Search Results

Overview

Uniprot ID	O95365
Protein Name	Zinc finger and BTB domain-containing protein 7A
Gene Name	ZBTB7A
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
383	IRAKAFQKCPICEKV
389	QKCPICEKVIQGAGK
396	KVIQGAGKLPRHIRT

Function

Transcription factor that represses the transcription of a wide range of genes involved in cell proliferation and differentiation (PubMed:14701838, PubMed:17595526, PubMed:20812024, PubMed:25514493, PubMed:26455326, PubMed:26816381). Directly and specifically binds to the consensus sequence 5'-[GA][CA]GACCCCCCCCC-3' and represses transcription both by regulating the organization of chromatin and through the direct recruitment of transcription factors to gene regulatory regions (PubMed:12004059, PubMed:17595526, PubMed:20812024, PubMed:25514493, PubMed:26816381). Negatively regulates SMAD4 transcriptional activity in the TGF-beta signaling pathway through these two mechanisms (PubMed:25514493). That is, recruits the chromatin regulator HDAC1 to the SMAD4-DNA complex and in parallel prevents the recruitment of the transcriptional activators CREBBP and EP300 (PubMed:25514493). Collaborates with transcription factors like RELA to modify the accessibility of gene transcription regulatory regions to secondary transcription factors (By similarity). Also directly interacts with transcription factors like SP1 to prevent their binding to DNA (PubMed:12004059). Functions as an androgen receptor/AR transcriptional corepressor by recruiting NCOR1 and NCOR2 to the androgen response elements/ARE on target genes (PubMed:20812024). Thereby, negatively regulates androgen receptor signaling and androgen-induced cell proliferation (PubMed:20812024). Involved in the switch between fetal and adult globin expression during erythroid cells maturation (PubMed:26816381). Through its interaction with the NuRD complex regulates chromatin at the fetal globin genes to repress their transcription (PubMed:26816381). Specifically represses the transcription of the tumor suppressor ARF isoform from the CDKN2A gene (By similarity). Efficiently abrogates E2F1-dependent CDKN2A transactivation (By similarity). Regulates chondrogenesis through the transcriptional repression of specific genes via a mechanism that also requires histone deacetylation (By similarity). Regulates cell proliferation through the transcriptional regulation of genes involved in glycolysis (PubMed:26455326). Involved in adipogenesis through the regulation of genes involved in adipocyte differentiation (PubMed:14701838). Plays a key role in the differentiation of lymphoid progenitors into B and T lineages (By similarity). Promotes differentiation towards the B lineage by inhibiting the T-cell instructive Notch signaling pathway through the specific transcriptional repression of Notch downstream target genes (By similarity). Also regulates osteoclast differentiation (By similarity). May also play a role, independently of its transcriptional activity, in double-strand break repair via classical non-homologous end joining/cNHEJ (By similarity). Recruited to double-strand break sites on damage DNA, interacts with the DNA-dependent protein kinase complex and directly regulates its stability and activity in DNA repair (By similarity). May also modulate the splicing activity of KHDRBS1 toward BCL2L1 in a mechanism which is histone deacetylase-dependent and thereby negatively regulates the pro-apoptotic effect of KHDRBS1 (PubMed:24514149)

Protein Sequence

10 MAGGVDGPIG 20 IPFPDHSSDI 30 LSGLNEQRTQ 40 GLLCDVVILV 50 EGREFPTHRS 60 VLAACSQYFK 70 KLFTSGAVVD 80 QQNVYEIDFV 90 SAEALTALMD 100 FAYTATLTVS 110 TANVGDILSA 120 ARLLEIPAVS 130 HVCADLLDRQ 140 ILAADAGADA 150 GQLDLVDQID 160 QRNLLRAKEY 170 LEFFQSNPMN 180 SLPPAAAAAA 190 ASFPWSAFGA 200 SDDDLDATKE 210 AVAAAVAAVA 220 AGDCNGLDFY 230 GPGPPAERPP 240 TGDGDEGDSN 250 PGLWPERDED 260 APTGGLFPPP 270 VAPPAATQNG 280 HYGRGGEEEA 290 ASLSEAAPEP 300 GDSPGFLSGA 310 AEGEDGDGPD 320 VDGLAASTLL 330 QQMMSSVGRA 340 GAAAGDSDEE 350 SRADDKGVMD 360 YYLKYFSGAH 370 DGDVYPAWSQ 380 KVEKKIRAKA 390 FQKCPICEKV 400 IQGAGKLPRH 410 IRTHTGEKPY 420 ECNICKVRFT 430 RQDKLKVHMR 440 KHTGEKPYLC 450 QQCGAAFAHN 460 YDLKNHMRVH 470 TGLRPYQCDS 480 CCKTFVRSDH 490 LHRHLKKDGC 500 NGVPSRRGRK 510 PRVRGGAPDP 520 SPGATATPGA 530 PAQPSSPDAR 540 RNGQEKHFKD 550 EDEDEDVASP 560 DGLGRLNVAG 570 AGGGGDSGGG 580 PGAATDGNFT AGLA

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0070418	DNA-dependent protein kinase complex
Cellular Component	GO:0005634	nucleus
Cellular Component	GO:0035861	site of double-strand break
Molecular Function	GO:0003677	DNA binding
Molecular Function	GO:0003700	DNA-binding transcription factor activity
Molecular Function	GO:0000981	DNA-binding transcription factor activity, RNA polymerase II-specific
Molecular Function	GO:0140297	DNA-binding transcription factor binding
Molecular Function	GO:0001227	DNA-binding transcription repressor activity, RNA polymerase II-specific
Molecular Function	GO:0035035	histone acetyltransferase binding
Molecular Function	GO:0050681	nuclear androgen receptor binding
Molecular Function	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding
Molecular Function	GO:1990837	sequence-specific double-stranded DNA binding
Molecular Function	GO:0046332	SMAD binding
Molecular Function	GO:0001222	transcription corepressor binding
Molecular Function	GO:0008270	zinc ion binding
Biological Process	GO:0030183	B cell differentiation
Biological Process	GO:0006325	chromatin organization
Biological Process	GO:0006338	chromatin remodeling
Biological Process	GO:0006351	DNA-templated transcription
Biological Process	GO:0097680	double-strand break repair via classical nonhomologous end joining
Biological Process	GO:0043249	erythrocyte maturation
Biological Process	GO:0045444	fat cell differentiation
Biological Process	GO:0060766	negative regulation of androgen receptor signaling pathway
Biological Process	GO:0045892	negative regulation of DNA-templated transcription
Biological Process	GO:0045746	negative regulation of Notch signaling pathway
Biological Process	GO:0000122	negative regulation of transcription by RNA polymerase II
Biological Process	GO:0030512	negative regulation of transforming growth factor beta receptor signaling pathway
Biological Process	GO:0034504	protein localization to nucleus
Biological Process	GO:0000381	regulation of alternative mRNA splicing, via spliceosome
Biological Process	GO:0042981	regulation of apoptotic process
Biological Process	GO:0006110	regulation of glycolytic process
Biological Process	GO:0006357	regulation of transcription by RNA polymerase II
Biological Process	GO:2000677	regulation of transcription regulatory region DNA binding

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[3] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[4] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[5] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[6] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.