O15541 · R113A_HUMAN
- ProteinE3 ubiquitin-protein ligase RNF113A
- GeneRNF113A
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids343 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Required for pre-mRNA splicing as component of the spliceosome (PubMed:29360106, PubMed:29361316).
As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). E3 ubiquitin-protein ligase that catalyzes the transfer of ubiquitin onto target proteins (PubMed:28978524, PubMed:29144457).
Catalyzes polyubiquitination of SNRNP200/BRR2 with non-canonical 'Lys-63'-linked polyubiquitin chains (PubMed:29144457).
Plays a role in DNA repair via its role in the synthesis of 'Lys-63'-linked polyubiquitin chains that recruit ALKBH3 and the ASCC complex to sites of DNA damage by alkylating agents (PubMed:29144457).
Ubiquitinates CXCR4, leading to its degradation, and thereby contributes to the termination of CXCR4 signaling (PubMed:28978524).
As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). E3 ubiquitin-protein ligase that catalyzes the transfer of ubiquitin onto target proteins (PubMed:28978524, PubMed:29144457).
Catalyzes polyubiquitination of SNRNP200/BRR2 with non-canonical 'Lys-63'-linked polyubiquitin chains (PubMed:29144457).
Plays a role in DNA repair via its role in the synthesis of 'Lys-63'-linked polyubiquitin chains that recruit ALKBH3 and the ASCC complex to sites of DNA damage by alkylating agents (PubMed:29144457).
Ubiquitinates CXCR4, leading to its degradation, and thereby contributes to the termination of CXCR4 signaling (PubMed:28978524).
Catalytic activity
Pathway
Protein modification; protein ubiquitination.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nuclear speck | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | U2-type precatalytic spliceosome | |
Cellular Component | U2-type spliceosomal complex | |
Molecular Function | metal ion binding | |
Molecular Function | ubiquitin protein ligase activity | |
Biological Process | DNA repair | |
Biological Process | mRNA splicing, via spliceosome | |
Biological Process | negative regulation of chemokine-mediated signaling pathway | |
Biological Process | protein ubiquitination | |
Biological Process | snoRNA splicing |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase RNF113A
- 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 accessionO15541
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalizes with ASCC2 in nuclear foci after DNA damage by alkylating agents. In the absence of DNA damage, colocalizes with the spliceosome components SNRNP200/BRR2 and PRPF8 in nuclear speckles.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Trichothiodystrophy 5, non-photosensitive (TTD5)
- Note
- DescriptionAn X-linked form of trichothiodystrophy, a disease characterized by sulfur-deficient brittle hair and multisystem variable abnormalities. The spectrum of clinical features varies from mild disease with only hair involvement to severe disease with cutaneous, neurologic and profound developmental defects. Ichthyosis, intellectual and developmental disabilities, decreased fertility, abnormal characteristics at birth, ocular abnormalities, short stature, and infections are common manifestations. There are both photosensitive and non-photosensitive forms of the disorder. TTD5 features include microcephaly, profound intellectual disability, sparse brittle hair, aged appearance, short stature, facial dysmorphism, seizures, an immunoglobulin deficiency, multiple endocrine abnormalities, cerebellar hypoplasia and partial absence of the corpus callosum, in the absence of cellular photosensitivity and ichthyosis.
