ZBT17_HUMAN
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 03-AUG-2022, entry version 217.
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; Q92870-2: APBB2; NbExp=3; IntAct=EBI-372156, EBI-21535880;
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}.
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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 PDB; 7AZW; X-ray; 2.10 A; A/B=1-115.
DR PDB; 7AZX; X-ray; 2.25 A; A/B=1-115.
DR PDB; 7MC1; NMR; -; A=556-639.
DR PDB; 7MC2; NMR; -; A=556-639.
DR PDB; 7MC3; NMR; -; A=556-639.
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 PDBsum; 7AZW; -.
DR PDBsum; 7AZX; -.
DR PDBsum; 7MC1; -.
DR PDBsum; 7MC2; -.
DR PDBsum; 7MC3; -.
DR AlphaFoldDB; Q13105; -.
DR SMR; Q13105; -.
DR BioGRID; 113503; 40.
DR CORUM; Q13105; -.
DR DIP; DIP-5968N; -.
DR IntAct; Q13105; 25.
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; 151 antibodies from 25 providers.
DR DNASU; 7709; -.
DR Ensembl; ENST00000375733.6; ENSP00000364885.2; ENSG00000116809.12. [Q13105-2]
DR Ensembl; ENST00000375743.9; ENSP00000364895.4; ENSG00000116809.12. [Q13105-1]
DR Ensembl; ENST00000537142.5; ENSP00000438529.1; ENSG00000116809.12. [Q13105-3]
DR GeneID; 7709; -.
DR KEGG; hsa:7709; -.
DR MANE-Select; ENST00000375743.9; ENSP00000364895.4; NM_003443.3; NP_003434.2.
DR UCSC; uc001axl.5; human. [Q13105-1]
DR CTD; 7709; -.
DR DisGeNET; 7709; -.
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 VEuPathDB; HostDB:ENSG00000116809; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000159957; -.
DR HOGENOM; CLU_002678_30_1_1; -.
DR InParanoid; Q13105; -.
DR OMA; DKGHKCP; -.
DR PhylomeDB; Q13105; -.
DR TreeFam; TF332047; -.
DR PathwayCommons; Q13105; -.
DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
DR SignaLink; Q13105; -.
DR SIGNOR; Q13105; -.
DR BioGRID-ORCS; 7709; 622 hits in 1146 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 lower esophagus mucosa and 174 other tissues.
DR ExpressionAtlas; Q13105; baseline and differential.
DR Genevisible; Q13105; HS.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0032993; C:protein-DNA complex; IMP:CAFA.
DR GO; GO:0001046; F:core promoter sequence-specific DNA 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:0140297; F:DNA-binding transcription factor binding; IPI:CAFA.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
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:0007398; P:ectoderm development; IEA:Ensembl.
DR GO; GO:0070314; P:G1 to G0 transition; IDA:CAFA.
DR GO; GO:0001702; P:gastrulation with mouth forming second; IEA:Ensembl.
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:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.710.10; -; 1.
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 116..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 REGION 779..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|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:0007829|PDB:2Q81"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:4U2M"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:2Q81"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:2Q81"
FT HELIX 39..45
FT /evidence="ECO:0007829|PDB:2Q81"
FT HELIX 47..55
FT /evidence="ECO:0007829|PDB:2Q81"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:3M52"
FT HELIX 59..64
FT /evidence="ECO:0007829|PDB:2Q81"
FT HELIX 67..79
FT /evidence="ECO:0007829|PDB:2Q81"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:4U2M"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:2Q81"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:2Q81"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:2Q81"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:2N25"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:2N25"
FT HELIX 348..356
FT /evidence="ECO:0007829|PDB:2N25"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:2N26"
FT STRAND 370..373
FT /evidence="ECO:0007829|PDB:2N26"
FT HELIX 374..384
FT /evidence="ECO:0007829|PDB:2N26"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:2N26"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:2N26"
FT HELIX 402..409
FT /evidence="ECO:0007829|PDB:2N26"
FT TURN 421..423
FT /evidence="ECO:0007829|PDB:2M0D"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:2M0D"
FT HELIX 430..438
FT /evidence="ECO:0007829|PDB:2M0D"
FT TURN 457..459
FT /evidence="ECO:0007829|PDB:2M0E"
FT HELIX 460..469
FT /evidence="ECO:0007829|PDB:2M0E"
FT TURN 477..479
FT /evidence="ECO:0007829|PDB:2M0F"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:2M0F"
FT HELIX 486..497
FT /evidence="ECO:0007829|PDB:2M0F"
FT TURN 505..507
FT /evidence="ECO:0007829|PDB:2LVR"
FT STRAND 510..512
FT /evidence="ECO:0007829|PDB:2LVR"
FT HELIX 514..525
FT /evidence="ECO:0007829|PDB:2LVR"
FT TURN 533..535
FT /evidence="ECO:0007829|PDB:2LVT"
FT STRAND 538..541
FT /evidence="ECO:0007829|PDB:2LVT"
FT HELIX 542..553
FT /evidence="ECO:0007829|PDB:2LVT"
FT TURN 561..563
FT /evidence="ECO:0007829|PDB:2LVU"
FT STRAND 566..568
FT /evidence="ECO:0007829|PDB:7MC1"
FT HELIX 570..578
FT /evidence="ECO:0007829|PDB:2LVU"
FT TURN 579..583
FT /evidence="ECO:0007829|PDB:7MC1"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:7MC2"
FT HELIX 589..591
FT /evidence="ECO:0007829|PDB:7MC2"
FT STRAND 593..595
FT /evidence="ECO:0007829|PDB:7MC2"
FT HELIX 598..608
FT /evidence="ECO:0007829|PDB:7MC2"
FT TURN 617..619
FT /evidence="ECO:0007829|PDB:7MC3"
FT STRAND 622..624
FT /evidence="ECO:0007829|PDB:7MC3"
FT HELIX 626..636
FT /evidence="ECO:0007829|PDB:7MC3"
FT STRAND 717..719
FT /evidence="ECO:0007829|PDB:5ION"
FT TURN 720..723
FT /evidence="ECO:0007829|PDB:5ION"
FT STRAND 724..727
FT /evidence="ECO:0007829|PDB:5ION"
FT HELIX 729..740
FT /evidence="ECO:0007829|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
