Search results

Developmental pluripotency-associated 5 proteins (DPPA5) is a 116 amino acid protein, which localizes to the cytoplasm and contains one KH domain. DPPA5 is expressed in embryonic germ (EG), primordial germ (PG) and embryonic stem (ES) cells. DPPA5 has an imperative role in the maintenance of ES cell pluripotency and may be essential for proper embryogenesis.

VAMP8 also called endobrevin, is the main component of a SNARE complex involved in the docking and fusion of synaptic vesicles with the presynaptic membrane. VAMP8 protein is involved in the regulatation of enzyme secretion in pancreatic acinar cells and plays a part in the abscission of the midbody during cell division, which leads to completely separate daughter cells. VAMP8 is essential for dense-granule secretion in platelets. VAMP8 is related with the perinuclear vesicular structures of the early endocytic compartment. VAMP8 interacts particularly with the soluble NSF-attachment protein (alpha-SNAP), through an VAMP8-containing SNARE complex.

ERP44 is an endoplasmic reticulum chaperone that takes part in thiol-dependent retention of the primary secretory pathway, forming mixed disulfides with substrate proteins through its conserved CRFS motif. ERP44 inhibits the calcium channel activity of ITPR1. ERP44 is involved in the control of oxidative protein folding in the endoplasmic reticulum.

IGFBP3 is a member of the insulin-like growth factor binding protein (IGFBP) family and encodes a protein with an IGFBP domain and a thyroglobulin type-I domain. The protein forms a ternary complex with insulin-like growth factor acid-labile subunit (IGFALS) and either insulin-like growth factor (IGF) I or II. In this form, it circulates in the plasma, prolonging the half-life of IGFs and altering their interaction with cell surface receptors. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.

GNAI2 is an alpha subunit of guanine nucleotide binding proteins (G proteins) and holds a guanine nucleotide binding site. GNAI2 takes part in the hormonal regulation of adenylate cyclase. GNAI2 has varies transcript variants encoding different isoforms yet only two full-length isoforms were identified up to date.

SH2 domain-containing protein 1B, also known as SH2D1B activates NK cells. SH2D1B participates in controlling signal transduction through at least 4 receptors, CD84, SLAMF1, LY9 and CD244, expressed on the surface of professional antigen-presenting cells. Two isoforms of the human SH2D1B are produced by alternative splicing. Superior Mesenteric Artery Syndrome is one of the diseases which is associated with SH2D1B.

Receptor Transporter Protein 4 (RTP4) is a member of the TMEM7 family.

Ganglioside GM2 activator (GM2A) is a small glycolipid transport protein which functions as a substrate specific co-factor for the lysosomal enzyme beta-hexosaminidase A. GM2A participates in lipid metabolism. GM2A protein is localized in lysosomes. The GM2A protein forms a large binding pocket for a number of single chain phospholipids and fatty acids. GM2A demonstrates calcium-independent phospholipase activity. GM2A stimulates ganglioside GM2 degradation by presenting GM2 to beta-hexosaminidase A. The Beta-hexosaminidase A, along with GM2A, catalyzes the degradation of the ganglioside GM2, and other molecules containing terminal N-acetyl hexosamines. GM2A gene mutations result in GM2-gangliosidosis type AB or the AB variant of Tay-Sachs disease.

Mitochondrial Ribosomal Protein L1 (MRPL1) exists as a component of the 39S ribosomal subunit and operates in conjunction with other MRPs to mediate protein synthesis. Mitochondrial ribosomes consist of a large 39S subunit and a small 28S subunit, both of which are consist of multiple mitochondrial ribosomal proteins (MRPs) that are encoded by nuclear genes and are vital for protein synthesis within mitochondria. MRPL1 exists as 2 isoforms produced by alternative splicing. Isoform 1 of MRPL1 is ubiquitously expressed while isoform 2 is particularly expressed in heart.

NPPC is proteolytically managed to create a secreted hormone of the natriuretic peptide family. NPPC is vasoactive and natriuretic and controls the evolution and differentiation of cartilaginous growth plate chondrocytes.

CRIP1 also known as Cysteine-Rich Protein 1is a member to the LIM/double zinc finger protein family, membersof which comprise cysteine- and glycine-rich protein-1, rhombotin-1, rhombotin-2, and rhombotin-3. CRIP1 may beimplicated in zinc absorption and also may function as an intracellular zinc transport protein. Among the diseases associated with CRIP1 are situs inversus, and osteosarcoma.

Recoverin is a member of the recoverin family of neuronal calcium sensors. Recoverin is a heterogeneously acylated calcium-binding and intracellular signal transduction 23kDa protein in the photoreceptor cells of retina. Recoverin contains four EF-hands, of which two bind Ca. Ca-induced extrusion of the acyl group from a hydrophobic cleft in the protein drives the translocation of recoverin from solution to the disc membrane. Recoverin may prolong the termination of the phototransduction cascade in the retina by blocking the phosphorylation of photo-activated rhodopsin. Recoverin plays a key role in the inhibition of rhodopsin kinase, a molecule that regulates the phosphorylation of rhodopsin. This in due course controls the ability of the eye to adapt to, and recover from, exposure to the presence of light. Recoverin is a detectable serologic protein that is expressed in patients with cancer-associated retinopathy, a paraneoplastic syndrome.

