Q8K1J5 · SDE2_MOUSE
- ProteinSplicing regulator SDE2
- GeneSde2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids448 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Inhibits translesion DNA synthesis by preventing monoubiquitination of PCNA, this is necessary to counteract damage due to ultraviolet light-induced replication stress (By similarity).
SDE2 is cleaved following PCNA binding, and its complete degradation is necessary to allow S-phase progression following DNA damage (By similarity).
SDE2 is cleaved following PCNA binding, and its complete degradation is necessary to allow S-phase progression following DNA damage (By similarity).
Plays a role in pre-mRNA splicing by facilitating excision of relatively short introns featuring weak 3'-splice sites (ss) and high GC content (By similarity).
May recruit CACTIN to the spliceosome (By similarity).
May recruit CACTIN to the spliceosome (By similarity).
Plays a role in ribosome biogenesis by enabling SNORD3- and SNORD118-dependent cleavage of the 47S rRNA precursor (By similarity).
Binds ncRNA (non-coding RNA) including the snoRNAs SNORD3 and SNORD118 (By similarity).
Binds ncRNA (non-coding RNA) including the snoRNAs SNORD3 and SNORD118 (By similarity).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 77-78 | Cleavage | ||||
Sequence: GK |
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 | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | Golgi apparatus | |
Cellular Component | nuclear speck | |
Cellular Component | nucleus | |
Cellular Component | plasma membrane | |
Molecular Function | damaged DNA binding | |
Molecular Function | snoRNA binding | |
Biological Process | cell division | |
Biological Process | cellular response to UV | |
Biological Process | DNA replication | |
Biological Process | endonucleolytic cleavage of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) | |
Biological Process | mitotic G1 DNA damage checkpoint signaling | |
Biological Process | mRNA cis splicing, via spliceosome | |
Biological Process | protein processing | |
Biological Process | protein ubiquitination |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSplicing regulator SDE2
- 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 accessionQ8K1J5
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for propeptide, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Propeptide | PRO_0000442522 | 1-77 | UBL | |||
Sequence: MAEAAVVAWVRGPGTVWKALPCASVGCSVRDVIYRHCQEQEVPVECFFVTCNGVLVNAGDKVQHGAVYSLEPRLRGG | ||||||
Chain | PRO_0000286085 | 78-448 | Splicing regulator SDE2 | |||
Sequence: KGGFGSMLRALGAQIEKTTNREACRDLSGRRLRDVNHEKAMAEWVKQQAEREAEKEQRRLERLQRKLAEPAHCFTSPDYQRQCHEMAERLEDSVLKGMQAASSKMVSAEITETRKRPNKSKTDQETSAKKRKRKCFWLGMDGLEAAEGSSTGSSEDSSEDDSEDAPGTSEQSCCAREDGIDAVEVAADRPGSPRSSASGTHSESPEKLQCPVTEPGQGILENTGTEPGETSDKECNERKTVTDPEETPARKETESHEATEKDQKTGMSGGDRAAMVLSGEDRKSVPAANLEGNNSGDTALGLEAVDLSAFSSAAELESLGLERLKCELMVLGLKCGGTLQERAARLFSVRGLTKELIDPALFAKPSKGKKK | ||||||
Modified residue | 269 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 277 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 281 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 324 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 332 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Upon binding to PCNA, the N-terminal UBL (ubiquitin-like) propeptide is cleaved at Gly-77 by an unidentified deubiquitinating enzyme; the resulting mature SDE2 is degraded by the DCX(DTL) complex in a cell cycle- and DNA damage dependent manner.
Both SDE2-UBL and the mature SDE2 are polyubiquitinated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Interacts (via PIP-box) with PCNA; the interaction is direct and prevents ultraviolet light induced monoubiquitination of PCNA (By similarity).
Interacts with FBL/fibrillarin (By similarity).
Interacts with CACTIN (By similarity).
Interacts with SF3B1 (By similarity).
Interacts with U2AF1 (By similarity).
Interacts with FBL/fibrillarin (By similarity).
Interacts with CACTIN (By similarity).
Interacts with SF3B1 (By similarity).
Interacts with U2AF1 (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for motif, coiled coil, region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 39-52 | PIP-box | ||||
Sequence: EQEVPVECFFVTCN | ||||||
Coiled coil | 109-149 | |||||
Sequence: LRDVNHEKAMAEWVKQQAEREAEKEQRRLERLQRKLAEPAH | ||||||
Region | 175-252 | Disordered | ||||
Sequence: MQAASSKMVSAEITETRKRPNKSKTDQETSAKKRKRKCFWLGMDGLEAAEGSSTGSSEDSSEDDSEDAPGTSEQSCCA | ||||||
Compositional bias | 186-215 | Basic and acidic residues | ||||
Sequence: EITETRKRPNKSKTDQETSAKKRKRKCFWL | ||||||
Region | 264-372 | Disordered | ||||
Sequence: ADRPGSPRSSASGTHSESPEKLQCPVTEPGQGILENTGTEPGETSDKECNERKTVTDPEETPARKETESHEATEKDQKTGMSGGDRAAMVLSGEDRKSVPAANLEGNNS | ||||||
Compositional bias | 270-284 | Polar residues | ||||
Sequence: PRSSASGTHSESPEK | ||||||
Compositional bias | 304-344 | Basic and acidic residues | ||||
Sequence: PGETSDKECNERKTVTDPEETPARKETESHEATEKDQKTGM | ||||||
Domain | 393-427 | SAP | ||||
Sequence: LESLGLERLKCELMVLGLKCGGTLQERAARLFSVR |
Domain
The PIP-box (PCNA interacting peptide) motif mediates both the interaction with PCNA and cleavage of the SDE2 precursor by a deubiquitinating enzyme.
The SAP domain is necessary for specific binding to DNA.
The propeptide displays a ubiquitin-like fold.
Sequence similarities
Belongs to the SDE2 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length448
- Mass (Da)48,580
- Last updated2002-10-01 v1
- ChecksumB2A8DBDB795FFA36
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 186-215 | Basic and acidic residues | ||||
Sequence: EITETRKRPNKSKTDQETSAKKRKRKCFWL | ||||||
Compositional bias | 270-284 | Polar residues | ||||
Sequence: PRSSASGTHSESPEK | ||||||
Compositional bias | 304-344 | Basic and acidic residues | ||||
Sequence: PGETSDKECNERKTVTDPEETPARKETESHEATEKDQKTGM |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BC031781 EMBL· GenBank· DDBJ | AAH31781.1 EMBL· GenBank· DDBJ | mRNA | ||
AK078485 EMBL· GenBank· DDBJ | BAC37302.2 EMBL· GenBank· DDBJ | mRNA |