Full Link:
  • Version:
  • 10.0 (archived version)
STRINGSTRING
SPSB2 SPSB2 UBE2D4 UBE2D4 UFL1 UFL1 VPRBP VPRBP UBE2E2 UBE2E2 LRRC41 LRRC41 FBXL13 FBXL13 UBR4 UBR4 UBE3D UBE3D FBXO44 FBXO44 UBE2B UBE2B CDC34 CDC34 FBXO41 FBXO41 FBXO15 FBXO15 SPSB4 SPSB4 RNF123 RNF123 UBE2G1 UBE2G1 UBE2N UBE2N CDC26 CDC26 TRIM32 TRIM32 MIB2 MIB2 UBE2Z UBE2Z ZNRF2 ZNRF2 ANAPC1 ANAPC1 ANAPC13 ANAPC13 KBTBD6 KBTBD6
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
Node Color
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)
UBE2D4ubiquitin-conjugating enzyme E2D 4 (putative); Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, but may prefer ’Lys-11’ and ’Lys-48’-linked polyubiquitination (147 aa)
FBXO44F-box protein 44; Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex (255 aa)
UBE2Bubiquitin-conjugating enzyme E2B; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In association with the E3 enzyme BRE1 (RNF20 and/or RNF40), it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B at ’Lys-120’ to form H2BK120ub1. H2BK120ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. In vitro catalyzes ’Lys-11’-, as well as ’Lys-48’- and ’Lys-63’-linked polyubiquiti [...] (152 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)
UBE2Nubiquitin-conjugating enzyme E2N; The UBE2V1-UBE2N and UBE2V2-UBE2N heterodimers catalyze the synthesis of non-canonical ’Lys-63’-linked polyubiquitin chains. This type of polyubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Acts together with the E3 ligases, HLTF and SHPRH, in the ’Lys-63’-linked poly-ubiquitination of PC [...] (152 aa)
FBXL13F-box and leucine-rich repeat protein 13 (735 aa)
ZNRF2zinc and ring finger 2; May play a role in the establishment and maintenance of neuronal transmission and plasticity via its ubiquitin ligase activity. 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 (242 aa)
RNF123ring finger protein 123 (1314 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)
LRRC41leucine rich repeat containing 41; Probable substrate recognition component of an ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (812 aa)
ANAPC13anaphase promoting complex subunit 13; 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 (74 aa)
UBE2Zubiquitin-conjugating enzyme E2Z; Catalyzes the covalent attachment of ubiquitin to other proteins (By similarity). Specific substrate for UBA6, not charged with ubiquitin by UBE1. May be involved in apoptosis regulation (354 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)
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)
CDC26cell division cycle 26 homolog (S. cerevisiae); 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 (85 aa)
UBR4ubiquitin protein ligase E3 component n-recognin 4 (5183 aa)
KBTBD6kelch repeat and BTB (POZ) domain containing 6 (674 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)
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)
FBXO15F-box protein 15; Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex (By similarity) (510 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)
MIB2mindbomb E3 ubiquitin protein ligase 2 (1070 aa)
SPSB2splA/ryanodine receptor domain and SOCS box containing 2; 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 (263 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
Server load: medium (54%)