Search results

Cold inducible RNA-binding protein (CIRBP) has a protective role in the genotoxic stress response by stabilizing transcripts of genes involved in cell survival. CIRBP localizes to the nucleus and contains one RRM (RNA recognition motif) domain. Expressed ubiquitously, CIRBP is believed to play a crucial role in the suppression of cellular proliferation in response to UV irradiation or extreme cold.

Sterile Alpha Motif Domain Containing 13 (SAMD13) is a putative protein interaction module which is present in various proteins involved in numerous biological processes. SAMD13 contains one SAM (sterile alpha motif) domain. The SAM domain, which spreads over around 70 residues, is found in various eukaryotic organisms. SAM domains are known to homo- and hetero-oligomerise, forming multiple self-association constructions and also binding to various non-SAM domain-containing proteins, however with a low affinity constant.

Prefoldin subunit 3 (VBP1) is a member of the prefoldin subunit alpha family. VBP1 interacts with the Von Hippel-Lindau protein in order to create an intracellular complex. Since VBP1 serves as a chaperone protein, it is assumed to have a role in the transport of the Von Hippel-Lindau protein from the perinuclear granules to the nucleus or cytoplasm. VBP1 binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. VBP1 also binds to nascent polypeptide chain and stimulates folding in an environment in which there are numerous competing pathways for nonnative proteins.

Nucleobindin-2 (NUCB2) is a EF-hand calcium-binding protein. Nucleobindin-2 takes part in calcium homeostasis and is a multifunctional protein that interacts with Ca(2+) nucleic acids & various regulatory proteins in different signaling pathways. NUCB2 is localized in neuronal perikarya and dendrites of mouse brain.

SNRPB is one of several nuclear proteins which are found in common among U1, U2, U4/U6, and U5 small ribonucleoprotein particles (snRNPs). These snRNPs are involved in pre-mRNA splicing, and the SNRPB protein may also have a role in pre-mRNA splicing or snRNP structure. SNRPB binds to the downstream cleavage product (DCP) of histone pre-mRNA in a U7 snRNP dependent manner. SNRPB functions in the U7 snRNP complex which is involved in histone 3'-end processing.

Replication Protein A2 (RPA2) is a single stranded DNA binding protein. Human RPA2 is a heterotrimeric protein containing subunits of 14, 32 and 70kDa. The RPA2 protein complex is highly conserved in eukaryotes and is crucial in DNA replication, homologous recombination and nucleotide excision repair. RPA2 C-terminus specifically interacts with the DNA repair enzyme UNG2 and repair factors XPA and Rad52, each of which functions in a different repair pathway. Additionally, RPA2 binds specifically to the SH2 domain of Stat3 in vivo, and overexpression of RPA2 corresponds to the augmented growth factor-stimulated tyrosine phosphorylation and transcription activities of Stat3.

NFKB inhibitor interacting Ras-like 2 (NKIRAS2) is an inhibitor of the transcription factor NF-kappaB. NKIRAS2 is similar to the Ras-like small GTPases which associate with IkappaB. The Ras-like proteins- NKIRAS1 and NKIRAS2, interact with the PEST domains of I?B? and I?B? and reduce their rate of degradation. NKIRAS2 is an atypical Ras-like protein which functions as a potent regulator of NF-kappa-B activity by preventing the degradation of NF-kappa-B inhibitor beta (NFKBIB) by most signals, explaining why NFKBIB is more impervious to degradation.

ATG5 is a member of the autophagy-related (ATG) genes family. Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents. ATG5 protein is essential for autophagy. It conjugates to ATG12 and associates with isolation membrane to form autophagosomes. In addition ATG5 takes a vital part in the apoptotic process and it is expressed relatively late in the apoptotic process, downstream of caspase activity.

Regulatory Factor X-Associated Ankyrin-Containing Protein (RFXANK) contains ankyrin repeats involved in protein-protein interactions. RFXANK, along with regulatory factor X-associated protein and regulatory factor-5, figures a complex which binds to the X box motif of certain MHC class II gene promoters and activates their transcription. After bound to the promoter, this complex associates with the non-DNA-binding factor MHC class II transactivator, which controls the cell type specificity and inducibility of MHC class II gene expression. Mutations in RFXANK have been linked to bare lymphocyte syndrome type II, complementation group B.

