NSE2_HUMAN
ID NSE2_HUMAN Reviewed; 247 AA.
AC Q96MF7; Q8N549;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=E3 SUMO-protein ligase NSE2;
DE EC=2.3.2.- {ECO:0000269|PubMed:17589526, ECO:0000269|PubMed:31400850};
DE AltName: Full=E3 SUMO-protein transferase NSE2 {ECO:0000305};
DE AltName: Full=MMS21 homolog;
DE Short=hMMS21;
DE AltName: Full=Non-structural maintenance of chromosomes element 2 homolog;
DE Short=Non-SMC element 2 homolog;
GN Name=NSMCE2; Synonyms=C8orf36, MMS21;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
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).
RN [3]
RP FUNCTION, SUMOYLATION, INTERACTION WITH SMC5 AND SMC6, AND MUTAGENESIS OF
RP CYS-169; CYS-185; HIS-187; CYS-210 AND CYS-215.
RX PubMed=16055714; DOI=10.1128/mcb.25.16.7021-7032.2005;
RA Potts P.R., Yu H.;
RT "Human MMS21/NSE2 is a SUMO ligase required for DNA repair.";
RL Mol. Cell. Biol. 25:7021-7032(2005).
RN [4]
RP FUNCTION.
RX PubMed=16810316; DOI=10.1038/sj.emboj.7601218;
RA Potts P.R., Porteus M.H., Yu H.;
RT "Human SMC5/6 complex promotes sister chromatid homologous recombination by
RT recruiting the SMC1/3 cohesin complex to double-strand breaks.";
RL EMBO J. 25:3377-3388(2006).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17589526; DOI=10.1038/nsmb1259;
RA Potts P.R., Yu H.;
RT "The SMC5/6 complex maintains telomere length in ALT cancer cells through
RT SUMOylation of telomere-binding proteins.";
RL Nat. Struct. Mol. Biol. 14:581-590(2007).
RN [6]
RP SUBCELLULAR LOCATION, INTERACTION WITH NSMCE1, IDENTIFICATION IN THE
RP SMC5-SMC6 COMPLEX, AND SUMOYLATION.
RX PubMed=18086888; DOI=10.1128/mcb.00767-07;
RA Taylor E.M., Copsey A.C., Hudson J.J., Vidot S., Lehmann A.R.;
RT "Identification of the proteins, including MAGEG1, that make up the human
RT SMC5-6 protein complex.";
RL Mol. Cell. Biol. 28:1197-1206(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP FUNCTION.
RX PubMed=19502785; DOI=10.4161/cc.8.14.8979;
RA Behlke-Steinert S., Touat-Todeschini L., Skoufias D.A., Margolis R.L.;
RT "SMC5 and MMS21 are required for chromosome cohesion and mitotic
RT progression.";
RL Cell Cycle 8:2211-2218(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP INVOLVEMENT IN SCKL10.
RX PubMed=25105364; DOI=10.1172/jci73264;
RA Payne F., Colnaghi R., Rocha N., Seth A., Harris J., Carpenter G.,
RA Bottomley W.E., Wheeler E., Wong S., Saudek V., Savage D., O'Rahilly S.,
RA Carel J.C., Barroso I., O'Driscoll M., Semple R.;
RT "Hypomorphism in human NSMCE2 linked to primordial dwarfism and insulin
RT resistance.";
RL J. Clin. Invest. 124:4028-4038(2014).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-90; LYS-107; LYS-125 AND LYS-130,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [15]
RP FUNCTION.
RX PubMed=31400850; DOI=10.1016/j.molcel.2019.06.043;
RA Barroso-Gonzalez J., Garcia-Exposito L., Hoang S.M., Lynskey M.L.,
RA Roncaioli J.L., Ghosh A., Wallace C.T., de Vitis M., Modesti M.,
RA Bernstein K.A., Sarkar S.N., Watkins S.C., O'Sullivan R.J.;
RT "RAD51AP1 is an essential mediator of alternative lengthening of
RT telomeres.";
RL Mol. Cell 76:11-26(2019).
RN [16]
RP ERRATUM OF PUBMED:31400850.
RX PubMed=31585101; DOI=10.1016/j.molcel.2019.08.009;
RA Barroso-Gonzalez J., Garcia-Exposito L., Hoang S.M., Lynskey M.L.,
RA Roncaioli J.L., Ghosh A., Wallace C.T., Modesti M., Bernstein K.A.,
RA Sarkar S.N., Watkins S.C., O'Sullivan R.J.;
RT "RAD51AP1 is an essential mediator of alternative lengthening of
RT telomeres.";
RL Mol. Cell 76:217-217(2019).
RN [17]
RP STRUCTURE BY NMR OF 168-247.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SP-RING domain in non-SMC element 2 homolog
RT (MMS21, S. cerevisiae).";
RL Submitted (OCT-2007) to the PDB data bank.
RN [18]
RP VARIANT [LARGE SCALE ANALYSIS] PHE-27.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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 (PubMed:16055714, PubMed:16810316). Is not be required
CC for the stability of the complex (PubMed:16055714, PubMed:16810316).
