Target Name: PITHD1
NCBI ID: G57095
Review Report on PITHD1 Target / Biomarker Content of Review Report on PITHD1 Target / Biomarker
PITHD1
Other Name(s): PITH domain-containing protein 1 | PITH domain containing 1 | C1orf128 | HT014 | TXNL1CL | PITH1_HUMAN | TXNL1 C-terminal like | RP5-886K2.4 | PITH (C-terminal proteasome-interacting domain of thioredoxin-like) domain containing 1

PITHD1: A Potential Drug Target Or Biomarker

PITHD1, also known as PITH domain-containing protein 1, is a protein that has been identified as a potential drug target or biomarker. It is a member of the PATH domain family, which is known for its role in intracellular signaling pathways. PATH domain proteins have been implicated in a wide range of cellular processes, including cell signaling, cell division, and tissue homeostasis.

The PITHD1 protein

PITHD1 is a 21-kDa protein that is expressed in a variety of tissues, including brain, heart, and muscle. It is localized to the endoplasmic reticulum (ER) and can interact with various protein partners, including the protein kinase PDK4. PITHD1 has a unique structure that consists of a catalytic domain, a transmembrane region, and an optional cytoplasmic tail.

The catalytic domain

The catalytic domain of PITHD1 is the region that contains the protein's active site, where it interacts with other proteins to perform various cellular functions. The catalytic domain is characterized by a unique Rossmann-fold, which is a type of hydrogen bonding network that is commonly found in protein structures. This structural feature allows PITHD1 to form a stable complex with PDK4 and other protein partners, which are known to play important roles in intracellular signaling pathways.

The transmembrane region

The transmembrane region of PITHD1 is the region that spans the cell membrane and is involved in the protein's localization and interactions with other proteins. This region is characterized by a variety of conserved carbohydrates, including a glycine residue at its carboxyl end and a Asn residue at its amino acid residue 20. The transmembrane region is also involved in the regulation of PITHD1's activity, as changes in its localization can affect the protein's ability to interact with other proteins.

The cytoplasmic tail

The cytoplasmic tail of PITHD1 is the region that extends beyond the cell membrane and is involved in the protein's stability and functions. This region is characterized by a variety of conserved carbohydrates, including a Gln residue at its carboxyl end and a Asn residue at its amino acid residue 18. The cytoplasmic tail is also involved in the regulation of PITHD1's activity, as changes in its localization can affect the protein's ability to interact with other proteins.

Potential drug target or biomarker

The unique structure of PITHD1, including its catalytic domain, transmembrane region, and cytoplasmic tail, makes it a promising candidate for drug targeting or biomarker development. PITHD1 has been shown to play a role in a wide range of cellular processes, including cell signaling, cell division, and tissue homeostasis.

In addition, PITHD1 has been shown to interact with the protein PDK4, which is a known regulator of cell signaling pathways. The interaction between PITHD1 and PDK4 has been shown to play a role in the regulation of cellular processes, including cell proliferation, cell migration , and tissue formation.

Possible drug targets

The catalytic domain of PITHD1 is the region that contains the protein's active site, where it interacts with other proteins to perform various cellular functions. This suggests that PITHD1 may be a good candidate for drug targeting. By modulating the activity of PATH domain proteins, including PDK4, researchers may be able to achieve a wide range of cellular

Protein Name: PITH Domain Containing 1

Functions: Promotes megakaryocyte differentiation by up-regulating RUNX1 expression (PubMed:25134913). Regulates RUNX1 expression by activating the proximal promoter of the RUNX1 gene and by enhancing the translation activity of an internal ribosome entry site (IRES) element in the RUNX1 gene (PubMed:25134913)

The "PITHD1 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 PITHD1 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

PITPNA | PITPNA-AS1 | PITPNB | PITPNC1 | PITPNM1 | PITPNM2 | PITPNM2-AS1 | PITPNM3 | PITRM1 | PITRM1-AS1 | PITX1 | PITX1-AS1 | PITX2 | PITX3 | PIWIL1 | PIWIL2 | PIWIL2-DT | PIWIL3 | PIWIL4 | PIWIL4-AS1 | PJA1 | PJA2 | PJVK | PKD1 | PKD1-AS1 | PKD1L1 | PKD1L1-AS1 | PKD1L2 | PKD1L3 | PKD1P1 | PKD1P4-NPIPA8 | PKD1P6 | PKD2 | PKD2L1 | PKD2L2 | PKD2L2-DT | PKDCC | PKDREJ | PKHD1 | PKHD1L1 | PKIA | PKIA-AS1 | PKIB | PKIG | PKLR | PKM | PKMP1 | PKMYT1 | PKN1 | PKN2 | PKN2-AS1 | PKN3 | PKNOX1 | PKNOX2 | PKNOX2-DT | PKP1 | PKP2 | PKP3 | PKP4 | PKP4-AS1 | PLA1A | PLA2G10 | PLA2G12A | PLA2G12AP1 | PLA2G12B | PLA2G15 | PLA2G1B | PLA2G2A | PLA2G2C | PLA2G2D | PLA2G2E | PLA2G2F | PLA2G3 | PLA2G4A | PLA2G4B | PLA2G4C | PLA2G4D | PLA2G4E | PLA2G4F | PLA2G5 | PLA2G6 | PLA2G7 | PLA2R1 | PLAA | PLAAT1 | PLAAT2 | PLAAT3 | PLAAT4 | PLAAT5 | PLAC1 | PLAC4 | PLAC8 | PLAC8L1 | PLAC9 | PLAC9P1 | PLAG1 | PLAGL1 | PLAGL2 | Plasma Membrane Calcium ATPase | PLAT