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https://en.wikipedia.org/wiki/LAIR1 | Leukocyte-associated immunoglobulin-like receptor 1 is a protein that in humans is encoded by the LAIR1 gene. LAIR1 has also been designated as CD305 (cluster of differentiation 305).
Function
The protein encoded by this gene is an inhibitory receptor found on peripheral mononuclear cells, including NK cells, T cells, and B cells. Inhibitory receptors regulate the immune response to prevent lysis of cells recognized as self. The gene is a member of both the immunoglobulin superfamily and the leukocyte-associated inhibitory receptor family. The gene maps to a region of 19q13.4 called the leukocyte receptor cluster, which contains at least 29 genes encoding leukocyte-expressed receptors of the immunoglobulin superfamily.
Interactions
LAIR1 has been shown to interact with PTPN11 and PTPN6.
References
Further reading
External links
Clusters of differentiation
Immunoglobulin superfamily |
https://en.wikipedia.org/wiki/MAGEA3 | Melanoma-associated antigen 3 (MAGE-A3) is a protein that in humans is encoded by the MAGEA3 gene.
Genetics
This gene is a member of the melanoma-associated antigen gene family. The members of this family encode proteins with 50 to 80% sequence identity to each other. The promoters and first exons of the MAGEA genes show considerable variability, suggesting that the existence of this gene family enables the same function to be expressed under different transcriptional controls. The MAGEA genes are clustered at chromosomal location Xq28. They have been implicated in some hereditary disorders, such as dyskeratosis congenita.
Function and Clinical relevance
The normal function of MAGE-A3 in healthy cells is unknown. The presence of the antigen on tumor cells has been associated with worse prognosis. In one study, high levels of MAGE-A3 in lung adenocarcinoma were associated with shorter survival.
MAGE-A3 is a tumor-specific protein, and has been identified on many tumors including melanoma, non-small cell lung cancer, hematologic malignancies, among others. Currently, GlaxoSmithKline is developing a cancer vaccine targeting MAGE-A3. The vaccine is a fusion protein of MAGE-A3 and Haemophilus influenzae protein D, combined with a proprietary immunoadjuvant.
References
Further reading |
https://en.wikipedia.org/wiki/MMP19 | Matrix metalloproteinase-19 (MMP-19) also known as matrix metalloproteinase RASI is an enzyme that in humans is encoded by the MMP19 gene.
Function
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. This protein is expressed in human epidermis and endothelial cells and it has a role in cellular proliferation, migration, angiogenesis and adhesion. Multiple transcript variants encoding distinct isoforms have been identified for this gene.
References
Further reading
External links
The MEROPS online database for peptidases and their inhibitors: M10.021
Matrix metalloproteinases
EC 3.4.24 |
https://en.wikipedia.org/wiki/MTAP | S-methyl-5'-thioadenosine phosphorylase (MTAP) is an enzyme in humans responsible for polyamine metabolism. It is encoded by the methylthioadenosine phosphorylase (MTAP) gene on chromosome 9. Multiple alternatively spliced transcript variants have been described for this gene, but their full-length natures remain unknown.
This gene encodes an enzyme that plays a major role in polyamine metabolism and is important for the salvage of both adenine and methionine. It is responsible for the first step in this pathway, where it catalyzes the reversible phosphorylation of MTA to adenine and 5-methylthioribose-1-phosphate. This takes place after MTA is generated from S-adenosylmethionine.
MTAP was identified for the first time and characterized likely as a phosphorylase in 1969 by Pegg and Williams-Ashman. The first purification that allowed characterization was by a group in 1986. This purification allowed researchers to investigate why there is the lower expression of MTAP in some types of cancer.
Increased levels of MTA in tumor cells along with lower expression of MTAP. The enzyme is deficient in many cancers because this gene and the tumor-suppressive p16 gene are co-deleted.