FGF-1 Intracellular-Binding Protein (FIBP) which is a member of Fibroblast growth factors (FGFs) binds to internalized FGF-1 and is thought to be involved in mitogenic function of FGF-1. FGF activity effects development, adult tissue homeostasis, angiogenesis and cancer progression. FIBP localizes to the nucleus and is greatly expressed in heart, skeletal muscle and pancreas and at lower levels in brain, placenta, liver and kidney.

Antigen 85B Mycobacterium Tuberculosis-is the most abundant protein exposed by M. Tuberculosis, as well as a potent immunoprotective antigen and a leading drug target. Ag85 induces strong T-cell proliferation and IFN-g secretion in most healthy individuals exposed to M. tuberculosis, in BCG-vaccinated mice and humans, whereas the antibody against Ag85 are more prevalent in active tuberculosis patients with decreased cellular immune response.

BTB/POZ domain-containing protein KCTD5 (KCTD5), is a 234 amino acid protein which localizes mainly in the cytoplasm however translocates to the nucleus on interaction with REP proteins. The expression of KCTD5 is up regulated post-transcriptionally in peripheral blood lymphocytes stimulated via the T-cell receptor. KCTD5 interacts particularly with cullin3, attaches ubiquitinated proteins, and created oligomers through its BTB domain.

RAB, Member RAS Oncogene Family-Like 5 (RABL5) belongs to the Ras superfamily of small GTP-binding proteins. The Ras-related superfamily of guanine nucleotide binding proteins includes the R-Ras, Rap, Ral/Rec and Rho/Rab subfamilies. Rab proteins have an essential role in endocytosis or in biosynthetic protein transport. The transporting process of newly synthesized proteins from the endoplasmic reticulum to various stacks of the Golgi complex and to secretory vesicles includes the movement of carrier vesicles and requires Rab protein function.

PEDF is a neurotrophic protein that induces extensive neuronal differentiation in retinoblastoma cells. SerpinF1 is a potent inhibitor of angiogenesis. EPC1 doesn’t undergo the stressed to relaxed conformation transition characteristic as of the active serpins since it exhibits no serine protease inhibitory activity.
Aqueous humour level of asymmetric dimethylarginine is correlated with PEDF in humans. ADMA and PEDF levels are increased in response to inflammation in uveitis.
Lack of PEDF expression is a potent factor for the enhancement of tumor growth and angiogenesis in breast cancer.
PEDF & VEGF genes contribute to the development of diabetic retinopathy.
PEDF and VEGF structural changes in blood vessel wall play an important role in the pathophysiology of PD patients.
PEDF-overexpressing tumors exhibited reduced intratumoral angiogenesis.
SerpinF1 is a new promising approach for the treatment of osteosarcoma.
Levels of the natural ocular anti-angiogenic factor SentrinF1 (PEDF) is associated with proliferative retinopathy.
VEGF secreted by retinal pigment epithelial cells upregulates PEDF expression via VEGFR-1 in an autocrine manner.
Sentrin-F1 concentration in the aqueous humor of diabetic patients predicts who will develop progression of retinopathy.
PEDF blocks angiogenic effects of leptin through its anti-oxidative properties.

Albumin is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted albumin. Albumin is a soluble, monomeric protein which comprises about one-half of the blood serum protein. Albumin functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume. Mutations in this gene on chromosome 4 result in various anomalous proteins. Albumin is a globular unglycosylated serum protein of molecular weight 65,000. The human albumin gene is 16,961 nucleotides long from the putative 'cap' site to the first poly (A) addition site. It is split into 15 exons which are symmetrically placed within the 3 domains that are thought to have arisen by triplication of a single primordial domain.
HSA is widely used to stabilize

IMP3 is the human homolog of the yeast Imp3 protein and Essential for the early cleavages during pre-18S ribosomal RNA processing. IMP3 is a Part of the 60-80S U3 small nucleolar ribonucleoprotein (U3 snoRNP). IMP3 is a member of to the ribosomal protein S4P family and localizes to the nucleoli and interacts with the U3 snoRNP complex. IMP3 contains an S4 domain. U3 small nucleolar ribonucleoprotein protein IMP3 is a protein which in humans is encoded by the IMP3 gene.

