ID ZBT17_HUMAN Reviewed; 803 AA. AC Q13105; A0AV07; B4DXB4; B7ZLQ9; F5H411; Q15932; Q5JYB2; Q9NUC9; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2005, sequence version 3. DT 17-JUN-2020, entry version 207. DE RecName: Full=Zinc finger and BTB domain-containing protein 17; DE AltName: Full=Myc-interacting zinc finger protein 1; DE Short=Miz-1; DE AltName: Full=Zinc finger protein 151; DE AltName: Full=Zinc finger protein 60; GN Name=ZBTB17; Synonyms=MIZ1, ZNF151, ZNF60; 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] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND RP INTERACTION WITH MYC. RX PubMed=9312026; DOI=10.1093/emboj/16.18.5672; RA Peukert K., Staller P., Schneider A., Carmichael G., Haenel F., Eilers M.; RT "An alternative pathway for gene regulation by Myc."; RL EMBO J. 16:5672-5686(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). 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] (ISOFORMS 1 AND 2). RC TISSUE=Brain; 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 327-342. RC TISSUE=Placenta; RX PubMed=1505991; DOI=10.1016/0888-7543(92)90013-i; RA Lichter P., Bray P., Ried T., Dawid I.B., Ward D.C.; RT "Clustering of C2-H2 zinc finger motif sequences within telomeric and RT fragile site regions of human chromosomes."; RL Genomics 13:999-1007(1992). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 580-803 (ISOFORM 1). RC TISSUE=Insulinoma; RX PubMed=7557990; DOI=10.1006/geno.1995.1040; RA Tommerup N., Vissing H.; RT "Isolation and fine mapping of 16 novel human zinc finger-encoding cDNAs RT identify putative candidate genes for developmental and malignant RT disorders."; RL Genomics 27:259-264(1995). RN [7] RP FUNCTION. RC TISSUE=Cervix carcinoma; RX PubMed=9308237; DOI=10.1007/978-3-642-60801-8_14; RA Schneider A., Peukert K., Eilers M., Haenel F.; RT "Association of Myc with the zinc-finger protein Miz-1 defines a novel RT pathway for gene regulation by Myc."; RL Curr. Top. Microbiol. Immunol. 224:137-146(1997). RN [8] RP INTERACTION WITH HCFC1. RX PubMed=12244100; DOI=10.1074/jbc.m206226200; RA Piluso D., Bilan P., Capone J.P.; RT "Host cell factor-1 interacts with and antagonizes transactivation by the RT cell cycle regulatory factor Miz-1."; RL J. Biol. Chem. 277:46799-46808(2002). RN [9] RP INTERACTION WITH MYC. RX PubMed=12545156; DOI=10.1038/sj.onc.1206145; RA Wu S., Cetinkaya C., Munoz-Alonso M.J., von der Lehr N., Bahram F., RA Beuger V., Eilers M., Leon J., Larsson L.-G.; RT "Myc represses differentiation-induced p21CIP1 expression via Miz-1- RT dependent interaction with the p21 core promoter."; RL Oncogene 22:351-360(2003). RN [10] RP INTERACTION WITH MAGEA4, AND SUBCELLULAR LOCATION. RX PubMed=14739298; DOI=10.1074/jbc.m310437200; RA Sakurai T., Itoh K., Higashitsuji H., Nagao T., Nonoguchi K., Chiba T., RA Fujita J.; RT "A cleaved form of MAGE-A4 binds to Miz-1 and induces apoptosis in human RT cells."; RL J. Biol. Chem. 279:15505-15514(2004). RN [11] RP INTERACTION WITH TMPRSS11A. RX PubMed=15095404; DOI=10.1002/jcb.20025; RA Zhao N., Wang J., Cui Y., Guo L., Lu S.