ZBTB1 (ZNF909) , Ryhmän C2H2 Znf proteiineja , 14q23.3) , ilmenee
luuytimessä, lymfasolmukkeessa ja 25 muussa kudoksessa
https://www.ncbi.nlm.nih.gov/protein/NP_001116801.1
https://www.ncbi.nlm.nih.gov/protein/NP_001116801.1
ORIGIN 1 makpshssyv lqqlnnqrew gflcdcciai ddiyfqahka vlaacssyfr mffmnhqhst 61 aqlnlsnmki saecfdlilq fmylgkimta pssfeqfkva mnylqlynvp dclediqdad 121 cssskcsssa sskqnskmif gvrmyedtva rngneanrwc aepsstvntp hnreadeesl 181 qlgnfpeplf dvckkssvsk lstpkervsr rfgrsftcds cgfgfscekl ldehvltctn 241 rhlyqntrsy hrivdirdgk dsnikaefge kdssktfsaq tdkyrgdtsq aaddsasttg 301 srksstvese iaseeksraa erkriiikme pediptdelk dfniikvtdk dcnestdnde 361 ledepeepfy ryyveedvsi kksgrktlkp rmsvsaderg glenmrppnn sspvqedaen 421 ascelcglti teedlsshyl akhienicac gkcgqilvkg rqlqehaqrc gepqdltmng 481 lgnteekmdl eenpdeqsei rdmfvemldd frdnhyqins iqkkqlfkhs acpfrcpncg 541 qrfetenlvv ehmsscldqd mfksaimeen erdhrrkhfc nlcgkgfyqr chlrehytvh 601 tkekqfvcqt cgkqflrerq lrlhndmhkg maryvcsicd qgnfrkhdhv rhmishlsag 661 eticqvcfqi fpnneqleqh mdvhlytcgi cgakfnlrkd mrshynakhl krt //
- Novel human BTB/POZ domain-containing zinc finger protein ZBTB1 inhibits transcriptional activities of CRE. Liu Q, et al. Mol Cell Biochem, 2011 Nov. PMID 21706167
- Transcription factor zinc finger and BTB domain 1 is essential for lymphocyte development. Punwani D, et al. J Immunol, 2012 Aug 1. PMID 22753936, Free PMC Article
- Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif. Matic I, et al. Mol Cell, 2010 Aug 27. PMID 20797634 Reversible protein modification by small ubiquitin-like modifiers (SUMOs) is critical for eukaryotic life. Mass spectrometry-based proteomics has proven effective at identifying hundreds of potential SUMO target proteins. However, direct identification of SUMO acceptor lysines in complex samples by mass spectrometry is still very challenging. We have developed a generic method for the identification of SUMO acceptor lysines in target proteins. We have identified 103 SUMO-2 acceptor lysines in endogenous target proteins. Of these acceptor lysines, 76 are situated in the SUMOylation consensus site [VILMFPC]KxE. Interestingly, eight sites fit the inverted SUMOylation consensus motif [ED]xK[VILFP]. In addition, we found direct mass spectrometric evidence for crosstalk between SUMOylation and phosphorylation with a preferred spacer between the SUMOylated lysine and the phosphorylated serine of four residues. In 16 proteins we identified a hydrophobic cluster SUMOylation motif (HCSM). SUMO conjugation of RanGAP1 and ZBTB1 via HCSMs is remarkably efficient.
- Functional screening of FxxLF-like peptide motifs identifies SMARCD1/BAF60a as an androgen receptor cofactor that modulates TMPRSS2 expression. van de Wijngaart DJ, et al. Mol Endocrinol, 2009 Nov. PMID 19762545, Free PMC Article
- EDAG positively regulates erythroid differentiation and modifies GATA1 acetylation through recruiting p300. Zheng WW, et al. Stem Cells, 2014 Aug. PMID 24740910
- ZBTB1 is required for localizing phospho-KAP-1 to chromatin and enhancing RAD18 accessibility during chromatin remodeling/DNA repair.
- ZBTB1 protein may act as a transcription repressor in the activation of CREB and cAMP-mediated signal transduction pathways to mediate cellular functions.
Mol Endocrinol. 2009 Nov;23(11):1776-86. doi: 10.1210/me.2008-0280. Epub 2009 Sep 17.
Functional screening of FxxLF-like peptide motifs identifies SMARCD1/BAF60a as an androgen receptor cofactor that modulates TMPRSS2 expression.van de Wijngaart DJ1, Dubbink HJ, Molier M, de Vos C, Trapman J, Jenster G. Abstract
Androgen
receptor (AR) transcriptional activity is tightly regulated by
interacting cofactors and cofactor complexes. The best described
cofactor interaction site in the AR is the hormone-induced coactivator
binding groove in the ligand-binding domain, which serves as a
high-affinity docking site for FxxLF-like motifs. This study aimed at
identifying novel AR cofactors by in silico selection and functional
screening of FxxLF-like peptide motifs.
Candidate interacting motifs were selected from a proteome-wide screening and from a supervised screening focusing on components of protein complexes involved in transcriptional regulation. Of the 104 peptides tested, 12 displayed moderate to strong in vivo hormone-dependent interactions with AR. For three of these, ZBTB16/PLZF, SMARCA4/BRG1, and SMARCD1/BAF60a, the full-length protein was tested for interaction with AR. Of these, BAF60a, a subunit of the SWI/SNF chromatin remodeling complex, displayed hormone-dependent interactions with AR through its FxxFF motif. Vice versa, recruitment of BAF60a by the AR required an intact coactivator groove. BAF60a depletion by small interfering RNA in LNCaP cells demonstrated differential effects on expression of endogenous AR target genes. AR-driven expression of TMPRSS2 was almost completely blocked by BAF60a small interfering RNA. In summary, our data demonstrate that BAF60a directly interacts with the coactivator groove in the AR ligand-binding domain via its FxxFF motif, thereby selectively activating specific AR-driven promoters.
Candidate interacting motifs were selected from a proteome-wide screening and from a supervised screening focusing on components of protein complexes involved in transcriptional regulation. Of the 104 peptides tested, 12 displayed moderate to strong in vivo hormone-dependent interactions with AR. For three of these, ZBTB16/PLZF, SMARCA4/BRG1, and SMARCD1/BAF60a, the full-length protein was tested for interaction with AR. Of these, BAF60a, a subunit of the SWI/SNF chromatin remodeling complex, displayed hormone-dependent interactions with AR through its FxxFF motif. Vice versa, recruitment of BAF60a by the AR required an intact coactivator groove. BAF60a depletion by small interfering RNA in LNCaP cells demonstrated differential effects on expression of endogenous AR target genes. AR-driven expression of TMPRSS2 was almost completely blocked by BAF60a small interfering RNA. In summary, our data demonstrate that BAF60a directly interacts with the coactivator groove in the AR ligand-binding domain via its FxxFF motif, thereby selectively activating specific AR-driven promoters.
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