Gene
The MTAP gene location is 9p21.3 which is chromosome 9, p arm, band 2, sub-band1, and sub-sub-band 3. The MTAP gene has seven isomers which are created when mRNA’s of the same locus have different transcription start sites. Due to the nature of the MTAP gene and the surrounding genes of chromosome |
https://en.wikipedia.org/wiki/MT-CYB | Cytochrome b is a protein that in humans is encoded by the MT-CYB gene. Its gene product is a subunit of the respiratory chain protein ubiquinol–cytochrome c reductase (UQCR, complex III or cytochrome bc1 complex), which consists of the products of one mitochondrially encoded gene, MT-CYB (mitochondrial cytochrome b), and ten nuclear genes—UQCRC1, UQCRC2, CYC1, UQCRFS1 (Rieske protein), UQCRB, "11kDa protein", UQCRH (cyt c1 Hinge protein), Rieske protein presequence, "cyt c1 associated protein", and Rieske-associated protein.
Structure
The MT-CYB gene is located on the p arm of mitochondrial DNA in position 12 and spans 1,140 base pairs. The gene produces a 42.7 kDa protein named cytochrome b composed of 380 amino acids. Cytochrome b is an integral membrane protein with hydrophobic properties. The catalytic core of the enzyme is composed of eight transmembrane helices, the iron-sulfur protein, and cytochrome c1. Cytochrome b is a fundamental component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. The structure of the complex is a symmetric homodimer. It is composed of eleven structural subunits, including one mitochondrial genome encoded cytochrome b and ten other nucleus encoded subunits. These subunits include three respiratory subunits (MT-CYB, CYC1 and UQCRFS1), two core proteins (UQCRC1 and UQCRC2) a |
https://en.wikipedia.org/wiki/NACA%20%28gene%29 | Nascent-polypeptide-associated complex alpha polypeptide, also known as NACA, is a protein which in humans is encoded by the NACA gene.
Function
NACA prevents short recently synthesized (i.e., nascent) ribosome-associated polypeptides from inappropriate interactions with cytosolic proteins. NACA binds nascent-polypeptide domains emerging from ribosomes unless it contains a signal peptide which is fully exposed. Depletion of NACA from ribosomes carrying nascent polypeptides allows the signal recognition particle (SRP) to crosslink to polypeptides regardless of whether or not they contain signal peptides or not. In the absence of NACA, proteins lacking signal peptides can be mis-translocated into the endoplasmic reticulum.
The NACA protein is expressed in bone during development and acts as a transcriptional coactivator in conjunction with acidic activators.
Interactions
NACA has been shown to interact with BTF3, FADD, C-jun, and 3 members of taxilin family.
References
Further reading
Human proteins |
https://en.wikipedia.org/wiki/NFATC4 | Nuclear factor of activated T-cells, cytoplasmic 4 is a protein that in humans is encoded by the NFATC4 gene.
Function
The product of this gene is a member of the nuclear factors of activated T cells DNA-binding transcription complex. This complex consists of at least two components: a preexisting cytosolic component that translocates to the nucleus upon T cell receptor (TCR) stimulation and an inducible nuclear component. Other members of this family of nuclear factors of activated T cells also participate in the formation of this complex. The product of this gene plays a role in the inducible expression of cytokine genes in T cells, especially in the induction of the IL-2 and IL-4.
Interactions
NFATC4 has been shown to interact with CREB-binding protein.
See also
NFAT
References
Further reading
External links
Transcription factors
Human proteins |
https://en.wikipedia.org/wiki/SERPINB9 | Serpin B9 is a protein that in humans is encoded by the SERPINB9 gene.
PI9 belongs to the large superfamily of serine proteinase inhibitors (serpins), which bind to and inactivate serine proteinases. These interactions are involved in many cellular processes, including coagulation, fibrinolysis, complement fixation, matrix remodeling, and apoptosis (Sprecher et al., 1995).[supplied by OMIM]
See also
Serpin
References
Further reading
External links
The MEROPS online database for peptidases and their inhibitors: I04.014
Serine protease inhibitors |
https://en.wikipedia.org/wiki/PIK3C2B | Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing beta polypeptide is an enzyme that in humans is encoded by the PIK3C2B gene.
