NSE2_XENLA
ID NSE2_XENLA Reviewed; 238 AA.
AC Q7ZXH2;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=MMS21 homolog;
DE AltName: Full=Non-structural maintenance of chromosomes element 2 homolog;
DE Short=Non-SMC element 2 homolog;
GN Name=nsmce2; Synonyms=mms21;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 SUMO-protein ligase component of the SMC5-SMC6 complex, a
CC complex involved in repair of DNA double-strand breaks 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. The
CC complex is required for telomere maintenance via recombination and
CC mediates sumoylation of shelterin complex (telosome) components.
CC Required for recruitment of telomeres to PML nuclear bodies. SUMO
CC protein-ligase activity is required for the prevention of DNA damage-
CC induced apoptosis by facilitating DNA repair. Required for sister
CC chromatid cohesion during prometaphase and mitotic progression (By
CC similarity). {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 and nsmce4a. {ECO:0000250|UniProtKB:Q96MF7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96MF7}.
CC Chromosome, telomere {ECO:0000250|UniProtKB:Q96MF7}.
CC -!- SIMILARITY: Belongs to the NSE2 family. {ECO:0000305}.
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DR EMBL; BC044994; AAH44994.1; -; mRNA.
DR RefSeq; NP_001079585.1; NM_001086116.1.
DR AlphaFoldDB; Q7ZXH2; -.
DR SMR; Q7ZXH2; -.
DR BioGRID; 97515; 1.
DR MaxQB; Q7ZXH2; -.
DR DNASU; 379272; -.
DR GeneID; 379272; -.
DR KEGG; xla:379272; -.
DR CTD; 379272; -.
DR Xenbase; XB-GENE-6256344; nsmce2.L.
DR OrthoDB; 1434342at2759; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 379272; Expressed in testis and 19 other tissues.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR GO; GO:0030915; C:Smc5-Smc6 complex; ISS:UniProtKB.
DR GO; GO:0019789; F:SUMO transferase activity; ISS:UniProtKB.
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: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; IPR004181; Znf_MIZ.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR21330; PTHR21330; 1.
DR Pfam; PF11789; zf-Nse; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Chromosome; DNA damage; DNA recombination;
KW DNA repair; Metal-binding; Mitosis; Nucleus; Reference proteome; Telomere;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..238
FT /note="E3 SUMO-protein ligase NSE2"
FT /id="PRO_0000270942"
FT ZN_FING 147..233
FT /note="SP-RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
SQ SEQUENCE 238 AA; 27226 MW; 90379FAC444DAE14 CRC64;
MSGRSAPVVS FSSVDNSLSS LKNCQGYLHT GMDITVSVAL DLLETGCEST EVDAMESVML
EYSAMERDLK QYIHAVEETV QKLRREQMEQ VPDLQSLVQE KYATIQKKND DEDLKKNDRF
VQFKDQLREM RKQMGEKEEG DAAFENVDED IAVLPSQQNL TCPITQMEMT NPVKNKVCGH
TYEKEAIERM IQDRHQKKKR VKCPKVGCVH SDMQISDLVP DTALKRTIDI LNKQKGRH
