ID ZBED1_HUMAN Reviewed; 694 AA. AC O96006; Q96BY4; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 191. DE RecName: Full=E3 SUMO-protein ligase ZBED1 {ECO:0000305}; DE EC=2.3.2.- {ECO:0000269|PubMed:27068747}; DE AltName: Full=DNA replication-related element-binding factor {ECO:0000303|PubMed:27068747}; DE AltName: Full=Putative Ac-like transposable element; DE AltName: Full=Zinc finger BED domain-containing protein 1 {ECO:0000305}; DE AltName: Full=dREF homolog; GN Name=ZBED1; GN Synonyms=ALTE, DREF {ECO:0000303|PubMed:17209048}, hDREF GN {ECO:0000303|PubMed:27068747}, KIAA0785, TRAMP; 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 [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Teratocarcinoma; RX PubMed=9887332; DOI=10.1093/hmg/8.1.61; RA Esposito T., Gianfrancesco F., Ciccodicola A., Montanini L., Mumm S., RA D'Urso M., Forabosco A.; RT "A novel pseudoautosomal human gene encodes a putative protein similar to RT Ac-like transposases."; RL Hum. Mol. Genet. 8:61-67(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=9872452; DOI=10.1093/dnares/5.5.277; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., RA Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XI. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 5:277-286(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Uterus; 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 [5] RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION. RX PubMed=12663651; DOI=10.1074/jbc.m303109200; RA Ohshima N., Takahashi M., Hirose F.; RT "Identification of a human homologue of the DREF transcription factor with RT a potential role in regulation of the histone H1 gene."; RL J. Biol. Chem. 278:22928-22938(2003). RN [6] RP FUNCTION, SUBUNIT, INTERACTION WITH KPNB1, SUBCELLULAR LOCATION, AND RP MUTAGENESIS OF 530-LYS-LYS-531; ARG-534; 590-TRP-TRP-591; PRO-599; RP 600-LEU-LEU-601; 604-VAL-LEU-605; 619-GLU-ARG-620; PHE-622 AND ARG-633. RX PubMed=17209048; DOI=10.1074/jbc.m607180200; RA Yamashita D., Komori H., Higuchi Y., Yamaguchi T., Osumi T., Hirose F.; RT "Human DNA replication-related element binding factor (hDREF) self- RT association via hATC domain is necessary for its nuclear accumulation and RT DNA binding."; RL J. Biol. Chem. 282:7563-7575(2007). RN [7] RP FUNCTION. RX PubMed=17220279; DOI=10.1128/mcb.01462-06; RA Yamashita D., Sano Y., Adachi Y., Okamoto Y., Osada H., Takahashi T., RA Yamaguchi T., Osumi T., Hirose F.; RT "hDREF regulates cell proliferation and expression of ribosomal protein RT genes."; RL Mol. Cell. Biol. 27:2003-2013(2007). RN [8] 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 [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [10] RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH HUMAN ADENOVIRUS EARLY E1A RP PROTEIN (MICROBIAL INFECTION), SUBCELLULAR LOCATION, SUBCELLULAR LOCATION RP (MICROBIAL INFECTION), AND SUMOYLATION. RX PubMed=25210186; DOI=10.1128/jvi.02538-14; RA Radko S., Koleva M., James K.M., Jung R., Mymryk J.S., Pelka P.; RT "Adenovirus E1A targets the DREF nuclear factor to regulate virus gene RT expression, DNA replication, and growth."; RL J. Virol. 