A2A7Q9 · RN19B_MOUSE

  • Protein
    E3 ubiquitin-protein ligase RNF19B
  • Gene
    Rnf19b
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as UCKL1. Involved in the cytolytic activity of natural killer cells and cytotoxic T-cells. Protects against staurosporin-induced cell death (By similarity).

Catalytic activity

  • [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine.
    EC:2.3.2.31 (UniProtKB | ENZYME | Rhea)

Pathway

Protein modification; protein ubiquitination.

Features

Showing features for binding site, active site.

1732100200300400500600700
TypeIDPosition(s)Description
Binding site116Zn2+ 1 (UniProtKB | ChEBI)
Binding site119Zn2+ 1 (UniProtKB | ChEBI)
Binding site139Zn2+ 1 (UniProtKB | ChEBI)
Binding site142Zn2+ 1 (UniProtKB | ChEBI)
Binding site203Zn2+ 2 (UniProtKB | ChEBI)
Binding site208Zn2+ 2 (UniProtKB | ChEBI)
Binding site225Zn2+ 2 (UniProtKB | ChEBI)
Binding site230Zn2+ 2 (UniProtKB | ChEBI)
Binding site235Zn2+ 3 (UniProtKB | ChEBI)
Binding site238Zn2+ 3 (UniProtKB | ChEBI)
Binding site243Zn2+ 3 (UniProtKB | ChEBI)
Binding site248Zn2+ 3 (UniProtKB | ChEBI)
Binding site284Zn2+ 4 (UniProtKB | ChEBI)
Binding site287Zn2+ 4 (UniProtKB | ChEBI)
Active site299
Binding site304Zn2+ 4 (UniProtKB | ChEBI)
Binding site307Zn2+ 4 (UniProtKB | ChEBI)
Binding site312Zn2+ 5 (UniProtKB | ChEBI)
Binding site315Zn2+ 5 (UniProtKB | ChEBI)
Binding site323Zn2+ 5 (UniProtKB | ChEBI)
Binding site330Zn2+ 5 (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytolytic granule
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentendoplasmic reticulum
Cellular Componentendoplasmic reticulum membrane
Cellular Componentubiquitin ligase complex
Molecular Functionubiquitin binding
Molecular Functionubiquitin conjugating enzyme binding
Molecular Functionubiquitin protein ligase activity
Molecular Functionzinc ion binding
Biological Processadaptive immune response
Biological Processnatural killer cell mediated cytotoxicity
Biological Processprotein autoubiquitination
Biological Processprotein polyubiquitination
Biological Processubiquitin-dependent protein catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    E3 ubiquitin-protein ligase RNF19B
  • EC number
  • Alternative names
    • IBR domain-containing protein 3
    • Natural killer lytic-associated molecule
    • RING finger protein 19B

Gene names

    • Name
      Rnf19b
    • Synonyms
      Ibrdc3, Nklam

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • Czech II
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    A2A7Q9
  • Secondary accessions
    • A0AUN9
    • Q7TT05

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane351-371Helical
Transmembrane412-432Helical

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003071881-732E3 ubiquitin-protein ligase RNF19B

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed specifically in natural killer cells, activated macrophages and cytotoxic T-cells (PubMed:10912506).
Present in macrophages (at protein level) (PubMed:10912506).
Ubiquitously expressed with high expression in testis (PubMed:27485036).

Induction

By IFNG and LPS in macrophages. By IL2 in natural killer cells and cytotoxic T-cells.

Gene expression databases

Interaction

Subunit

Interacts with UBE2L3, UBE2L6 and UCKL1.

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias, zinc finger.

TypeIDPosition(s)Description
Region1-109Disordered
Region1-315Required for ubiquitin ligase activity and for protection against staurosporin-induced cell death
Compositional bias52-77Pro residues
Region112-334TRIAD supradomain
Zinc finger116-165RING-type 1
Zinc finger183-248IBR-type
Zinc finger284-315RING-type 2; atypical
Region598-644Disordered
Region660-732Disordered

Domain

The first IBR-type zinc finger is the most crucial for interaction with UBE2L3, UBE2L6 and UCKL1.
Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING domain, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved cysteine residue in the second RING domain.

Sequence similarities

Belongs to the RBR family. RNF19 subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    732
  • Mass (Da)
    78,127
  • Last updated
    2007-10-23 v2
  • Checksum
    81AAF64F9AE566F7
MGSEKDSESPRSTSLHAAAPDPKCRSGGRRRRLTFHSVFSASARGRRARTKPQAEPPPPAAPPPPPPPAPAPVEAQAPPVEALPSEPAAEAEAEAVAAGPEEDEAAEGGGAEEVECPLCLVRLPPERAPRLLSCPHRSCRDCLRHYLRLEISESRVPISCPECSERLNPHDIRLLLADPPLMHKYEEFMLRRYLASDPDCRWCPAPDCGYAVIAYGCASCPKLTCEREGCQTEFCYHCKQIWHPNQTCDMARQQRAQTLRVRTKHTSGLSYGQESGPADDIKPCPRCSAYIIKMNDGSCNHMTCAVCGCEFCWLCMKEISDLHYLSPSGCTFWGKKPWSRKKKILWQLGTLIGAPVGISLIAGIAIPAMVIGIPVYVGRKIHSRYEGRKTSKHKRNLAITGGVTLSVIASPVIAAVSVGIGVPIMLAYVYGVVPISLCRGGGCGVSTANGKGVKIEFDEDDGPITVADAWRALKNPSIGESSIEGLTSVLSTSGSPTDGLSVMQGPYSETASFAALSGGTLSGGILSSGKGKYSRLEVQADVQKEIFPKDTASLGAISDSASTRAMAGSIISSYNPQDRECNNMEIQVDIEAKPSHYQLVSGSSTEDSLHVHAQVAEKEEEGNGAGGGSGGSEDDPPYKHQSCEQKDCLASKAWDISLAQPESIRSDLESSDTQSDDVPDITSDECGSPRSHAAACPSTPQVHGAPSPSAHKNLAAPAEGQTVLKSEEYEVE

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
E9Q2L7E9Q2L7_MOUSERnf19b731
A2A7Q8A2A7Q8_MOUSERnf19b352
F6TQN1F6TQN1_MOUSERnf19b247
B2KG08B2KG08_MOUSERnf19b551

Sequence caution

The sequence AAH52529.1 differs from that shown. Reason: Erroneous initiation
The sequence CAM19707.1 differs from that shown. Reason: Erroneous initiation

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias52-77Pro residues
Sequence conflict278in Ref. 1 and 3; AAI17808
Sequence conflict721in Ref. 3; AAH52529

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL606977
EMBL· GenBank· DDBJ
CAM19707.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation
BC052529
EMBL· GenBank· DDBJ
AAH52529.1
EMBL· GenBank· DDBJ
mRNA Different initiation
BC117807
EMBL· GenBank· DDBJ
AAI17808.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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