-H.; RT "Induction of G1 cell cycle arrest and P15INK4b expression by ECRG1 through RT interaction with Miz-1."; RL J. Cell. Biochem. 92:65-76(2004). RN [12] RP FUNCTION IN CELL CYCLE ARREST, INTERACTION WITH BCL6, AND TISSUE RP SPECIFICITY. RX PubMed=16142238; DOI=10.1038/ni1245; RA Phan R.T., Saito M., Basso K., Niu H., Dalla-Favera R.; RT "BCL6 interacts with the transcription factor Miz-1 to suppress the cyclin- RT dependent kinase inhibitor p21 and cell cycle arrest in germinal center B RT cells."; RL Nat. Immunol. 6:1054-1060(2005). RN [13] RP FUNCTION. RX PubMed=19164764; DOI=10.1073/pnas.0804863106; RA Basu S., Liu Q., Qiu Y., Dong F.; RT "Gfi-1 represses CDKN2B encoding p15INK4B through interaction with Miz-1."; RL Proc. Natl. Acad. Sci. U.S.A. 106:1433-1438(2009). RN [14] 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [16] RP FUNCTION, AND INTERACTION WITH ZBTB49. RX PubMed=25245946; DOI=10.1093/nar/gku857; RA Jeon B.N., Kim M.K., Yoon J.H., Kim M.Y., An H., Noh H.J., Choi W.I., RA Koh D.I., Hur M.W.; RT "Two ZNF509 (ZBTB49) isoforms induce cell-cycle arrest by activating RT transcription of p21/CDKN1A and RB upon exposure to genotoxic stress."; RL Nucleic Acids Res. 42:11447-11461(2014). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-115, AND SUBUNIT. RX PubMed=17880999; DOI=10.1016/j.jmb.2007.08.026; RA Stead M.A., Trinh C.H., Garnett J.A., Carr S.B., Baron A.J., Edwards T.A., RA Wright S.C.; RT "A beta-sheet interaction interface directs the tetramerisation of the Miz- RT 1 POZ domain."; RL J. Mol. Biol. 373:820-826(2007). CC -!- FUNCTION: Transcription factor that can function as an activator or CC repressor depending on its binding partners, and by targeting negative CC regulators of cell cycle progression. Plays a critical role in early CC lymphocyte development, where it is essential to prevent apoptosis in CC lymphoid precursors, allowing them to survive in response to IL7 and CC undergo proper lineage commitment. Has been shown to bind to the CC promoters of adenovirus major late protein and cyclin D1 and activate CC transcription. Required for early embryonic development during CC gastrulation. Represses RB1 transcription; this repression can be CC blocked by interaction with ZBTB49 isoform 3/ZNF509S1 CC (PubMed:25245946). {ECO:0000269|PubMed:16142238, CC ECO:0000269|PubMed:19164764, ECO:0000269|PubMed:25245946, CC ECO:0000269|PubMed:9308237, ECO:0000269|PubMed:9312026}. CC -!