Function
The protein encoded by this gene belongs to the phosphoinositide 3-kinase (PI3K) family. PI3-kinases play roles in signaling pathways involved in cell proliferation, oncogenic transformation, cell survival, cell migration, and intracellular protein trafficking. This protein contains a lipid kinase catalytic domain as well as a C-terminal C2 domain, a characteristic of class II PI3-kinases. C2 domains act as calcium-dependent phospholipid binding motifs that mediate translocation of proteins to membranes, and may also mediate protein-protein interactions. The PI3-kinase activity of this protein is sensitive to low nanomolar levels of the inhibitor wortmannin. The C2 domain of this protein was shown to bind phospholipids but not Ca2+, which suggests that this enzyme may function in a calcium-independent manner.
References
Further reading |
https://en.wikipedia.org/wiki/PLXNB1 | Plexin B1 is a protein of the plexin family that in humans is encoded by the PLXNB1 gene.
Function
Within neural tissues, the plexin family serves as transmembrane receptors for Semaphorins. Outside of neural tissues, Plexin B1 is implicated in the control of cell migration.
Interactions
PLXNB1 has been shown to interact with ARHGEF12, Rnd1 and ARHGEF11.
References
Chapoval SP, Hritzo M, Qi X, Tamagnone L, Golding A and Keegan AD. "Semaphorin 4A Stabilizes Human Regulatory T Cell Phenotype via Plexin B1". ImmunoHorizons, February 1, 2019, 3 (2) 71-87;
Further reading
External links |
https://en.wikipedia.org/wiki/SEPT5 | Septin-5 is a protein that in humans is encoded by the SEPT5 gene.
Function
This gene is a member of the septin gene family of nucleotide binding proteins, originally described in yeast as cell division cycle regulatory proteins. Septins are highly conserved in yeast, Drosophila, and mouse and appear to regulate cytoskeletal organization. Disruption of septin function disturbs cytokinesis and results in large multinucleate or polyploid cells. This gene is mapped to 22q11, the region frequently deleted in DiGeorge and velocardiofacial syndromes. A translocation involving the MLL gene and this gene has also been reported in patients with acute myeloid leukemia. Two transcripts of this gene, a major one of 2.2 kb and a minor one of 3.5 kb, have been observed. The 2.2 kb form results from the utilization of a non-consensus polyA signal (AACAAT). In the absence of polyadenylation from this imperfect site, the consensus polyA signal of the downstream neighboring gene (GP1BB; platelet glycoprotein Ib) is used, resulting in the 3.5 kb transcript. An alternatively spliced transcript variant with a different 5' end has also been identified, but its full-length nature has not been completely determined.
Interactions
SEPT5 has been shown to interact with:
PARK2, and
SEPT8
References
Further reading |
https://en.wikipedia.org/wiki/PODXL | Podocalyxin-like protein 1 is a protein that in humans is encoded by the PODXL gene.
Function
This gene encodes a member of the CD34 sialomucin protein family. The encoded protein was originally identified as an important component of glomerular podocytes. Inactivation of the encoding gene in mice leads to anuria, omphalocele and perinatal death. Podocytes are highly differentiated epithelial cells with interdigitating foot processes covering the outer aspect of the glomerular basement membrane. Other biological activities of the encoded protein include: binding in a membrane protein complex with Na+/H+ exchanger regulatory factor to intracellular cytoskeletal elements, playing a role in hematopoietic cell differentiation, and being expressed in vascular endothelium cells and binding to L-selectin.
