ID BEND3_HUMAN Reviewed; 828 AA. AC Q5T5X7; A2RRH2; Q9HCL9; DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 27-MAR-2024, entry version 142. DE RecName: Full=BEN domain-containing protein 3; GN Name=BEND3; Synonyms=KIAA1553; 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 GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 159-828. RX PubMed=10997877; DOI=10.1093/dnares/7.4.271; RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVIII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:273-281(2000). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-489, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [5] 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 [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164 AND SER-379, AND RP IDENTIFICATION BY MASS 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 [7] RP FUNCTION, INTERACTION WITH HDAC2; HDAC3 AND SALL4, SUBCELLULAR LOCATION, RP TISSUE SPECIFICITY, DOMAIN, SUMOYLATION AT LYS-20 AND LYS-512, AND RP MUTAGENESIS OF LYS-20 AND LYS-512. RX PubMed=21914818; DOI=10.1242/jcs.086603; RA Sathyan K.M., Shen Z., Tripathi V., Prasanth K.V., Prasanth S.G.; RT "A BEN-domain-containing protein associates with heterochromatin and RT represses transcription."; RL J. Cell Sci. 124:3149-3163(2011). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164; SER-379 AND SER-489, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [9] RP TISSUE SPECIFICITY. RX PubMed=25400923; DOI=10.1002/iid3.17; RA Shiheido H., Kitagori K., Sasaki C., Kobayashi S., Aoyama T., Urata K., RA Oku T., Hirayama Y., Yoshitomi H., Hikida M., Yoshifuji H., Mimori T., RA Watanabe T., Shimizu J.; RT "Human T cells expressing BEND3 on their surface represent a novel RT subpopulation that preferentially produces IL-6 and IL-8."; RL Immun. Inflammation. Dis. 2:35-43(2014). RN [10] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-20; LYS-129 AND LYS-427, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [11] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-20, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [12] RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-56; ARG-57 AND LYS-58. RX PubMed=25600804; DOI=10.1016/j.bbrc.2015.01.029; RA Shiheido H., Shimizu J.; RT "Basic amino acid residues located in the N-terminal region of BEND3 are RT essential for its nuclear localization."; RL Biochem. Biophys. Res. Commun. 457:589-594(2015). RN [13] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-56 AND LYS-142, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [14] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-20, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [15] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SMARCA5; BAZ2A AND USP21, RP AND MUTAGENESIS OF LYS-20 AND LYS-512. RX PubMed=26100909; DOI=10.1073/pnas.1424705112; RA Khan A., Giri S., Wang Y., Chakraborty A., Ghosh A.K., Anantharaman A., RA Aggarwal V., Sathyan K.M., Ha T., Prasanth K.V., Prasanth S.G.; RT "BEND3 represses rDNA transcription by stabilizing a NoRC component via RT USP21 deubiquitinase."; RL Proc. Natl. Acad. Sci. U.S.A. 112:8338-8343(2015). RN [16] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-20; LYS-41; LYS-56; LYS-58; RP LYS-73; LYS-128; LYS-129; LYS-137; LYS-142; LYS-158; LYS-176; LYS-427; RP LYS-512; LYS-528 AND LYS-700, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [17] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 236-347 IN COMPLEX WITH ERCC6L, RP FUNCTION, INTERACTION WITH ERCC6L, SUBUNIT, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=28977671; DOI=10.1093/nar/gkx792; RA Pitchai G.P., Kaulich M., Bizard A.H., Mesa P., Yao Q., Sarlos K., RA Streicher W.W., Nigg E.A., Montoya G., Hickson I.D.; RT "A novel TPR-BEN domain interaction mediates PICH-BEND3 association."; RL Nucleic Acids Res. 45:11413-11424(2017). CC -!