- SUBUNIT: Homooligomerizes (via the BTB/POZ domain), multimerization is CC required for DNA binding. Interacts (via the C-terminal zinc fingers) CC with GIF1; the interaction results in the recruitment of MYB to the CC CDKN1A/p21 and CDKN1B promoters and repression of transcription. CC Interacts with TRAF2, interfering with the binding of UBC13 to TRAF2, CC and inhibiting TRAF2 E3 ligase activity. Interacts with MYC (via the C- CC terminal helix-loop-helix motif); the interaction inhibits ZBTB17 CC transactivation and growth arrest activities and renders it insoluble CC in the nucleus. Also interacts with HCFC1, MAGEA4 and TMPRSS11A. CC Interacts with BCL6; the interaction inhibits ZBTB17 transactivation CC activity on target genes involved in cell cycle arrest. Interacts with CC ZBTB49 isoform 3/ZNF509S1; this interaction blocks ZBTB17-mediated CC repression of RB1 (PubMed:25245946). {ECO:0000269|PubMed:12244100, CC ECO:0000269|PubMed:12545156, ECO:0000269|PubMed:14739298, CC ECO:0000269|PubMed:15095404, ECO:0000269|PubMed:16142238, CC ECO:0000269|PubMed:17880999, ECO:0000269|PubMed:25245946, CC ECO:0000269|PubMed:9312026}. CC -!- INTERACTION: CC Q13105; P51610: HCFC1; NbExp=9; IntAct=EBI-372156, EBI-396176; CC Q13105; P43358: MAGEA4; NbExp=5; IntAct=EBI-372156, EBI-743122; CC Q13105; P01106: MYC; NbExp=9; IntAct=EBI-372156, EBI-447544; CC Q13105; P04198: MYCN; NbExp=3; IntAct=EBI-372156, EBI-878369; CC Q13105; Q92547: TOPBP1; NbExp=2; IntAct=EBI-372156, EBI-308302; CC Q13105; Q96BR9: ZBTB8A; NbExp=3; IntAct=EBI-372156, EBI-742740; CC Q13105-1; Q07120: Gfi1; Xeno; NbExp=2; IntAct=EBI-15753185, EBI-4289236; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14739298, CC ECO:0000269|PubMed:9312026}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q13105-1; Sequence=Displayed; CC Name=2; CC IsoId=Q13105-2; Sequence=VSP_013424; CC Name=3; CC IsoId=Q13105-3; Sequence=VSP_044564; CC -!- TISSUE SPECIFICITY: Expressed in germinal center B-cells. CC {ECO:0000269|PubMed:16142238}. CC -!- PTM: Undergoes 'Lys-48'-linked polyubiquitination at Lys-397 and Lys- CC 481 and subsequent proteasomal degradation in a TRAF2-dependent manner. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. {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; Y09723; CAA70889.1; -; mRNA. DR EMBL; AK301896; BAG63326.1; -; mRNA. DR EMBL; AL034555; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL355994; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC126163; AAI26164.1; -; mRNA. DR EMBL; BC143965; AAI43966.1; -; mRNA. DR EMBL; M88369; AAA61327.1; -; Genomic_DNA. DR EMBL; U20647; AAC50256.1; -; mRNA. DR CCDS; CCDS165.1; -. [Q13105-1] DR CCDS; CCDS55576.1; -. [Q13105-3] DR CCDS; CCDS72712.1; -. [Q13105-2] DR PIR; D45193; D45193. DR PIR; I38940; I38940. DR RefSeq; NP_001229813.1; NM_001242884.1. [Q13105-3] DR RefSeq; NP_001274532.1; NM_001287603.1. [Q13105-2] DR RefSeq; NP_003434.2; NM_003443.2. [Q13105-1] DR RefSeq; XP_011540390.1; XM_011542088.1. [Q13105-3] DR PDB; 2LVR; NMR; -; A=500-581. DR PDB; 2LVT; NMR; -; A=500-581. DR PDB; 2LVU; NMR; -; A=500-581. DR PDB; 2M0D; NMR; -; A=416-526. DR PDB; 2M0E; NMR; -; A=416-526. DR PDB; 2M0F; NMR; -; A=416-526. DR PDB; 2N25; NMR; -; A=304-414. DR PDB; 2N26; NMR; -; A=304-414. DR PDB; 2Q81; X-ray; 2.10 A; A/B/C/D=2-115. DR PDB; 3M52; X-ray; 2.59 A; A/B=1-115. DR PDB; 4U2M; X-ray; 2.23 A; A/B/C/D=2-115. DR PDB; 4U2N; X-ray; 2.30 A; A/B=2-115. DR