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BARD1 BARD1 STUB1 STUB1 RNF103 RNF103 BRCA1 BRCA1 RNF8 RNF8 RNF19A RNF19A PARK2 PARK2 SIAH1 SIAH1 CUL9 CUL9 UBE2L3 UBE2L3 RNF14 RNF14 UBC UBC UNG UNG UBE2E2 UBE2E2 UBE2L6 UBE2L6 PTBP2 PTBP2 CUL3 CUL3 RNF125 RNF125 ARIH1 ARIH1 UBA1 UBA1 TRIP12 TRIP12 UBOX5 UBOX5 ISG15 ISG15 SPEN SPEN MID1 MID1 IPO11 IPO11
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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.
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small nodes:
protein of unknown 3D structure
large protein node
large nodes:
some 3D structure is known or predicted
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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.
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from curated databases
experiment edge
experimentally determined
Predicted Interactions
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gene neighborhood
fusion edge
gene fusions
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gene co-occurrence
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textmining
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co-expression
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UBOX5U-box domain containing 5 (541 aa)
RNF125ring finger protein 125, E3 ubiquitin protein ligase; E3 ubiquitin-protein ligase that acts as a positive regulator of T-cell activation. E3 ligase proteins mediate ubiquitination and subsequent proteasomal degradation of target proteins (232 aa)
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)
RNF103ring finger protein 103; Acts as an E2-dependent E3 ubiquitin-protein ligase, probably involved in the ER-associated protein degradation pathway (685 aa)
UNGuracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine (By similarity) (313 aa)
CUL9cullin 9; Cytoplasmic anchor protein in p53-associated protein complex. Regulates the subcellular localization of p53 and subsequent function. Seems to be part of an atypical cullin-RING- based E3 ubiquitin-protein ligase complex. In vitro, complexes of CUL9/PARC with either CUL7 or TP53 contain E3 ubiquitin-protein ligase activity (2517 aa)
BARD1BRCA1 associated RING domain 1; Probable E3 ubiquitin-protein ligase. The BRCA1-BARD1 heterodimer specifically mediates the formation of ’Lys-6’-linked polyubiquitin chains and coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Plays a central role in the control of the cell cycle in response to DNA damage. Acts by mediating ubiquitin E3 ligase activity that is required for its tumor suppressor function. Also forms a heterodimer with CSTF1/CSTF-50 to modulate mRNA processing and RNAP I [...] (777 aa)
CUL3cullin 3; Core component of multiple cullin-RING-based BCR (BTB- CUL3-RBX1) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1 (By similarity). The functional specificity of the BCR comple [...] (768 aa)
TRIP12thyroid hormone receptor interactor 12; E3 ubiquitin-protein ligase involved in ubiquitin fusion degradation (UFD) pathway and regulation of DNA repair. Part of the ubiquitin fusion degradation (UFD) pathway, a process that mediates ubiquitination of protein at their N-terminus, regardeless of the presence of lysine residues in target proteins. In normal cells, mediates ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A, a lysine-less tumor suppressor required for p53/TP53 activation under oncogenic stress. In cancer cells, however, isoform p19ARF/ARF and TRIP12 are located [...] (1992 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)
MID1midline 1 (Opitz/BBB syndrome); Has E3 ubiquitin ligase activity towards IGBP1, promoting its monoubiquitination, which results in deprotection of the catalytic subunit of protein phosphatase PP2A, and its subsequent degradation by polyubiquitination (667 aa)
RNF14ring finger protein 14 (474 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)
RNF19Aring finger protein 19A, E3 ubiquitin protein ligase; 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 SNCAIP or CASR. Specifically ubiquitinates pathogenic SOD1 variants, which leads to their proteasomal degradation and to neuronal protection (838 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)
UBCubiquitin C (685 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)
PARK2parkinson protein 2, E3 ubiquitin protein ligase (parkin) (465 aa)
RNF8ring finger protein 8, E3 ubiquitin protein ligase; E3 ubiquitin-protein ligase that plays a key role in DNA damage signaling via 2 distinct roles- by mediating the ’Lys-63’- linked ubiquitination of histones H2A and H2AX and promoting the recruitment of DNA repair proteins at double-strand breaks (DSBs) sites, and by catalyzing ’Lys-48’-linked ubiquitination to remove target proteins from DNA damage sites. Following DNA DSBs, it is recruited to the sites of damage by ATM-phosphorylated MDC1 and catalyzes the ’Lys-63’-linked ubiquitination of histones H2A and H2AX, thereby promoting th [...] (485 aa)
SPENspen homolog, transcriptional regulator (Drosophila); May serve as a nuclear matrix platform that organizes and integrates transcriptional responses. In osteoblasts, supports transcription activation- synergizes with RUNX2 to enhance FGFR2- mediated activation of the osteocalcin FGF-responsive element (OCFRE) (By similarity). Has also been shown to be an essential corepressor protein, which probably regulates different key pathways such as the Notch pathway. Negative regulator of the Notch pathway via its interaction with RBPSUH, which prevents the association between NOTCH1 and RBPSUH [...] (3664 aa)
ISG15ISG15 ubiquitin-like modifier; Ubiquitin-like protein that is conjugated to intracellular target proteins after IFN-alpha or IFN-beta stimulation. Its enzymatic pathway is partially distinct from that of ubiquitin, differing in substrate specificity and interaction with ligating enzymes. ISG15 conjugation pathway uses a dedicated E1 enzyme, but seems to converge with the Ub conjugation pathway at the level of a specific E2 enzyme. Targets include STAT1, SERPINA3G/SPI2A, JAK1, MAPK3/ERK1, PLCG1, EIF2AK2/PKR, MX1/MxA, and RIG-1. Deconjugated by USP18/UBP43. Shows specific chemotactic act [...] (165 aa)
ARIH1ariadne homolog, ubiquitin-conjugating enzyme E2 binding protein, 1 (Drosophila); E3 ubiquitin-protein ligase, which catalyzes polyubiquitination of target proteins together with ubiquitin- conjugating enzyme E2 UBE2L3. May play a role in protein translation by mediating polyubiquitination of EIF4E2, leading to its subsequent degradation (557 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)
IPO11importin 11; Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran- dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis r [...] (1015 aa)
PTBP2polypyrimidine tract binding protein 2; RNA-binding protein which binds to intronic polypyrimidine tracts and mediates negative regulation of exons splicing. May antagonize in a tissue-specific manner the ability of NOVA1 to activate exon selection. Beside its function in pre- mRNA splicing, plays also a role in the regulation of translation. Isoform 5 has a reduced affinity for RNA (531 aa)
BRCA1breast cancer 1, early onset; E3 ubiquitin-protein ligase that specifically mediates the formation of ’Lys-6’-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. It is unclear whether it also mediates the formation of other types of polyubiquitin chains. The E3 ubiquitin-protein ligase activity is required for its tumor suppressor function. The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Reg [...] (1884 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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