ZBED1_HUMAN
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 03-AUG-2022, entry version 182.
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},
GN hDREF {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; Q9Y2J4-4: AMOTL2; NbExp=3; IntAct=EBI-740037, EBI-10187270;
CC O96006; Q9NX04: C1orf109; NbExp=7; IntAct=EBI-740037, EBI-8643161;
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};
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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; 107.
DR IntAct; O96006; 75.
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; O96006; -.
DR PeptideAtlas; O96006; -.
DR PRIDE; O96006; -.
DR ProteomicsDB; 51185; -.
DR Antibodypedia; 35127; 443 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 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 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; EHQMVNT; -.
DR OrthoDB; 223749at2759; -.
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 587 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 RNAct; O96006; protein.
DR Bgee; ENSG00000214717; Expressed in gluteal muscle and 199 other tissues.
DR ExpressionAtlas; O96006; baseline and differential.
DR Genevisible; O96006; HS.
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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR InterPro; IPR008906; HATC_C_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR003656; Znf_BED.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR Pfam; PF05699; Dimer_Tnp_hAT; 1.
DR Pfam; PF02892; zf-BED; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50808; ZF_BED; 1.
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 A-530-A-A-
FT 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