- FUNCTION: Transcriptional repressor which associates with the NoRC CC (nucleolar remodeling complex) complex and plays a key role in CC repressing rDNA transcription. The sumoylated form modulates the CC stability of the NoRC complex component BAZ2A/TIP5 by controlling its CC USP21-mediated deubiquitination (PubMed:21914818, PubMed:26100909). CC Binds to unmethylated major satellite DNA and is involved in the CC recruitment of the Polycomb repressive complex 2 (PRC2) to major CC satellites (By similarity). Stimulates the ERCC6L translocase and CC ATPase activities (PubMed:28977671). {ECO:0000250|UniProtKB:Q6PAL0, CC ECO:0000269|PubMed:21914818, ECO:0000269|PubMed:26100909, CC ECO:0000269|PubMed:28977671}. CC -!- SUBUNIT: Homooligomer, probably a homooctamer (PubMed:28977671). CC Interacts with HDAC2 and HDAC3, but not HDAC1. Interacts with SALL4 CC (PubMed:21914818). Interacts with SMARCA5/SNF2H, BAZ2A/TIP5 and USP21 CC (PubMed:26100909). Interacts with the nucleosome remodeling and histone CC deacetylase (NuRD) repressor complex (By similarity). Interacts (via CC BEN domains 1 and 3) with ERCC6L (via N-terminal TPR repeat); the CC interaction is direct (PubMed:28977671). {ECO:0000250|UniProtKB:Q6PAL0, CC ECO:0000269|PubMed:21914818, ECO:0000269|PubMed:26100909, CC ECO:0000269|PubMed:28977671}. CC -!- INTERACTION: CC Q5T5X7; Q9C005: DPY30; NbExp=3; IntAct=EBI-1211496, EBI-744973; CC Q5T5X7; Q3B820: FAM161A; NbExp=3; IntAct=EBI-1211496, EBI-719941; CC Q5T5X7; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-1211496, EBI-348259; CC Q5T5X7; Q8NDC4: MORN4; NbExp=6; IntAct=EBI-1211496, EBI-10269566; CC Q5T5X7; P0CB47: UBTFL1; NbExp=3; IntAct=EBI-1211496, EBI-17208936; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21914818, CC ECO:0000269|PubMed:25600804}. Nucleus, nucleolus CC {ECO:0000269|PubMed:26100909}. Note=In the nucleus, observed in CC heterochromatic foci containing CBX1, CBX3, CBX5 and histone H3 CC trimethylated at 'Lys-9'. Released from chromatin during CC decondensation. Association with heterochromatin does not depend on CC sumoylation. {ECO:0000269|PubMed:21914818}. CC -!- TISSUE SPECIFICITY: Expressed at least in heart, kidney, liver, ovary CC and spleen, with highest levels in spleen and lowest in heart. CC Expressed on the surface of T-cells. {ECO:0000269|PubMed:21914818, CC ECO:0000269|PubMed:25400923}. CC -!- DOMAIN: The BEN domain 4 is necessary and sufficient for the CC localization of BEND3 to heterochromatic regions. CC {ECO:0000269|PubMed:21914818}. CC -!- PTM: Sumoylated at Lys-20 by SUMO1 and at Lys-512 by SUMO1, SUMO2 and CC SUMO3. Sumoylation probably occurs sequentially, with that of Lys-20 CC preceding that of Lys-512. It does not alter association with CC heterochromatin, but is required for the repression of transcription. CC {ECO:0000269|PubMed:21914818}. 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; AL355586; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC131628; AAI31629.1; -; mRNA. DR EMBL; AB046773; BAB13379.1; -; mRNA. DR CCDS; CCDS34507.1; -. DR RefSeq; NP_001073919.1; NM_001080450.2. DR RefSeq; XP_005267136.1; XM_005267079.3. DR RefSeq; XP_005267137.1; XM_005267080.3. DR RefSeq; XP_011534307.1; XM_011536005.2. DR RefSeq; XP_016866627.1; XM_017011138.1. DR PDB; 5JNO; X-ray; 2.20 A; A=236-347. DR PDB; 7W27; X-ray; 1.49 A; C=715-825. DR PDBsum; 5JNO; -. DR PDBsum; 7W27; -. DR AlphaFoldDB; Q5T5X7; -. DR SMR; Q5T5X7; -. DR BioGRID; 121704; 124. DR IntAct; Q5T5X7; 35. DR MINT; Q5T5X7; -. DR STRING; 9606.ENSP00000411268; -. DR GlyGen; Q5T5X7; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q5T5X7; -. DR PhosphoSitePlus; Q5T5X7; -. DR SwissPalm; Q5T5X7; -. DR