ID ZBT48_HUMAN Reviewed; 688 AA. AC P10074; Q5SY19; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 02-SEP-2026, entry version 233. DE RecName: Full=Zinc finger and BTB domain-containing protein 48 {ECO:0000312|HGNC:HGNC:4930}; DE AltName: Full=Krueppel-related zinc finger protein 3 {ECO:0000303|PubMed:9516840}; DE Short=hKR3 {ECO:0000303|Ref.12}; DE AltName: Full=Telomere zinc finger-associated protein {ECO:0000303|PubMed:28082411}; DE Short=TZAP {ECO:0000303|PubMed:28082411}; DE AltName: Full=Telomere-binding protein and transcriptional activator ZBTB48; DE AltName: Full=Zinc finger protein 855 {ECO:0000312|HGNC:HGNC:4930}; GN Name=ZBTB48 {ECO:0000312|HGNC:HGNC:4930}; GN Synonyms=HKR3 {ECO:0000303|PubMed:9516840}, TZAP GN {ECO:0000303|PubMed:28082411}, ZNF855 {ECO:0000312|HGNC:HGNC:4930}; 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 [MRNA], DNA-BINDING, AND FUNCTION. RX PubMed=7969177; DOI=10.1128/mcb.14.12.8438-8450.1994; RA Sugawara M., Scholl T., Ponath P.D., Strominger J.L.; RT "A factor that regulates the class II major histocompatibility complex gene RT DPA is a member of a subfamily of zinc finger proteins that includes a RT Drosophila developmental control protein."; RL Mol. Cell. Biol. 14:8438-8450(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY. RX PubMed=9516840; DOI=10.1016/s0959-8049(97)00279-7; RA Maris J.M., Jensen J., Sulman E.P., Beltinger C.P., Allen C., Biegel J.A., RA Brodeur G.M., White P.S.; RT "Human Kruppel-related 3 (HKR3): a candidate for the 1p36 neuroblastoma RT tumour suppressor gene?"; RL Eur. J. Cancer 33:1991-1996(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 461-488. RX PubMed=2850480; DOI=10.1128/mcb.8.8.3104-3113.1988; RA Ruppert J.M., Kinzler K.W., Wong A.J., Bigner S.H., Kao F.T., Law M.L., RA Seuanez H.N., O'Brien S.J., Vogelstein B.; RT "The GLI-Kruppel family of human genes."; RL Mol. Cell. Biol. 8:3104-3113(1988). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [7] RP FUNCTION, AND INTERACTION WITH EP300. RX PubMed=24382891; DOI=10.1074/jbc.m113.526855; RA Yoon J.H., Choi W.I., Jeon B.N., Koh D.I., Kim M.K., Kim M.H., Kim J., RA Hur S.S., Kim K.S., Hur M.W.; RT "Human Kruppel-related 3 (HKR3) is a novel transcription activator of RT alternate reading frame (ARF) gene."; RL J. Biol. Chem. 289:4018-4031(2014). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-171 AND SER-179, AND 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 [9] RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF HIS-596. RX PubMed=28500257; DOI=10.15252/embr.201744095; RA Jahn A., Rane G., Paszkowski-Rogacz M., Sayols S., Bluhm A., Han C.T., RA Draskovic I., Londono-Vallejo J.A., Kumar A.P., Buchholz F., Butter F., RA Kappei D.; RT "ZBTB48 is both a vertebrate telomere-binding protein and a transcriptional RT activator."; RL EMBO Rep. 18:929-946(2017). RN [10] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-143 AND LYS-263, AND RP 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 [11] RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN. RX PubMed=28082411; DOI=10.1126/science.aah6752; RA Li J.S., Miralles Fuste J., Simavorian T., Bartocci C., Tsai J., RA Karlseder J., Lazzerini Denchi E.; RT "TZAP: A telomere-associated protein involved in telomere length control."; RL Science 355:638-641(2017). RN [12] RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 2-120. RG Structural genomics consortium (SGC); RT "Crystal structure of the human BTB domain of the krueppel-related zinc RT finger protein 3 (hKR3)."; RL Submitted (NOV-2007) to the PDB data bank. RN [13] RP FUNCTION, AND RNA-BINDING. RX PubMed=39300486; DOI=10.1186/s13059-024-03392-7; RA Nabeel-Shah S., Pu S., Burke G.L., Ahmed N., Braunschweig U., RA Farhangmehr S., Lee H., Wu M., Ni Z., Tang H., Zhong G., Marcon E., RA Zhang Z., Blencowe B.J., Greenblatt J.F.; RT "Recruitment of the m6A/m6Am demethylase FTO to target RNAs by the RT telomeric zinc finger protein ZBTB48."; RL Genome Biol. 25:246-246(2024). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 516-620 IN COMPLEX WITH CIITA RP PROMOTER AND ZN(2+), FUNCTION, AND DOMAIN. RX PubMed=39562739; DOI=10.1038/s44318-024-00306-y; RA Rane G., Kuan V.L.S., Wang S., Mok M.M.H., Khanchandani V., Hansen J., RA Norvaisaite I., Zulkaflee N., Yong W.K., Jahn A., Mukundan V.T., Shi Y., RA Osato M., Li F., Kappei D.; RT "ZBTB48 is a priming factor regulating B-cell-specific CIITA expression."; RL EMBO J. 43:6236-6263(2024). CC -!- FUNCTION: Plays a critical role in transcriptional regulation and CC chromatin remodeling. Acts as a regulator of telomere length CC (PubMed:28082411, PubMed:28500257). Directly binds the telomeric CC double-stranded 5'-TTAGGG-3' repeat (PubMed:28082411, PubMed:28500257). CC Preferentially binds to telomeres that have a low concentration of CC shelterin complex and acts as a regulator of telomere length by CC initiating telomere trimming, a process that prevents the accumulation CC of aberrantly long telomeres (PubMed:28082411). Also acts as a CC transcription regulator that binds to promoter regions CC (PubMed:24382891, PubMed:28500257, PubMed:7969177). Regulates CC expression of a small subset of genes, including MTFP1 CC (PubMed:28500257). Acts as a negative regulator of cell proliferation CC by specifically activating expression of ARF, a tumor suppressor CC isoform of CDKN2A (PubMed:24382891). Acts as a transcription regulator CC of CIITA, the major factor regulating MHC class II gene expression CC (PubMed:39562739). In addition, regulates cellular m6A/m6Am methylation CC on RNA by facilitating the recruitment of the RNA demethylase, FTO, to CC target mRNAs (PubMed:39300486). {ECO:0000269|PubMed:24382891, CC ECO:0000269|PubMed:28082411, ECO:0000269|PubMed:28500257, CC ECO:0000269|PubMed:39300486, ECO:0000269|PubMed:39562739, CC ECO:0000269|PubMed:7969177}. CC -!- SUBUNIT: Interacts with EP300 (PubMed:24382891). CC {ECO:0000269|PubMed:24382891}. CC -!- INTERACTION: CC P10074; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-744864, EBI-739624; CC P10074; Q92997: DVL3; NbExp=4; IntAct=EBI-744864, EBI-739789; CC P10074; Q9NWQ4: GPATCH2L; NbExp=3; IntAct=EBI-744864, EBI-5666657; CC P10074; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-744864, EBI-11959885; CC P10074; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-744864, EBI-10172150; CC P10074; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-744864, EBI-10172290; CC P10074; Q969R5: L3MBTL2; NbExp=3; IntAct=EBI-744864, EBI-739909; CC P10074; P02545: LMNA; NbExp=3; IntAct=EBI-744864, EBI-351935; CC P10074; P23508: MCC; NbExp=3; IntAct=EBI-744864, EBI-307531; CC P10074; Q9Y5B8: NME7; NbExp=6; IntAct=EBI-744864, EBI-744782; CC P10074; Q96CV9: OPTN; NbExp=3; IntAct=EBI-744864, EBI-748974; CC P10074; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-744864, EBI-12023934; CC P10074; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-744864, EBI-741515; CC P10074; Q8WV44: TRIM41; NbExp=4; IntAct=EBI-744864, EBI-725997; CC P10074; Q9H2G4: TSPYL2; NbExp=3; IntAct=EBI-744864, EBI-947459; CC P10074; P61964: WDR5; NbExp=3; IntAct=EBI-744864, EBI-540834; CC P10074; Q9HCK0: ZBTB26; NbExp=3; IntAct=EBI-744864, EBI-3918996; CC P10074; P10074: ZBTB48; NbExp=4; IntAct=EBI-744864, EBI-744864; CC P10074; Q15916: ZBTB6; NbExp=3; IntAct=EBI-744864, EBI-7227791; CC P10074; Q96BR9: ZBTB8A; NbExp=7; IntAct=EBI-744864, EBI-742740; CC P10074; Q96C00: ZBTB9; NbExp=3; IntAct=EBI-744864, EBI-395708; CC P10074; Q96PQ6: ZNF317; NbExp=3; IntAct=EBI-744864, EBI-1210473; CC P10074; Q9H9D4: ZNF408; NbExp=3; IntAct=EBI-744864, EBI-347633; CC P10074; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-744864, EBI-11962574; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome, telomere CC {ECO:0000269|PubMed:28082411, ECO:0000269|PubMed:28500257}. CC Note=Directly binds the telomeric double-stranded 5'-TTAGGG-3' repeat CC (PubMed:28082411, PubMed:28500257). According to a report, CC preferentially binds to long telomeres that have a low concentration of CC shelterin complex, competing with the telomeric repeat binding factors CC TERF1 and TERF2 (PubMed:28082411). According to another report, binds CC telomeres regardless of their length (PubMed:28500257). CC {ECO:0000269|PubMed:28082411, ECO:0000269|PubMed:28500257}. CC -!- TISSUE SPECIFICITY: Detected in adrenal gland and neuroblastoma. CC {ECO:0000269|PubMed:9516840}. CC -!- DOMAIN: The C2H2-type zinc fingers mediate binding to the telomeric CC double-stranded 5'-TTAGGG-3' repeats (PubMed:28082411). The last C2H2- CC type zinc finger is required for telomeric-binding (PubMed:28500257). CC The two last C2H2-type zinc fingers are required for CIITA promoter III CC binding (PubMed:39562739). {ECO:0000269|PubMed:28082411, CC ECO:0000269|PubMed:28500257, ECO:0000269|PubMed:39562739}. CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. {ECO:0000305}. CC -!- CAUTION: According to a study, preferentially binds to long telomeres CC that have a low concentration of shelterin complex (PubMed:28082411). CC According to another report, binds telomeres regardless of their length CC (PubMed:28500257). {ECO:0000269|PubMed:28082411, CC ECO:0000269|PubMed:28500257}. 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; L16896; AAA65124.1; -; mRNA. DR EMBL; U45325; AAB08973.1; -; Genomic_DNA. DR EMBL; U45324; AAB08973.1; JOINED; Genomic_DNA. DR EMBL; AL591866; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC013573; AAH13573.1; -; mRNA. DR EMBL; M20677; AAA35989.1; -; Genomic_DNA. DR CCDS; CCDS84.1; -. DR PIR; A56360; A56360. DR RefSeq; NP_001265576.1; NM_001278647.2. DR RefSeq; NP_001265577.1; NM_001278648.2. DR RefSeq; NP_005332.1; NM_005341.4. DR RefSeq; XP_047274820.1; XM_047418864.1. DR PDB; 3B84; X-ray; 1.74 A; A=4-120. DR PDB; 5YJ3; X-ray; 2.85 A; C/D=516-620. DR AlphaFoldDB; P10074; -. DR SMR; P10074; -. DR BioGRID; 109349; 154. DR FunCoup; P10074; 425. DR IntAct; P10074; 126. DR