Zinc finger and BTB domain-containing protein 16

Zinc finger and BTB domain containing 16

PDB rendering based on 1buo.

Available structures
PDB	1BUO, 1CS3

Identifiers

Symbols

ZBTB16; PLZF; ZNF145

External IDs

OMIM: 176797 MGI: 103222 HomoloGene: 21214 GeneCards: ZBTB16 Gene

Gene Ontology
Molecular function	• DNA binding • DNA binding • double-stranded DNA binding • sequence-specific DNA binding transcription factor activity • protein binding • protein C-terminus binding • zinc ion binding • protein domain specific binding • identical protein binding • protein homodimerization activity • metal ion binding
Cellular component	• intracellular • nucleus • cytosol • plasma membrane • nuclear body • PML body • nuclear speck • transcriptional repressor complex
Biological process	• mesonephros development • apoptosis • central nervous system development • hemopoiesis • hemopoiesis • myeloid cell differentiation • protein localization to nucleus • embryonic hindlimb morphogenesis • embryonic digit morphogenesis • negative regulation of myeloid cell differentiation • negative regulation of transcription, DNA-dependent • negative regulation of transcription, DNA-dependent
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

n/a

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 11:
113.93 – 114.12 Mb

Chr 9:
48.46 – 48.64 Mb

PubMed search

[1]

[2]

Zinc finger and BTB domain-containing protein 16 is a protein that in humans is encoded by the ZBTB16 gene.

1 Function
2 Interactions
3 See also
4 References
5 Further reading
6 External links

Function

This gene is a member of the Krueppel C2H2-type zinc-finger protein family and encodes a zinc finger transcription factor that contains nine Kruppel-type zinc finger domains at the carboxyl terminus. This protein is located in the nucleus, is involved in cell cycle progression, and interacts with a histone deacetylase. Specific instances of aberrant gene rearrangement at this locus have been associated with acute promyelocytic leukemia (APL)^[1] and physiological roles have been identified in mouse Natural Killer T cells^[2]^[3] and gamma-delta T cells.^[4] Alternate transcriptional splice variants have been characterized in human.^[5]^[6]

Interactions

Zinc finger and BTB domain-containing protein 16 has been shown to interact with ZBTB32,^[7] Heparin-binding EGF-like growth factor,^[8]^[9] Histone deacetylase 5,^[10]^[11] HDAC6,^[10] FHL2,^[12] SIN3B,^[13] Nuclear receptor co-repressor 2,^[14]^[15]^[16] Angiotensin II receptor type 1,^[17] HDAC1,^[10]^[13]^[15] Retinoic acid receptor alpha,^[18] SIN3A,^[13]^[15]^[19] BCL6,^[20] RUNX1T1,^[21]^[22] HDAC4,^[10]^[11] BMI1,^[23] GATA1,^[24] GATA2,^[25] Promyelocytic leukemia protein^[26] and Calcitriol receptor.^[19]^[27]

