BTB/POZ domain

{{Infobox protein family

| Symbol = BTB

| Name = BTB/POZ domain

| image = PDB_1buo_EBI.jpg

| width =

| caption = Structure of the BTB domain from PLZF.{{cite journal | vauthors = Ahmad KF, Engel CK, Privé GG | title = Crystal structure of the BTB domain from PLZF | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 95 | issue = 21 | pages = 12123–12128 | date = October 1998 | pmid = 9770450 | pmc = 22795 | doi = 10.1073/pnas.95.21.12123 | doi-access = free | bibcode = 1998PNAS...9512123F }}

| Pfam = PF00651

| InterPro = IPR013069

| SMART =

| PROSITE = PS50097

| SCOP = 1buo

| TCDB =

| OPM family =

| OPM protein =

| PDB = {{PDB2|1buo}} , {{PDB2|1cs3}} , {{PDB2|1r28}} , {{PDB2|1r29}} , {{PDB2|1r2b}} , {{PDB2|2nn2}} , {{PDB2|3bim}}

}}

The BTB/POZ domain (BTB for BR-C, ttk and bab{{cite journal | vauthors = Zollman S, Godt D, Privé GG, Couderc JL, Laski FA | title = The BTB domain, found primarily in zinc finger proteins, defines an evolutionarily conserved family that includes several developmentally regulated genes in Drosophila | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 91 | issue = 22 | pages = 10717–10721 | date = October 1994 | pmid = 7938017 | pmc = 45093 | doi = 10.1073/pnas.91.22.10717 | bibcode = 1994PNAS...9110717Z | doi-access = free }} or POZ for Pox virus and Zinc finger{{cite journal | vauthors = Bardwell VJ, Treisman R | title = The POZ domain: a conserved protein-protein interaction motif | journal = Genes & Development | volume = 8 | issue = 14 | pages = 1664–1677 | date = July 1994 | pmid = 7958847 | doi = 10.1101/gad.8.14.1664 | s2cid = 27334252 | doi-access = free }}) is a structural domain found in proteins across the domain Eukarya.{{cite journal | vauthors = Stogios PJ, Downs GS, Jauhal JJ, Nandra SK, Privé GG | title = Sequence and structural analysis of BTB domain proteins | journal = Genome Biology | volume = 6 | issue = 10 | pages = R82 | date = 2005-09-15 | pmid = 16207353 | pmc = 1257465 | doi = 10.1186/gb-2005-6-10-r82 | doi-access = free }} Given its prevalence in eukaryotes and its absence in Archaea and bacteria, it likely arose after the origin of eukaryotes.{{cite journal | vauthors = Perez-Torrado R, Yamada D, Defossez PA | title = Born to bind: the BTB protein-protein interaction domain | journal = BioEssays | volume = 28 | issue = 12 | pages = 1194–1202 | date = December 2006 | pmid = 17120193 | doi = 10.1002/bies.20500 | s2cid = 23248814 }} While primarily a protein-protein interaction domain, some BTB domains have additional functionality in transcriptional regulation,{{cite journal | vauthors = Melnick A, Ahmad KF, Arai S, Polinger A, Ball H, Borden KL, Carlile GW, Prive GG, Licht JD | display-authors = 6 | title = In-depth mutational analysis of the promyelocytic leukemia zinc finger BTB/POZ domain reveals motifs and residues required for biological and transcriptional functions | journal = Molecular and Cellular Biology | volume = 20 | issue = 17 | pages = 6550–6567 | date = September 2000 | pmid = 10938130 | pmc = 86130 | doi = 10.1128/MCB.20.17.6550-6567.2000 }} cytoskeletal mobility,{{cite journal | vauthors = Bomont P, Cavalier L, Blondeau F, Ben Hamida C, Belal S, Tazir M, Demir E, Topaloglu H, Korinthenberg R, Tüysüz B, Landrieu P, Hentati F, Koenig M | display-authors = 6 | title = The gene encoding gigaxonin, a new member of the cytoskeletal BTB/kelch repeat family, is mutated in giant axonal neuropathy | journal = Nature Genetics | volume = 26 | issue = 3 | pages = 370–374 | date = November 2000 | pmid = 11062483 | doi = 10.1038/81701 | s2cid = 2917153 }} protein ubiquitination and degradation,{{cite journal | vauthors = Furukawa M, He YJ, Borchers C, Xiong Y | title = Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin ligases | journal = Nature Cell Biology | volume = 5 | issue = 11 | pages = 1001–1007 | date = November 2003 | pmid = 14528312 | doi = 10.1038/ncb1056 | s2cid = 22937928 }}{{cite journal | vauthors = Pintard L, Willis JH, Willems A, Johnson JL, Srayko M, Kurz T, Glaser S, Mains PE, Tyers M, Bowerman B, Peter M | display-authors = 6 | title = The BTB protein MEL-26 is a substrate-specific adaptor of the CUL-3 ubiquitin-ligase | journal = Nature | volume = 425 | issue = 6955 | pages = 311–316 | date = September 2003 | pmid = 13679921 | doi = 10.1038/nature01959 | bibcode = 2003Natur.425..311P | s2cid = 4425748 }}{{cite journal | vauthors = Geyer R, Wee S, Anderson S, Yates J, Wolf DA | title = BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases | journal = Molecular Cell | volume = 12 | issue = 3 | pages = 783–790 | date = September 2003 | pmid = 14527422 | doi = 10.1016/s1097-2765(03)00341-1 | doi-access = free }} and ion channel formation and operation.{{cite journal | vauthors = Minor DL, Lin YF, Mobley BC, Avelar A, Jan YN, Jan LY, Berger JM | title = The polar T1 interface is linked to conformational changes that open the voltage-gated potassium channel | journal = Cell | volume = 102 | issue = 5 | pages = 657–670 | date = September 2000 | pmid = 11007484 | doi = 10.1016/s0092-8674(00)00088-x | s2cid = 776305 | doi-access = free }} BTB domains have traditionally been classified by the other structural features present in the protein.