A2A7Q9 · RN19B_MOUSE
- ProteinE3 ubiquitin-protein ligase RNF19B
- GeneRnf19b
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids732 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
Pathway
Protein modification; protein ubiquitination.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 116 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 119 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 139 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 142 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 203 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 208 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 225 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 230 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 235 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 238 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 243 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 248 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 284 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 287 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Active site | 299 | |||||
Sequence: C | ||||||
Binding site | 304 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 307 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 312 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 315 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 323 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 330 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytolytic granule | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | ubiquitin ligase complex | |
Molecular Function | ubiquitin binding | |
Molecular Function | ubiquitin conjugating enzyme binding | |
Molecular Function | ubiquitin protein ligase activity | |
Molecular Function | zinc ion binding | |
Biological Process | adaptive immune response | |
Biological Process | natural killer cell mediated cytotoxicity | |
Biological Process | protein autoubiquitination | |
Biological Process | protein polyubiquitination | |
Biological Process | ubiquitin-dependent protein catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase RNF19B
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionA2A7Q9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cytoplasmic granule membrane ; Multi-pass membrane protein
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 351-371 | Helical | ||||
Sequence: LIGAPVGISLIAGIAIPAMVI | ||||||
Transmembrane | 412-432 | Helical | ||||
Sequence: VIAAVSVGIGVPIMLAYVYGV |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000307188 | 1-732 | E3 ubiquitin-protein ligase RNF19B | |||
Sequence: MGSEKDSESPRSTSLHAAAPDPKCRSGGRRRRLTFHSVFSASARGRRARTKPQAEPPPPAAPPPPPPPAPAPVEAQAPPVEALPSEPAAEAEAEAVAAGPEEDEAAEGGGAEEVECPLCLVRLPPERAPRLLSCPHRSCRDCLRHYLRLEISESRVPISCPECSERLNPHDIRLLLADPPLMHKYEEFMLRRYLASDPDCRWCPAPDCGYAVIAYGCASCPKLTCEREGCQTEFCYHCKQIWHPNQTCDMARQQRAQTLRVRTKHTSGLSYGQESGPADDIKPCPRCSAYIIKMNDGSCNHMTCAVCGCEFCWLCMKEISDLHYLSPSGCTFWGKKPWSRKKKILWQLGTLIGAPVGISLIAGIAIPAMVIGIPVYVGRKIHSRYEGRKTSKHKRNLAITGGVTLSVIASPVIAAVSVGIGVPIMLAYVYGVVPISLCRGGGCGVSTANGKGVKIEFDEDDGPITVADAWRALKNPSIGESSIEGLTSVLSTSGSPTDGLSVMQGPYSETASFAALSGGTLSGGILSSGKGKYSRLEVQADVQKEIFPKDTASLGAISDSASTRAMAGSIISSYNPQDRECNNMEIQVDIEAKPSHYQLVSGSSTEDSLHVHAQVAEKEEEGNGAGGGSGGSEDDPPYKHQSCEQKDCLASKAWDISLAQPESIRSDLESSDTQSDDVPDITSDECGSPRSHAAACPSTPQVHGAPSPSAHKNLAAPAEGQTVLKSEEYEVE |
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).
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
Structure
Family & Domains
Features
Showing features for region, compositional bias, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-109 | Disordered | ||||
Sequence: MGSEKDSESPRSTSLHAAAPDPKCRSGGRRRRLTFHSVFSASARGRRARTKPQAEPPPPAAPPPPPPPAPAPVEAQAPPVEALPSEPAAEAEAEAVAAGPEEDEAAEGG | ||||||
Region | 1-315 | Required for ubiquitin ligase activity and for protection against staurosporin-induced cell death | ||||
Sequence: MGSEKDSESPRSTSLHAAAPDPKCRSGGRRRRLTFHSVFSASARGRRARTKPQAEPPPPAAPPPPPPPAPAPVEAQAPPVEALPSEPAAEAEAEAVAAGPEEDEAAEGGGAEEVECPLCLVRLPPERAPRLLSCPHRSCRDCLRHYLRLEISESRVPISCPECSERLNPHDIRLLLADPPLMHKYEEFMLRRYLASDPDCRWCPAPDCGYAVIAYGCASCPKLTCEREGCQTEFCYHCKQIWHPNQTCDMARQQRAQTLRVRTKHTSGLSYGQESGPADDIKPCPRCSAYIIKMNDGSCNHMTCAVCGCEFCWLC | ||||||
Compositional bias | 52-77 | Pro residues | ||||
Sequence: PQAEPPPPAAPPPPPPPAPAPVEAQA | ||||||
Region | 112-334 | TRIAD supradomain | ||||
Sequence: EEVECPLCLVRLPPERAPRLLSCPHRSCRDCLRHYLRLEISESRVPISCPECSERLNPHDIRLLLADPPLMHKYEEFMLRRYLASDPDCRWCPAPDCGYAVIAYGCASCPKLTCEREGCQTEFCYHCKQIWHPNQTCDMARQQRAQTLRVRTKHTSGLSYGQESGPADDIKPCPRCSAYIIKMNDGSCNHMTCAVCGCEFCWLCMKEISDLHYLSPSGCTFWG | ||||||
Zinc finger | 116-165 | RING-type 1 | ||||
Sequence: CPLCLVRLPPERAPRLLSCPHRSCRDCLRHYLRLEISESRVPISCPECSE | ||||||
Zinc finger | 183-248 | IBR-type | ||||
Sequence: HKYEEFMLRRYLASDPDCRWCPAPDCGYAVIAYGCASCPKLTCEREGCQTEFCYHCKQIWHPNQTC | ||||||
Zinc finger | 284-315 | RING-type 2; atypical | ||||
Sequence: CPRCSAYIIKMNDGSCNHMTCAVCGCEFCWLC | ||||||
Region | 598-644 | Disordered | ||||
Sequence: QLVSGSSTEDSLHVHAQVAEKEEEGNGAGGGSGGSEDDPPYKHQSCE | ||||||
Region | 660-732 | Disordered | ||||
Sequence: QPESIRSDLESSDTQSDDVPDITSDECGSPRSHAAACPSTPQVHGAPSPSAHKNLAAPAEGQTVLKSEEYEVE |
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
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length732
- Mass (Da)78,127
- Last updated2007-10-23 v2
- Checksum81AAF64F9AE566F7
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 52-77 | Pro residues | ||||
Sequence: PQAEPPPPAAPPPPPPPAPAPVEAQA | ||||||
Sequence conflict | 278 | in Ref. 1 and 3; AAI17808 | ||||
Sequence: Missing | ||||||
Sequence conflict | 721 | in Ref. 3; AAH52529 | ||||
Sequence: Q → P |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |