In response to DNA damage and replication blocks, cell cycle progression is halted through the control of critical cell cycle regulators. The protein encoded by this gene is a cell cycle checkpoint regulator and putative tumor suppressor. It contains a forkhead-associated protein interaction domain essential for activation in response to DNA damage and is rapidly phosphorylated in response to replication blocks and DNA damage. When activated, the encoded protein is known to inhibit CDC25C phosphatase, preventing entry into mitosis, and has been shown to stabilize the tumor suppressor protein p53, leading to cell cycle arrest in G1. In addition, this protein interacts with and phosphorylates BRCA1, allowing BRCA1 to restore survival after DNA damage. Mutations in this gene have been linked with Li-Fraumeni syndrome, a highly penetrant familial cancer phenotype usually associated with inherited mutations in TP53. Also, mutations in this gene are thought to confer a predisposition to sarcomas, breast cancer, and brain tumors. This nuclear protein is a member of the CDS1 subfamily of serine/threonine protein kinases. Several transcript variants encoding different isoforms have been found for this gene.
CHMP2B(Charged multivesicular body protein 2b) is a protein that is encoded by the CHMP2B gene in human. It forms part of one of the endosomal sorting complexes required for transport (ESCRT) - specifically ESCRT-III - which are a series of complexes involved in cell membrane remodelling. CHMP2B forms long chains that spiral around the neck of a budding vesicle. Along with the other components of ESCRT-III, CHMP2B constricts the neck of the vesicle just before it is cleaved away from the membrane.
This gene encodes a member of the CCAAT/enhancer-binding protein (C/EBP) family of transcription factors. The protein functions as a dominant-negative inhibitor by forming heterodimers with other C/EBP members, such as C/EBP and LAP (liver activator protein), and preventing their DNA binding activity. The protein is implicated in adipogenesis and erythropoiesis, is activated by endoplasmic reticulum stress, and promotes apoptosis. Fusion of this gene and FUS on chromosome 16 or EWSR1 on chromosome 22 induced by translocation generates chimeric proteins in myxoid liposarcomas or Ewing sarcoma. Multiple alternatively spliced transcript variants encoding two isoforms with different length have been identified.
Chordin is a secreted glycoprotein that regulates dorsoventral patterning during gastrulation. Chordin functions as a bone morphogenetic protein (BMP) antagonist that blocks their ventralizing activity by binding to the BMPs and inhibiting their interaction with their receptors. Mouse Chordin cDNA encodes a 948 amino acid (aa) residue precursor protein with a putative 26 aa residue signal peptide. Chordin contains four internal cysteine-rich repeats (CRs) that are conserved in the spacing of their ten cysteine residues. The CRs of chordin, especially CR1 and CR3, have been shown to be the functional domains for BMP binding. These conserved CRs are present in an expanding family of secreted molecules that antagonize BMP signaling. Xolloid (an extracellular zinc metalloproteinase) can cleave chordin at two specific sites resulting in chordin fragments with lower BMP-affinity. Cleavage of the chordin/BMP complex can reverse the BMP antagonist activity of chordin. Mouse chordin is expressed at high levels in 7 day postcoitum mouse embryos. Chordin expression is also detected in multiple fetal and adult tissues, most notably liver and cerebellum, suggesting additional roles for chordin in organogenesis and homeostasis.
Human Chromogranin A (CHGA) an acidic protein and a member of the chromogranin/secretogranin family of neuroendocrine secretory proteins. It is located in secretory vesicles of neurons and endocrine cells such as islet beta cell secretory granules in pancreas. Chromogranin A expression has been oberserved in neuroendocrine tumors, medullary thyroid carcinoma, as well as carcinoid tumors.
The protein encoded by this gene is a member of the chromogranin/secretogranin family of neuroendocrine secretory proteins. It is found in secretory vesicles of neurons and endocrine cells. This gene product is a precursor to three biologically active peptides; vasostatin, pancreastatin, and parastatin. These peptides act as autocrine or paracrine negative modulators of the neuroendocrine system. Two other peptides, catestatin and chromofungin, have antimicrobial activity and antifungal activity, respectively. Two transcript variants encoding different isoforms have been found for this gene.
This gene encodes a member of the IAP family of proteins that inhibit apoptosis by binding to tumor necrosis factor receptor-associated factors TRAF1 and TRAF2, probably by interfering with activation of ICE-like proteases. The encoded protein inhibits apoptosis induced by serum deprivation but does not affect apoptosis resulting from exposure to menadione, a potent inducer of free radicals. It contains 3 baculovirus IAP repeats and a ring finger domain. Transcript variants encoding the same isoform have been identified.
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