MINT; P10074; -. DR STRING; 9606.ENSP00000366902; -. DR ChEMBL; CHEMBL5069366; -. DR GlyGen; P10074; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; P10074; -. DR PhosphoSitePlus; P10074; -. DR BioMuta; ZBTB48; -. DR DMDM; 1708212; -. DR jPOST; P10074; -. DR MassIVE; P10074; -. DR PaxDb; 9606-ENSP00000366902; -. DR PeptideAtlas; P10074; -. DR ProteomicsDB; 52561; -. DR Pumba; P10074; -. DR Antibodypedia; 13109; 145 antibodies from 29 providers. DR DNASU; 3104; -. DR Ensembl; ENST00000377674.9; ENSP00000366902.4; ENSG00000204859.14. DR Ensembl; ENST00000902993.1; ENSP00000573052.1; ENSG00000204859.14. DR Ensembl; ENST00000902996.1; ENSP00000573055.1; ENSG00000204859.14. DR Ensembl; ENST00000953435.1; ENSP00000623494.1; ENSG00000204859.14. DR GeneID; 3104; -. DR KEGG; hsa:3104; -. DR MANE-Select; ENST00000377674.9; ENSP00000366902.4; NM_005341.4; NP_005332.1. DR UCSC; uc001anx.5; human. DR AGR; HGNC:4930; -. DR ClinPGx; PA162409481; -. DR CTD; 3104; -. DR DisGeNET; 3104; -. DR GeneCards; ZBTB48; -. DR HGNC; HGNC:4930; ZBTB48. DR HPA; ENSG00000204859; Low tissue specificity. DR MIM; 165270; gene. DR OpenTargets; ENSG00000204859; -. DR VEuPathDB; HostDB:ENSG00000204859; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000158981; -. DR HOGENOM; CLU_002678_70_0_1; -. DR InParanoid; P10074; -. DR OMA; EPPGNRK; -. DR OrthoDB; 3156061at2759; -. DR PAN-GO; P10074; 3 GO annotations based on evolutionary models. DR PhylomeDB; P10074; -. DR PathwayCommons; P10074; -. DR SignaLink; P10074; -. DR Agora; ENSG00000204859; -. DR BioGRID-ORCS; 3104; 14 hits in 1217 CRISPR screens. DR ChiTaRS; ZBTB48; human. DR EvolutionaryTrace; P10074; -. DR GenomeRNAi; 3104; -. DR Pharos; P10074; Tbio. DR PRO; PR:P10074; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P10074; protein. DR Bgee; ENSG00000204859; Expressed in right lobe of liver and 129 other cell types or tissues. DR ExpressionAtlas; P10074; baseline and differential. DR GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central. DR GO; GO:0003691; F:double-stranded telomeric DNA binding; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:UniProtKB. DR GO; GO:0051252; P:regulation of RNA metabolic process; IMP:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0010833; P:telomere maintenance via telomere lengthening; IMP:UniProtKB. DR CDD; cd18232; BTB_POZ_ZBTB48_TZAP_KR3; 1. DR FunFam; 3.30.160.60:FF:000657; GDNF inducible zinc finger protein 1; 1. DR FunFam; 3.30.160.60:FF:001732; Zgc:162936; 1. DR FunFam; 3.30.160.60:FF:001113; Zinc finger and BTB domain containing 48; 1. DR FunFam; 3.30.160.60:FF:001117; Zinc finger and BTB domain containing 48; 1. DR FunFam; 3.30.160.60:FF:000809; Zinc finger and BTB domain-containing 48; 1. DR FunFam; 3.30.160.60:FF:001252; Zinc finger and BTB domain-containing 48; 1. DR FunFam; 3.30.160.60:FF:001257; Zinc finger and BTB domain-containing 48; 1. DR FunFam; 3.30.710.10:FF:000074; Zinc finger and BTB domain-containing 48; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 10. DR Gene3D; 3.30.710.10; Potassium Channel Kv1.1, Chain A; 1. DR InterPro; IPR000210; BTB/POZ_dom. DR InterPro; IPR011333; SKP1/BTB/POZ_sf. DR InterPro; IPR050758; Znf_C2H2-type. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR23234:SF10; RIKEN CDNA 6720489N17 GENE-RELATED; 1. DR PANTHER; PTHR23234; ZNF44 PROTEIN; 1. DR Pfam; PF00651; BTB; 1. DR Pfam; PF00096; zf-C2H2; 6. DR SMART; SM00225; BTB; 1. DR SMART; SM00355; ZnF_C2H2; 11. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 6. DR SUPFAM; SSF54695; POZ domain; 1. DR PROSITE; PS50097; BTB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11. DR PDBsum; 3B84; -. DR PDBsum; 5YJ3; -. PE 1: Evidence at protein level; KW 3D-structure; Activator; Chromosome; DNA-binding; Isopeptide bond; KW Metal-binding; Nucleus; Phosphoprotein; Proteomics identification; KW Reference proteome; Repeat; RNA-binding; Telomere; Transcription; KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..688 FT /note="Zinc finger and BTB domain-containing protein 48" FT /id="PRO_0000047272" FT DOMAIN 26..89 FT /note="BTB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037" FT ZN_FING 291..313 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 319..344 FT /note="CCHC-type" FT /evidence="ECO:0000250|UniProtKB:Q1H9T6" FT ZN_FING 350..372 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 378..401 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 407..430 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 436..459 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 465..487 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 493..515 FT /note="C2H2-type 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 521..544 FT /note="C2H2-type 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 550..572 FT /note="C2H2-type 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 578..600 FT /note="C2H2-type 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 119..140 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 161..192 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 170..186 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 293 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q1H9T6" FT BINDING 296 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q1H9T6" FT BINDING 309 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q1H9T6" FT BINDING 313 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q1H9T6" FT BINDING 321 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q1H9T6" FT BINDING 324 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q1H9T6" FT BINDING 337 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q1H9T6" FT BINDING 342 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q1H9T6" FT BINDING 352 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:Q1H9T6" FT BINDING 355 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:Q1H9T6" FT BINDING 368 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:Q1H9T6" FT BINDING 372 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:Q1H9T6" FT BINDING 380 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:Q1H9T6" FT BINDING 383 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:Q1H9T6" FT BINDING 396 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:Q1H9T6" FT BINDING 401 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:Q1H9T6" FT BINDING 552 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000269|PubMed:39562739, FT ECO:0007744|PDB:5YJ3" FT BINDING 555 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000269|PubMed:39562739, FT ECO:0007744|PDB:5YJ3" FT BINDING 568 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000269|PubMed:39562739, FT