88:13469-13481(2014). RN [11] RP FUNCTION, PATHWAY, INTERACTION WITH CHD3; SUMO1 AND UBC9, SUBCELLULAR RP LOCATION, SUMOYLATION, AND MUTAGENESIS OF CYS-47; CYS-50; HIS-71; MET-360; RP LEU-401; 590-TRP-TRP-591; 600-LEU-LEU-601 AND 604-VAL-LEU-605. RX PubMed=27068747; DOI=10.1074/jbc.m115.713370; RA Yamashita D., Moriuchi T., Osumi T., Hirose F.; RT "Transcription Factor hDREF Is a Novel SUMO E3 Ligase of Mi2alpha."; RL J. Biol. Chem. 291:11619-11634(2016). RN [12] RP STRUCTURE BY NMR OF 23-82. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the zinc finger BED domain of the zinc finger BED RT domain containing protein 1."; RL Submitted (NOV-2005) to the PDB data bank. CC -!- FUNCTION: Functions as an E3-type small ubiquitin-like modifier (SUMO) CC ligase which sumoylates CHD3/Mi2-alpha, causing its release from DNA CC (PubMed:27068747). This results in suppression of CHD3/Mi2-alpha CC transcription repression, increased recruitment of RNA polymerase II to CC gene promoters and positive regulation of transcription including H1-5 CC and ribosomal proteins such as: RPS6, RPL10A, and RPL12 CC (PubMed:12663651, PubMed:17209048, PubMed:17220279, PubMed:27068747). CC The resulting increased transcriptional activity drives cell CC proliferation (PubMed:12663651, PubMed:17220279). Binds to 5'- CC TGTCG[CT]GA[CT]A-3' consensus sequences in gene promoters of ribosomal CC proteins (PubMed:12663651, PubMed:17209048, PubMed:17220279, CC PubMed:27068747). {ECO:0000269|PubMed:12663651, CC ECO:0000269|PubMed:17209048, ECO:0000269|PubMed:17220279, CC ECO:0000269|PubMed:27068747}. CC -!- FUNCTION: (Microbial infection) Binds to human adenovirus gene CC promoters and contributes to transcriptional repression and virus CC growth inhibition during early stages of infection. CC {ECO:0000269|PubMed:25210186}. CC -!- PATHWAY: Protein modification; protein sumoylation. CC {ECO:0000269|PubMed:27068747}. CC -!- SUBUNIT: Homodimer and homomultimer (PubMed:17209048). Homodimerization CC is necessary for protein nuclear localization and DNA binding CC (PubMed:17209048). Interacts with KPNB1; required for nuclear import of CC ZBED1/hDREF (PubMed:17209048). Interacts with CHD3/Mi2-alpha CC (PubMed:27068747). Interacts with SUMO1 (PubMed:27068747). Interacts CC with UBE2I/UBC9 (PubMed:27068747). {ECO:0000269|PubMed:17209048, CC ECO:0000269|PubMed:27068747}. CC -!- SUBUNIT: (Microbial infection) Interacts (via C-terminus) with human CC adenovirus early E1A protein (via C-terminus); the interaction is CC direct. {ECO:0000269|PubMed:25210186}. CC -!- INTERACTION: CC O96006; Q9NX04: AIRIM; NbExp=7; IntAct=EBI-740037, EBI-8643161; CC O96006; Q9Y2J4-4: AMOTL2; NbExp=3; IntAct=EBI-740037, EBI-10187270; CC O96006; Q8IYE1: CCDC13; NbExp=3; IntAct=EBI-740037, EBI-10961312; CC O96006; Q16543: CDC37; NbExp=3; IntAct=EBI-740037, EBI-295634; CC O96006; Q9UBT7: CTNNAL1; NbExp=3; IntAct=EBI-740037, EBI-514206; CC O96006; Q5JVL4: EFHC1; NbExp=6; IntAct=EBI-740037, EBI-743105; CC O96006; Q9H5Z6-2: FAM124B; NbExp=3; IntAct=EBI-740037, EBI-11986315; CC O96006; Q9BVV2: FNDC11; NbExp=3; IntAct=EBI-740037, EBI-744935; CC O96006; Q9BVM4: GGACT; NbExp=3; IntAct=EBI-740037, EBI-10299852; CC O96006; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-740037, EBI-739467; CC