"Bioss"

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Transcription factor. Involved in SHH-dependent neural patterning. Together with NKX2-2 and NKX6-1 acts to restrict the generation of motor neurons to the appropriate region of the neural tube. Belongs to the class I proteins of neuronal progenitor factors, which are repressed by SHH signals. Involved in the transcriptional repression of MNX1 in non-motor neuron cells (By similarity).

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The steroid receptor superfamily acts through direct association with DNA sequences known as hormone response elements (HREs) and binds DNA as either homo- or heterodimers. The promiscuous mediator of heterodimerization, RXR, is the receptor for 9-cis retinoic acid, and dimerizes with VDR, TR, PPAR, and several novel receptors including LXR (also referred to as RLD-1) and FXR. FXR and LXR fall into a category of proteins termed “orphan receptors” because of their lack of a defined function, and in the case of LXR, the lack of a defined ligand. FXR has been shown to bind a class of lipid molecules called farnesoids. LXR/RXR heterodimers have highest affinity for DR-4 DNA elements while FXR/RXR heterodimers bind IR-1 elements. Both LXR/RXR and FXR/RXR heterodimers retain their responsiveness to 9-cis retinoic acid.

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Mediates the binding, internalization, and catabolism of lipoprotein particles. It can serve as a ligand for the LDL (apo B/E) receptor and for the specific apo-E receptor (chylomicron remnant) of hepatic tissues.

Supplier: Bioss

Receptor to interleukin-8, which is a powerful neutrophils chemotactic factor. Binding of IL-8 to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activate a phosphatidylinositol-calcium second messenger system. This receptor binds to IL-8 with a high affinity and to MGSA (GRO) with a low affinity.

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Syntaxin 1a is potentially involved in docking of synaptic vesicles at presynaptic active zones and may play a critical role in neurotransmitter exocytosis. Haploinsufficiency of STX1A may be the cause of certain cardiovascular and musculo skeletal abnormalities observed in Williams-Beuren syndrome (WBS), a rare developmental disorder.

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Forms a high-affinity link between the actin cytoskeleton and the membrane. Isoform 1 (archvillin) is among the first costameric proteins to assemble during myogenesis and it contributes to myogenic membrane structure and differentiation. Appears to be involved in myosin II assembly. May modulate myosin II regulation through MLCK during cell spreading, an initial step in cell migration. May play a role in invadopodial function. Isoform 2 may be involved in modulation of focal adhesions. Supervillin-mediated down-regulation of focal adhesions involves binding to TRIP6. Plays a role in cytokinesis through KIF14 interaction (By similarity).

Supplier: Bioss

Involved in the transcriptional regulation of genes required for mesoderm differentiation. Probably plays a role in limb pattern formation. Acts as a negative regulator of PML function in cellular senescence. May be required for cardiac atrioventricular canal formation (By similarity).

Supplier: Bioss

This gene encodes a member of a family of neuronal cell surface proteins. Members of this family may act as splice site-specific ligands for beta-neurexins and may be involved in the formation and remodeling of central nervous system synapses. Mutations in this gene may be associated with autism and Asperger syndrome. Multiple transcript variants encoding distinct isoforms have been identified for this gene. [provided by RefSeq, Oct 2009].

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RIMS-binding proteins (RIM-BPs) serve as adaptors during vesicle fusion and release by forming links between synaptic-vesicle fusion apparatuses and calcium channels. Specifically, RIM-BP2 (RIMS binding protein 2), also known as RBP2, is a 1,052 amino acid protein that links L-type Ca++ CP Alpha1D, N-type Ca++ CP Alpha1B, Rim1 and Rim2 during synaptic transmission. RIM-BP2 contains three fibronectin type-III domains and three SH3 domains, which are used to mediate binding to a proline-rich motifs. Existing as three alternatively spliced isoforms, RIM-BP2 is encoded by a gene that maps to human chromosome 12q24.33 and mouse chromosome 5 G1.3.

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Protein transport across the nucleus is a selective, multi-step process involving several cytoplasmic factors that mediate protein passage through the nuclear pore complex (NPC). Cytoplasmic proteins that contain nuclear localization signals (NLSs) must be recognized as import substrates, dock at the nuclear pore complex and translocate across the nuclear envelope in an ATP-dependent fashion. Karyopherin alpha 1 and karyopherin alpha 6 are widely expressed nuclear import proteins that act as adaptors for karyopherin ∫1, specifically binding to and guiding NLS-containing proteins to the NPC. Both karyopherin alpha 1 and karyopherin alpha 6 contain one IBB domain and ten ARM repeats through which they convey their protein binding and localization function. Together, karyopherin å1 and karyopherin å6 are responsible for ensuring the nuclear import of NLS-containing substrates

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Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. They can phosphorylate a large number of proteins. Participates in Wnt signaling.

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Activates the metallothionein I promoter. Binds to the metal responsive element (MRE).

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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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Acts as a substrate adapter protein for the E3 ubiquitin ligase complex formed by CUL3 and RBX1 and targets NFE2L2/NRF2 for ubiquitination and degradation by the proteasome, thus resulting in the suppression of its transcriptional activity and the repression of antioxidant response element-mediated detoxifying enzyme gene expression. Retains NFE2L2/NRF2 and may also retain BPTF in the cytosol. Targets PGAM5 for ubiquitination and degradation by the proteasome.

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Transcriptional repressor. Down-regulates transcription activation by NF-kappa-B by promoting the deacetylation of RELA at 'Lys-310'. Promotes HDAC1 binding to promoter regions. Down-regulates expression of anti-apoptotic genes that are controlled by NF-kappa-B. Promotes apoptosis in cells that have inadequate adherence to a substrate, a process called anoikis, and may thereby inhibit metastasis. May be a mediator of metastasis suppression in breast carcinoma.

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JIP-4 is a 1,321 amino acid protein encoded by the human gene SPAG9. It contains a large N-terminal extracellular domain, a short transmembrane helical domain, and a cytoplasmic domain. There are 6 N-glycosylation sites, several phosphorylation sites for cAMP/cGMP-dependent protein kinase, protein kinase C, and casein kinase II, and 10 putative myristoylation sites. There is also a leucine zipper motif, with 6 leucine repeats, that may aid in dimerization since there is no upstream basic domain characteristic of DNA binding proteins. The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. JIP-4 is a cytoplasmic, perinuclear protein that has eight known isoforms whose expression varies by tissue and disease state.