PDB; 5ION; NMR; -; A=714-742. DR PDBsum; 2LVR; -. DR PDBsum; 2LVT; -. DR PDBsum; 2LVU; -. DR PDBsum; 2M0D; -. DR PDBsum; 2M0E; -. DR PDBsum; 2M0F; -. DR PDBsum; 2N25; -. DR PDBsum; 2N26; -. DR PDBsum; 2Q81; -. DR PDBsum; 3M52; -. DR PDBsum; 4U2M; -. DR PDBsum; 4U2N; -. DR PDBsum; 5ION; -. DR SMR; Q13105; -. DR BioGRID; 113503; 33. DR CORUM; Q13105; -. DR DIP; DIP-5968N; -. DR IntAct; Q13105; 24. DR MINT; Q13105; -. DR STRING; 9606.ENSP00000364885; -. DR iPTMnet; Q13105; -. DR PhosphoSitePlus; Q13105; -. DR BioMuta; ZBTB17; -. DR DMDM; 62906906; -. DR EPD; Q13105; -. DR jPOST; Q13105; -. DR MassIVE; Q13105; -. DR MaxQB; Q13105; -. DR PaxDb; Q13105; -. DR PeptideAtlas; Q13105; -. DR PRIDE; Q13105; -. DR ProteomicsDB; 26435; -. DR ProteomicsDB; 59155; -. [Q13105-1] DR ProteomicsDB; 59156; -. [Q13105-2] DR Antibodypedia; 904; 133 antibodies. DR Ensembl; ENST00000375733; ENSP00000364885; ENSG00000116809. [Q13105-2] DR Ensembl; ENST00000375743; ENSP00000364895; ENSG00000116809. [Q13105-1] DR Ensembl; ENST00000537142; ENSP00000438529; ENSG00000116809. [Q13105-3] DR GeneID; 7709; -. DR KEGG; hsa:7709; -. DR UCSC; uc001axl.5; human. [Q13105-1] DR CTD; 7709; -. DR DisGeNET; 7709; -. DR EuPathDB; HostDB:ENSG00000116809.11; -. DR GeneCards; ZBTB17; -. DR HGNC; HGNC:12936; ZBTB17. DR HPA; ENSG00000116809; Low tissue specificity. DR MIM; 604084; gene. DR neXtProt; NX_Q13105; -. DR OpenTargets; ENSG00000116809; -. DR PharmGKB; PA37522; -. DR eggNOG; KOG1721; Eukaryota. DR eggNOG; COG5048; LUCA. DR GeneTree; ENSGT00940000159957; -. DR HOGENOM; CLU_002678_30_1_1; -. DR InParanoid; Q13105; -. DR KO; K10500; -. DR OMA; CSAYQSM; -. DR PhylomeDB; Q13105; -. DR TreeFam; TF332047; -. DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes. DR SIGNOR; Q13105; -. DR BioGRID-ORCS; 7709; 566 hits in 809 CRISPR screens. DR ChiTaRS; ZBTB17; human. DR EvolutionaryTrace; Q13105; -. DR GeneWiki; ZBTB17; -. DR GenomeRNAi; 7709; -. DR Pharos; Q13105; Tbio. DR PRO; PR:Q13105; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q13105; protein. DR Bgee; ENSG00000116809; Expressed in tendon of biceps brachii and 200 other tissues. DR ExpressionAtlas; Q13105; baseline and differential. DR Genevisible; Q13105; HS. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA. DR GO; GO:0032993; C:protein-DNA complex; IMP:CAFA. DR GO; GO:0001047; F:core promoter binding; IDA:CAFA. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IMP:NTNU_SB. DR GO; GO:0001223; F:transcription coactivator binding; IPI:CAFA. DR GO; GO:0008134; F:transcription factor binding; IPI:CAFA. DR GO; GO:0007398; P:ectoderm development; IEA:Ensembl. DR GO; GO:0001702; P:gastrulation with mouth forming second; IEA:Ensembl. DR GO; GO:0036498; P:IRE1-mediated unfolded protein response; TAS:Reactome. DR GO; GO:0045786; P:negative regulation of cell cycle; TAS:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:CAFA. DR GO; GO:0071158; P:positive regulation of cell cycle arrest; IDA:CAFA. