Target Name: CPT2
NCBI ID: G1376
Other Name(s): CPT-2 | testicular secretory protein Li 13 | CPT1 | Carnitine palmitoyltransferase 2, transcript variant 1 | Carnitine palmitoyltransferase II | CPT2_HUMAN | CPT II | CPT2 variant 1 | CPTASE | Carnitine O-palmitoyltransferase 2, mitochondrial (isoform 1) | Carnitine O-palmitoyltransferase 2, mitochondrial | IIAE4 | carnitine palmitoyltransferase II | carnitine palmitoyltransferase 2

Understanding CPT2: Potential Drug Target and Biomarker

CPT2 (CPT-2) is a protein that is expressed in various tissues of the body, including the brain, heart, and kidneys. It is a key regulator of cell proliferation and has been implicated in a number of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

One of the most promising aspects of CPT2 is its potential as a drug target. CPT2 has been shown to play a role in a variety of cellular processes that are important for human health, including cell signaling, cell division, and inflammation. It has also has been shown to be involved in the development and progression of a number of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

In addition to its potential as a drug target, CPT2 is also a potential biomarker for a number of diseases. Its expression has been shown to be associated with a number of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. This suggests that CPT2 may be a useful indicator of disease status, and that its levels may be able to be used as a diagnostic tool.

One of the challenges in studying CPT2 as a drug target is its complex structure. CPT2 is a large protein that is composed of multiple domains, including an extracellular domain, a transmembrane domain, and an intracellular domain. These domains give CPT2 its unique structure and function, and they are involved in a variety of cellular processes.

One of the most well-studied domains of CPT2 is the extracellular domain. This domain is responsible for CPT2's ability to interact with other proteins, both within and outside the cell. It is composed of a variety of repeats, including the so-called N -terminal alpha-helix and the C-terminal beta-sheet. These repeats are thought to play a role in CPT2's ability to interact with other proteins, and they may be involved in CPT2's regulation of cellular processes.

The transmembrane domain of CPT2 is responsible for its ability to interact with the cytoskeleton and the cell membrane. It is composed of a variety of helices and is thought to play a role in the regulation of cell signaling and cell division.

The intracellular domain of CPT2 is responsible for its ability to interact with other proteins within the cell. It is composed of a variety of helices and is thought to play a role in the regulation of cellular processes, including the regulation of cell growth, differentiation, and inflammation.

CPT2 is also involved in the regulation of cellular processes that are important for human health, including cell signaling, cell division, and inflammation. It has been shown to play a role in the development and progression of a number of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

In addition to its potential as a drug target, CPT2 is also a potential biomarker for a number of diseases. Its expression has been shown to be associated with a number of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. This suggests that CPT2 may be a useful indicator of disease status, and that its levels may be able to be used as a diagnostic tool.

Overall, CPT2 is a complex protein that is involved in a variety of cellular processes that are important for human health. Its structure and function are still being fully understood, and its potential as a drug target and biomarker continue to be explored. Further research is needed to fully understand the role of CPT2 in human health and to develop effective treatments for the diseases associated with its dysfunction.

Protein Name: Carnitine Palmitoyltransferase 2

Functions: Involved in the intramitochondrial synthesis of acylcarnitines from accumulated acyl-CoA metabolites (PubMed:20538056, PubMed:24780397). Reconverts acylcarnitines back into the respective acyl-CoA esters that can then undergo beta-oxidation, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion. Active with medium (C8-C12) and long-chain (C14-C18) acyl-CoA esters (PubMed:20538056)

More Common Targets

CPTP | CPVL | CPVL-AS2 | CPXCR1 | CPXM1 | CPXM2 | CPZ | CR1 | CR1L | CR2 | CRABP1 | CRABP2 | CRACD | CRACDL | CRACR2A | CRACR2B | CRADD | CRADD-AS1 | CRAMP1 | CRAT | CRAT37 | CRB1 | CRB2 | CRB3 | CRBN | CRCP | CRCT1 | Creatine Kinase | CREB1 | CREB3 | CREB3L1 | CREB3L2 | CREB3L3 | CREB3L4 | CREB5 | CREBBP | CREBL2 | CREBRF | CREBZF | CREG1 | CREG2 | CRELD1 | CRELD2 | CREM | CRH | CRHBP | CRHR1 | CRHR2 | CRIM1 | CRIM1-DT | CRIP1 | CRIP1P1 | CRIP2 | CRIP3 | CRIPAK | CRIPT | CRISP1 | CRISP2 | CRISP3 | CRISPLD1 | CRISPLD2 | CRK | CRKL | CRLF1 | CRLF2 | CRLF3 | CRLS1 | CRMA | CRMP1 | CRNDE | CRNKL1 | CRNN | CROCC | CROCC2 | CROCCP2 | CROCCP3 | CROT | CRP | CRPPA | CRPPA-AS1 | CRTAC1 | CRTAM | CRTAP | CRTC1 | CRTC2 | CRTC3 | CRTC3-AS1 | CRX | CRY1 | CRY2 | CRYAA | CRYAB | CRYBA1 | CRYBA2 | CRYBA4 | CRYBB1 | CRYBB2 | CRYBB2P1 | CRYBB3 | CRYBG1