Target Name: ZMYND8
NCBI ID: G23613
Review Report on ZMYND8 Target / Biomarker Content of Review Report on ZMYND8 Target / Biomarker
ZMYND8
Other Name(s): Zinc finger MYND domain containing protein 8 | Protein kinase C-binding protein 1 | Protein kinase C-binding protein 1 (isoform g) | ZMYND8 variant 1 | cutaneous T-cell lymphoma-associated antigen se14-3 | predicted protein of HQ2893 | Zinc finger MYND-type containing 8, transcript variant 1 | Cutaneous T-cell lymphoma associated antigen se14-3 | CTCL tumor antigen se14-3 | Zinc finger MYND-type containing 8, transcript variant 7 | RACK7 | zinc finger MYND-type containing 8 | MGC31836 | KIAA1125 | PKCB1_HUMAN | Cutaneous T-cell lymphoma-associated antigen se14-3 | Protein kinase C binding protein 1 | ZMYND8 variant 7 | Predicted protein of HQ2893 | PRO2893 | PRKCBP1 | Protein kinase C-binding protein 1 (isoform a) | Rack7 | RACK like clone 7 | zinc finger MYND domain-containing protein 8 | Zinc finger MYND domain-containing protein 8 | CTCL-associated antigen se14-3

ZMYND8: A Zinc FingerMYND Domain Containing Protein as a Potential Drug Target and Biomarker

Abstract:

ZMYND8, a zinc finger MYND domain containing protein, has been identified as a potential drug target and biomarker. Its unique structure and function make it an attractive target for drug development. This article discusses the biology of ZMYND8, its potential as a drug target, and its potential as a biomarker for various diseases.

Introduction:

Zinc finger proteins (ZFPs) are a family of transmembrane proteins that contain a conserved domain of zinc fingers and are involved in various cellular processes. MYND domain containing proteins are a subgroup of ZFPs that contain a unique domain called the MYND (M domain) domain. This domain is responsible for the protein's unique structure and function. ZMYND8, a member of the ZMYND domain containing protein family, has been identified and its unique properties make it an attractive drug target and biomarker.

Structure and Function:

ZMYND8 is a 21-kDa protein that contains a N-terminal ZMYND domain, a unique C-terminal extension, and a C-terminal Zn finger. The ZMYND domain is a conserved domain that is found in various proteins, including ZNF2, TCF7L1, and ZF21. The ZMYND domain contains a unique structural feature, including a conserved nucleotide loop and a conserved acidic residue that is involved in protein-protein interactions.

The ZMYND domain is responsible for the unique structure and function of ZMYND8. The conserved nucleotide loop and acidic residue are involved in the formation of a distinct domain-protein interaction that is crucial for the protein's stability and function. ZMYND8 contains a unique C-terminal extension that is responsible for its unique stability and function. The C-terminal extension is rich in acidic and basic residues, including Asp, Asn, Asp, Asn, and Glu. These residues play a crucial role in the protein's stability and function.

Potential Drug Target:

ZMYND8's unique structure and function make it an attractive target for drug development. The conserved nucleotide loop and acidic residue in the ZMYND domain are involved in protein-protein interactions, making it an attractive target for small molecule inhibitors. Additionally, the ZMYND domain's unique structure and function make it a potential target for monoclonal antibodies (MCAs), as well as antibody-drug conjugates (ADCs).

Potential Biomarkers:

ZMYND8 can also be used as a biomarker for various diseases. The ZMYND domain is involved in the regulation of various cellular processes, including cell growth, apoptosis, and inflammation. Therefore, ZMYND8 can be used as a biomarker for diseases that are associated with these processes, such as cancer, neurodegenerative diseases, and inflammatory diseases. Additionally, the ZMYND domain's unique structure and function make it an attractive target for diagnostic biomarkers.