Tumor-associated calcium signal transducer 2 (TACSTD2), is a member of to the EPCAM family. TACSTD2 is an intronless gene which encodes a carcinoma-associated antigen. TACSTD2 may act as a growth factor receptor and as a cell surface receptor that transduces calcium signals. Mutations of TACSTD2 have been associated with gelatinous drop-like corneal dystrophy.

Toll interacting protein (TOLLIP) is an inhibitory adaptor protein within Toll-like receptors. The TLR pathway is a part of the innate immune system which recognizes structurally conserved molecular patterns of microbial pathogens, initiating an inflammatory immune response. Negative regulation of TLR signaling by TOLLIP might restrict the production of proinflammatory mediators during inflammation and infection. Furthermore, TOLLIP forms a complex with Tom1 to regulate endosomal transferring of ubiquitinated proteins.

NusA is an important player in both prevention and enhancement of transcriptional termination. NusA is important both in Rho-dependent and intrinsic termination, as well as in lambda and other phage antitermination systems. The NusA gene was first identified by isolation of the nusAl mutation, which limits bacteriophage-l growth by preventing the antitermination activity of the l N protein. NusA plays a role in transcriptional antitermination in the cell. It has been shown to specifically aid in read-through of the RNA polymerase genes rpoB and rpoC, as well as in successful synthesis of the ribosomal RNA genes. Additionally to its anti-termination role, NusA is needed for both Rho-dependent and intrinsic transcriptional termination. NusA is obligatory for Rho-dependent termination in lambda phage and in the cell. NusA plays a role in intrinsic termination and the inhibition of RNA elongation. However NusA interacts with all three subunits of RNA polymerase, its termination activity primarily depends on its interaction with the carboxy-terminus of RpoA. NusA induces conformational change in RNA polymerase & prevents RNA interaction with RpoA. This binding sequentially activates NusA, allowing it to bind RNA and promote formation of hairpins at intrinsic termination sites. NusA binds Rho, and participates with sigma70 for binding to the core RNA polymerase complex. NusA does not compete with NusG for binding to either Rho or the polymerase, despite modulating the same process as NusG in both cases.

C17orf103 is a member of the GTLF3B family and is encoded by a gene which is located in human chromosome 17p11.2. BRCA1 and p53 are 2 main tumor suppressor genes which are linked to chromosome 17. Tumor suppressor p53 is necessary for maintenance of cellular genetic integrity by moderating cell fate through DNA repair versus cell death. C17orf103 is also related to neurofibromatosis, a disorder characterized by neural and epidermal lesions, and dysregulated Schwann cell growth.

Ephrin type-B receptor 4 isoform b (Ephb4) belongs to the Eph receptor tyrosine kinase family which functions in neuronal guidance and mediate venal/arterial separation. EPHB4-mediated forward signaling regulates cellular repulsion and segregation form EFNB2-expressing cells. Furthermore, Ephb4 has a role in postnatal blood vessel remodeling, morphogenesis and permeability and is therefore essential in the context of tumor angiogenesis.

Protein Tyrosine Phosphatase Non Receptor Type-4, also known asPTPN4 belongs to the protein tyrosine phosphatase, PTP family. PTPs are identified as signaling molecules which regulate a variety of cellular processes as well as cell growth, differentiation, mitotic cycle, and oncogenic transformation. PTPN4 is broadly expressed non-receptor protein tyrosine phosphatase. In addition, PTPN4 interacts with glutamate receptor delta 2 & epsilon, and affects glutamate receptors signaling and/or in regulation of their activities through tyrosine dephosphorylation.