Q91VT1 · NSE2_MOUSE
- ProteinE3 SUMO-protein ligase NSE2
- GeneNsmce2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids247 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
E3 SUMO-protein ligase component of the SMC5-SMC6 complex, a complex involved in DNA double-strand break repair by homologous recombination. Is not be required for the stability of the complex. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. Acts as an E3 ligase mediating SUMO attachment to various proteins such as SMC6L1 and TSNAX, the shelterin complex subunits TERF1, TERF2, TINF2 and TERF2IP, RAD51AP1, and maybe the cohesin components RAD21 and STAG2. Required for recruitment of telomeres to PML nuclear bodies. Required for sister chromatid cohesion during prometaphase and mitotic progression.
Pathway
Protein modification; protein sumoylation.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 185 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 187 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 210 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 215 | Zn2+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chromosome, telomeric region | |
Cellular Component | PML body | |
Cellular Component | Smc5-Smc6 complex | |
Molecular Function | SUMO transferase activity | |
Molecular Function | ubiquitin-protein transferase activity | |
Molecular Function | zinc ion binding | |
Biological Process | cell division | |
Biological Process | cellular senescence | |
Biological Process | double-strand break repair via homologous recombination | |
Biological Process | positive regulation of maintenance of mitotic sister chromatid cohesion | |
Biological Process | positive regulation of mitotic metaphase/anaphase transition | |
Biological Process | protein sumoylation | |
Biological Process | protein ubiquitination | |
Biological Process | telomere maintenance via recombination |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 SUMO-protein ligase NSE2
- 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 accessionQ91VT1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes to PML nuclear bodies in ALT cell lines.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for modified residue, chain, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | ||
---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | |||
Chain | PRO_0000270940 | 1-247 | UniProt | E3 SUMO-protein ligase NSE2 | ||
Modified residue (large scale data) | 16 | PTMeXchange | Phosphoserine | |||
Cross-link | 90 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | |||
Cross-link | 107 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | |||
Modified residue | 116 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 116 | PTMeXchange | Phosphoserine | |||
Cross-link | 125 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | |||
Cross-link | 130 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | |||
Modified residue (large scale data) | 223 | PTMeXchange | Phosphoserine | |||
Post-translational modification
Sumoylated, possibly via autosumoylation.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for zinc finger.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Zinc finger | 154-240 | SP-RING-type | |||
Sequence similarities
Belongs to the NSE2 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q91VT1-1
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
- Length247
- Mass (Da)28,231
- Last updated2001-12-01 v1
- MD5 Checksum07561A5CE630C198F6D62DE708865DCA
Q91VT1-2
- Name2
- Differences from canonical
- 140-247: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2I3BS18 | A0A2I3BS18_MOUSE | Nsmce2 | 273 |
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Sequence conflict | 47 | in Ref. 1; BAB22938 | |||
Alternative sequence | VSP_022250 | 140-247 | in isoform 2 | ||
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK003685 EMBL· GenBank· DDBJ | BAB22938.1 EMBL· GenBank· DDBJ | mRNA | ||
AK051277 EMBL· GenBank· DDBJ | BAC34589.1 EMBL· GenBank· DDBJ | mRNA | ||
BC009125 EMBL· GenBank· DDBJ | AAH09125.1 EMBL· GenBank· DDBJ | mRNA |