STRINGSTRING
KXD1 KXD1 UBC UBC A0A5G2QQZ4_PIG A0A5G2QQZ4_PIG RPS27A RPS27A FAU FAU NEDD8 NEDD8 UBL4B UBL4B USP14 USP14 UBB UBB BAG6 BAG6
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 Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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 to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
KXD1Ubiquitin-60S ribosomal protein L40; [Ubiquitin]: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be in [...] (305 aa)
UBCUbiquitin-related; [Ubiquitin]: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repa [...] (837 aa)
A0A5G2QQZ4_PIGUbiquitin-like domain-containing protein. (135 aa)
RPS27AUbiquitin-like domain-containing protein. (204 aa)
FAUUbiquitin-like protein FUBI. (133 aa)
NEDD8NEDD8 ubiquitin like modifier. (71 aa)
UBL4BUbiquitin-like domain-containing protein. (62 aa)
USP14Ubiquitin carboxyl-terminal hydrolase; Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes. Belongs to the peptidase C19 family. (505 aa)
UBBUbiquitin B. (229 aa)
BAG6Large proline-rich protein BAG6; ATP-independent molecular chaperone preventing the aggregation of misfolded and hydrophobic patches-containing proteins. Functions as part of a cytosolic protein quality control complex, the BAG6/BAT3 complex, which maintains these client proteins in a soluble state and participates to their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation. The BAG6/BAT3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endo [...] (1163 aa)
Your Current Organism:
Sus scrofa
NCBI taxonomy Id: 9823
Other names: S. scrofa, pig, pigs, swine, wild boar
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