References

^ Chen, Zhu; Brand, Nigel J.; Chen, Alex; Chen, Sai-Juan; Tong, Jian-Hua; Wang, Zhen-Yi; Waxman, Samuel; Zelent, Arthur (1993). "Fusion between a novel Krüppel-like zinc finger gene and the retinoic acid receptor-alpha locus due to a variant t(11;17) translocation associated with acute promyelocytic leukaemia". The EMBO journal 12 (3): 1161–7. PMC 413318. PMID 8384553. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=413318.
^ Kovalovsky, Damian; Uche, Olisambu U.; Eladad, Sonia; Hobbs, Robin M.; Yi, Woelsung; Alonzo, Eric; Chua, Kevin; Eidson, Maggie et al. (2008). "The BTB-zinc finger transcriptional regulator, PLZF, controls the development of iNKT cell effector functions". Nature Immunology 9 (9): 1055–64. doi:10.1038/ni.1641. PMC 2662733. PMID 18660811. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2662733.
^ Savage, Adam K.; Constantinides, Michael G.; Han, Jin; Picard, Damien; Martin, Emmanuel; Li, Bofeng; Lantz, Olivier; Bendelac, Albert (2008). "The transcription factor PLZF (Zbtb16) directs the effector program of the NKT cell lineage". Immunity 29 (3): 391–403. doi:10.1016/j.immuni.2008.07.011. PMC 2613001. PMID 18703361. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2613001.
^ Kreslavsky, Taras; Savage, Adam K.; Hobbs, Robin; Gounari, Fotini; Bronson, Roderick; Pereira, Pablo; Pandolfi, Pier Paolo; Bendelac, Albert et al. (2009). "TCR-inducible PLZF transcription factor required for innate phenotype of a subset of γδ T cells with restricted TCR diversity". Proceedings of the National Academy of Sciences of the United States of America 106 (30): 12453–8. doi:10.1073/pnas.0903895106. PMC 2718370. PMID 19617548. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2718370.
^ Zhang, T.; Xiong, H.; Kan, L.-X.; Zhang, C.-K.; Jiao, X.-F.; Fu, G.; Zhang, Q.-H.; Lu, L. et al. (1999). "Genomic sequence, structural organization, molecular evolution, and aberrant rearrangement of promyelocytic leukemia zinc finger gene". Proceedings of the National Academy of Sciences of the United States of America 96 (20): 11422–7. doi:10.1073/pnas.96.20.11422. PMC 18049. PMID 10500192. http://www.pnas.org/content/96/20/11422.full.
^ "ZBTB16 zinc finger and BTB domain containing 16". Entrez. 4 October 2009. http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7704. Retrieved 10 October 2009.
^ Hoatlin, Maureen E.; Zhi, Yu; Ball, Helen; Silvey, Kirsten; Melnick, Ari; Stone, Stacie; Arai, Sally; Hawe, Nicola et al. (1999). "A novel BTB/POZ transcriptional repressor protein interacts with the Fanconi anemia group C protein and PLZF". Blood 94 (11): 3737–47. PMID 10572087. http://bloodjournal.hematologylibrary.org/cgi/content/full/94/11/3737.
^ Nanba, Daisuke; Mammoto, Akiko; Hashimoto, Koji; Higashiyama, Shigeki (2003). "Proteolytic release of the carboxy-terminal fragment of proHB-EGF causes nuclear export of PLZF". The Journal of cell biology 163 (3): 489–502. doi:10.1083/jcb.200303017. PMC 2173632. PMID 14597771. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2173632.
^ Nanba, D; Toki, F; Higashiyama, S (2004). "Roles of charged amino acid residues in the cytoplasmic domain of proHB-EGF". Biochemical and biophysical research communications 320 (2): 376–82. doi:10.1016/j.bbrc.2004.05.176. PMID 15219838.
^ ^a ^b ^c ^d Chauchereau, A; Mathieu, M; De Saintignon, J; Ferreira, R; Pritchard, LL; Mishal, Z; Dejean, A; Harel-bellan, A (2004). "HDAC4 mediates transcriptional repression by the acute promyelocytic leukaemia-associated protein PLZF". Oncogene 23 (54): 8777–84. doi:10.1038/sj.onc.1208128. PMID 15467736.
^ ^a ^b Lemercier, C; Brocard, MP; Puvion-dutilleul, F; Kao, HY; Albagli, O; Khochbin, S (2002). "Class II histone deacetylases are directly recruited by BCL6 transcriptional repressor". The Journal of biological chemistry 277 (24): 22045–52. doi:10.1074/jbc.M201736200. PMID 11929873.
^ McLoughlin, P; Ehler, E; Carlile, G; Licht, JD; Schäfer, BW (2002). "The LIM-only protein DRAL/FHL2 interacts with and is a corepressor for the promyelocytic leukemia zinc finger protein". The Journal of biological chemistry 277 (40): 37045–53. doi:10.1074/jbc.M203336200. PMID 12145280.
^ ^a ^b ^c David, G; Alland, L; Hong, SH; Wong, CW; Depinho, RA; Dejean, A (1998). "Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein". Oncogene 16 (19): 2549–56. doi:10.1038/sj.onc.1202043. PMID 9627120.
