Q8K1J5 · SDE2_MOUSE

  • Protein
    Splicing regulator SDE2
  • Gene
    Sde2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).
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).
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).

Features

Showing features for site.

144850100150200250300350400
TypeIDPosition(s)Description
Site77-78Cleavage

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 Componentcytoplasm
Cellular Componentcytosol
Cellular ComponentGolgi apparatus
Cellular Componentnuclear speck
Cellular Componentnucleus
Cellular Componentplasma membrane
Molecular Functiondamaged DNA binding
Molecular FunctionsnoRNA binding
Biological Processcell division
Biological Processcellular response to UV
Biological ProcessDNA replication
Biological Processendonucleolytic cleavage of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
Biological Processmitotic G1 DNA damage checkpoint signaling
Biological ProcessmRNA cis splicing, via spliceosome
Biological Processprotein processing
Biological Processprotein ubiquitination

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Splicing regulator SDE2
  • Alternative names
    • Replication stress response regulator SDE2

Gene names

    • Name
      Sde2

Organism names

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

Accessions

  • Primary accession
    Q8K1J5
  • Secondary accessions
    • Q8BJX1

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for propeptide, chain, modified residue.

TypeIDPosition(s)Description
PropeptidePRO_00004425221-77UBL
ChainPRO_000028608578-448Splicing regulator SDE2
Modified residue269Phosphoserine
Modified residue277Phosphothreonine
Modified residue281Phosphoserine
Modified residue324Phosphothreonine
Modified residue332Phosphoserine

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

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).

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for motif, coiled coil, region, compositional bias, domain.

TypeIDPosition(s)Description
Motif39-52PIP-box
Coiled coil109-149
Region175-252Disordered
Compositional bias186-215Basic and acidic residues
Region264-372Disordered
Compositional bias270-284Polar residues
Compositional bias304-344Basic and acidic residues
Domain393-427SAP

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    448
  • Mass (Da)
    48,580
  • Last updated
    2002-10-01 v1
  • Checksum
    B2A8DBDB795FFA36
MAEAAVVAWVRGPGTVWKALPCASVGCSVRDVIYRHCQEQEVPVECFFVTCNGVLVNAGDKVQHGAVYSLEPRLRGGKGGFGSMLRALGAQIEKTTNREACRDLSGRRLRDVNHEKAMAEWVKQQAEREAEKEQRRLERLQRKLAEPAHCFTSPDYQRQCHEMAERLEDSVLKGMQAASSKMVSAEITETRKRPNKSKTDQETSAKKRKRKCFWLGMDGLEAAEGSSTGSSEDSSEDDSEDAPGTSEQSCCAREDGIDAVEVAADRPGSPRSSASGTHSESPEKLQCPVTEPGQGILENTGTEPGETSDKECNERKTVTDPEETPARKETESHEATEKDQKTGMSGGDRAAMVLSGEDRKSVPAANLEGNNSGDTALGLEAVDLSAFSSAAELESLGLERLKCELMVLGLKCGGTLQERAARLFSVRGLTKELIDPALFAKPSKGKKK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias186-215Basic and acidic residues
Compositional bias270-284Polar residues
Compositional bias304-344Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BC031781
EMBL· GenBank· DDBJ
AAH31781.1
EMBL· GenBank· DDBJ
mRNA
AK078485
EMBL· GenBank· DDBJ
BAC37302.2
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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