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TXNDC17 TXNDC17 TWF1 TWF1 WDR61 WDR61 UBE2H UBE2H VCL VCL DSTN DSTN PRDX2 PRDX2 UFC1 UFC1 KLK3 KLK3 IMPA2 IMPA2 UBC UBC UBA3 UBA3 NT5DC1 NT5DC1 TMEFF2 TMEFF2 NEDD8 NEDD8 UIMC1 UIMC1 CPNE2 CPNE2 UBA52 UBA52 UBE2M UBE2M CUL5 CUL5 FBXO11 FBXO11 NAE1 NAE1 NUDCD2 NUDCD2 CUL1 CUL1 UBE2F UBE2F NEDD8-MDP1 NEDD8-MDP1
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:
VCLvinculin; Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell- surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion (1134 aa)
DSTNdestrin (actin depolymerizing factor); Actin-depolymerizing protein. Severs actin filaments (F- actin) and binds to actin monomers (G-actin). Acts in a pH- independent manner (165 aa)
TXNDC17thioredoxin domain containing 17; Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide (123 aa)
NEDD8neural precursor cell expressed, developmentally down-regulated 8; Ubiquitin-like protein which plays an important role in cell cycle control and embryogenesis. Covalent attachment to its substrates requires prior activation by the E1 complex UBE1C- APPBP1 and linkage to the E2 enzyme UBE2M. Attachment of NEDD8 to cullins activates their associated E3 ubiquitin ligase activity, and thus promotes polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins (81 aa)
UBE2Mubiquitin-conjugating enzyme E2M; Accepts the ubiquitin-like protein NEDD8 from the UBA3- NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX1, but not RBX2, suggests that the RBX1-UBE2M complex neddylates specific target proteins, such as CUL1, CUL2, CUL3 and CUL4. Involved in cell proliferation (183 aa)
WDR61WD repeat domain 61; Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non- phosphorylated and ’Ser-2’- and ’Ser-5’-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target gene [...] (305 aa)
IMPA2inositol(myo)-1(or 4)-monophosphatase 2; Can use myo-inositol monophosphates, scylloinositol 1,4- diphosphate, glucose-1-phosphate, beta-glycerophosphate, and 2’- AMP as substrates. Has been implicated as the pharmacological target for lithium Li(+) action in brain (288 aa)
TMEFF2transmembrane protein with EGF-like and two follistatin-like domains 2 (374 aa)
UBE2Fubiquitin-conjugating enzyme E2F (putative); Accepts the ubiquitin-like protein NEDD8 from the UBA3- NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX2, but not RBX1, suggests that the RBX2-UBE2F complex neddylates specific target proteins, such as CUL5 (185 aa)
CPNE2copine II (548 aa)
NAE1NEDD8 activating enzyme E1 subunit 1; Regulatory 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. Necessary for cell cycle progression through the S-M checkpoint. Overexpression of NAE1 causes apoptosis through deregulation of NEDD8 conjugation (534 aa)
PRDX2peroxiredoxin 2; Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system. It is not able to receive electrons from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2) (198 aa)
NUDCD2NudC domain containing 2; May regulate the LIS1/dynein pathway by stabilizing LIS1 with Hsp90 chaperone (157 aa)
KLK3kallikrein-related peptidase 3; Hydrolyzes semenogelin-1 thus leading to the liquefaction of the seminal coagulum (261 aa)
CUL1cullin 1; Core component of multiple cullin-RING-based SCF (SKP1- CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. 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 exchange of the substrate [...] (776 aa)
NT5DC15’-nucleotidase domain containing 1 (455 aa)
UBCubiquitin C (685 aa)
UBE2Hubiquitin-conjugating enzyme E2H; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys- 11’- and ’Lys-48’-linked polyubiquitination. Capable, in vitro, to ubiquitinate histone H2A (183 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)
UFC1ubiquitin-fold modifier conjugating enzyme 1; E2-like enzyme which forms an intermediate with UFM1 via a thioester linkage (167 aa)
UIMC1ubiquitin interaction motif containing 1 (719 aa)
CUL5cullin 5; Core component of multiple SCF-like ECS (Elongin-Cullin 2/5-SOCS-box protein) 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 functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition component. ECS(SOCS1) seems to direct ubiquitination of JAk2. Seems to be involved poteosomal degradation of p53/TP53 stimulated by [...] (780 aa)
FBXO11F-box protein 11 (927 aa)
UBA52ubiquitin A-52 residue ribosomal protein fusion product 1 (128 aa)
NEDD8-MDP1NEDD8-MDP1 readthrough (170 aa)
TWF1twinfilin, actin-binding protein, homolog 1 (Drosophila) (357 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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