Q9ULX5 · RN112_HUMAN
- ProteinRING finger protein 112
- GeneRNF112
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids631 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
E3 ubiquitin-protein ligase that plays an important role in neuronal differentiation, including neurogenesis and gliogenesis, during brain development. During embryonic development initiates neuronal differentiation by inducing cell cycle arrest at the G0/G1 phase through up-regulation of cell-cycle regulatory proteins (PubMed:28684796).
Plays a role not only in the fetal period during the development of the nervous system, but also in the adult brain, where it is involved in the maintenance of neural functions and protection of the nervous tissue cells from oxidative stress-induced damage. Exhibits GTPase and E3 ubiquitin-protein ligase activities. Regulates dendritic spine density and synaptic neurotransmission; its ability to hydrolyze GTP is involved in the maintenance of dendritic spine density (By similarity).
Plays a role not only in the fetal period during the development of the nervous system, but also in the adult brain, where it is involved in the maintenance of neural functions and protection of the nervous tissue cells from oxidative stress-induced damage. Exhibits GTPase and E3 ubiquitin-protein ligase activities. Regulates dendritic spine density and synaptic neurotransmission; its ability to hydrolyze GTP is involved in the maintenance of dendritic spine density (By similarity).
Catalytic activity
Pathway
Protein modification; protein ubiquitination.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell body | |
Cellular Component | cytoplasm | |
Cellular Component | endosome | |
Cellular Component | membrane | |
Cellular Component | neuron projection | |
Cellular Component | nuclear body | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | perikaryon | |
Cellular Component | postsynaptic density | |
Cellular Component | synaptic vesicle | |
Molecular Function | GTP binding | |
Molecular Function | GTPase activity | |
Molecular Function | ubiquitin protein ligase activity | |
Molecular Function | zinc ion binding | |
Biological Process | embryonic brain development | |
Biological Process | endoplasmic reticulum organization | |
Biological Process | G1 to G0 transition involved in cell differentiation | |
Biological Process | neuron differentiation | |
Biological Process | positive regulation of glial cell differentiation | |
Biological Process | positive regulation of neuron differentiation | |
Biological Process | protein autoubiquitination | |
Biological Process | protein homooligomerization | |
Biological Process | regulation of cell cycle | |
Biological Process | response to hydroperoxide |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRING finger protein 112
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9ULX5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Membrane ; Peripheral membrane protein
Note: Predominantly in the nucleus, but some amounts were also found in the cytoplasm. Oxidative stress stimulates its shuttling from the cytoplasm into the nucleus. Recruited to nuclear bodies via its interaction with ZBTB16. Localizes to the cell soma and neuritis and only slightly to the nucleus in the neurons of most brain areas.
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 547-567 | Helical | ||||
Sequence: LAAVGGAVGAGLMGLAGGVVG | ||||||
Transmembrane | 580-600 | Helical | ||||
Sequence: GMVAAGAAVGATGAAVVGGGV |
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 675 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000056301 | 1-631 | RING finger protein 112 | |||
Sequence: MPRPALSVTSFCHRLGKRERKQSFMGNSGNSWSHTPFPKLELGLGPQPMAPRELPTCSICLERLRDPISLDCGHDFCIRCFSTHRLPGCEPPCCPECRKICKQKRGLRSLGEKMKLLPQRPLPPALQETCPVRAEPLLLVRINASGGLILRMGAINRCLKHPLARDTPVCLLAVLGEQHSGKSFLLNHLLQGLPGLESGEGGRPRGGEASLQGCRWGANGLARGIWMWSHPFLLGKEGKKVAVFLVDTGDAMSPELSRETRIKLCALTTMLSSYQILSTSQELKDTDLDYLEMFVHVAEVMGKHYGMVPIQHLDLLVRDSSHPNKAGQGHVGNIFQRLSGRYPKVQELLQGKRARCCLLPAPGRRRMNQGHASPGDTDDDFRHLLGAYVSDVLSAAPQHAKSRCQGYWNEGRAVARGDRRLLTGQQLAQEIKNLSGWMGRTGPGFTSPDEMAAQLHDLRKVEAAKREFEEYVRQQDVATKRIFSALRVLPDTMRNLLSTQKDAILARHGVALLCKGRDQTLEALEAELQATAKAFMDSYTMRFCGHLAAVGGAVGAGLMGLAGGVVGAGMAAAALAAEAGMVAAGAAVGATGAAVVGGGVGAGLAATVGCMEKEEDERLLEGDREPLLQEE |
Post-translational modification
Auto-ubiquitinated.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Self-associates. Interacts with SP1 in an oxidative stress-regulated manner. Interacts with SIGMAR1 in an oxidative stress-regulated manner. Interacts with ZBTB16 (via C2H2-type zinc finger domains 1 and 2).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for zinc finger, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 57-98 | RING-type | ||||
Sequence: CSICLERLRDPISLDCGHDFCIRCFSTHRLPGCEPPCCPECR | ||||||
Region | 131-631 | Interaction with ZBTB16 | ||||
Sequence: PVRAEPLLLVRINASGGLILRMGAINRCLKHPLARDTPVCLLAVLGEQHSGKSFLLNHLLQGLPGLESGEGGRPRGGEASLQGCRWGANGLARGIWMWSHPFLLGKEGKKVAVFLVDTGDAMSPELSRETRIKLCALTTMLSSYQILSTSQELKDTDLDYLEMFVHVAEVMGKHYGMVPIQHLDLLVRDSSHPNKAGQGHVGNIFQRLSGRYPKVQELLQGKRARCCLLPAPGRRRMNQGHASPGDTDDDFRHLLGAYVSDVLSAAPQHAKSRCQGYWNEGRAVARGDRRLLTGQQLAQEIKNLSGWMGRTGPGFTSPDEMAAQLHDLRKVEAAKREFEEYVRQQDVATKRIFSALRVLPDTMRNLLSTQKDAILARHGVALLCKGRDQTLEALEAELQATAKAFMDSYTMRFCGHLAAVGGAVGAGLMGLAGGVVGAGMAAAALAAEAGMVAAGAAVGATGAAVVGGGVGAGLAATVGCMEKEEDERLLEGDREPLLQEE | ||||||
Domain | 166-397 | GB1/RHD3-type G | ||||
Sequence: DTPVCLLAVLGEQHSGKSFLLNHLLQGLPGLESGEGGRPRGGEASLQGCRWGANGLARGIWMWSHPFLLGKEGKKVAVFLVDTGDAMSPELSRETRIKLCALTTMLSSYQILSTSQELKDTDLDYLEMFVHVAEVMGKHYGMVPIQHLDLLVRDSSHPNKAGQGHVGNIFQRLSGRYPKVQELLQGKRARCCLLPAPGRRRMNQGHASPGDTDDDFRHLLGAYVSDVLSAAP |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9ULX5-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length631
- Mass (Da)68,298
- Last updated2012-02-22 v2
- Checksum770C4F33B1395954
Q9ULX5-2
- Name2
- Differences from canonical
- 374-374: P → PG
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
J3QRB8 | J3QRB8_HUMAN | RNF112 | 123 |
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_042377 | 374 | in isoform 2 | |||
Sequence: P → PG |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB026054 EMBL· GenBank· DDBJ | BAA84698.1 EMBL· GenBank· DDBJ | mRNA | ||
AC004448 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC053989 EMBL· GenBank· DDBJ | AAH53989.1 EMBL· GenBank· DDBJ | mRNA | ||
AF054587 EMBL· GenBank· DDBJ | AAC08584.1 EMBL· GenBank· DDBJ | Genomic DNA |