O96006; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-740037, EBI-14103818; CC O96006; O60341: KDM1A; NbExp=4; IntAct=EBI-740037, EBI-710124; CC O96006; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-740037, EBI-14069005; CC O96006; P80188: LCN2; NbExp=3; IntAct=EBI-740037, EBI-11911016; CC O96006; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-740037, EBI-739832; CC O96006; Q8TCA0: LRRC20; NbExp=6; IntAct=EBI-740037, EBI-10274039; CC O96006; Q9UI95: MAD2L2; NbExp=3; IntAct=EBI-740037, EBI-77889; CC O96006; O15479: MAGEB2; NbExp=3; IntAct=EBI-740037, EBI-1057615; CC O96006; Q9NPJ1: MKKS; NbExp=3; IntAct=EBI-740037, EBI-721319; CC O96006; P25325: MPST; NbExp=3; IntAct=EBI-740037, EBI-2515082; CC O96006; Q9UBB6: NCDN; NbExp=3; IntAct=EBI-740037, EBI-1053490; CC O96006; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-740037, EBI-741158; CC O96006; P26367: PAX6; NbExp=3; IntAct=EBI-740037, EBI-747278; CC O96006; O75928: PIAS2; NbExp=3; IntAct=EBI-740037, EBI-348555; CC O96006; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-740037, EBI-79165; CC O96006; P56282: POLE2; NbExp=3; IntAct=EBI-740037, EBI-713847; CC O96006; O15160: POLR1C; NbExp=3; IntAct=EBI-740037, EBI-1055079; CC O96006; Q13131: PRKAA1; NbExp=3; IntAct=EBI-740037, EBI-1181405; CC O96006; P07602: PSAP; NbExp=4; IntAct=EBI-740037, EBI-716699; CC O96006; Q13671: RIN1; NbExp=3; IntAct=EBI-740037, EBI-366017; CC O96006; Q16385: SSX2B; NbExp=3; IntAct=EBI-740037, EBI-2210673; CC O96006; P0DI81-3: TRAPPC2; NbExp=3; IntAct=EBI-740037, EBI-11961968; CC O96006; Q8N7C3: TRIML2; NbExp=3; IntAct=EBI-740037, EBI-11059915; CC O96006; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-740037, EBI-9090990; CC O96006; Q7KZS0: UBE2I; NbExp=6; IntAct=EBI-740037, EBI-10180829; CC O96006; Q9Y5K5: UCHL5; NbExp=3; IntAct=EBI-740037, EBI-1051183; CC O96006; O75604: USP2; NbExp=3; IntAct=EBI-740037, EBI-743272; CC O96006; O96006: ZBED1; NbExp=4; IntAct=EBI-740037, EBI-740037; CC O96006; A8K5H9; NbExp=3; IntAct=EBI-740037, EBI-10174421; CC -!- SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000269|PubMed:25210186, CC ECO:0000269|PubMed:27068747}. Nucleus {ECO:0000269|PubMed:12663651, CC ECO:0000269|PubMed:17209048}. Note=In granular structures. CC {ECO:0000269|PubMed:12663651, ECO:0000269|PubMed:17209048}. CC -!- SUBCELLULAR LOCATION: Nucleus, PML body. Note=(Microbial infection) CC Upon interaction with human adenovirus early E1A protein, the protein CC is redistributed to the peripheral areas of PML bodies. CC {ECO:0000269|PubMed:25210186}. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed at low levels CC (PubMed:9887332). Expression is highest in skeletal muscle, heart, CC spleen and placenta (PubMed:9887332). {ECO:0000269|PubMed:9887332}. CC -!- INDUCTION: Expression is linked to the cell cycle: low in serum-starved CC fibroblasts, increasing during the G1/S phase, highest during the S/G2 CC phase and then decreasing again. {ECO:0000269|PubMed:12663651}. CC -!- PTM: Autosumoylated with SUMO1, SUMO2, and SUMO3. CC {ECO:0000269|PubMed:25210186, ECO:0000269|PubMed:27068747}. CC -!- MISCELLANEOUS: The gene coding for this protein is located in the CC pseudoautosomal region 1 (PAR1) of X and Y chromosomes. CC -!