Expression
The expression and localisation of PODXL in human cells, tissues and organs have been investigated by the Human Protein Atlas consortium. According to antibody-based profiling, the protein is present in glomerular podocytes, endothelial cells, glandular cells in fallopian tube, uterus and seminal vesicle and according to RNA expression analysis, the PODXL transcripts are present in all analysed human tissues. Based on confocal microscopy, the protein is mainly localised to the plasma membrane and microtubule organizing center and in addition localized to vesicles.
Interactions
PODXL has been shown to interact with Sodium-hydrogen exchange regulatory cofactor 2.
|
https://en.wikipedia.org/wiki/Periplakin | Periplakin is a protein that in humans is encoded by the PPL gene.
The protein encoded by this gene is a component of desmosomes and of the epidermal cornified envelope in keratinocytes. The N-terminal domain of this protein interacts with the plasma membrane and its C-terminus interacts with intermediate filaments. Through its rod domain, this protein forms complexes with envoplakin. This protein may serve as a link between the cornified envelope and desmosomes as well as intermediate filaments. AKT1/PKB, a protein kinase mediating a variety of cell growth and survival signaling processes, is reported to interact with this protein, suggesting a possible role for this protein as a localization signal in AKT1-mediated signaling.
Interactions
PPL (gene) has been shown to interact with Keratin 8 and Envoplakin.
See also
List of target antigens in pemphigus
References
Further reading
External links
Plakins |
https://en.wikipedia.org/wiki/MAP2K5 | Dual specificity mitogen-activated protein kinase kinase 5 is an enzyme that in humans is encoded by the MAP2K5 gene.
Function
The protein encoded by this gene is a dual specificity protein kinase that belongs to the MAP kinase kinase family. This kinase specifically interacts with and activates MAPK7/ERK5. This kinase itself can be phosphorylated and activated by MAP3K3/MEKK3, as well as by atypical protein kinase C isoforms (aPKCs). The signal cascade mediated by this kinase is involved in growth factor stimulated cell proliferation and muscle cell differentiation. Four alternatively spliced transcript variants of this gene encoding distinct isoforms have been described.
Upstream
This kinase itself can be phosphorylated and activated by MAP3K3/MEKK3, as well as by atypical protein kinase C isoforms (aPKCs).
Downstream
This kinase specifically interacts with and activates MAPK7/ERK5.
Interactions
MAP2K5 has been shown to interact with MAPK7, MAP3K2, Protein kinase Mζ and MAP3K3.
References
Further reading
EC 2.7.12 |
https://en.wikipedia.org/wiki/RDH5 | 11-cis retinol dehydrogenase is an enzyme that in humans is encoded by the RDH5 gene.
References
Further reading |
https://en.wikipedia.org/wiki/RFC3 | Replication factor C subunit 3 is a protein that in humans is encoded by the RFC3 gene.
Function
The elongation of primed DNA templates by DNA polymerase delta and DNA polymerase epsilon requires the accessory proteins proliferating cell nuclear antigen (PCNA) and replication factor C (RFC). RFC, also named activator 1, is a protein complex consisting of five distinct subunits of 140, 40, 38, 37, and 36 kDa. This gene encodes the 38 kDa subunit. This subunit is essential for the interaction between the 140 kDa subunit and the core complex that consists of the 36, 37, and 40 kDa subunits. Alternatively spliced transcript variants encoding distinct isoforms have been described.
Interactions
RFC3 has been shown to interact with:
BRD4,
CHTF18,
PCNA,
RFC1, and
RFC4.
References
Further reading |
https://en.wikipedia.org/wiki/Dual%20oxidase%202 | Dual oxidase 2, also known as DUOX2 or ThOX2 (for thyroid oxidase), is an enzyme that in humans is encoded by the DUOX2 gene. Dual oxidase is an enzyme that was first identified in the mammalian thyroid gland. In humans, two isoforms are found; hDUOX1 and hDUOX2 (this enzyme). The protein location is not exclusive to thyroid tissue; hDUOX1 is prominent in airway epithelial cells and hDUOX2 in the salivary glands and gastrointestinal tract.
