Target Name: PRAP1
NCBI ID: G118471
Review Report on PRAP1 Target / Biomarker Content of Review Report on PRAP1 Target / Biomarker
PRAP1
Other Name(s): UPA | epididymis tissue protein Li 178 | PRO1195 | Uterine-specific proline-rich acidic protein | Proline rich acidic protein 1, transcript variant 1 | PRAP1_HUMAN | Proline-rich acidic protein 1 | proline rich acidic protein 1 | PRAP1 variant 1 | epididymis secretory sperm binding protein | Epididymis tissue protein Li 178 | Proline-rich acidic protein 1 (isoform 1)

PRAP1: A Drug Target / Disease Biomarker

PRAP1, also known as PRAI1, is a protein that is expressed in many different tissues throughout the body. It is a member of the PRAJ1 family of proteins, which are involved in various cellular processes such as cell signaling, DNA replication, and chromatin remodeling. PRAP1 has been shown to play a role in the regulation of cell proliferation and has been identified as a potential drug target in the field of cancer.

One of the key functions of PRAP1 is its role in the regulation of cell proliferation. PRAP1 has been shown to be involved in the G1/S transition, which is the process by which cells prepare for cell division. During the G1 phase, cells produce more DNA and RNA in order to prepare for cell division. In the S phase, the cell divides and the new daughter cells are produced. PRAP1 has been shown to play a role in regulating the amount of DNA that is synthesized during the G1 phase, as well as the timing of the cell's entry into the S phase.

In addition to its role in cell proliferation, PRAP1 has also been shown to be involved in the regulation of cell apoptosis, which is the process by which cells die. During apoptosis, PRAP1 has been shown to play a role in the formation of DNA-protein complexes, which are thought to play a key role in the regulation of cell death.

Another function of PRAP1 is its role in chromatin remodeling. Chromatin remodeling is the process by which the structure of chromosomes is changed in order to facilitate the proper expression of genes. PRAP1 has been shown to play a role in the regulation of chromatin remodeling, as well as the maintenance of chromosomal stability.

In conclusion, PRAP1 is a protein that is involved in various cellular processes throughout the body. Its role in cell proliferation, apoptosis, and chromatin remodeling makes it a potential drug target in the field of cancer. Further research is needed to fully understand the mechanisms of PRAP1's role in these processes and to identify potential small molecules that can inhibit its activity.

Protein Name: Proline Rich Acidic Protein 1

Functions: Lipid-binding protein which promotes lipid absorption by facilitating MTTP-mediated lipid transfer (mainly triglycerides and phospholipids) and MTTP-mediated apoB lipoprotein assembly and secretion (By similarity). Protects the gastrointestinal epithelium from irradiation-induced apoptosis (By similarity). May play an important role in maintaining normal growth homeostasis in epithelial cells (PubMed:14583459). Involved in p53/TP53-dependent cell survival after DNA damage (PubMed:23235459). May down-regulate the expression of MAD1L1 and exert a suppressive role in mitotic spindle assembly checkpoint in hepatocellular carcinomas (PubMed:24374861)

The "PRAP1 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 PRAP1 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

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PRB1 | PRB2 | PRB3 | PRB4 | PRC1 | PRC1-AS1 | PRCC | PRCD | PRCP | PRDM1 | PRDM10 | PRDM10-DT | PRDM11 | PRDM12 | PRDM13 | PRDM14 | PRDM15 | PRDM16 | PRDM16-DT | PRDM2 | PRDM4 | PRDM5 | PRDM6 | PRDM7 | PRDM8 | PRDM9 | PRDX1 | PRDX2 | PRDX2P4 | PRDX3 | PRDX4 | PRDX5 | PRDX6 | Pre-mRNA cleavage complex II | PREB | PRECSIT | Prefoldin complex | PRELID1 | PRELID1P6 | PRELID2 | PRELID3A | PRELID3B | PRELP | Prenyl diphosphate synthase | Prenyltransferase | PREP | PREPL | Presenilin | PREX1 | PREX2 | PRF1 | PRG1 | PRG2 | PRG3 | PRG4 | PRH1 | PRH1-PRR4 | PRH1-TAS2R14 | PRH2 | PRICKLE1 | PRICKLE2 | PRICKLE2-AS1 | PRICKLE2-AS2 | PRICKLE3 | PRICKLE4 | PRIM1 | PRIM2 | PRIM2BP | PRIMA1 | PRIMPOL | PRINS | PRKAA1 | PRKAA2 | PRKAB1 | PRKAB2 | PRKACA | PRKACB | PRKACG | PRKAG1 | PRKAG2 | PRKAG2-AS1 | PRKAG2-AS2 | PRKAG3 | PRKAR1A | PRKAR1B | PRKAR2A | PRKAR2A-AS1 | PRKAR2B | PRKCA | PRKCA-AS1 | PRKCB | PRKCD | PRKCE | PRKCG | PRKCH | PRKCI | PRKCQ | PRKCQ-AS1 | PRKCSH | PRKCZ