- CAUTION: Was first identified as gene weakly similar to Ac transposable CC elements, but does not code for any transposase activity. CC {ECO:0000305|PubMed:9887332}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA34505.2; Type=Erroneous initiation; Evidence={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; Y16947; CAA76545.1; -; mRNA. DR EMBL; Y17156; CAA76660.1; -; Genomic_DNA. DR EMBL; AB018328; BAA34505.2; ALT_INIT; mRNA. DR EMBL; AC079176; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC015030; AAH15030.1; -; mRNA. DR CCDS; CCDS14118.1; -. DR RefSeq; NP_001164606.1; NM_001171135.1. DR RefSeq; NP_001164607.1; NM_001171136.1. DR RefSeq; NP_004720.1; NM_004729.3. DR PDB; 2CT5; NMR; -; A=23-82. DR PDBsum; 2CT5; -. DR AlphaFoldDB; O96006; -. DR BMRB; O96006; -. DR SMR; O96006; -. DR BioGRID; 114626; 110. DR IntAct; O96006; 76. DR MINT; O96006; -. DR STRING; 9606.ENSP00000370621; -. DR iPTMnet; O96006; -. DR PhosphoSitePlus; O96006; -. DR BioMuta; ZBED1; -. DR EPD; O96006; -. DR jPOST; O96006; -. DR MassIVE; O96006; -. DR MaxQB; O96006; -. DR PaxDb; 9606-ENSP00000370621; -. DR PeptideAtlas; O96006; -. DR ProteomicsDB; 51185; -. DR Pumba; O96006; -. DR Antibodypedia; 35127; 486 antibodies from 27 providers. DR DNASU; 9189; -. DR Ensembl; ENST00000381218.8; ENSP00000370616.3; ENSG00000214717.12. DR Ensembl; ENST00000381222.8; ENSP00000370620.2; ENSG00000214717.12. DR Ensembl; ENST00000381223.9; ENSP00000370621.4; ENSG00000214717.12. DR Ensembl; ENST00000652001.1; ENSP00000498725.1; ENSG00000214717.12. DR Ensembl; ENST00000711169.1; ENSP00000518653.1; ENSG00000292345.1. DR Ensembl; ENST00000711171.1; ENSP00000518654.1; ENSG00000292345.1. DR Ensembl; ENST00000711172.1; ENSP00000518655.1; ENSG00000292345.1. DR Ensembl; ENST00000711173.1; ENSP00000518656.1; ENSG00000292345.1. DR GeneID; 9189; -. DR KEGG; hsa:9189; -. DR MANE-Select; ENST00000652001.1; ENSP00000498725.1; NM_001171136.2; NP_001164607.1. DR UCSC; uc004cqg.3; human. DR AGR; HGNC:447; -. DR CTD; 9189; -. DR DisGeNET; 9189; -. DR GeneCards; ZBED1; -. DR HGNC; HGNC:447; ZBED1. DR HPA; ENSG00000214717; Tissue enhanced (skeletal). DR MIM; 300178; gene. DR neXtProt; NX_O96006; -. DR OpenTargets; ENSG00000214717; -. DR PharmGKB; PA24753; -. DR VEuPathDB; HostDB:ENSG00000214717; -. DR eggNOG; KOG1121; Eukaryota. DR GeneTree; ENSGT00940000163186; -. DR HOGENOM; CLU_009123_12_2_1; -. DR InParanoid; O96006; -. DR OMA; LDICHIP; -. DR OrthoDB; 3027603at2759; -. DR PhylomeDB; O96006; -. DR TreeFam; TF322818; -. DR PathwayCommons; O96006; -. DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins. DR SignaLink; O96006; -. DR SIGNOR; O96006; -. DR UniPathway; UPA00886; -. DR BioGRID-ORCS; 9189; 9 hits in 627 CRISPR screens. DR EvolutionaryTrace; O96006; -. DR GeneWiki; ZBED1; -. DR GenomeRNAi; 9189; -. DR Pharos; O96006; Tbio. DR PRO; PR:O96006; -. DR Proteomes; UP000005640; Chromosome X. DR Proteomes; UP000005640; Chromosome Y. DR RNAct; O96006; Protein. DR Bgee; ENSG00000214717; Expressed in gluteal muscle and 201 other cell types or tissues. DR ExpressionAtlas; O96006; baseline and differential. DR GO; GO:0005813; C:centrosome; IDA:HPA. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0031965; C:nuclear membrane; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0016605; C:PML body; IDA:UniProtKB. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0061665; F:SUMO ligase activity; IDA:UniProtKB. DR GO; GO:0019789; F:SUMO transferase activity; EXP:Reactome. DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB. DR GO; GO:0003712; F:transcription coregulator activity; IDA:UniProtKB. DR GO; GO:0044828; P:negative regulation by host of viral genome replication; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:1990466; P:protein autosumoylation; IMP:UniProtKB. DR GO; GO:0016925; P:protein sumoylation; TAS:Reactome. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR InterPro; IPR008906; HATC_C_dom. DR InterPro; IPR012337; RNaseH-like_sf. DR InterPro; IPR003656; Znf_BED. DR InterPro; IPR036236; Znf_C2H2_sf. DR PANTHER; PTHR46169; DNA REPLICATION-RELATED ELEMENT FACTOR, ISOFORM A; 1. DR PANTHER; PTHR46169:SF2; E3 SUMO-PROTEIN LIGASE ZBED1; 1. DR Pfam; PF05699; Dimer_Tnp_hAT; 1. DR Pfam; PF02892; zf-BED; 1. DR SMART; SM00614; ZnF_BED; 1. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1. DR SUPFAM; SSF140996; Hermes dimerisation domain; 1. DR SUPFAM; SSF53098; Ribonuclease H-like; 1. DR PROSITE; PS50808; ZF_BED; 1. DR Genevisible; O96006; HS. PE 1: Evidence at protein level; KW 3D-structure; DNA-binding; Host-virus interaction; Metal-binding; Nucleus; KW Reference proteome; Transcription; Transcription regulation; Transferase; KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. FT CHAIN 1..694 FT /note="E3 SUMO-protein ligase ZBED1" FT /id="PRO_0000066560" FT ZN_FING 20..78 FT /note="BED-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027" FT REGION 315..694 FT /note="Required for interaction with human adenovirus early FT E1A protein" FT /evidence="ECO:0000269|PubMed:25210186" FT REGION 552..624 FT /note="Required for DNA binding" FT /evidence="ECO:0000269|PubMed:17209048" FT REGION 571..651 FT /note="Required for nuclear localization and FT homodimerization" FT /evidence="ECO:0000269|PubMed:17209048" FT REGION 652..694 FT /note="Required for the formation of higher order complexes FT of ZBED1 with consensus DNA binding sequences" FT /evidence="ECO:0000269|PubMed:17209048" FT MOTIF 530..534 FT /note="Nuclear localization signal" FT /evidence="ECO:0000269|PubMed:17209048" FT BINDING 47 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027" FT BINDING 50 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027" FT BINDING 66 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027" FT BINDING 71 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027" FT MUTAGEN 47 FT /note="C->A: Abolishes autosumoylation." FT /evidence="ECO:0000269|PubMed:27068747" FT MUTAGEN 50 FT /note="C->A: Abolishes autosumoylation." FT /evidence="ECO:0000269|PubMed:27068747" FT MUTAGEN 71 FT /note="H->A: Abolishes autosumoylation." FT /evidence="ECO:0000269|PubMed:27068747" FT MUTAGEN 360 FT /note="Missing: Abolishes interaction with SUMO1." FT /evidence="ECO:0000269|PubMed:27068747" FT MUTAGEN 401 FT /note="Missing: Abolishes interaction with SUMO1." FT /evidence="ECO:0000269|PubMed:27068747" FT MUTAGEN 530..531 FT /note="KK->AA: Abolishes nuclear localization, however