"Bioss"

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Component of the SKA1 complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. Required for timely anaphase onset during mitosis, when chromosomes undergo bipolar attachment on spindle microtubules leading to silencing of the spindle checkpoint. The SKA1 complex is a direct component of the kinetochore-microtubule interface and directly associates with microtubules as oligomeric assemblies. The complex facilitates the processive movement of microspheres along a microtubule in a depolymerization-coupled manner. In the complex, it mediates the interaction with microtubules.

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Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS).

Supplier: Bioss

ZBED2

Supplier: Bioss

Seems to be involved in epithelial-mesenchymal signaling during morphogenesis of ectodermal organs. Isoform 1 binds only to the receptor EDAR, while isoform 3 binds exclusively to the receptor XEDAR.

Supplier: Bioss

The helix-loop-helix (HLH) structures are known motifs commonly found in membrane-active and DNA-binding proteins. The helix-loop-helix proteins HEN1 and HEN2 are DNA-binding proteins that may be involved in cell-type determination in the early nervous system. Studies of expression in normal tissues have demonstrated expression of NHLH1/NSCL-1 and NHLH2/NSCL-2, the genes encoding HEN1 and HEN2, in the developing central and peripheral nervous system, specifically in developing neurons.

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Glycosyltransferase.

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Regulatory subunit of cyclin-dependent kinases that mediates activation of target kinases. Plays a role in transcriptional regulation via its role in regulating the phosphorylation of the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A).

Supplier: Bioss

A scaffold protein that directs CASP3 to certain substrates and facilitates their ordered degradation during apoptosis. May also play a role in mediating CASP3 cleavage of KRT18. Regulates degradation of intermediate filaments during apoptosis. May play a role in the general transcription machinery in the nucleus and might be an important regulator of the activity of GTF3C3. Inhibits DNA transcription in vitro (By similarity).

Supplier: Bioss

WW domain-binding protein 2 (WBP2) is a 261 amino acid protein expressed in most tissues. The WW domain is composed of 38 to 40 semi-conserved amino acids and is shared by various groups of proteins, including structural, regulatory and signaling proteins. The domain mediates protein-protein interactions through the binding of polyproline ligands. WBP2 binds to the WW domain of Yes-associated protein (YAP), WW domain containing E3 ubiquitin protein ligase 1 (AIP5) and WW domain containing E3 ubiquitin protein ligase 2 (AIP2). The gene encoding WBP2 is located on human chromosome 17, which comprises over 2.5% of the human genome and encodes over 1,200 genes, some of which are involved in tumor suppression and in the pathogenesis of Li-Fraumeni syndrome, early onset breast cancer and a predisposition to cancers of the ovary, colon, prostate gland and fallopian tubes.

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Apoptosis is a cell death process that removes toxic and/or useless cells during mammalian development. The apoptotic process is accompanied by shrinkage and fragmentation of the cells and nuclei and degradation of the chromosomal DNA into nucleosomal units. DNA fragmentation factor (DFF) is a heterodimeric protein of 40-kD (DFFB) and 45-kD (DFFA) subunits. DFFA is the substrate for caspase-3 and triggers DNA fragmentation during apoptosis. DFF becomes activated when DFFA is cleaved by caspase-3. The cleaved fragments of DFFA dissociate from DFFB, the active component of DFF. DFFB has been found to trigger both DNA fragmentation and chromatin condensation during apoptosis. Alternatively spliced transcript variants encoding distinct isoforms have been found for this gene but the biological validity of these variants has not been determined. [provided by RefSeq, Jul 2008].

Supplier: Bioss

Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes.

Supplier: Bioss

CD135 is a tyrosine kinase receptor expressed on normal cells including CD34+ hematopoietic stem cells, myelomonocytic progenitors, primitive B cell progenitors, and thymocytes. CD135 is also expressed on malignant hematopoietic cells including AML, ALL and CML BC. CD135, also known as FMS-like tyrosine kinase 3, FLT3, STK1, and Flk2, is a growth factor receptor that binds the FLT3 ligand to promote the growth and differentiation of primitive hematopoietic cells. The intracytoplasmic domain of CD135 is modified by phosphorylation and has been shown to interact with Grb2, SOCS1, VAV1, and Shc. In humans, expression of Flt3 is restricted to subsets of CD34 positive as well as CD34 negative normal bone marrow cells. In these cells, the level of expression of Flt3 is rather low. Most of the CD34 bright Flt3+ cells co-express CD117 at high levels. They may represent early cycling, but not quiescent stem cells. Flt3+ cells in the CD34lo and CD34- populations do not co-express CD117 molecule and may represent B lymphoid precursors.

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CC85C

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NP60 is a 553 amino acid nuclear protein that regulates the phosphorylation and activation of p38 alpha in response to stress. There are five isoforms of NP60 that are produced as a result of alternative splicing events.

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The serine proteinase inhibitors (serpins) compose a superfamily of proteins with a diverse set of functions, including the control of blood coagulation, complement activation, programmed cell death and development. Serpins are secreted glycoproteins that contain a stretch of peptide that mimics a true substrate for a corresponding serine protease. SERPINB12 appears to be an inhibitor of trypsin-like serine proteinases, including mast cell tryptases.

Supplier: Bioss

Syntaxin 13 is an integral membrane protein that belongs to the t-SNARE family, a group of proteins involved in protein transport. Confocal immunofluoresence and electron microscopy studies have shown that syntaxin 13 is primarily localized to tubular early and recycling endosomes, where it colocalizes with transferrin receptor, and it is also localized in endosomal vacuoles. Syntaxin 13 has been found to be expressed in all tissues, with higher levels of the protein found in brain, lung, spleen, thymus and testes. Immunoprecipitation studies show that syntaxin 13 complexes with beta-SNAP, VAMP2/3, and SNAP25. The binding of this complex to alpha-SNAP and NSF is terminated in the presence of ATP. These results suggest that syntaxin 13 is a SNARE protein which mediates the recycling protein flow through tubulo vesicular recycling endosomes.