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TMED10 TMED10 SEC61A1 SEC61A1 UBL4A UBL4A TRIP12 TRIP12 SEC61A2 SEC61A2 ERN1 ERN1 UBE2R2 UBE2R2 UBB UBB FAF2 FAF2 MARCH6 MARCH6 RNF139 RNF139 UBC UBC CDC34 CDC34 UBE2J2 UBE2J2 AMFR AMFR UBE2G2 UBE2G2 AUP1 AUP1 RBX1 RBX1 SYVN1 SYVN1 EMC1 EMC1 UBE2G1 UBE2G1 PARK2 PARK2 ERN2 ERN2 EMC4 EMC4 GPR37 GPR37 RNASEL RNASEL
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
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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:
CDC34cell division cycle 34 homolog (S. cerevisiae); Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys- 48’-linked polyubiquitination. Cooperates with the E2 UBCH5C and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Performs ubiquitin chain elongation building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. UBE2D3 acts as an initiator E2, priming the phosphorylated NFKBIA target at positions ’Lys-21’ and/or ’Lys-22’ with a monoubiqu [...] (236 aa)
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)
SEC61A1Sec61 alpha 1 subunit (S. cerevisiae) (476 aa)
ERN2endoplasmic reticulum to nucleus signaling 2; Induces translational repression through 28S ribosomal RNA cleavage in response to ER stress. Pro-apoptotic. Appears to play no role in the unfolded-protein response, unlike closely related proteins (974 aa)
FAF2Fas associated factor family member 2; May play a role in the translocation of terminally misfolded proteins from the endoplasmic reticulum lumen to the cytoplasm and their degradation by the proteasome (445 aa)
UBE2R2ubiquitin-conjugating enzyme E2R 2; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes monoubiquitination and ’Lys-48’-linked polyubiquitination. May be involved in degradation of katenin (238 aa)
EMC4ER membrane protein complex subunit 4; May mediate anti-apoptotic activity (183 aa)
MARCH6membrane-associated ring finger (C3HC4) 6, E3 ubiquitin protein ligase; E3 ubiquitin-protein ligase that promotes ubiquitination of DIO2, leading to its degradation. 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. May cooperate with UBE2G1 (910 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)
AMFRautocrine motility factor receptor, E3 ubiquitin protein ligase; E3 ubiquitin-protein ligase that mediates the polyubiquitination of a number of proteins such as CD3D, CYP3A4, CFTR and APOB for proteasomal degradation. Component of a VCP/p97- AMFR/gp78 complex that participates in the final step of endoplasmic reticulum-associated degradation (ERAD). The VCP/p97- AMFR/gp78 complex is involved in the sterol-accelerated ERAD degradation of HMGCR through binding to the HMGCR-INSIG complex at the ER membrane and initiating ubiquitination of HMGCR. The ubiquitinated HMGCR is then released f [...] (643 aa)
SEC61A2Sec61 alpha 2 subunit (S. cerevisiae); Appears to play a crucial role in the insertion of secretory and membrane polypeptides into the ER. It is required for assembly of membrane and secretory proteins. Found to be tightly associated with membrane-bound ribosomes, either directly or through adaptor proteins (By similarity) (476 aa)
TMED10transmembrane emp24-like trafficking protein 10 (yeast); Involved in vesicular protein trafficking. Mainly functions in the early secretory pathway. Thought to act as cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and to be involved in vesicle coat formation at the cytoplasmic side. In COPII vesicle-mediated anterograde transport involved in the transport of GPI-anchored proteins and proposed to act togther with TMED2 as their cargo receptor; the function specifically implies SEC24C and SEC24D of the COPII vesicle coat and lipi [...] (219 aa)
RNF139ring finger protein 139; E3-ubiquitin ligase; acts as a negative regulator of the cell proliferation through mechanisms involving G2/M arrest and cell death. Required for MHC class I ubiquitination in cells expressing the cytomegalovirus protein US2 before dislocation from the endoplasmic reticulum (ER). Affects SREBP processing by hindering the SREBP/SCAP complex translocation from the ER to the Golgi, thereby reducing SREBF2 target gene expression. Required for INSIG1 ubiquitination. May be required for EIF3 complex ubiquitination. May function as a signaling receptor (664 aa)
UBBubiquitin B (229 aa)
GPR37G protein-coupled receptor 37 (endothelin receptor type B-like); Orphan receptor. May have a unique functional role in the central nervous system (613 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)
UBCubiquitin C (685 aa)
PARK2parkinson protein 2, E3 ubiquitin protein ligase (parkin) (465 aa)
RNASELribonuclease L (2’,5’-oligoisoadenylate synthetase-dependent); Endoribonuclease that functions in the interferon (IFN) antiviral response. In INF treated and virus infected cells, RNASEL probably mediates its antiviral effects through a combination of direct cleavage of single-stranded viral RNAs, inhibition of protein synthesis through the degradation of rRNA, induction of apoptosis, and induction of other antiviral genes. RNASEL mediated apoptosis is the result of a JNK-dependent stress- response pathway leading to cytochrome c release from mitochondria and caspase-dependent apoptosi [...] (741 aa)
UBL4Aubiquitin-like 4A; Component of the BAT3 complex, a multiprotein complex involved in the post-translational delivery of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane. TA membrane proteins, also named type II transmembrane proteins, contain a single C-terminal transmembrane region. The complex acts by facilitating TA proteins capture by ASNA1/TRC40- it is recruited to ribosomes synthesizing membrane proteins, interacts with the transmembrane region of newly released TA proteins, and transfers them to ASNA1/TRC40 for targeting (157 aa)
SYVN1synovial apoptosis inhibitor 1, synoviolin; Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC7 E2 ligase and transfers it to substrates, promoting their degradation. Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Also promotes the degradation of normal but naturally short-lived proteins such as SGK. Protects cells from ER stress-induced apoptosis. Protects neurons f [...] (617 aa)
AUP1ancient ubiquitous protein 1; May play a role in the translocation of terminally misfolded proteins from the endoplasmic reticulum lumen to the cytoplasm and their degradation by the proteasome (410 aa)
UBE2G1ubiquitin-conjugating enzyme E2G 1; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys- 48’-, as well as ’Lys-63’-linked polyubiquitination. May be involved in degradation of muscle-specific proteins. Mediates polyubiquitination of CYP3A4 (170 aa)
UBE2J2ubiquitin-conjugating enzyme E2, J2; Catalyzes the covalent attachment of ubiquitin to other proteins. Seems to function in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD) (By similarity) (275 aa)
ERN1endoplasmic reticulum to nucleus signaling 1; Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto- activation. The active endoribonuclease domain splices XBP1 mRNA to generate a new C-terminus, converting it into a potent unfolded-protein response transcriptional activator and triggering growth arrest and apoptosis (977 aa)
EMC1ER membrane protein complex subunit 1 (993 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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