NSE2_MOUSE
ID NSE2_MOUSE Reviewed; 247 AA.
AC Q91VT1; Q8BQ88; Q9D1D3;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=129; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91VT1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91VT1-2; Sequence=VSP_022250;
CC -!- PTM: Sumoylated, possibly via autosumoylation.
CC {ECO:0000250|UniProtKB:Q96MF7}.
CC -!- SIMILARITY: Belongs to the NSE2 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK003685; BAB22938.1; -; mRNA.
DR EMBL; AK051277; BAC34589.1; -; mRNA.
DR EMBL; BC009125; AAH09125.1; -; mRNA.
DR CCDS; CCDS27498.1; -. [Q91VT1-1]
DR CCDS; CCDS49611.1; -. [Q91VT1-2]
DR RefSeq; NP_001158076.1; NM_001164604.1. [Q91VT1-2]
DR RefSeq; NP_081022.2; NM_026746.3. [Q91VT1-1]
DR AlphaFoldDB; Q91VT1; -.
DR SMR; Q91VT1; -.
DR BioGRID; 212891; 4.
DR IntAct; Q91VT1; 1.
DR STRING; 10090.ENSMUSP00000078641; -.
DR iPTMnet; Q91VT1; -.
DR PhosphoSitePlus; Q91VT1; -.
DR EPD; Q91VT1; -.
DR MaxQB; Q91VT1; -.
DR PaxDb; Q91VT1; -.
DR PeptideAtlas; Q91VT1; -.
DR PRIDE; Q91VT1; -.
DR ProteomicsDB; 295527; -. [Q91VT1-1]
DR ProteomicsDB; 295528; -. [Q91VT1-2]
DR Antibodypedia; 27202; 317 antibodies from 34 providers.
DR DNASU; 68501; -.
DR Ensembl; ENSMUST00000079703; ENSMUSP00000078641; ENSMUSG00000059586. [Q91VT1-1]
DR Ensembl; ENSMUST00000168722; ENSMUSP00000128893; ENSMUSG00000059586. [Q91VT1-2]
DR GeneID; 68501; -.
DR KEGG; mmu:68501; -.
DR UCSC; uc007vxu.2; mouse. [Q91VT1-1]
DR CTD; 286053; -.
DR MGI; MGI:1915751; Nsmce2.
DR VEuPathDB; HostDB:ENSMUSG00000059586; -.
DR eggNOG; KOG2979; Eukaryota.
DR GeneTree; ENSGT00390000013961; -.
DR HOGENOM; CLU_106543_0_0_1; -.
DR InParanoid; Q91VT1; -.
DR OMA; HTHQKVM; -.
DR PhylomeDB; Q91VT1; -.
DR TreeFam; TF324383; -.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR UniPathway; UPA00886; -.
DR BioGRID-ORCS; 68501; 20 hits in 108 CRISPR screens.
DR ChiTaRS; Nsmce2; mouse.
DR PRO; PR:Q91VT1; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q91VT1; protein.
DR Bgee; ENSMUSG00000059586; Expressed in animal zygote and 220 other tissues.
DR ExpressionAtlas; Q91VT1; baseline and differential.
DR Genevisible; Q91VT1; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; Alternative splicing; Cell cycle; Cell division; Chromosome;
KW DNA damage; DNA recombination; DNA repair; Isopeptide bond; Metal-binding;
KW Mitosis; Nucleus; Phosphoprotein; Reference proteome; Telomere;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..247
FT /note="E3 SUMO-protein ligase NSE2"
FT /id="PRO_0000270940"
FT ZN_FING 154..240
FT /note="SP-RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 215
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 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96MF7"
FT CROSSLNK 90
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96MF7"
FT CROSSLNK 107
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96MF7"
FT CROSSLNK 125
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96MF7"
FT CROSSLNK 130
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96MF7"
FT VAR_SEQ 140..247
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022250"
FT CONFLICT 47
FT /note="D -> G (in Ref. 1; BAB22938)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 247 AA; 28231 MW; 605E11F7F8785980 CRC64;
MPGRSSTSSG STRYISFSGI ESALSSLKNF QSCISSGMDT VSSVALDLVE TQTEVSSEYS
MDKAMVEFAK MDRELSHYVK AVQSTINHVK EERPEKVPDL KLLVEKKFLA LQDKNSDADF
KENEKFVQFK QQLRELKKQY GIHADRENDL TEGVDEDMIV TQSQTNFICP ITQLEMKKPV
KNKMCGHTYE EEAIVRMIES KHKRKKKACC PKIGCSHTDM RMSDLIPDEA LRRAIESHNK
KKKRHSE
