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KLHDC5 KLHDC5 UFL1 UFL1 SPSB4 SPSB4 FBXO22 FBXO22 DTX3L DTX3L MGRN1 MGRN1 LTN1 LTN1 RNF144B RNF144B FBXL19 FBXL19 UNKL UNKL RCHY1 RCHY1 ANAPC11 ANAPC11 RNF123 RNF123 UBE3D UBE3D FBXL3 FBXL3 BTRC BTRC RNF126 RNF126 STUB1 STUB1 MIB2 MIB2 ARIH2 ARIH2 SMURF2 SMURF2 RNF182 RNF182 FBXW12 FBXW12 KCTD6 KCTD6 TRAIP TRAIP HECTD3 HECTD3
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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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query proteins and first shell of interactors
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second shell of interactors
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STUB1STIP1 homology and U-box containing protein 1, E3 ubiquitin protein ligase; 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 th [...] (303 aa)
RNF144Bring finger protein 144B; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates such as LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin-dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se (303 aa)
MGRN1mahogunin 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)
SMURF2SMAD specific E3 ubiquitin protein ligase 2 (748 aa)
RNF126ring finger protein 126 (311 aa)
DTX3Ldeltex 3-like (Drosophila); Ubiquitin ligase that mediates monoubiquitination of ’Lys-91’ of histone H4 (H4K91ub1), in response to DNA damage. Protects cells exposed to DNA-damaging agents. The exact role of H4K91ub1 in DNA damage response is still unclear but it may function as a licensing signal for additional histone H4 post- translational modifications such as H4 ’Lys-20’ methylation (H4K20me). Involved in the recruitment of 53BP1/TP53BP1 to sites of DNA damage by mediating H4K91ub1 formation. In concert with PARP9, plays a role in PARP1-dependent DNA damage repair. PARP1- dependen [...] (740 aa)
FBXW12F-box and WD repeat domain containing 12; Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex (By similarity) (464 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)
SPSB4splA/ryanodine receptor domain and SOCS box containing 4; Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (273 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)
TRAIPTRAF interacting protein; Inhibits activation of NF-kappa-B mediated by TNF (By similarity) (469 aa)
RNF123ring finger protein 123 (1314 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)
ARIH2ariadne homolog 2 (Drosophila); E3 ubiquitin-protein ligase mediating ’Lys-48’-and ’Lys- 63’-linked polyubiquitination and subsequent proteasomal degradation of modified proteins. May play a role in myelopoiesis (493 aa)
ANAPC11anaphase 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)
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)
UBE3Dubiquitin protein ligase E3D; E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome (389 aa)
BTRCbeta-transducin repeat containing 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. Recognizes and binds to phosphorylated target proteins. SCF(BTRC) mediates the ubiquitination of CTNNB1 and participates in Wnt signaling. SCF(BTRC) mediates the ubiquitination of NFKBIA, NFKBIB and NFKBIE; the degradation frees the associated NFKB1 to translocate into the nucleus and to activate transcription. Ubiquitination of N [...] (605 aa)
HECTD3HECT domain containing E3 ubiquitin protein ligase 3; E3 ubiquitin ligases accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ubiquitination of TRIOBP and its subsequent proteasomal degradation, thus faciliting cell cycle progression by regulating the turn-over of TRIOBP. Mediates also ubiquitination of STX8 (By similarity) (861 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)
KLHDC5kelch domain containing 5; Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for mitotic progression and cytokinesis. The BCR(KLHL42) E3 ubiquitin ligase complex mediates the ubiquitination and subsequent degradation of KATNA1. Involved in microtubule dynamics throughout mitosis (505 aa)
LTN1listerin E3 ubiquitin protein ligase 1 (1812 aa)
UNKLunkempt homolog (Drosophila)-like; May participate in a protein complex showing an E3 ligase activity regulated by RAC1. Ubiquitination is directed towards itself and possibly other substrates, such as SMARCD2/BAF60b. Intrinsic E3 ligase activity has not been proven (680 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)
MIB2mindbomb E3 ubiquitin protein ligase 2 (1070 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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