Q91VT1 · NSE2_MOUSE

  • Protein
    E3 SUMO-protein ligase NSE2
  • Gene
    Nsmce2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    5/5

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.

124720406080100120140160180200220240
TypeIDPosition(s)Description
Binding site185Zn2+ (UniProtKB | ChEBI)
Binding site187Zn2+ (UniProtKB | ChEBI)
Binding site210Zn2+ (UniProtKB | ChEBI)
Binding site215Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentchromosome, telomeric region
Cellular ComponentPML body
Cellular ComponentSmc5-Smc6 complex
Molecular FunctionSUMO transferase activity
Molecular Functionubiquitin-protein transferase activity
Molecular Functionzinc ion binding
Biological Processcell division
Biological Processcellular senescence
Biological Processdouble-strand break repair via homologous recombination
Biological Processpositive regulation of maintenance of mitotic sister chromatid cohesion
Biological Processpositive regulation of mitotic metaphase/anaphase transition
Biological Processprotein sumoylation
Biological Processprotein ubiquitination
Biological Processtelomere maintenance via recombination

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    E3 SUMO-protein ligase NSE2
  • EC number
  • Alternative names
    • E3 SUMO-protein transferase NSE2
    • MMS21 homolog
    • Non-structural maintenance of chromosomes element 2 homolog (Non-SMC element 2 homolog)

Gene names

    • Name
      Nsmce2
    • Synonyms
      Mms21

Organism names

  • Taxonomic identifier
  • Strains
    • 129
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q91VT1
  • Secondary accessions
    • Q8BQ88
    • Q9D1D3

Proteomes

Organism-specific databases

Subcellular Location

Nucleus
Chromosome, telomere
Nucleus, PML body
Note: Localizes to PML nuclear bodies in ALT cell lines.

Keywords

PTM/Processing

Features

Showing features for modified residue, chain, modified residue (large scale data), cross-link.

Type
IDPosition(s)Source
Description
Modified residue1UniProtN-acetylmethionine
ChainPRO_00002709401-247UniProtE3 SUMO-protein ligase NSE2
Modified residue (large scale data)16PTMeXchangePhosphoserine
Cross-link90UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link107UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue116UniProtPhosphoserine
Modified residue (large scale data)116PTMeXchangePhosphoserine
Cross-link125UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link130UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)223PTMeXchangePhosphoserine

Post-translational modification

Sumoylated, possibly via autosumoylation.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Component of the SMC5-SMC6 complex which consists at least of SMC5, SMC6, NSMCE2, NSMCE1, NSMCE4A or EID3 and NSMCE3.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for zinc finger.

TypeIDPosition(s)Description
Zinc finger154-240SP-RING-type

Sequence similarities

Belongs to the NSE2 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

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.

  • Length
    247
  • Mass (Da)
    28,231
  • Last updated
    2001-12-01 v1
  • MD5 Checksum
    07561A5CE630C198F6D62DE708865DCA
MPGRSSTSSGSTRYISFSGIESALSSLKNFQSCISSGMDTVSSVALDLVETQTEVSSEYSMDKAMVEFAKMDRELSHYVKAVQSTINHVKEERPEKVPDLKLLVEKKFLALQDKNSDADFKENEKFVQFKQQLRELKKQYGIHADRENDLTEGVDEDMIVTQSQTNFICPITQLEMKKPVKNKMCGHTYEEEAIVRMIESKHKRKKKACCPKIGCSHTDMRMSDLIPDEALRRAIESHNKKKKRHSE

Q91VT1-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A2I3BS18A0A2I3BS18_MOUSENsmce2273

Features

Showing features for sequence conflict, alternative sequence.

Type
IDPosition(s)Description
Sequence conflict47in Ref. 1; BAB22938
Alternative sequenceVSP_022250140-247in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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