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RNF123 RNF123 FBXO41 FBXO41 KBTBD13 KBTBD13 SIAH1 SIAH1 PLAU PLAU TRIM32 TRIM32 TRIM63 TRIM63 UBA1 UBA1 MKRN1 MKRN1 KBTBD6 KBTBD6 VPRBP VPRBP FBXW4 FBXW4 TCEB2 TCEB2 KIAA0317 KIAA0317 FBXO44 FBXO44 RBX1 RBX1 FBXL19 FBXL19 BTBD6 BTBD6 UBA3 UBA3 CCNF CCNF ANAPC4 ANAPC4 UBA5 UBA5 UFL1 UFL1 CDC20 CDC20 ANAPC1 ANAPC1 UBA6 UBA6
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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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second shell of interactors
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RBX1ring-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)
FBXO44F-box protein 44; Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex (255 aa)
MKRN1makorin ring finger protein 1 (482 aa)
TCEB2transcription elongation factor B (SIII), polypeptide 2 (18kDa, elongin B); 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) (161 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)
UBA6ubiquitin-like modifier activating enzyme 6 (1052 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)
RNF123ring finger protein 123 (1314 aa)
UBA1ubiquitin-like modifier activating enzyme 1; Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin- E1 thioester and free AMP (1058 aa)
ANAPC1anaphase promoting complex subunit 1; 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 (1944 aa)
UBA5ubiquitin-like modifier activating enzyme 5; E1-like enzyme which activates UFM1 and SUMO2 (404 aa)
KIAA0317KIAA0317 (823 aa)
SIAH1siah E3 ubiquitin protein ligase 1; E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin- conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates E3 ubiquitin ligase activity either through direct binding to substrates or by functioning as the essential RING domain subunit of larger E3 complexes. Triggers the ubiquitin-mediated degradation of many substrates, including proteins involved in transcriptio [...] (313 aa)
UBA3ubiquitin-like modifier activating enzyme 3; Catalytic subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Down-regulates steroid receptor activity. Necessary for cell cycle progression (463 aa)
UFL1UFM1-specific ligase 1; E3 UFM1-protein ligase that mediates ufmylation of target proteins such as DDRGK1/C20orf116. The function of ufmylation is unknown. May act as a tumor suppressor by inhibiting cell invasion, blocking NF-kappa-B signaling and increasing stability of CDK5RAP3 (794 aa)
PLAUplasminogen activator, urokinase; Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin (431 aa)
TRIM32tripartite motif containing 32; Has an E3 ubiquitin ligase activity. Ubiquitinates DTNBP1 (dysbindin) and promotes its degradation. May play a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo. Binds specifically to the activation domain of HIV-1 Tat and can also interact with the HIV-2 and EIAV Tat proteins in vivo (653 aa)
TRIM63tripartite 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)
KBTBD6kelch repeat and BTB (POZ) domain containing 6 (674 aa)
FBXL19F-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)
FBXW4F-box and WD repeat domain containing 4; Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. Likely to be involved in key signaling pathways crucial for normal limb development. May participate in Wnt signaling (412 aa)
BTBD6BTB (POZ) domain containing 6; Adapter protein for the CUL3 E3 ubiquitin-protein ligase complex. Involved in late neuronal development and muscle formation (By similarity) (485 aa)
CCNFcyclin F; 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 CP110 during G2 phase, thereby acting as an inhibitor of centrosome reduplication (786 aa)
KBTBD13kelch repeat and BTB (POZ) domain containing 13; Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex (458 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)
FBXO41F-box protein 41; Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex (By similarity) (875 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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