BioMuta; BEND3; -. DR DMDM; 74745144; -. DR EPD; Q5T5X7; -. DR jPOST; Q5T5X7; -. DR MassIVE; Q5T5X7; -. DR MaxQB; Q5T5X7; -. DR PaxDb; 9606-ENSP00000411268; -. DR PeptideAtlas; Q5T5X7; -. DR ProteomicsDB; 64557; -. DR Pumba; Q5T5X7; -. DR Antibodypedia; 2976; 139 antibodies from 20 providers. DR DNASU; 57673; -. DR Ensembl; ENST00000369042.6; ENSP00000358038.1; ENSG00000178409.14. DR Ensembl; ENST00000429433.3; ENSP00000411268.2; ENSG00000178409.14. DR GeneID; 57673; -. DR KEGG; hsa:57673; -. DR MANE-Select; ENST00000369042.6; ENSP00000358038.1; NM_001367314.1; NP_001354243.1. DR UCSC; uc003prs.3; human. DR AGR; HGNC:23040; -. DR CTD; 57673; -. DR DisGeNET; 57673; -. DR GeneCards; BEND3; -. DR HGNC; HGNC:23040; BEND3. DR HPA; ENSG00000178409; Low tissue specificity. DR MIM; 616374; gene. DR neXtProt; NX_Q5T5X7; -. DR OpenTargets; ENSG00000178409; -. DR PharmGKB; PA164716540; -. DR VEuPathDB; HostDB:ENSG00000178409; -. DR eggNOG; ENOG502QQWG; Eukaryota. DR GeneTree; ENSGT00390000010827; -. DR HOGENOM; CLU_017582_0_0_1; -. DR InParanoid; Q5T5X7; -. DR OMA; TYRFINE; -. DR OrthoDB; 2905331at2759; -. DR PhylomeDB; Q5T5X7; -. DR TreeFam; TF300204; -. DR PathwayCommons; Q5T5X7; -. DR SignaLink; Q5T5X7; -. DR BioGRID-ORCS; 57673; 36 hits in 1155 CRISPR screens. DR ChiTaRS; BEND3; human. DR GenomeRNAi; 57673; -. DR Pharos; Q5T5X7; Tbio. DR PRO; PR:Q5T5X7; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q5T5X7; Protein. DR Bgee; ENSG00000178409; Expressed in ileal mucosa and 154 other cell types or tissues. DR GO; GO:0000792; C:heterochromatin; IDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0000182; F:rDNA binding; IDA:UniProtKB. DR GO; GO:0006306; P:DNA methylation; IMP:UniProtKB. DR GO; GO:0016479; P:negative regulation of transcription by RNA polymerase I; IDA:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:1903580; P:positive regulation of ATP metabolic process; IDA:UniProtKB. DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB. DR GO; GO:0000183; P:rDNA heterochromatin formation; IMP:UniProtKB. DR InterPro; IPR018379; BEN_domain. DR InterPro; IPR033583; BEND3. DR PANTHER; PTHR28665; BEN DOMAIN-CONTAINING PROTEIN 3; 1. DR PANTHER; PTHR28665:SF1; BEN DOMAIN-CONTAINING PROTEIN 3; 1. DR Pfam; PF10523; BEN; 4. DR SMART; SM01025; BEN; 4. DR PROSITE; PS51457; BEN; 4. DR Genevisible; Q5T5X7; HS. PE 1: Evidence at protein level; KW 3D-structure; Chromatin regulator; DNA-binding; Isopeptide bond; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..828 FT /note="BEN domain-containing protein 3" FT /id="PRO_0000290200" FT DOMAIN 242..343 FT /note="BEN 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00784" FT DOMAIN 387..487 FT /note="BEN 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00784" FT DOMAIN 548..650 FT /note="BEN 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00784" FT DOMAIN 715..816 FT /note="BEN 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00784" FT REGION 164..184 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 483..504 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 56..58 FT /note="Nuclear localization signal" FT /evidence="ECO:0000269|PubMed:25600804" FT MOD_RES 164 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 379 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 489 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:21406692" FT CROSSLNK 20 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT /evidence="ECO:0000269|PubMed:21914818" FT CROSSLNK 20 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 20 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733" FT CROSSLNK 41 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 56 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 58 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 73 