- See alsoMIM:300953
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 2-60 | Strongly decreased interaction with SNRNP200/BRR2. | ||||
Sequence: Missing | ||||||
Mutagenesis | 50-61 | Strongly decreased interaction with CXCR4. Abolishes the ability to promote CXCR4 degradation. | ||||
Sequence: Missing | ||||||
Mutagenesis | 262 | Loss of E3 ubiquitin ligase activity. | ||||
Sequence: C → A | ||||||
Mutagenesis | 264 | Strongly reduced E3 ubiquitin ligase activity. | ||||
Sequence: I → A | ||||||
Mutagenesis | 277 | Loss of E3 ubiquitin ligase activity. | ||||
Sequence: C → A | ||||||
Mutagenesis | 301-343 | Cells are hypersensitive to DNA damage by alkylating agents. | ||||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 251 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 initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000056087 | 2-343 | UniProt | E3 ubiquitin-protein ligase RNF113A | |||
Sequence: AEQLSPGKAVDQVCTFLFKKPGRKGAAGRRKRPACDPEPGESGSSSDEGCTVVRPEKKRVTHNPMIQKTRDSGKQKAAYGDLSSEEEEENEPESLGVVYKSTRSAKPVGPEDMGATAVYELDTEKERDAQAIFERSQKIQEELRGKEDDKIYRGINNYQKYMKPKDTSMGNASSGMVRKGPIRAPEHLRATVRWDYQPDICKDYKETGFCGFGDSCKFLHDRSDYKHGWQIERELDEGRYGVYEDENYEVGSDDEEIPFKCFICRQSFQNPVVTKCRHYFCESCALQHFRTTPRCYVCDQQTNGVFNPAKELIAKLEKHRATGEGGASDLPEDPDEDAIPIT | |||||||
Modified residue | 6 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 6 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 47 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 80 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 84 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 84 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 85 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 85 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 169 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 249 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 253 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 253 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 268 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 323 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 329 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Component of pre-catalytic and catalytic spliceosome complexes (PubMed:22365833, PubMed:29360106, PubMed:29361316).
Interacts (via N-terminus) with the spliceosome subunit SNRNP200/BRR2 (PubMed:29144457).
Component of the minor spliceosome, which splices U12-type introns. Within this complex, interacts with SCNM1 and CRIPT (PubMed:33509932).
Interacts (via N-terminus) with the spliceosome subunit SNRNP200/BRR2 (PubMed:29144457).
Component of the minor spliceosome, which splices U12-type introns. Within this complex, interacts with SCNM1 and CRIPT (PubMed:33509932).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O15541 | IK Q13123 | 2 | EBI-2130294, EBI-713456 | |
BINARY | O15541 | SF3B2 Q13435 | 2 | EBI-2130294, EBI-749111 | |
BINARY | O15541 | SNRNP200 O75643 | 2 | EBI-2130294, EBI-1045395 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 2-60 | Important for interaction with SNRNP200/BRR2 | ||||
Sequence: AEQLSPGKAVDQVCTFLFKKPGRKGAAGRRKRPACDPEPGESGSSSDEGCTVVRPEKKR | ||||||
Region | 22-96 | Disordered | ||||
Sequence: PGRKGAAGRRKRPACDPEPGESGSSSDEGCTVVRPEKKRVTHNPMIQKTRDSGKQKAAYGDLSSEEEEENEPESL | ||||||
Region | 50-61 | Important for interaction with CXCR4 | ||||
Sequence: GCTVVRPEKKRV | ||||||
Compositional bias | 52-66 | Basic and acidic residues | ||||
Sequence: TVVRPEKKRVTHNPM | ||||||
Zinc finger | 196-224 | C3H1-type | ||||
Sequence: DYQPDICKDYKETGFCGFGDSCKFLHDRS | ||||||
Zinc finger | 262-300 | RING-type | ||||
Sequence: CFICRQSFQNPVVTKCRHYFCESCALQHFRTTPRCYVCD | ||||||
Region | 322-343 | Disordered | ||||
Sequence: ATGEGGASDLPEDPDEDAIPIT |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length343
- Mass (Da)38,787
- Last updated1998-01-01 v1
- ChecksumF76E28037A6FF78B
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 21 | in Ref. 2; BAG37314 | ||||
Sequence: K → R | ||||||
Compositional bias | 52-66 | Basic and acidic residues | ||||
Sequence: TVVRPEKKRVTHNPM |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X98253 EMBL· GenBank· DDBJ | CAA66907.1 EMBL· GenBank· DDBJ | mRNA | ||
AK314778 EMBL· GenBank· DDBJ | BAG37314.1 EMBL· GenBank· DDBJ | mRNA | ||
BT007175 EMBL· GenBank· DDBJ | AAP35839.1 EMBL· GenBank· DDBJ | mRNA | ||
AC002477 EMBL· GenBank· DDBJ | AAB67605.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC000832 EMBL· GenBank· DDBJ | AAH00832.1 EMBL· GenBank· DDBJ | mRNA | ||
BC020556 EMBL· GenBank· DDBJ | AAH20556.1 EMBL· GenBank· DDBJ | mRNA |