Target Name: NUMA1
NCBI ID: G4926
Other Name(s): structural nuclear protein | Nuclear matrix protein-22 | NMP22 | Nuclear mitotic apparatus protein 1 | SP-H antigen | NUMA1_HUMAN | nuclear matrix protein-22 | Nuclear mitotic apparatus protein 1, transcript variant 1 | NUMA | NUMA1 variant 1 | NMP-22 | Nuclear mitotic apparatus protein | Centrophilin stabilizes mitotic spindle in mitotic cells | Nuclear mitotic apparatus protein 1 (isoform 1) | nuclear mitotic apparatus protein 1 | NuMA protein | Structural nuclear protein | centrophilin stabilizes mitotic spindle in mitotic cells

NUMA1: A Structure-Binding Protein as a Potential Drug Target and Biomarker

Nucleoproteins are a ubiquitous class of biomolecules that play critical roles in various cellular processes, including DNA replication, gene expression, and cellular signaling. Among the nucleoproteins, structural proteins, such as nucleosomes, histones, and transports, have been implicated in numerous diseases, including cancer, neurodegenerative diseases, and genetic disorders. One of the protein families, NUMA proteins, has emerged as a promising drug target and biomarker due to its unique structural features and diverse functions. In this article, we will explore the structure and function of NUMA1, its potential as a drug target, and its potential as a biomarker for various diseases.

Structure and Function of NUMA1

The NUMA protein family consists of four structurally similar proteins: NUMA1, NUMA2, NUMA3, and NUMA4. All of these proteins share a conserved N-terminal domain, a unique feature in the nucleoprotein family. The N-terminal domain is responsible for protein-protein interactions, localization, and regulation of protein stability. The NUMA proteins differ from each other in their secondary structure, including the presence or absence of various domains and their arrangement.

NUMA1, a 19-kDa protein, has a unique structure that consists of a core domain, a transmembrane region, and a cytoplasmic tail. The core domain is composed of a nucleotide-binding oligomerization domain (NBO), a structural domain that binds nucleotides with high affinity. This domain is responsible for the protein's stability and functions as a potential drug target.

The NUMA1 transmembrane region is made up of multiple domains, including an amino-terminal domain (ATD), a catalytic domain (CAD), and a carboxy-terminal domain (CTD). The ATD and CAD domains are involved in protein-protein interactions and nucleotide binding, while the CTD is involved in protein stability and localization.

The NUMA1 cytoplasmic tail is long and complex, composed of multiple domains, including a hypervariable region (HVR), a basic domain (BDD), and a terminal hypervariable region (TVR). The HVR is involved in protein-protein interactions and localization, while the BDD and TVR are involved in protein stability and localization, respectively.

NUMA1 Functions and Potential as a Drug Target

NUMA1 has been implicated in various cellular processes, including DNA replication, gene expression, and cellular signaling. Its unique structure and functions make it an attractive drug target. One of the key functions of NUMA1 is its role in the replication of DNA in the nucleus. NUMA1 has been shown to interact with the protein Smap, which is involved in DNA replication.

In addition to its role in DNA replication, NUMA1 has also been shown to play a role in gene expression. NUMA1 has been shown to interact with the protein p21, which is involved in cell cycle progression and apoptosis. This interaction between NUMA1 and p21 suggests that NUMA1 may be involved in regulating gene expression.

NUMA1 has also been shown to play a role in cellular signaling. Its unique structure and functions make it a potential signaling protein. One of the signaling pathways that NUMA1 is involved in is the regulation of cell adhesion. NUMA1 has been shown to interact with the protein tight junction protein (TJP), which is involved in

Protein Name: Nuclear Mitotic Apparatus Protein 1

Functions: Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division (PubMed:7769006, PubMed:17172455, PubMed:19255246, PubMed:24996901, PubMed:26195665, PubMed:27462074). Functions to tether the minus ends of MTs at the spindle poles, which is critical for the establishment and maintenance of the spindle poles (PubMed:12445386, PubMed:11956313). Plays a role in the establishment of the mitotic spindle orientation during metaphase and elongation during anaphase in a dynein-dynactin-dependent manner (PubMed:23870127, PubMed:24109598, PubMed:24996901, PubMed:26765568). In metaphase, part of a ternary complex composed of GPSM2 and G(i) alpha proteins, that regulates the recruitment and anchorage of the dynein-dynactin complex in the mitotic cell cortex regions situated above the two spindle poles, and hence regulates the correct oritentation of the mitotic spindle (PubMed:23027904, PubMed:22327364, PubMed:23921553). During anaphase, mediates the recruitment and accumulation of the dynein-dynactin complex at the cell membrane of the polar cortical region through direct association with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), and hence participates in the regulation of the spindle elongation and chromosome segregation (PubMed:22327364, PubMed:23921553, PubMed:24996901, PubMed:24371089). Binds also to other polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate (PIP3), in vitro (PubMed:24996901, PubMed:24371089). Also required for proper orientation of the mitotic spindle during asymmetric cell divisions (PubMed:21816348). Plays a role in mitotic MT aster assembly (PubMed:11163243, PubMed:11229403, PubMed:12445386). Involved in anastral spindle assembly (PubMed:25657325). Positively regulates TNKS protein localization to spindle poles in mitosis (PubMed:16076287). Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority of the nuclear volume (PubMed:10075938). Required for epidermal differentiation and hair follicle morphogenesis (By similarity)

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NUMB | NUMBL | NUP107 | Nup107-160 complex | NUP133 | NUP153 | NUP155 | NUP160 | NUP188 | NUP205 | NUP210 | NUP210L | NUP210P1 | NUP210P2 | NUP214 | NUP35 | NUP37 | NUP42 | NUP43 | NUP50 | NUP50-DT | NUP54 | NUP58 | NUP62 | NUP62CL | NUP85 | NUP88 | NUP93 | NUP98 | NUPR1 | NUPR2 | NUS1 | NUS1P1 | NUS1P3 | NUSAP1 | NUTF2 | NUTF2P4 | NUTM1 | NUTM2A | NUTM2A-AS1 | NUTM2B | NUTM2B-AS1 | NUTM2D | NUTM2E | NUTM2F | NUTM2G | NVL | NWD1 | NWD2 | NXF1 | NXF2 | NXF3 | NXF4 | NXF5 | NXN | NXNL1 | NXNL2 | NXPE1 | NXPE2 | NXPE3 | NXPE4 | NXPH1 | NXPH2 | NXPH3 | NXPH4 | NXT1 | NXT2 | NXTAR | NYAP1 | NYAP2 | NYNRIN | NYX | OACYLP | OAF | OARD1 | OAS1 | OAS2 | OAS3 | OASL | OAT | OATP1 | OAZ1 | OAZ2 | OAZ3 | OBI1 | OBI1-AS1 | OBP2A | OBP2B | OBSCN | OBSCN-AS1 | OBSL1 | OC90 | OCA2 | OCEL1 | OCIAD1 | OCIAD2 | OCLM | OCLN | OCLNP1 | OCM