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Beschreibung:
Hemogen is a 484 amino acid protein encoded by the human gene HEMGN. Hemogen is a nuclear protein that is expressed in hematopoietic precursor cells and can be detected in CD34+ and K-562 leukemia cell line. It is also expressed in bone marrow, testis, thymus and thyroid tumors, non-Hodgkin lymphoma, various leukemia cell lines, peripheral blood mononuclear cells (PBMCs) and bone marrow mononuclear cells (BMMCs) of patients with leukemia. Hemogen is down-regulated during megakaryocytic differentiation of K-562 cells by 12-O-tetradecanoylphorbol-13-acetate (TPA) (at protein level). It can be up-regulated in normal PBMCs by mitogens.
Beschreibung:
FGFR1OP2 belongs to the SIKE family. The FGFR1OP2 (FGFR1 oncogene partner 2) gene was identified through its involvement in a fusion with the FGFR1 gene. FGFR1OP2 may be involved in the wound healing pathway. It is expressed in bone marrow, spleen and thymus. A chromosomal aberration involving FGFR1OP2 may be a cause of stem cell myeloproliferative disorder (MPD). Insertion ins(12;8)(p11;p11p22) with FGFR1. MPD is characterized by myeloid hyperplasia, eosinophilia and T cell or B cell lymphoblastic lymphoma. In general it progresses to acute myeloid leukemia. The fusion protein FGFR1OP2-FGFR1 may exhibit constitutive kinase activity and be responsible for the transforming activity.
Beschreibung:
The Annexins constitute a family of structurally-related, relatively abundant proteins that exhibit Ca2+-dependent binding to phospholipids. Annexins function in multiple aspects of cell biology including regulation of membrane trafficking, transmembrane channel activity, inhibition of phospholipase A2, inhibition of coagulation and mediation of cell-matrix interactions. Annexin A13 is considered the original progenitor of the 12 members of vertebrate Annexins. The expression of Annexin A13 is highly tissue-specific, being expressed only in intestinal and kidney epithelial cells. This expression is associated with a highly differentiated intracellular transport function. Two alternative splicing isoforms of Annexin A13 exist, both of which bind to rafts.
Beschreibung:
Neuroligins are a family of plasma membrane proteins that possess an N-terminal hydrophobic domain, a large esterase homology domain, a single transmembrane region, a short cytoplasmic domain, and an EF-hand binding domain (1,2). Members of the neuroligin family include Neuroligin 1, Neuroligin 2 and Neuroligin 3. Neuroligins are expressed in excitatory neuronal synaptic clefts. Neuroligins play a role in the formation and remodeling of CNS synapses by binding to b-neurexins, a family of neuronal cell surface proteins. Neuroexin 1b binds to the EF-hand domain of Neuroligin 1 and requires calcium ion. Neuroligins also bind to PSD-95, which may recruit ion channels and neurotransmitter receptors to the synapses.
Beschreibung:
PHC1 is a 1,004 amino acid nuclear protein that is a component of the PcG multiprotein PRC1 complex. Specifically, the PcG PRC1 complex modifies histones, remodels chromatin and mediates monoubiquination of Histone H2A. Other constituent proteins involved in the PcG PRC1 complex are Mel-18, Bmi-1, M33, MPc2, MPc3, RING1, Ring1b, as well as several others. Existing as a homodimer, PHC1 contains one FCS-type zinc finger and a SAM (sterile alpha motif) domain. PHC1 is encoded by a gene located on human chromosome 12, which encodes over 1,100 genes and comprises approximately 4.5% of the human genome.
Beschreibung:
Several protein-protein interactions are essential to membrane fusion during endocytosis. Membrane fusion requires interaction among SNARE1 proteins associated with both donor and acceptor membranes (1,2). Following membrane fusion, the α-SNAP cytoplasmic adapter protein binds to the SNARE complex. N-ethylmaleimide-sensitive factor (NSF), a hexameric ATPase, then associates with the α-SNAP/SNARE complex to mediate SNARE disassembly during membrane fusion (3,4). The ATPase activity of NSF induces a conformational change in the α-SNAP/SNARE complex that leads to its dissociation from the membrane, membrane fusion and eventual recycling of the SNARE complex for subsequent membrane fusion (3,4).
Beschreibung:
The smallest of the human chromosomes, 21 makes up about 1.5% of the human genome. Chromosome 21 contains nearly 300 genes and 47 million base pairs. Down syndrome, also known as trisomy 21, is the disease most commonly associated with chromosome 21. Alzheimer's disease, Jervell and Lange-Nielsen syndrome and amyotrophic lateral sclerosis are also associated with chromosome 21. Translocations are found to occur between chromosome 21 and 8, and chromosome 21 and 12, in certain leukaemias. C2CD2 is an 696 amino acid protein that is secreted. The C2CD2 gene product has been provisionally designated C2CD2 pending further characterisation.
Beschreibung:
Heterotrimeric G protein-mediated signal transduction is a dynamically regulated process with the intensity of signal decreasing over time despite the continued presence of the agonist (1,2). G protein-coupled receptor kinases (GRKs) are activated by activated G protein-coupled receptors, and they function to phosphorylate and inactivate cell surface receptors in the heterotrimeric G protein signaling cascade (3,4). GIT1 (for GRK-interactor 1) and GIT2 are GTPase-activating proteins (GAP) for members of the ADP ribosylation factor (ARF) family of small GTP-binding proteins, which are involved in vesicular trafficking (5,6). GIT1 overexpression results in reduced internalization and resensitization of b2-adrenergic receptor, thus reducing b2-adrenergic receptor signaling (5).
Beschreibung:
C9 is a plasma protein synthesized in the liver and monocytes consisting of a single polypeptide chain. C9 is a part of the membrane attack complex (MAC), an important component of the immune system. The MAC forms upon complement system activation by invading pathogenic bacteria and consists of the four major complement proteins: C5b, C6, C7 and C8. These complement proteins bind to the outer surface of the plasma membrane of the invading cell. C9 binds to the membrane associated C5b-8 protein, which leads to the circular polymerization of 12-18 C9 molecules. These polymerized C9 molecules form a ring structure in the membrane. Molecules can then diffuse freely through this transmembrane channel, causing cell lysis and destruction of the invading bacterial cell.
Beschreibung:
C9 is a plasma protein synthesised in the liver and monocytes consisting of a single polypeptide chain. C9 is a part of the membrane attack complex (MAC), an important component of the immune system. The MAC forms upon complement system activation by invading pathogenic bacteria and consists of the four major complement proteins: C5b, C6, C7 and C8. These complement proteins bind to the outer surface of the plasma membrane of the invading cell. C9 binds to the membrane associated C5b-8 protein, which leads to the circular polymerisation of 12-18 C9 molecules. These polymerised C9 molecules form a ring structure in the membrane. Molecules can then diffuse freely through this transmembrane channel, causing cell lysis and destruction of the invading bacterial cell.
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