ECO:0007744|PDB:5YJ3" FT BINDING 580 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0000269|PubMed:39562739, FT ECO:0007744|PDB:5YJ3" FT BINDING 583 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0000269|PubMed:39562739, FT ECO:0007744|PDB:5YJ3" FT BINDING 596 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000269|PubMed:39562739, FT ECO:0007744|PDB:5YJ3" FT BINDING 596 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0000269|PubMed:39562739, FT ECO:0007744|PDB:5YJ3" FT BINDING 600 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0000269|PubMed:39562739, FT ECO:0007744|PDB:5YJ3" FT MOD_RES 169 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 171 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 179 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT CROSSLNK 143 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 263 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 675 FT /note="S -> A (in dbSNP:rs2229330)" FT /id="VAR_052925" FT MUTAGEN 596 FT /note="H->A: Abolishes binding to the telomeric FT double-stranded 5'-TTAGGG-3' repeat." FT /evidence="ECO:0000269|PubMed:28500257" FT CONFLICT 201 FT /note="P -> S (in Ref. 1; AAA65124)" FT /evidence="ECO:0000305" FT CONFLICT 244 FT /note="D -> S (in Ref. 1; AAA65124)" FT /evidence="ECO:0000305" FT CONFLICT 350..351 FT /note="FT -> LP (in Ref. 1; AAA65124)" FT /evidence="ECO:0000305" FT CONFLICT 607 FT /note="N -> K (in Ref. 1; AAA65124)" FT /evidence="ECO:0000305" FT HELIX 5..22 FT /evidence="ECO:0007829|PDB:3B84" FT STRAND 28..32 FT /evidence="ECO:0007829|PDB:3B84" FT STRAND 35..39 FT /evidence="ECO:0007829|PDB:3B84" FT HELIX 41..47 FT /evidence="ECO:0007829|PDB:3B84" FT HELIX 49..55 FT /evidence="ECO:0007829|PDB:3B84" FT TURN 56..59 FT /evidence="ECO:0007829|PDB:3B84" FT STRAND 63..65 FT /evidence="ECO:0007829|PDB:3B84" FT HELIX 67..69 FT /evidence="ECO:0007829|PDB:3B84" FT HELIX 70..82 FT /evidence="ECO:0007829|PDB:3B84" FT TURN 89..91 FT /evidence="ECO:0007829|PDB:3B84" FT HELIX 92..101 FT /evidence="ECO:0007829|PDB:3B84" FT HELIX 105..113 FT /evidence="ECO:0007829|PDB:3B84" FT STRAND 553..555 FT /evidence="ECO:0007829|PDB:5YJ3" FT STRAND 558..562 FT /evidence="ECO:0007829|PDB:5YJ3" FT HELIX 563..570 FT /evidence="ECO:0007829|PDB:5YJ3" FT TURN 581..583 FT /evidence="ECO:0007829|PDB:5YJ3" FT STRAND 586..589 FT /evidence="ECO:0007829|PDB:5YJ3" FT HELIX 590..600 FT /evidence="ECO:0007829|PDB:5YJ3" FT HELIX 608..613 FT /evidence="ECO:0007829|PDB:5YJ3" SQ SEQUENCE 688 AA; 77054 MW; EBECCE3D6CBBD524 CRC64; MDGSFVQHSV RVLQELNKQR EKGQYCDATL DVGGLVFKAH WSVLACCSHF FQSLYGDGSG GSVVLPAGFA EIFGLLLDFF YTGHLALTSG NRDQVLLAAR ELRVPEAVEL CQSFKPKTSV GQAAGGQSGL GPPASQNVNS HVKEPAGLEE EEVSRTLGLV PRDQEPRGSH SPQRPQLHSP AQSEGPSSLC GKLKQALKPC PLEDKKPEDC KVPPRPLEAE GAQLQGGSNE WEVVVQVEDD GDGDYMSEPE AVLTRRKSNV IRKPCAAEPA LSAGSLAAEP AENRKGTAVP VECPTCHKKF LSKYYLKVHN RKHTGEKPFE CPKCGKCYFR KENLLEHEAR NCMNRSEQVF TCSVCQETFR RRMELRVHMV SHTGEMPYKC SSCSQQFMQK KDLQSHMIKL HGAPKPHACP TCAKCFLSRT ELQLHEAFKH RGEKLFVCEE CGHRASSRNG LQMHIKAKHR NERPHVCEFC SHAFTQKANL NMHLRTHTGE KPFQCHLCGK TFRTQASLDK HNRTHTGERP FSCEFCEQRF TEKGPLLRHV ASRHQEGRPH FCQICGKTFK AVEQLRVHVR RHKGVRKFEC TECGYKFTRQ AHLRRHMEIH DRVENYNPRQ RKLRNLIIED EKMVVVALQP PAELEVGSAE VIVESLAQGG LASQLPGQRL CAEESFTGPG VLEPSLIITA AVPEDCDT //