^ Takahashi, S; McConnell, MJ; Harigae, H; Kaku, M; Sasaki, T; Melnick, AM; Licht, JD (2004). "The Flt3 internal tandem duplication mutant inhibits the function of transcriptional repressors by blocking interactions with SMRT". Blood 103 (12): 4650–8. doi:10.1182/blood-2003-08-2759. PMID 14982881.
^ ^a ^b ^c Wong, CW; Privalsky, ML (1998). "Components of the SMRT corepressor complex exhibit distinctive interactions with the POZ domain oncoproteins PLZF, PLZF-RARalpha, and BCL-6". The Journal of biological chemistry 273 (42): 27695–702. doi:10.1074/jbc.273.42.27695. PMID 9765306.
^ Hong, SH; David, G; Wong, CW; Dejean, A; Privalsky, ML (1997). "SMRT corepressor interacts with PLZF and with the PML-retinoic acid receptor α (RARα) and PLZF-RARα oncoproteins associated with acute promyelocytic leukemia". Proceedings of the National Academy of Sciences of the United States of America 94 (17): 9028–33. doi:10.1073/pnas.94.17.9028. PMC 23013. PMID 9256429. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=23013.
^ Senbonmatsu, T; Saito, T; Landon, EJ; Watanabe, O; Price Jr, E; Roberts, RL; Imboden, H; Fitzgerald, TG et al. (2003). "A novel angiotensin II type 2 receptor signaling pathway: possible role in cardiac hypertrophy". The EMBO journal 22 (24): 6471–82. doi:10.1093/emboj/cdg637. PMC 291832. PMID 14657020. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=291832.
^ Martin, PJ; Delmotte, MH; Formstecher, P; Lefebvre, P (2003). "PLZF is a negative regulator of retinoic acid receptor transcriptional activity". Nuclear receptor 1 (1): 6. doi:10.1186/1478-1336-1-6. PMC 212040. PMID 14521715. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=212040.
^ ^a ^b Ward, JO; McConnell, MJ; Carlile, GW; Pandolfi, PP; Licht, JD; Freedman, LP (2001). "The acute promyelocytic leukemia-associated protein, promyelocytic leukemia zinc finger, regulates 1,25-dihydroxyvitamin D(3)-induced monocytic differentiation of U937 cells through a physical interaction with vitamin D(3) receptor". Blood 98 (12): 3290–300. doi:10.1182/blood.V98.12.3290. PMID 11719366.
^ Dhordain, P; Albagli, O; Honore, N; Guidez, F; Lantoine, D; Schmid, M; The, HD; Zelent, A et al. (2000). "Colocalization and heteromerization between the two human oncogene POZ/zinc finger proteins, LAZ3 (BCL6) and PLZF". Oncogene 19 (54): 6240–50. doi:10.1038/sj.onc.1203976. PMID 11175338.
^ Melnick, AM; Westendorf, JJ; Polinger, A; Carlile, GW; Arai, S; Ball, HJ; Lutterbach, B; Hiebert, SW et al. (2000). "The ETO Protein Disrupted in t(8;21)-Associated Acute Myeloid Leukemia Is a Corepressor for the Promyelocytic Leukemia Zinc Finger Protein". Molecular and cellular biology 20 (6): 2075–86. doi:10.1128/MCB.20.6.2075-2086.2000. PMC 110824. PMID 10688654. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=110824.
^ Melnick, A; Carlile, GW; McConnell, MJ; Polinger, A; Hiebert, SW; Licht, JD (2000). "AML-1/ETO fusion protein is a dominant negative inhibitor of transcriptional repression by the promyelocytic leukemia zinc finger protein". Blood 96 (12): 3939–47. PMID 11090081.
^ Barna, M; Merghoub, T; Costoya, JA; Ruggero, D; Branford, M; Bergia, A; Samori, B; Pandolfi, PP (2002). "Plzf mediates transcriptional repression of HoxD gene expression through chromatin remodeling". Developmental cell 3 (4): 499–510. doi:10.1016/S1534-5807(02)00289-7. PMID 12408802.
^ Labbaye, C; Quaranta, MT; Pagliuca, A; Militi, S; Licht, JD; Testa, U; Peschle, C (2002). "PLZF induces megakaryocytic development, activates Tpo receptor expression and interacts with GATA1 protein". Oncogene 21 (43): 6669–79. doi:10.1038/sj.onc.1205884. PMID 12242665.
^ Tsuzuki, S; Enver, T (2002). "Interactions of GATA-2 with the promyelocytic leukemia zinc finger (PLZF) protein, its homologue FAZF, and the t(11;17)-generated PLZF-retinoic acid receptor alpha oncoprotein". Blood 99 (9): 3404–10. doi:10.1182/blood.V99.9.3404. PMID 11964310.
^ Koken, MH; Reid, A; Quignon, F; Chelbi-alix, MK; Davies, JM; Kabarowski, JH; Zhu, J; Dong, S et al. (1997). "Leukemia-associated retinoic acid receptor α fusion partners, PML and PLZF, heterodimerize and colocalize to nuclear bodies". Proceedings of the National Academy of Sciences of the United States of America 94 (19): 10255–60. doi:10.1073/pnas.94.19.10255. PMC 23349. PMID 9294197. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=23349.
^ Puccetti, E; Obradovic, D; Beissert, T; Bianchini, A; Washburn, B; Chiaradonna, F; Boehrer, S; Hoelzer, D et al. (2002). "AML-associated translocation products block vitamin D(3)-induced differentiation by sequestering the vitamin D(3) receptor". Cancer research 62 (23): 7050–8. PMID 12460926.