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR InterPro; IPR000210; BTB/POZ_dom. DR InterPro; IPR011333; SKP1/BTB/POZ_sf. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR Pfam; PF00651; BTB; 1. DR Pfam; PF00096; zf-C2H2; 9. DR SMART; SM00225; BTB; 1. DR SMART; SM00355; ZnF_C2H2; 13. DR SUPFAM; SSF54695; SSF54695; 1. DR SUPFAM; SSF57667; SSF57667; 9. DR PROSITE; PS50097; BTB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 13. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Developmental protein; DNA-binding; KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Transcription; Transcription regulation; KW Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..803 FT /note="Zinc finger and BTB domain-containing protein 17" FT /id="PRO_0000047730" FT DOMAIN 1..104 FT /note="BTB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037" FT ZN_FING 306..328 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 334..356 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 362..384 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 390..412 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 418..440 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 446..468 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 474..496 FT /note="C2H2-type 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 502..524 FT /note="C2H2-type 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 530..552 FT /note="C2H2-type 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 558..580 FT /note="C2H2-type 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 586..608 FT /note="C2H2-type 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 614..637 FT /note="C2H2-type 12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 717..739 FT /note="C2H2-type 13" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 269..308 FT /note="Interaction with MYC" FT REGION 637..803 FT /note="Interaction with HCFC1" FT /evidence="ECO:0000269|PubMed:12244100" FT REGION 637..718 FT /note="Interaction with MYC" FT MOD_RES 120 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163" FT CROSSLNK 397 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:Q60821" FT CROSSLNK 481 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:Q60821" FT VAR_SEQ 1..131 FT /note="MDFPQHSQHVLEQLNQQRQLGLLCDCTFVVDGVHFKAHKAVLAACSEYFKML FT FVDQKDVVHLDISNAAGLGQVLEFMYTAKLSLSPENVDDVLAVATFLQMQDIITACHAL FT KSLAEPATSPGGNAEALATE -> MMCWPWPLSSKCRTSSRPAMPSSHLLSRLPALGEM FT RRPWPQKVCPVPSP (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044564" FT VAR_SEQ 679 FT /note="T -> TGPATLPA (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_013424" FT CONFLICT 73 FT /note="V -> M (in Ref. 1; CAA70889)" FT /evidence="ECO:0000305" FT CONFLICT 334 FT /note="F -> S (in Ref. 2; BAG63326)" FT /evidence="ECO:0000305" FT HELIX 3..20 FT /evidence="ECO:0000244|PDB:2Q81" FT TURN 21..23 FT /evidence="ECO:0000244|PDB:4U2M" FT STRAND 26..30 FT /evidence="ECO:0000244|PDB:2Q81" FT STRAND 33..37 FT /evidence="ECO:0000244|PDB:2Q81" FT