Function
Investigations into reactive oxygen species (ROS) in biological systems have, until recently, focused on characterization of phagocytic cell processes. It is now well accepted that production of such species is not restricted to phagocytic cells and can occur in eukaryotic non-phagocytic cell types via NADPH oxidase (NOX) or dual oxidase (DUOX). This new family of proteins, termed the NOX/DUOX family or NOX family of NADPH oxidases, consists of homologs to the catalytic moiety of phagocytic NADPH-oxidase, gp91phox. Members of the NOX/DUOX family have been found throughout eukaryotic species, including invertebrates, insects, nematodes, fungi, amoeba, algae, and plants (not found in prokaryotes). These enzymes clearly demonstrate regulated production of ROS as their sole function. Genetic analyses have implicated NOX/DUOX derived ROS in biological roles and pathological conditions including hypertension (NOX1), innate immunity (NOX2/DUOX), otoconia formation in the inner ear (NOX3) and thyroid hormone biosynthesis (DUOX1/2).DUOX2 |
https://en.wikipedia.org/wiki/DMAP1 | DNA methyltransferase 1-associated protein 1 is an enzyme that in humans is encoded by the DMAP1 gene.
Function
This gene encodes a subunit of several, distinct complexes involved in the repression or activation of transcription. The encoded protein can independently repress transcription and is targeted to replication foci throughout S phase by interacting directly with the N-terminus of DNA methyltransferase 1. During late S phase, histone deacetylase 2 is added to this complex, providing a means to deacetylate histones in transcriptionally inactive heterochromatin following replication. The encoded protein is also a component of the nucleosome acetyltransferase of H4 complex and interacts with the transcriptional corepressor tumor susceptibility gene 101 and the pro-apoptotic death-associated protein 6, among others. Alternatively spliced transcript variants encoding the same protein have been described.
Interactions
DMAP1 has been shown to interact with:
C19orf2,
DNMT1,
ING1, and
RGS6
References
Further reading |
https://en.wikipedia.org/wiki/NDRG2 | Protein NDRG2 is a protein that in humans is encoded by the NDRG2 gene (NMYC downstream-regulated gene 2).
Function
This gene is a member of the N-myc downregulated gene family which belongs to the alpha/beta hydrolase superfamily. The protein encoded by this gene is a cytoplasmic protein that may play a role in neurite outgrowth. This gene may be involved in glioblastoma and aggressive meningioma carcinogenesis (via cell proliferation). Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been determined.
References
Further reading
Human proteins |
https://en.wikipedia.org/wiki/TRIM27 | Zinc finger protein RFP is a protein that in humans is encoded by the TRIM27 gene.
This gene encodes a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This protein localizes to the nuclear matrix. It interacts with the enhancer of polycomb protein and represses gene transcription. It is also thought to be involved in the differentiation of male germ cells. Fusion of the N-terminus of this protein with the truncated C-terminus of the RET gene product has been shown to result in production of the ret transforming protein.
Interactions
TRIM27 has been shown to interact with PRAM1 and EIF3S6.
References
Further reading |
https://en.wikipedia.org/wiki/RGS16 | Regulator of G-protein signaling 16 is a protein that in humans is encoded by the RGS16 gene.
Function
The protein encoded by this gene belongs to the 'regulator of G protein signaling' family. It inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits. It also may play a role in regulating the kinetics of signaling in the phototransduction cascade.
Interactions
RGS16 has been shown to interact with GNAQ and GNAI3.
References
Further reading |
https://en.wikipedia.org/wiki/RNF2 | E3 ubiquitin-protein ligase RING2 is an enzyme that in humans is encoded by the RNF2 gene.
