UniProt:Q99ML9 Rnf111

chain
  • chain:1-989
checksum 212E3C37BC70DCB5
comment
  • FUNCTION E3 ubiquitin-protein ligase required for mesoderm patterning during embryonic development (PubMed:11298452). Acts as an enhancer of the transcriptional responses of the SMAD2/SMAD3 effectors, which are activated downstream of BMP (PubMed:14657019). Acts by mediating ubiquitination and degradation of SMAD inhibitors such as SMAD7, inducing their proteasomal degradation and thereby enhancing the transcriptional activity of TGF-beta and BMP (PubMed:14657019). In addition to enhance transcription of SMAD2/SMAD3 effectors, also regulates their turnover by mediating their ubiquitination and subsequent degradation, coupling their activation with degradation, thereby ensuring that only effectors 'in use' are degraded (By similarity). Activates SMAD3/SMAD4-dependent transcription by triggering signal-induced degradation of SNON isoform of SKIL (By similarity). Associates with UBE2D2 as an E2 enzyme (By similarity). Specifically binds polysumoylated chains via SUMO interaction motifs (SIMs) and mediates ubiquitination of sumoylated substrates (PubMed:23530056). Catalyzes 'Lys-63'-linked ubiquitination of sumoylated XPC in response to UV irradiation, promoting nucleotide excision repair (By similarity). Mediates ubiquitination and degradation of sumoylated PML (PubMed:23530056). The regulation of the BMP-SMAD signaling is however independent of sumoylation and is not dependent of SUMO interaction motifs (SIMs) (PubMed:23530056).CATALYTIC ACTIVITY S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.ACTIVITY REGULATION Binds free ubiquitin non-covalently via its RING-type zinc finger. Ubiquitin-binding leads to enhance the E3 ubiquitin-protein ligase activity by stabilizing the ubiquitin-conjugating enzyme E2 (donor ubiquitin) in the 'closed' conformation and activating ubiquitin transfer.PATHWAY Protein modification; protein ubiquitination.SUBUNIT Monomer (By similarity). Interacts with SMAD6, SMAD7, AXIN1, AXIN2 and SKIL isoform SNON (PubMed:14657019). Interacts with (phosphorylated) SMAD2 and SMAD3 (PubMed:17341133). Part of a complex containing RNF111, AXIN1 and SMAD7 (By similarity). Interacts (via SIM domains) with SUMO1 and SUMO2 (PubMed:23530056).INTERACTION Upon TGF-beta treatment, translocates from nucleus to cytosol.ALTERNATIVE PRODUCTS Ubiquitously expressed.DEVELOPMENTAL STAGE Ubiquitously expressed from ES cells to midgestation.DOMAIN The SUMO interaction motifs (SIMs) mediates the binding to polysumoylated substrate.DOMAIN The RING-type zinc finger mediates the E3 ubiquitin-protein ligase activity and binds directly to free ubiquitin. Non-covalent ubiquitin-binding stabilizes the ubiquitin-conjugating enzyme E2 (donor ubiquitin) in the 'closed' conformation and stimulates ubiquitin transfer.DISRUPTION PHENOTYPE Mice rarely develop beyond 15 somites, have a reduced head, fail to undergo turning and die at midgestation.SIMILARITY Belongs to the Arkadia family.
created [InstanceEdit:217385] Schmidt, EE, 2008-03-27 06:23:53
crossReference
databaseName UniProt
dbId 246057
description
  • recommendedName: fullName evidence="12"E3 ubiquitin-protein ligase Arkadia ecNumber evidence="8"2.3.2.27 alternativeName: fullName evidence="13"RING finger protein 111 alternativeName: fullName evidence="11"RING-type E3 ubiquitin transferase Arkadia
displayName UniProt:Q99ML9 Rnf111
geneName
  • Rnf111
identifier Q99ML9
isSequenceChanged false
keyword
  • Alternative splicing
  • Cytoplasm
  • Developmental protein
  • DNA damage
  • DNA repair
  • Isopeptide bond
  • Metal-binding
  • Nucleus
  • Reference proteome
  • Transferase
  • Ubl conjugation
  • Ubl conjugation pathway
  • Zinc
  • Zinc-finger
modified [InstanceEdit:9852000] Weiser, Joel, 2023-11-03
moleculeType Protein
name
  • Rnf111
otherIdentifier
  • 10594785
  • 112943_at
  • 1423304_a_at
  • 163220_at
  • 17528597
  • 4425086
  • 4467858
  • 4500064
  • 4500584
  • 4506563
  • 4515786
  • 4591112
  • 4621726
  • 4649366
  • 4671441
  • 4695201
  • 4751412
  • 4763440
  • 4788004
  • 4908393
  • 4920669
  • 4931467
  • 4970098
  • 4991798
  • 5000259
  • 5022846
  • 5028446
  • 5031394
  • 5062894
  • 5074150
  • 5088286
  • 5092392
  • 5094670
  • 5245307
  • 5254773
  • 5263561
  • 5311490
  • 5334720
  • 5472305
  • 5505182
  • 5529323
  • 5539462
  • 5575952
  • 5584319
  • 5595067
  • 93836
  • A_52_P207151
  • A_52_P444368
  • A_55_P2093221
  • GE41929
  • GO:0000209
  • GO:0003824
  • GO:0004842
  • GO:0005515
  • GO:0005634
  • GO:0005654
  • GO:0005737
  • GO:0005829
  • GO:0006281
  • GO:0006511
  • GO:0006974
  • GO:0007389
  • GO:0008270
  • GO:0016567
  • GO:0016605
  • GO:0016740
  • GO:0030511
  • GO:0031398
  • GO:0032184
  • GO:0032991
  • GO:0046332
  • GO:0046872
  • GO:0061630
  • GO:0140096
  • ILMN_1252738
  • ILMN_2614080
  • ILMN_2700945
  • mMC023088
  • mMC024657
  • mMR028725
physicalEntity
referenceDatabase [ReferenceDatabase:2] UniProt
referenceGene
referenceTranscript
schemaClass ReferenceGeneProduct
secondaryIdentifier
  • RN111_MOUSE
  • Q3UVL7
  • Q6NSW2
  • Q7TMR3
  • Q8C881
  • Q8CBC0
sequenceLength 989
species [Species:48892] Mus musculus
stId uniprot:Q99ML9
url http://purl.uniprot.org/uniprot/Q99ML9
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