CC The complex may promote sister chromatid homologous recombination by
CC recruiting the SMC1-SMC3 cohesin complex to double-strand breaks
CC (PubMed:16055714, PubMed:16810316). The complex is required for
CC telomere maintenance via recombination in ALT (alternative lengthening
CC of telomeres) cell lines and mediates sumoylation of shelterin complex
CC (telosome) components which is proposed to lead to shelterin complex
CC disassembly in ALT-associated PML bodies (APBs) (PubMed:17589526). 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 STAG2
CC (PubMed:16055714, PubMed:16810316, PubMed:17589526, PubMed:31400850).
CC Required for recruitment of telomeres to PML nuclear bodies
CC (PubMed:17589526). SUMO protein-ligase activity is required for the
CC prevention of DNA damage-induced apoptosis by facilitating DNA repair,
CC and for formation of APBs in ALT cell lines (PubMed:17589526). Required
CC for sister chromatid cohesion during prometaphase and mitotic
CC progression (PubMed:19502785). {ECO:0000269|PubMed:16055714,
CC ECO:0000269|PubMed:16810316, ECO:0000269|PubMed:17589526,
CC ECO:0000269|PubMed:19502785, ECO:0000269|PubMed:31400850}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000269|PubMed:16055714, ECO:0000269|PubMed:16810316,
CC ECO:0000269|PubMed:17589526, ECO:0000269|PubMed:31400850}.
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:0000269|PubMed:18086888}.
CC -!- INTERACTION:
CC Q96MF7; G5E9A7: DMWD; NbExp=3; IntAct=EBI-2557388, EBI-10976677;
CC Q96MF7; P26378-2: ELAVL4; NbExp=3; IntAct=EBI-2557388, EBI-21603100;
CC Q96MF7; P22607: FGFR3; NbExp=3; IntAct=EBI-2557388, EBI-348399;
CC Q96MF7; P06396: GSN; NbExp=3; IntAct=EBI-2557388, EBI-351506;
CC Q96MF7; O60333-2: KIF1B; NbExp=3; IntAct=EBI-2557388, EBI-10975473;
CC Q96MF7; Q96SB8: SMC6; NbExp=3; IntAct=EBI-2557388, EBI-605415;
CC Q96MF7; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2557388, EBI-5235340;
CC Q96MF7; P40222: TXLNA; NbExp=6; IntAct=EBI-2557388, EBI-359793;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18086888}.
CC Chromosome, telomere {ECO:0000269|PubMed:17589526}. Nucleus, PML body
CC {ECO:0000269|PubMed:17589526}. Note=Localizes to PML nuclear bodies in
CC ALT cell lines. {ECO:0000269|PubMed:17589526}.
CC -!- PTM: Sumoylated, possibly via autosumoylation.
CC {ECO:0000269|PubMed:16055714, ECO:0000269|PubMed:18086888}.
CC -!- DISEASE: Seckel syndrome 10 (SCKL10) [MIM:617253]: A form of Seckel
CC syndrome, a rare autosomal recessive disorder characterized by
CC proportionate dwarfism of prenatal onset associated with low birth
CC weight, growth retardation, severe microcephaly with a bird-headed like
CC appearance, and intellectual disability. {ECO:0000269|PubMed:25105364}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the NSE2 family. {ECO:0000305}.
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DR EMBL; AK057002; BAB71338.1; -; mRNA.
DR EMBL; BC032797; AAH32797.1; -; mRNA.
DR CCDS; CCDS6356.1; -.
DR RefSeq; NP_775956.1; NM_173685.2.
DR RefSeq; XP_005250932.1; XM_005250875.2.
DR RefSeq; XP_005250933.1; XM_005250876.4.
DR RefSeq; XP_011515276.1; XM_011516974.2.
DR RefSeq; XP_011515277.1; XM_011516975.1.
DR RefSeq; XP_016868820.1; XM_017013331.1.
DR PDB; 2YU4; NMR; -; A=167-247.
DR PDBsum; 2YU4; -.
DR AlphaFoldDB; Q96MF7; -.
DR SMR; Q96MF7; -.
DR BioGRID; 130282; 38.
DR ComplexPortal; CPX-5992; SMC5-SMC6 SUMO ligase complex, EID3 variant.
DR ComplexPortal; CPX-6086; SMC5-SMC6 SUMO ligase complex, NSE4EA variant.
DR IntAct; Q96MF7; 26.
DR MINT; Q96MF7; -.
DR STRING; 9606.ENSP00000287437; -.
DR iPTMnet; Q96MF7; -.
DR PhosphoSitePlus; Q96MF7; -.
DR BioMuta; NSMCE2; -.
DR DMDM; 122064623; -.
DR EPD; Q96MF7; -.
DR jPOST; Q96MF7; -.
DR MassIVE; Q96MF7; -.
DR MaxQB; Q96MF7; -.
DR PaxDb; Q96MF7; -.
DR PeptideAtlas; Q96MF7; -.
DR PRIDE; Q96MF7; -.
DR ProteomicsDB; 77350; -.
DR Antibodypedia; 27202; 317 antibodies from 34 providers.
DR DNASU; 286053; -.