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 128 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 129 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 137 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 142 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 158 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 176 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 427 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 512 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT /evidence="ECO:0000269|PubMed:21914818" FT CROSSLNK 512 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 528 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 700 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT MUTAGEN 20 FT /note="K->R: Partial loss of sumoylation. Almost complete FT loss of sumoylation, partial loss of transcription FT repression, no effect on subcellular location, loss of rDNA FT silencing; when associated with R-512." FT /evidence="ECO:0000269|PubMed:21914818, FT ECO:0000269|PubMed:26100909" FT MUTAGEN 56 FT /note="K->A: Loss of nuclear localization." FT /evidence="ECO:0000269|PubMed:25600804" FT MUTAGEN 57 FT /note="R->A: Loss of nuclear localization." FT /evidence="ECO:0000269|PubMed:25600804" FT MUTAGEN 58 FT /note="K->A: Loss of nuclear localization." FT /evidence="ECO:0000269|PubMed:25600804" FT MUTAGEN 512 FT /note="K->R: Partial loss of sumoylation. Almost complete FT loss of sumoylation, partial loss of transcription FT repression, no effect on subcellular location, loss of rDNA FT silencing; when associated with R-20." FT /evidence="ECO:0000269|PubMed:21914818, FT ECO:0000269|PubMed:26100909" FT CONFLICT 409 FT /note="E -> D (in Ref. 3; BAB13379)" FT /evidence="ECO:0000305" FT CONFLICT 596 FT /note="N -> S (in Ref. 2; AAI31629)" FT /evidence="ECO:0000305" FT HELIX 244..246 FT /evidence="ECO:0007829|PDB:5JNO" FT HELIX 250..259 FT /evidence="ECO:0007829|PDB:5JNO" FT HELIX 263..274 FT /evidence="ECO:0007829|PDB:5JNO" FT HELIX 276..279 FT /evidence="ECO:0007829|PDB:5JNO" FT HELIX 301..314 FT /evidence="ECO:0007829|PDB:5JNO" FT HELIX 316..319 FT /evidence="ECO:0007829|PDB:5JNO" FT HELIX 321..326 FT /evidence="ECO:0007829|PDB:5JNO" FT HELIX 328..346 FT /evidence="ECO:0007829|PDB:5JNO" FT HELIX 723..730 FT /evidence="ECO:0007829|PDB:7W27" FT HELIX 736..747 FT /evidence="ECO:0007829|PDB:7W27" FT HELIX 749..751 FT /evidence="ECO:0007829|PDB:7W27" FT HELIX 757..760 FT /evidence="ECO:0007829|PDB:7W27" FT STRAND 761..764 FT /evidence="ECO:0007829|PDB:7W27" FT TURN 766..768 FT /evidence="ECO:0007829|PDB:7W27" FT HELIX 774..787 FT /evidence="ECO:0007829|PDB:7W27" FT HELIX 793..799 FT /evidence="ECO:0007829|PDB:7W27" FT HELIX 801..810 FT /evidence="ECO:0007829|PDB:7W27" FT HELIX 816..822 FT /evidence="ECO:0007829|PDB:7W27" SQ SEQUENCE 828 AA; 94475 MW; 28D8F39112DB7EAE CRC64; MNSTEFTEDV EEVLKSITVK VETEAEDAAL DCSVNSRTSE KHSVDSVLTA LQDSSKRKQL VSDGLLDSVP GVKRRRLIPE ALLAGMRNRE NSSPCQGNGE QAGRGRSLGN VWPGEEEPCN DATTPSYKKP LYGISHKIME KKNPPSGDLL NVYELFEKAN ASNSPSSLRL LNEPQKRDCG STGAGTDNDP NIYFLIQKMF YMLNTLTSNM SQLHSKVDLL SLEVSRIKKQ VSPTEMVAKF QPPPEYQLTA AELKQIVDQS LSGGDLACRL LVQLFPELFS DVDFSRGCSA CGFAAKRKLE SLHLQLIRNY VEVYYPSVKD TAVWQAECLP QLNDFFSRFW AQREMEDSQP SGQVASFFEA EQVDPGHFLD NKDQEEALSL DRSSTIASDH VVDTQDLTEF LDEASSPGEF AVFLLHRLFP ELFDHRKLGE QYSCYGDGGK QELDPQRLQI IRNYTEIYFP DMQEEEAWLQ QCAQRINDEL EGLGLDAGSE GDPPRDDCYD SSSLPDDISV VKVEDSFEGE RPGRRSKKIW LVPIDFDKLE IPQPDFEVPG ADCLLSKEQL RSIYESSLSI GNFASRLLVH LFPELFTHEN LRKQYNCSGS LGKKQLDPSR IKLIRHYVQL LYPRAKNDRV WTLEFVGKLD ERCRRRDTEQ RRSYQQQRKV HVPGPECRDL TSYAINPERF REEFEGPPLP PERSSKDFCK IPLDELVVPS PDFPVPSPYL LSDKEVREIV QQSLSVGNFA ARLLVRLFPE LFTAENLRLQ YNHSGACNKK QLDPTRLRLI RHYVEAVYPV EKMEEVWHYE CIPSIDERCR RPNRKKCDIL KKAKKVEK //