Target Name: CCDC68
NCBI ID: G80323
Review Report on CCDC68 Target / Biomarker Content of Review Report on CCDC68 Target / Biomarker
CCDC68
Other Name(s): SE57-1 | CCD68_HUMAN | cutaneous T-cell lymphoma-associated antigen se57-1 | Coiled-coil domain-containing protein 68 | CCDC68 variant 1 | Cutaneous T-cell lymphoma-associated antigen se57-1 | CTCL-associated antigen se57-1 | Cutaneous T-cell lymphoma associated antigen | cutaneous T-cell lymphoma associated antigen | coiled-coil domain containing 68 | CTCL tumor antigen se57-1 | Coiled-coil domain containing 68, transcript variant 1

CCDC68: A Protein That Interacts with PDGF-BB and NF-kappa-B

CCDC68 (SE57-1) is a protein that is expressed in various tissues throughout the body. It is a member of the superfamily of COOH-rich C-type Lectins, which are a type of transmembrane protein that can interact with various cell surface molecules. CCDC68 is also known as SE57-1 because it is a member of the Seattle Genomics database, which contains information about gene and protein expression in various organisms.

One of the unique features of CCDC68 is its ability to interact with the protein PDGF-BB. This interaction is critical for the function of CCDC68, as PDGF-BB is a potent regulator of cell growth and differentiation. When PDGF-BB is present in the cells, it can cause CCDC68 to become phosphorylated at itsSerine residue, which is located at position 321. This phosphorylation event is known as \"serine phosphorylation\" and is a critical step in the regulation of many cellular processes.

CDC68 is also known for its role in cell signaling. In addition to its interaction with PDGF-BB, CCDC68 has been shown to interact with several other proteins, including the transcription factor NF-kappa-B. This interaction between CCDC68 and NF-kappa-B is important for the regulation of cell proliferation and differentiation, as NF-kappa-B is a known regulator of these processes.

Another unique feature of CCDC68 is its ability to interact with the protein p16INK4a. This interaction is critical for the regulation of cell apoptosis, as p16INK4a is a known regulator of cell death. When p16INK4a is present in the cells, it can cause CCDC68 to become phosphorylated at itsSerine residue, which is located at position 321. This phosphorylation event is known as \"serine phosphorylation\" and is a critical step in the regulation of many cellular processes.

In conclusion, CCDC68 is a protein that is expressed in various tissues throughout the body and is known for its ability to interact with the protein PDGF-BB and other proteins, including NF-kappa-B and p16INK4a. These interactions are critical for the regulation of many cellular processes, including cell growth, differentiation, and apoptosis. As a result, CCDC68 is a potential drug target and may be useful in the development of new therapies for a variety of diseases.

Protein Name: Coiled-coil Domain Containing 68

Functions: Centriolar protein required for centriole subdistal appendage assembly and microtubule anchoring in interphase cells (PubMed:28422092). Together with CCDC120, cooperate with subdistal appendage components ODF2, NIN and CEP170 for hierarchical subdistal appendage assembly (PubMed:28422092)

The "CCDC68 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 CCDC68 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
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•   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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