DR Ensembl; ENST00000287437.8; ENSP00000287437.3; ENSG00000156831.8.
DR Ensembl; ENST00000522563.5; ENSP00000430668.1; ENSG00000156831.8.
DR GeneID; 286053; -.
DR KEGG; hsa:286053; -.
DR MANE-Select; ENST00000287437.8; ENSP00000287437.3; NM_173685.4; NP_775956.1.
DR UCSC; uc003yrw.3; human.
DR CTD; 286053; -.
DR DisGeNET; 286053; -.
DR GeneCards; NSMCE2; -.
DR HGNC; HGNC:26513; NSMCE2.
DR HPA; ENSG00000156831; Low tissue specificity.
DR MalaCards; NSMCE2; -.
DR MIM; 617246; gene.
DR MIM; 617253; phenotype.
DR neXtProt; NX_Q96MF7; -.
DR OpenTargets; ENSG00000156831; -.
DR Orphanet; 436182; Microcephalic primordial dwarfism-insulin resistance syndrome.
DR PharmGKB; PA142672355; -.
DR VEuPathDB; HostDB:ENSG00000156831; -.
DR eggNOG; KOG2979; Eukaryota.
DR GeneTree; ENSGT00390000013961; -.
DR HOGENOM; CLU_106543_0_0_1; -.
DR InParanoid; Q96MF7; -.
DR OMA; HTHQKVM; -.
DR OrthoDB; 1434342at2759; -.
DR PhylomeDB; Q96MF7; -.
DR TreeFam; TF324383; -.
DR PathwayCommons; Q96MF7; -.
DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR SignaLink; Q96MF7; -.
DR SIGNOR; Q96MF7; -.
DR UniPathway; UPA00886; -.
DR BioGRID-ORCS; 286053; 415 hits in 1076 CRISPR screens.
DR ChiTaRS; NSMCE2; human.
DR EvolutionaryTrace; Q96MF7; -.
DR GenomeRNAi; 286053; -.
DR Pharos; Q96MF7; Tbio.
DR PRO; PR:Q96MF7; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q96MF7; protein.
DR Bgee; ENSG00000156831; Expressed in colonic epithelium and 184 other tissues.
DR ExpressionAtlas; Q96MF7; baseline and differential.
DR Genevisible; Q96MF7; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IDA:UniProtKB.
DR GO; GO:0061665; F:SUMO ligase activity; IBA:GO_Central.
DR GO; GO:0019789; F:SUMO transferase activity; IDA: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; IMP:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0034184; P:positive regulation of maintenance of mitotic sister chromatid cohesion; IMP:UniProtKB.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IMP:UniProtKB.
DR GO; GO:0016925; P:protein sumoylation; IBA:GO_Central.
DR GO; GO:0032204; P:regulation of telomere maintenance; IC:ComplexPortal.
DR GO; GO:0000722; P:telomere maintenance via recombination; IMP: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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Cell division; Chromosome;
KW DNA damage; DNA recombination; DNA repair; Dwarfism;
KW Intellectual disability; Isopeptide bond; Metal-binding; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome; Telomere; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..247
FT /note="E3 SUMO-protein ligase NSE2"
FT /id="PRO_0000270939"
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:0007744|PubMed:20068231"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 90
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 107
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 125
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 130
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 27
FT /note="L -> F (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036327"
FT VARIANT 66
FT /note="V -> A (in dbSNP:rs11542104)"
FT /id="VAR_050537"
FT MUTAGEN 169
FT /note="C->A: Induces a strong decrease in SUMO ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:16055714"
FT MUTAGEN 185
FT /note="C->A: Induces a strong decrease in SUMO ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:16055714"
FT MUTAGEN 187
FT /note="H->A: Induces a strong decrease in SUMO ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:16055714"
FT MUTAGEN 210
FT /note="C->A: Induces a strong decrease in SUMO ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:16055714"
FT MUTAGEN 215
FT /note="C->A: Induces a strong decrease in SUMO ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:16055714"
FT CONFLICT 108
FT /note="F -> L (in Ref. 1; BAB71338)"
FT /evidence="ECO:0000305"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:2YU4"
FT STRAND 177..185
FT /evidence="ECO:0007829|PDB:2YU4"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:2YU4"
FT HELIX 191..202
FT /evidence="ECO:0007829|PDB:2YU4"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:2YU4"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:2YU4"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:2YU4"
FT HELIX 229..239
FT /evidence="ECO:0007829|PDB:2YU4"
SQ SEQUENCE 247 AA; 27932 MW; 24D945C8F16F58F8 CRC64;
MPGRSSSNSG STGFISFSGV ESALSSLKNF QACINSGMDT ASSVALDLVE SQTEVSSEYS
MDKAMVEFAT LDRQLNHYVK AVQSTINHVK EERPEKIPDL KLLVEKKFLA LQSKNSDADF
QNNEKFVQFK QQLKELKKQC GLQADREADG TEGVDEDIIV TQSQTNFTCP ITKEEMKKPV
KNKVCGHTYE EDAIVRMIES RQKRKKKAYC PQIGCSHTDI RKSDLIQDEA LRRAIENHNK
KRHRHSE