External links

MeSH ZBTB16+protein,+human

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

Transcription factors and intracellular receptors

(1) Basic domains

(1.1) Basic leucine zipper (bZIP)	Activating transcription factor (AATF, 1, 2, 3, 4, 5, 6, 7) · AP-1 (c-Fos, FOSB, FOSL1, FOSL2, JDP2, c-Jun, JUNB, JUND) · BACH (1, 2) · BATF · BLZF1 · C/EBP (α, β, γ, δ, ε, ζ) · CREB (1, 3, L1) · CREM · DBP · DDIT3 · GABPA · HLF · MAF (B, F, G, K) · NFE (2, L1, L2, L3) · NFIL3 · NRL · NRF (1, 2, 3) · XBP1

(1.2) Basic helix-loop-helix (bHLH)	ATOH1 · AhR · AHRR · ARNT · ASCL1 · BHLHB2 · BMAL (ARNTL, ARNTL2) · CLOCK · EPAS1 · FIGLA · HAND (1, 2) · HES (5, 6) · HEY (1, 2, L) · HES1 · HIF (1A, 3A) · ID (1, 2, 3, 4) · LYL1 · MESP2 · MXD4 · MYCL1 · MYCN · Myogenic regulatory factors (MyoD, Myogenin, MYF5, MYF6) · Neurogenins (1, 2, 3) · NeuroD (1, 2) · NPAS (1, 2, 3) · OLIG (1, 2) · Pho4 · Scleraxis · SIM (1, 2) · TAL (1, 2) · Twist · USF1

(1.3) bHLH-ZIP	AP-4 · MAX · MITF · MNT · MLX · MXI1 · Myc · SREBP (1, 2)

(1.4) NF-1	NFI (A, B, C, X) · SMAD (R-SMAD (1, 2, 3, 5, 9) - I-SMAD (6, 7) - 4)

(1.5) RF-X	RFX (1, 2, 3, 4, 5, ANK)

(1.6) Basic helix-span-helix (bHSH)	AP-2 (α, β, γ, δ, ε)

(2) Zinc finger DNA-binding domains

(2.1) Nuclear receptor (Cys₄)	subfamily 1 (Thyroid hormone (α, β), CAR, FXR, LXR (α, β), PPAR (α, β/δ, γ), PXR, RAR (α, β, γ), ROR (α, β, γ), Rev-ErbA (α, β), VDR) subfamily 2 (COUP-TF (I, II), Ear-2, HNF4 (α, γ), PNR, RXR (α, β, γ), Testicular receptor (2, 4), TLX) subfamily 3 (Steroid hormone (Androgen, Estrogen (α, β), Glucocorticoid, Mineralocorticoid, Progesterone), Estrogen related (α, β, γ)) subfamily 4 NUR (NGFIB, NOR1, NURR1) · subfamily 5 (LRH-1, SF1) · subfamily 6 (GCNF) · subfamily 0 (DAX1, SHP)

(2.2) Other Cys₄	GATA (1, 2, 3, 4, 5, 6) · MTA (1, 2, 3) · TRPS1

(2.3) Cys₂His₂	General transcription factors (TFIIA, TFIIB, TFIID, TFIIE (1, 2), TFIIF (1, 2), TFIIH (1, 2, 4, 2I, 3A, 3C1, 3C2)) ATBF1 · BCL (6, 11A, 11B) · CTCF · E4F1 · EGR (1, 2, 3, 4) · ERV3 · GFI1 · GLI-Krüppel family (1, 2, 3, REST, S2, YY1) · HIC (1, 2) · HIVEP (1, 2, 3) · IKZF (1, 2, 3) · ILF (2, 3) · KLF (2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 17) · MTF1 · MYT1 · OSR1 · PRDM9 · SALL (1, 2, 3, 4) · SP (1, 2, 4, 7, 8) · TSHZ3 · WT1 · Zbtb7 (7A, 7B) · ZBTB (16, 17, 20, 32, 33, 40) · zinc finger (3, 7, 9, 10, 19, 22, 24, 33B, 34, 35, 41, 43, 44, 51, 74, 143, 146, 148, 165, 202, 217, 219, 238, 239, 259, 267, 268, 281, 295, 300, 318, 330, 346, 350, 365, 366, 384, 423, 451, 452, 471, 593, 638, 644, 649, 655)

