. Plays a role in the regulation of endosome-to- lysosome trafficking. Impairs MC1R- and MC4R-signaling by competing with GNAS-binding to MCRs and inhibiting agonist-induced cAMP production. Does not inhibit ADRB2-signaling. Does not promote MC1R ubiquitination (576 aa) | ||
 | HUWE1 | HECT, UBA and WWE domain containing 1, E3 ubiquitin protein ligase (4374 aa) | ||
 | TCEB1 | transcription elongation factor B (SIII), polypeptide 1 (15kDa, elongin C); SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex) (112 aa) | ||
 | RNF111 | ring finger protein 111 (986 aa) | ||
 | KLHL3 | kelch-like 3 (Drosophila); Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of ion transport in the distal nephron. The BCR(KLHL3) complex may act by mediating ubiquitination of SLC12A3/NCC, thereby regulating SLC12A3/NCC subcellular location at the cell membrane (587 aa) | ||
 | FBXL16 | F-box and leucine-rich repeat protein 16; Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex (By similarity) (479 aa) | ||
 | TRIM50 | tripartite motif containing 50; E3 ubiquitin-protein ligase (487 aa) | ||
 | UBA7 | ubiquitin-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) | ||
 | UBE3B | ubiquitin protein ligase E3B; 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) (1068 aa) | ||
 | RNF6 | ring 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) | ||
 | FBXL5 | F-box and leucine-rich repeat protein 5 (691 aa) | ||
 | KIAA0317 | KIAA0317 (823 aa) | ||
 | ANAPC11 | anaphase promoting complex subunit 11; 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 (196 aa) | ||
 | DZIP3 | DAZ interacting protein 3, zinc finger (1208 aa) | ||
 | UBAC1 | UBA domain containing 1; Non-catalytic subunit of the KPC complex that acts as E3 ubiquitin-protein ligase. Required for poly-ubiquitination and proteasome-mediated degradation of CDKN1B during G1 phase of the cell cycle (405 aa) | ||
 | UBR2 | ubiquitin protein ligase E3 component n-recognin 2; E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Plays a critical role in chromatin inactivation and chromosome-wide transcriptional silencing during meiosis via ubiquitination of histone H2A. Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth (1755 aa) | ||
 | TRIM63 | tripartite motif containing 63, E3 ubiquitin protein ligase; E3 ubiquitin ligase. Mediates the ubiquitination and subsequent proteasomal degradation of CKM, GMEB1 and HIBADH. Regulates the proteasomal degradation of muscle proteins under amino acid starvation, where muscle protein is catabolized to provide other organs with amino acids. Inhibits de novo skeletal muscle protein synthesis under amino acid starvation. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertroph [...] (353 aa) | ||
 | FBXL19 | F-box and leucine-rich repeat protein 19; Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex (By similarity) (694 aa) | ||
 | FBXL18 | F-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) | ||
 | LTN1 | listerin E3 ubiquitin protein ligase 1 (1812 aa) | ||
 | HECTD1 | HECT 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) | ||
 | FBXO15 | F-box protein 15; Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex (By similarity) (510 aa) | ||
 | KLHL5 | kelch-like 5 (Drosophila) (755 aa) | ||
 | FBXO32 | F-box protein 32; 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. Probably recognizes and binds to phosphorylated target proteins during skeletal muscle atrophy. Recognizes TERF1 (355 aa) | ||
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
Other names: H. sapiens, Homo, Homo sapiens, human, man
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