HELIX 39..45 FT /evidence="ECO:0000244|PDB:2Q81" FT HELIX 47..55 FT /evidence="ECO:0000244|PDB:2Q81" FT HELIX 56..58 FT /evidence="ECO:0000244|PDB:3M52" FT HELIX 59..64 FT /evidence="ECO:0000244|PDB:2Q81" FT HELIX 67..79 FT /evidence="ECO:0000244|PDB:2Q81" FT STRAND 80..84 FT /evidence="ECO:0000244|PDB:4U2M" FT TURN 86..88 FT /evidence="ECO:0000244|PDB:2Q81" FT HELIX 89..98 FT /evidence="ECO:0000244|PDB:2Q81" FT HELIX 102..112 FT /evidence="ECO:0000244|PDB:2Q81" FT TURN 337..339 FT /evidence="ECO:0000244|PDB:2N25" FT STRAND 342..344 FT /evidence="ECO:0000244|PDB:2N25" FT HELIX 348..356 FT /evidence="ECO:0000244|PDB:2N25" FT TURN 365..367 FT /evidence="ECO:0000244|PDB:2N26" FT STRAND 370..373 FT /evidence="ECO:0000244|PDB:2N26" FT HELIX 374..384 FT /evidence="ECO:0000244|PDB:2N26" FT TURN 393..395 FT /evidence="ECO:0000244|PDB:2N26" FT STRAND 398..401 FT /evidence="ECO:0000244|PDB:2N26" FT HELIX 402..409 FT /evidence="ECO:0000244|PDB:2N26" FT TURN 421..423 FT /evidence="ECO:0000244|PDB:2M0D" FT STRAND 426..428 FT /evidence="ECO:0000244|PDB:2M0D" FT HELIX 430..438 FT /evidence="ECO:0000244|PDB:2M0D" FT TURN 457..459 FT /evidence="ECO:0000244|PDB:2M0E" FT HELIX 460..469 FT /evidence="ECO:0000244|PDB:2M0E" FT TURN 477..479 FT /evidence="ECO:0000244|PDB:2M0F" FT STRAND 482..484 FT /evidence="ECO:0000244|PDB:2M0F" FT HELIX 486..497 FT /evidence="ECO:0000244|PDB:2M0F" FT TURN 505..507 FT /evidence="ECO:0000244|PDB:2LVR" FT STRAND 510..512 FT /evidence="ECO:0000244|PDB:2LVR" FT HELIX 514..525 FT /evidence="ECO:0000244|PDB:2LVR" FT TURN 533..535 FT /evidence="ECO:0000244|PDB:2LVT" FT STRAND 538..541 FT /evidence="ECO:0000244|PDB:2LVT" FT HELIX 542..553 FT /evidence="ECO:0000244|PDB:2LVT" FT TURN 561..563 FT /evidence="ECO:0000244|PDB:2LVU" FT HELIX 570..578 FT /evidence="ECO:0000244|PDB:2LVU" FT STRAND 717..719 FT /evidence="ECO:0000244|PDB:5ION" FT TURN 720..723 FT /evidence="ECO:0000244|PDB:5ION" FT STRAND 724..727 FT /evidence="ECO:0000244|PDB:5ION" FT HELIX 729..740 FT /evidence="ECO:0000244|PDB:5ION" SQ SEQUENCE 803 AA; 87928 MW; C159D177C8A2D4A3 CRC64; MDFPQHSQHV LEQLNQQRQL GLLCDCTFVV DGVHFKAHKA VLAACSEYFK MLFVDQKDVV HLDISNAAGL GQVLEFMYTA KLSLSPENVD DVLAVATFLQ MQDIITACHA LKSLAEPATS PGGNAEALAT EGGDKRAKEE KVATSTLSRL EQAGRSTPIG PSRDLKEERG GQAQSAASGA EQTEKADAPR EPPPVELKPD PTSGMAAAEA EAALSESSEQ EMEVEPARKG EEEQKEQEEQ EEEGAGPAEV KEEGSQLENG EAPEENENEE SAGTDSGQEL GSEARGLRSG TYGDRTESKA YGSVIHKCED CGKEFTHTGN FKRHIRIHTG EKPFSCRECS KAFSDPAACK AHEKTHSPLK PYGCEECGKS YRLISLLNLH KKRHSGEARY RCEDCGKLFT TSGNLKRHQL VHSGEKPYQC DYCGRSFSDP TSKMRHLETH DTDKEHKCPH CDKKFNQVGN LKAHLKIHIA DGPLKCRECG KQFTTSGNLK RHLRIHSGEK PYVCIHCQRQ FADPGALQRH VRIHTGEKPC QCVMCGKAFT QASSLIAHVR QHTGEKPYVC ERCGKRFVQS SQLANHIRHH DNIRPHKCSV CSKAFVNVGD LSKHIIIHTG EKPYLCDKCG RGFNRVDNLR SHVKTVHQGK AGIKILEPEE GSEVSVVTVD DMVTLATEAL AATAVTQLTV VPVGAAVTAD ETEVLKAEIS KAVKQVQEED PNTHILYACD SCGDKFLDAN SLAQHVRIHT AQALVMFQTD ADFYQQYGPG GTWPAGQVLQ AGELVFRPRD GAEGQPALAE TSPTAPECPP PAE //