SERPINB2 is an inhibitory serpin produced primarily in keratinocytes, stimulated monocytes, and placental trophoblasts. SERPINB2 is found primarily as a 47 kDa non-glycosylated intracellular protein that is induced to be secreted as 60 kDa glycoprotein. The glycosylated and unglycosylated SERPINB2 are similarly effective as inhibitors of uPA, the only proven physiological target of SERPINB2.

CXADR Like Membrane Protein or CLMP, part of the CTX family within the immunoglobulin superfamily, is a type 1 transmembrane peptide. CLMP is expressed in the placenta and small intensine, skeletal muscle, colon, lungs and heart. CLMP is located in junction complexes across endothelial and epithelial cells and can take part in cell adhesion. The protein has influence on development of obesity via adipocyte differentiation.

Ribosomes are the organelles which catalyze protein synthesis and composed of a small and a large subunit that consist of over 80 different ribosomal proteins. RPL31, a member of the L31E family of ribosomal proteins, is a component of the 60S subunit ribosome protein located in the cytoplasm. High levels of expression of RPL31 were detected in familial adenomatous polyps. Multiple processed pseudogenes of this gene were detached through the genome, as is typical for genes encoding ribosomal proteins.

Endophilin-B1 (SH3GLB1) is a part of the endophilin family and highly expresses in heart, skeletal muscle, kidney and placenta. Endophilin B1 belongs to the B subgroup of the endophilin family which is needed for preservation of mitochondrial morphology and for the regulation of the outer mitochondrial membrane dynamics. SH3GLB1 is required for normal outer mitochondrial membrane dynamics. Furthermore, SH3GLB1 is required for coatomer-mediated retrograde transport in certain cells. SH3GLB1 interacts with SH3GLB2 and Bcl-2-associated X protein and involved in regulating apoptotic signaling pathways.

RAMP belongs to the type I transmembrane family of proteins called RAMP (receptor/calcitonin activity modifying proteins) which include an extracellular N terminus and a cytoplasmic C terminus. RAMPs are essential for CRLR transport to the plasma membrane. CRLR (calcitonin-receptor-like receptor) has seven transmembrane domains. Depending on which members of the RAMP family are expressed CRLR receptor functions as either an adrenomedullin receptor or a calcitonin-gene-related peptide (CGRP) receptor. In the presence of RAMP1, CRLR functions as a CGRP receptor. The RAMP1 protein takes part in the terminal glycosylation, maturation, and presentation of the CGRP receptor to the cell surface.

CST4 is a member of the cystatin superfamily which contains proteins that hold multiple cystatin-like sequences. Several family members are active cysteine protease inhibitors, whereas others have lost or possibly never attained this inhibitory activity. CST4 strongly inhibits papain (non-competitively) and ficin, partially inhibits stem bromelain and bovine cathepsin C, however does not inhibit porcine cathepsin B or clostripain.

Sorting nexin 3 (SNX3) belongs to the large family of hydrophilic proteins, which interact with various receptor types and are involved in intracellular trafficking. SNX3 interacts with phosphatidylinositol-3-phosphate, and is involved in protein trafficking. SNX3 comprises a distinct subgroup of nexins, which share less sequence similarity outside of the PX domain and have significantly different binding affinities for the tyrosine kinase receptors.

ADP-ribosylation factor-like 14 (ARL14) is a developmentally regulated member of the ADP-ribosylation factor/ARF-like protein (ARF/ARL) family of Ras-related GTPases. ARL14 is GTPase which recruits MYO1E to MHC class II-containing vesicles via the effector protein C11orf46/ARF7EP and thus controls the movement of these vesicles along the actin cytoskeleton in dendritic cells. MHC-II transport was controlled by the GTPase ARL14/ARF7, which recruits the motor myosin 1E via an effector protein ARF7EP.

Secreted frizzled-related protein 2 (SFRP2) belongs to the SFRP family which contains a cysteine-rich domain homologous to the putative Wnt-binding site of Frizzled proteins. SFRP2 functions as soluble modulators of Wnt signaling. Methylation of SFRP2 might indicate on colorectal cancer.

RAD51D is a member of the RAD51 protein family whose members are extremely similar to bacterial RecA and Saccharomyces cerevisiae Rad51. RAD51 protein family members take part in the homologous recombination and repair of DNA. RAD51D forms a complex with several other members of the RAD51 family which catalyzes homologous pairing between single- and double-stranded DNA, and participates in the early stage of recombinational repair of DNA.

Prolactin inducible protein (PIP) is a 17kDa glycoprotein existing in human seminal plasma. PIP is synthesized as a 146 amino acid long polypeptide exhibiting high sequence similarity with mouse submaxillary gland with a single glycosylation site. The precise biological functions of PIP are still ambiguous but various functions have been assigned to PIP due its existence at high concentration in biological fluids. PIP binds to various proteins such as fibrinogen, actin, keratin, myosin and tropomyosin. PIP is also expressed in pathological conditions of the mammary gland and in some exocrine tissues, such as the lacrimal, salivary and sweat glands. Due to PIP’s association with secretory cell differentiation, it has been used in diagnostic evaluation of tumors of breast, salivary gland, and skin.

USP15 belongs to the ubiquitin specific protease (USP) family of deubiquitinating enzymes which has a vital role in ubiquitin-dependent processes through polyubiquitin chain disassembly and hydrolysis of ubiquitin-substrate bonds. USP15 connects with the COP9 signalosome, and takes part in transforming growth factor beta signalling through deubiquitination of receptor-activated SMAD transcription factors. Alternatively spliced transcript variants encoding multiple isoforms of this gene are known, and a pseudo gene of USP15 is sited on the long arm of chromosome 2.