RAD6 protein (Saccharomyces cerevisiae) - STRING interaction network
"RAD6" - Ubiquitin-conjugating enzyme in Saccharomyces cerevisiae
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:
some 3D structure is known or predicted
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
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
protein homology
Your Input:
Gene Fusion
RAD6Ubiquitin-conjugating enzyme (E2), involved in postreplication repair (as a heterodimer with Rad18p), DSBR and checkpoint control (as a heterodimer with Bre1p), ubiquitin-mediated N-end rule protein degradation (as a heterodimer with Ubr1p; Catalyzes the covalent attachment of ubiquitin to other proteins. In association with the E3 enzyme BRE1 and LGE1, it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric si [...] (172 aa)    
Predicted Functional Partners:
E3 ubiqutin ligase, forms heterodimer with Rad6p to monoubiquitinate PCNA-K164; heterodimer binds single-stranded DNA and has single-stranded DNA dependent ATPase activity; required for postreplication repair; E3 RING-finger protein, member of the UBC2/RAD6 epistasis group. Associates to the E2 ubiquitin conjugating enzyme UBC2/RAD6 to form the UBC2-RAD18 ubiquitin ligase complex involved in postreplicative repair (PRR) of damaged DNA. The UBC2-RAD18 complex cooperates with RAD5 and the UBC13-MMS2 dimer to attach mono-ubiquitin chains on ’Lys-164’ of POL30, which is necessary for PRR. [...] (487 aa)
Ubiquitin, becomes conjugated to proteins, marking them for selective degradation via the ubiquitin-26S proteasome system; essential for the cellular stress response; encoded as a polyubiquitin precursor comprised of 5 head-to-tail repeats; 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 ubiqui [...] (381 aa)
Proliferating cell nuclear antigen (PCNA), functions as the sliding clamp for DNA polymerase delta; may function as a docking site for other proteins required for mitotic and meiotic chromosomal DNA replication and for DNA repair; This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase’s processibility during elongation of the leading strand. Involved in DNA repair (258 aa)
E3 ubiquitin ligase, forms heterodimer with Rad6p to monoubiquinate histone H2B-K123, which is required for the subsequent methylation of histone H3-K4 and H3-K79; required for DSBR, transcription, silencing, and checkpoint control; E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H2B to form H2BK123ub1 in association with the E2 enzyme RAD6/UBC2. H2BK123ub1 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. It thereby plays a central ro [...] (700 aa)
Ubiquitin activating enzyme (E1), involved in ubiquitin-mediated protein degradation and essential for viability; Catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin- proteasome system. 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 a ubiquitin-E1 thioester and free AMP (1024 aa)
Cytoplasmic ubiquitin-protein ligase (E3); required for ubiquitylation of Rpn4p; mediates formation of a Mub1p-Ubr2p-Rad6p complex; E3 ubiquitin-protein ligase which probably functions outside the N-end rule pathway, since it lacks the residues essential for the degradation of N-end rule substrates. Mediates RPN4 ubiquitination and subsequent degradation (1872 aa)
Ubiquitin-conjugating enzyme variant involved in error-free postreplication repair; forms a heteromeric complex with Ubc13p, an active ubiquitin-conjugating enzyme; cooperates with chromatin-associated RING finger proteins, Rad18p and Rad5p; Has a role in the DNA error-free postreplication repair (PRR) pathway. Lacks catalytic activity by itself. The UBC13/MMS2 heterodimer catalyzes the synthesis of non-canonical poly- ubiquitin chains that are linked through ’Lys-63’ (137 aa)
E3 ubiquitin ligase (N-recognin), forms heterodimer with Rad6p to ubiquitinate substrates in the N-end rule pathway; regulates peptide transport via Cup9p ubiquitination; mutation in human UBR1 causes Johansson-Blizzard Syndrome (JBS); Ubiquitin ligase protein which is a component of the N- end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation (1950 aa)
E1-like protein that activates Urm1p before urmylation; also acts in thiolation of the wobble base of cytoplasmic tRNAs by adenylating and then thiolating Urm1p; receives sulfur from Tum1p; Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Acts by mediating the C-terminal thiocarboxylation of sulfur carrier URM1. Its N-terminus first activates URM1 as acyl- adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 to form thiocarboxylation (-COSH) of its C-terminus. The re [...] (440 aa)
E3 ubiquitin ligase of the NEDD4 family; involved in regulating many cellular processes including MVB sorting, heat shock response, transcription, endocytosis, and ribosome stability; human homolog is involved in Liddle syndrome; mutant tolerates an /.../dy; ubiquitylates Sec23p; E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Component of a RSP5 ubiquitin ligase complex which specifies polyubiquitination and intracellular trafficking of the general a [...] (809 aa)
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
Server load: low (6%) [HD]