Phenazine Biosynthesis-Like Domain-Containing protein (PBLD) belongs to the phenazine biosynthesis-like protein (PhzF) family, which is expressed in most tissues. PBLD takes part in the MAPK signaling pathway, and is involved in multiple basic cellular functions. The expression of PBLD can be increased in several disease processes, including insulin resistance, folate deficiency and hypotension.
Pterin-4-α-Carbinolamine Dehydratase (PCBD1) is the founding member of the Pterin-4-α-Carbinolamine Dehydratase Family. PCBD1 is involved in Tetrahydrobiopterin biosynthesis. It seems to prevent the formation of 7-Pterins and accelerate the formation of Quinonoid-BH2. Furthermore, PCBD1 regulates the homodimerization of the transcription factor Hepatocyte Nuclear Factor 1 (HNF1) and enhances its transcriptional activity. Defects in PCBD1 are the cause of BH4-Deficient Hyperphenylalaninemia Type D (HPABH4D). HPABH4D is characterized by the excretion of 7-substituted Pterins in the urine of affected patients.
Poly(rC)-binding protein 1, also known as Heterogeneous nuclear ribonucleoprotein E1, Alpha-CP1, Nucleic acid-binding protein SUB2.3 and PCBP1, is a family member of heterogeneous nuclear ribonucleoproteins (hnRNPs) that belong to RNA-binding proteins and bear three KH domains. PCBP1 is loosely bound in the nucleus. It may shuttle between the nucleus and the cytoplasm. It is abundantly expressed in skeletal muscle, thymus and peripheral blood leukocytes while a lower expression is observed in prostate, spleen, testis, ovary, small intestine, heart, liver, adrenal and thyroid glands. PCBP1 is widely expressed in many human tissues and involved in regulation of transcription, transportation process, and function of RNA molecules. PCBP1 plays a pivotal role in post-transcriptional regulation for RNA metabolism and RNA function in gene expression. PCBP1 acts as a negative regulator of CD44 variants splicing in HepG2 cells, and loss of PCBP1 in human hepatic tumor contributes to the formation of a metastatic phenotype.
PCK2 (Phosphoenolpyruvate Carboxykinase 2, Mitochondrial) is a Protein Coding gene. Diseases associated with PCK2 include Pepck 1 Deficiency and Phosphoenolpyruvate Carboxykinase Deficiency, Mitochondrial. Among its related pathways are Glycosaminoglycan metabolism and DNA Damage Response (only ATM dependent). Gene Ontology (GO) annotations related to this gene include GTP binding and purine nucleotide binding. An important paralog of this gene is PCK1.
This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Induces a robust stimulatory effect on the 3'-5' exonuclease and 3'-phosphodiesterase, but not apurinic-apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2.
Proliferating Cell Nuclear Antigen (PCNA) is a protein only expresse in nomal proliferate cells and cancer cells. It is central to both DNA replication and repair. One of the well-established functions for PCNA is its role as the processivity factor for DNA polymerase delta and epsilon. PCNA tethers the polymerase catalytic unit to the DNA template for rapid and processive DNA synthesis. Two forms of PCNA exist in cells: (i) a detergent-insoluble trimeric form stably associated with the replicating forks during S phase and (ii) a soluble form in quiescent cells in G1 and G2 phases. PCNA forms a toroidal trimer in S phase with replication factor-C (RF-C) and DNA in an ATP-dependent manner and enables the loading of DNA polymerase delta and epsilon onto the complex. The close association of PCNA with kinase complexes involved in cell cycle machinery indicates that PCNA has a regulatory role in cell cycle progression. PCNA also participates in the processing of branched intermediates that arise during the lagging strand DNA synthesis.
Neuroendocrine convertase 1, also known as Prohormone convertase 1, Proprotein convertase 1, PCSK1 and NEC1, is anenzyme which belongs to thepeptidase S8 family and Furin subfamily. PCSK1 is an enzyme that performs the proteolytic cleavage of prohormones to their intermediate (or sometimes completely cleaved) forms. It is present only in neuroendocrine cells such as brain, pituitary and adrenal, and most often cleaves after a pair of basic residues within prohormones but can occasionally cleave after a single arginine. It binds to a protein known as proSAAS, which also represents its endogenous inhibitor. PCSK1 is involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. PCSK1 substrates include POMC, renin, enkephalin, dynorphin, somatostatin and insulin. Defects in PCSK1 are the cause of proprotein convertase 1 deficiency (PC1 deficiency). PC1 deficiency is characterized by obesity, hypogonadism, hypoadrenalism, reactive hypoglycemia as well as marked small-intestinal absorptive dysfunction. It is due to impaired processing of prohormones.
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