NSE2_BOVIN
ID NSE2_BOVIN Reviewed; 248 AA.
AC Q32KY9;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=E3 SUMO-protein ligase NSE2;
DE EC=2.3.2.- {ECO:0000250|UniProtKB:Q96MF7};
DE AltName: Full=E3 SUMO-protein transferase NSE2 {ECO:0000305};
DE AltName: Full=Non-structural maintenance of chromosomes element 2 homolog;
DE Short=Non-SMC element 2 homolog;
GN Name=NSMCE2; Synonyms=MMS21;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 SUMO-protein ligase component of the SMC5-SMC6 complex, a
CC complex involved in DNA double-strand break repair by homologous
CC recombination. Is not be required for the stability of the complex. The
CC complex may promote sister chromatid homologous recombination by
CC recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. Acts
CC as an E3 ligase mediating SUMO attachment to various proteins such as
CC SMC6L1 and TSNAX, the shelterin complex subunits TERF1, TERF2, TINF2
CC and TERF2IP, RAD51AP1, and maybe the cohesin components RAD21 and
CC STAG2. Required for recruitment of telomeres to PML nuclear bodies.
CC Required for sister chromatid cohesion during prometaphase and mitotic
CC progression. {ECO:0000250|UniProtKB:Q96MF7}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000250|UniProtKB:Q96MF7}.
CC -!- SUBUNIT: Component of the SMC5-SMC6 complex which consists at least of
CC SMC5, SMC6, NSMCE2, NSMCE1, NSMCE4A or EID3 and NSMCE3.
CC {ECO:0000250|UniProtKB:Q96MF7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96MF7}.
CC Chromosome, telomere {ECO:0000250|UniProtKB:Q96MF7}. Nucleus, PML body
CC {ECO:0000250|UniProtKB:Q96MF7}. Note=Localizes to PML nuclear bodies in
CC ALT cell lines. {ECO:0000250|UniProtKB:Q96MF7}.
CC -!- PTM: Sumoylated, possibly via autosumoylation.
CC {ECO:0000250|UniProtKB:Q96MF7}.
CC -!- SIMILARITY: Belongs to the NSE2 family. {ECO:0000305}.
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DR EMBL; BC109850; AAI09851.1; -; mRNA.
DR RefSeq; NP_001069265.1; NM_001075797.2.
DR AlphaFoldDB; Q32KY9; -.
DR SMR; Q32KY9; -.
DR PaxDb; Q32KY9; -.
DR PRIDE; Q32KY9; -.
DR GeneID; 519974; -.
DR KEGG; bta:519974; -.
DR CTD; 286053; -.
DR eggNOG; KOG2979; Eukaryota.
DR InParanoid; Q32KY9; -.
DR OrthoDB; 1434342at2759; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR GO; GO:0030915; C:Smc5-Smc6 complex; ISS:UniProtKB.
DR GO; GO:0061665; F:SUMO ligase activity; IBA:GO_Central.
DR GO; GO:0019789; F:SUMO transferase activity; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0090398; P:cellular senescence; ISS:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0034184; P:positive regulation of maintenance of mitotic sister chromatid cohesion; ISS:UniProtKB.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; ISS:UniProtKB.
DR GO; GO:0016925; P:protein sumoylation; IBA:GO_Central.
DR GO; GO:0000722; P:telomere maintenance via recombination; ISS:UniProtKB.
DR CDD; cd16651; SPL-RING_NSE2; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR026846; Nse2(Mms21).
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR21330; PTHR21330; 1.
DR Pfam; PF11789; zf-Nse; 1.
DR SMART; SM00504; Ubox; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell cycle; Cell division; Chromosome; DNA damage;
KW DNA recombination; DNA repair; Isopeptide bond; Metal-binding; Mitosis;
KW Nucleus; Phosphoprotein; Reference proteome; Telomere; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..248
FT /note="E3 SUMO-protein ligase NSE2"
FT /id="PRO_0000270938"
FT ZN_FING 156..242
FT /note="SP-RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96MF7"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96MF7"
FT CROSSLNK 92
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96MF7"
FT CROSSLNK 109
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96MF7"
FT CROSSLNK 127
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96MF7"
FT CROSSLNK 132
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96MF7"
SQ SEQUENCE 248 AA; 28119 MW; 2BBD36D3E81E9A29 CRC64;
MPGRSTSSSS SGSTGFISFS GVESALSSLK TFQSCISSGM DTASSVALDL VETQTEVSSE
YSMDKAMVEF AMMDRELNHY LKAVQSTINH VKEERSEKIP DLKLLVEKKF LALQNKNSDA
DFQNNEKFVQ FKQQLKELKK QYGLQSDREA DITEGVDEDM IVTQSQTNFI CPITQLEMKK
PVKNKVCGHT YEEEAIVRMI ESKHERKKKA CCPKIGCSHV DMRMSDLIQD EALRRAIESH
KKRRRQSN