(2.4) Cys₆	HIVEP1

(2.5) Alternating composition	AIRE · DIDO1 · GRLF1 · ING (1, 2, 4) · JARID (1A, 1B, 1C, 1D, 2) · JMJD1B

(3) Helix-turn-helix domains

(3.1) Homeodomain	ARX · CDX (1, 2) · CRX · CUTL1 · DBX (1, 2) · DLX (3, 4, 5) · EMX2 · EN (1, 2) · FHL (1, 2, 3) · HESX1 · HHEX · HLX · Homeobox (A1, A2, A3, A4, A5, A7, A9, A10, A11, A13, B1, B2, B3, B4, B5, B6, B7, B8, B9, B13, C4, C5, C6, C8, C9, C10, C11, C12, C13, D1, D3, D4, D8, D9, D10, D11, D12, D13) · HOPX · IRX (1, 2, 3, 4, 5, 6, MKX) · LMX (1A, 1B) · MEIS (1, 2) · MEOX2 · MNX1 · MSX (1, 2) · NANOG · NKX (2-1, 2-2, 2-3, 2-5, 3-1, 3-2, 6-1, 6-2) · NOBOX · PBX (1, 2, 3) · PHF (1, 3, 6, 8, 10, 16, 17, 20, 21A) · PHOX (2A, 2B) · PITX (1, 2, 3) · POU domain (PIT-1, BRN-3: A, B, C, Octamer transcription factor: 1, 2, 3/4, 6, 7, 11) · OTX (1, 2) · PDX1 · SATB2 · SHOX2 · VAX1 · ZEB (1, 2)

(3.2) Paired box	PAX (1, 2, 3, 4, 5, 6, 7, 8, 9)

(3.3) Fork head / winged helix	E2F (1, 2, 3, 4, 5) · FOX proteins (A1, A2, A3, C1, C2, D3, D4, E1, E3, F1, G1, H1, I1, J1, J2, K1, K2, L2, M1, N1, N3, O1, O3, O4, P1, P2, P3, P4)

(3.4) Heat Shock Factors	HSF (1, 2, 4)

(3.5) Tryptophan clusters	ELF (2, 4, 5) · EGF · ELK (1, 3, 4) · ERF · ETS (1, 2, ERG, SPIB) · ETV (1, 4, 5, 6) · FLI1 · Interferon regulatory factors (1, 2, 3, 4, 5, 6, 7, 8) · MYB · MYBL2

(3.6) TEA domain	transcriptional enhancer factor (1, 2, 3, 4)

(4) β-Scaffold factors with minor groove contacts

(4.1) Rel homology region	NF-κB (NFKB1, NFKB2, REL, RELA, RELB) · NFAT (C1, C2, C3, C4, 5)

(4.2) STAT	STAT (1, 2, 3, 4, 5, 6)

(4.3) p53	p53 · TBX (1, 2, 3, 5, 19, 21, 22, Brachyury, TBR1, TBR2) · TP63

(4.4) MADS box	Mef2 (A, B, C, D) · SRF

(4.6) TATA binding proteins	TBP · TBPL1

(4.7) High-mobility group	BBX · HMGB (1, 2, 3, 4) · HMGN (1, 2, 3, 4) · HNF (1A, 1B) · LEF1 · SOX (1, 2, 3, 4, 5, 6, 8, 9, 10, 11, 12, 13, 14, 15, 18, 21) · SRY · SSRP1 · TCF (3, 4) · TOX (1, 2, 3, 4)

(4.10) Cold-shock domain	CSDA, YBX1

(4.11) Runt	CBF (CBFA2T2, CBFA2T3, RUNX1, RUNX2, RUNX3, RUNX1T1)

(0) Other transcription factors

(0.2) HMGI(Y)	HMGA (1, 2) · HBP1

(0.3) Pocket domain	Rb · RBL1 · RBL2

(0.5) AP-2/EREBP-related factors	Apetala 2 · EREBP · B3

(0.6) Miscellaneous	ARID (1A, 1B, 2, 3A, 3B, 4A) · CAP · IFI (16, 35) · MLL (2, 3, T1) · MNDA · NFY (A, B, C) · Rho/Sigma

see also transcription factor/coregulator deficiencies
B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)

Zinc finger and BTB domain-containing protein 16

Contents

Function

Interactions

See also

References

Further reading

External links