Conclusion:

ZMYND8, a zinc finger MYND domain containing protein, has unique structure and function that make it an attractive drug target and biomarker. Its conserved nucleotide loop and acidic residue, as well as its unique C-terminal extension, make it a potential target for small molecule inhibitors and monoclonal antibodies. Additionally, its role in the regulation of various cellular processes makes it a potential biomarker for various diseases. Further research is needed to fully understand the biology of ZMYND8 and its potential as a drug target and biomarker.

Protein Name: Zinc Finger MYND-type Containing 8

Functions: Chromatin reader that recognizes dual histone modifications such as histone H3.1 dimethylated at 'Lys-36' and histone H4 acetylated at 'Lys-16' (H3.1K36me2-H4K16ac) and histone H3 methylated at 'Lys-4' and histone H4 acetylated at 'Lys-14' (H3K4me1-H3K14ac) (PubMed:26655721, PubMed:31965980, PubMed:36064715, PubMed:27477906). May act as a transcriptional corepressor for KDM5D by recognizing the dual histone signature H3K4me1-H3K14ac (PubMed:27477906). May also act as a transcriptional corepressor for KDM5C and EZH2 (PubMed:33323928). Recognizes acetylated histone H4 and recruits the NuRD chromatin remodeling complex to damaged chromatin for transcriptional repression and double-strand break repair by homologous recombination (PubMed:30134174, PubMed:25593309, PubMed:27732854). Also activates transcription elongation by RNA polymerase II through recruiting the P-TEFb complex to target promoters (PubMed:30134174, PubMed:26655721). Localizes to H3.1K36me2-H4K16ac marks at all-trans-retinoic acid (ATRA)-responsive genes and positively regulates their expression (PubMed:26655721). Promotes neuronal differentiation by associating with regulatory regions within the MAPT gene, to enhance transcription of a protein-coding MAPT isoform and suppress the non-coding MAPT213 isoform (PubMed:36064715, PubMed:35916866, PubMed:30134174). Suppresses breast cancer, and prostate cancer cell invasion and metastasis (PubMed:27477906, PubMed:31965980, PubMed:33323928)

The "ZMYND8 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about ZMYND8 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

More Common Targets

ZNF10 | ZNF100 | ZNF101 | ZNF106 | ZNF107 | ZNF112 | ZNF114 | ZNF117 | ZNF12 | ZNF121 | ZNF124 | ZNF131 | ZNF132 | ZNF133 | ZNF134 | ZNF135 | ZNF136 | ZNF137P | ZNF138 | ZNF14 | ZNF140 | ZNF141 | ZNF142 | ZNF143 | ZNF146 | ZNF148 | ZNF154 | ZNF155 | ZNF157 | ZNF16 | ZNF160 | ZNF165 | ZNF169 | ZNF17 | ZNF174 | ZNF175 | ZNF177 | ZNF18 | ZNF180 | ZNF181 | ZNF182 | ZNF184 | ZNF185 | ZNF189 | ZNF19 | ZNF195 | ZNF197 | ZNF2 | ZNF20 | ZNF200 | ZNF202 | ZNF204P | ZNF205 | ZNF205-AS1 | ZNF207 | ZNF208 | ZNF209P | ZNF211 | ZNF212 | ZNF213 | ZNF213-AS1 | ZNF214 | ZNF215 | ZNF217 | ZNF219 | ZNF22 | ZNF22-AS1 | ZNF221 | ZNF222 | ZNF223 | ZNF224 | ZNF225 | ZNF225-AS1 | ZNF226 | ZNF227 | ZNF229 | ZNF23 | ZNF230 | ZNF232 | ZNF232-AS1 | ZNF233 | ZNF234 | ZNF235 | ZNF236 | ZNF236-DT | ZNF239 | ZNF24 | ZNF248 | ZNF25 | ZNF250 | ZNF251 | ZNF252P | ZNF252P-AS1 | ZNF253 | ZNF254 | ZNF256 | ZNF257 | ZNF26 | ZNF260 | ZNF263