has FT no effect on homodimerization; when associated with A-534." FT /evidence="ECO:0000269|PubMed:17209048" FT MUTAGEN 534 FT /note="R->A: Abolishes nuclear localization, however has no FT effect on homodimerization; when associated with FT A-530-A-A-531." FT /evidence="ECO:0000269|PubMed:17209048" FT MUTAGEN 590..591 FT /note="WW->AA: Abolishes homodimerization, multimerization, FT interaction with KPNB1, nuclear localization and DNA FT binding activity. Abolishes interaction with SUMO1 and FT reduces SUMOylation of CHD3/Mi2-alpha." FT /evidence="ECO:0000269|PubMed:17209048, FT ECO:0000269|PubMed:27068747" FT MUTAGEN 599 FT /note="P->A: No effect on homodimerization or nuclear FT localization." FT /evidence="ECO:0000269|PubMed:17209048" FT MUTAGEN 600..601 FT /note="LL->AA: Abolishes homodimerization and nuclear FT localization. Abolishes homodimerization, multimerization, FT nuclear localization, and DNA binding activity; when FT associated with A-604-A-A-605. Abolishes interaction with FT SUMO1 and reduces sumoylation of CHD3/Mi2-alpha; when FT associated with 604-A-A-605." FT /evidence="ECO:0000269|PubMed:17209048, FT ECO:0000269|PubMed:27068747" FT MUTAGEN 604..605 FT /note="VL->AA: Reduces homodimerization and nuclear FT localization. Abolishes homodimerization, multimerization, FT nuclear localization, and DNA binding activity; when FT associated with A-600-A-A-601. Abolishes interaction with FT SUMO1 and reduces sumoylation of CHD3/Mi2-alpha; when FT associated with A-600-A-A-601." FT /evidence="ECO:0000269|PubMed:17209048, FT ECO:0000269|PubMed:27068747" FT MUTAGEN 619..620 FT /note="ER->AA: No effect on homodimerization or nuclear FT localization." FT /evidence="ECO:0000269|PubMed:17209048" FT MUTAGEN 622 FT /note="F->A: No effect on homodimerization or nuclear FT localization." FT /evidence="ECO:0000269|PubMed:17209048" FT MUTAGEN 633 FT /note="R->A: No effect on homodimerization or nuclear FT localization." FT /evidence="ECO:0000269|PubMed:17209048" FT CONFLICT 295 FT /note="F -> L (in Ref. 4; AAH15030)" FT /evidence="ECO:0000305" FT STRAND 27..29 FT /evidence="ECO:0007829|PDB:2CT5" FT STRAND 35..37 FT /evidence="ECO:0007829|PDB:2CT5" FT HELIX 39..41 FT /evidence="ECO:0007829|PDB:2CT5" FT TURN 48..51 FT /evidence="ECO:0007829|PDB:2CT5" FT HELIX 61..69 FT /evidence="ECO:0007829|PDB:2CT5" FT HELIX 72..78 FT /evidence="ECO:0007829|PDB:2CT5" SQ SEQUENCE 694 AA; 78156 MW; 40404497B17283AF CRC64; MENKSLESSQ TDLKLVAHPR AKSKVWKYFG FDTNAEGCIL QWKKIYCRIC MAQIAYSGNT SNLSYHLEKN HPEEFCEFVK SNTEQMREAF ATAFSKLKPE SSQQPGQDAL AVKAGHGYDS KKQQELTAAV LGLICEGLYP ASIVDEPTFK VLLKTADPRY ELPSRKYIST KAIPEKYGAV REVILKELAE ATWCGISTDM WRSENQNRAY VTLAAHFLGL GAPNCLSMGS RCLKTFEVPE ENTAETITRV LYEVFIEWGI SAKVFGATTN YGKDIVKACS LLDVAVHMPC LGHTFNAGIQ QAFQLPKLGA LLSRCRKLVE YFQQSAVAMY MLYEKQKQQN VAHCMLVSNR VSWWGSTLAM LQRLKEQQFV IAGVLVEDSN NHHLMLEASE WATIEGLVEL LQPFKQVAEM LSASRYPTIS MVKPLLHMLL NTTLNIKETD SKELSMAKEV IAKELSKTYQ ETPEIDMFLN VATFLDPRYK RLPFLSAFER QQVENRVVEE AKGLLDKVKD GGYRPAEDKI FPVPEEPPVK KLMRTSTPPP ASVINNMLAE IFCQTGGVED QEEWHAQVVE ELSNFKSQKV LGLNEDPLKW WSDRLALFPL LPKVLQKYWC VTATRVAPER LFGSAANVVS AKRNRLAPAH VDEQVFLYEN ARSGAEAEPE DQDEGEWGLD QEQVFSLGDG VSGGFFGIRD SSFL //