Polycomb group (PcG) of proteins form the multiprotein complexes that are important for the transcription repression of various genes involved in development and cell proliferation. The protein encoded by this gene is one of the PcG proteins. It has been shown to interact with, and suppress the activity of, transcription factor CP2 (TFCP2/CP2). Studies of the mouse counterpart suggested the involvement of this gene in the specification of anterior-posterior axis, as well as in cell proliferation in early development. This protein was also found to interact with huntingtin interacting protein 2 (HIP2), an ubiquitin-conjugating enzyme, and possess ubiquitin ligase activity.
Interactions
RNF2 has been shown to interact with TFCP2 and HIP2.
See also
RING finger domain
References
Further reading
External links
RING finger proteins |
https://en.wikipedia.org/wiki/60S%20acidic%20ribosomal%20protein%20P2 | 60S acidic ribosomal protein P2 is a protein that in humans is encoded by the RPLP2 gene.
Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal phosphoprotein that is a component of the 60S subunit. The protein, which is a functional equivalent of the Escherichia coli L7/L12 ribosomal protein, belongs to the L12P family of ribosomal proteins. It plays an important role in the elongation step of protein synthesis. Unlike most ribosomal proteins, which are basic, the encoded protein is acidic. Its C-terminal end is nearly identical to the C-terminal ends of the ribosomal phosphoproteins P0 and P1. The P2 protein can interact with P0 and P1 to form a pentameric complex consisting of P1 and P2 dimers, and a P0 monomer. The protein is located in the cytoplasm. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.
Interactions
RPLP2 has been shown to interact with RPLP1.
References
Further reading
Ribosomal proteins |
https://en.wikipedia.org/wiki/SFRS6 | Splicing factor, arginine/serine-rich 6 is a protein that in humans is encoded by the SFRS6 gene.
Function
The protein encoded by this gene is involved in mRNA splicing and may play a role in site selection in alternative splicing. The encoded nuclear protein belongs to the splicing factor SR family and has been shown to bind with and modulate another member of the family, SFRS12.
References
Further reading |
https://en.wikipedia.org/wiki/SFRS7 | Serine/arginine-rich splicing factor 7 (SRSF7) also known as splicing factor, arginine/serine-rich 7 (SFRS7) or splicing factor 9G8 is a protein that in humans is encoded by the SRSF7 gene.
Function
The protein encoded by this gene is a member of the serine/arginine (SR)-rich family of pre-mRNA splicing factors, which constitute part of the spliceosome. Each of these factors contains an RNA recognition motif (RRM) for binding RNA and an RS domain for binding other proteins. The RS domain is rich in serine and arginine residues and facilitates interaction between different SR splicing factors. In addition to being critical for mRNA splicing, the SR proteins have also been shown to be involved in mRNA export from the nucleus and in translation.
Model organisms
Model organisms have been used in the study of SRSF7 function. A conditional knockout mouse line called Srsf7tm1a(EUCOMM)Wtsi was generated at the Wellcome Trust Sanger Institute. Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Additional screens performed: - In-depth immunological phenotyping
References
Further reading |
https://en.wikipedia.org/wiki/SGSH | N-sulphoglucosamine sulphohydrolase is an enzyme that in humans is encoded by the SGSH gene.
Clinical significance
A number sign (#) is used with this entry because the phenotype is caused by mutation in the gene encoding N-sulfoglucosamine sulfohydrolase (SGSH; MIM 605270). The Sanfilippo syndrome, or mucopolysaccharidosis III, is a lysosomal storage disease due to impaired degradation of heparan sulfate. MPS III includes 4 types, each due to the deficiency of a different enzyme: heparan N-sulfatase (type A); alpha-N-acetylglucosaminidase (type B; MIM 252920); acetyl CoA:alpha-glucosaminide acetyltransferase (type C; MIM 252930); and N-acetylglucosamine 6-sulfatase (type D; MIM 252940). The Sanfilippo syndrome is characterized by severe central nervous system degeneration, but only mild somatic disease. Onset of clinical features usually occurs between 2 and 6 years; severe neurologic degeneration occurs in most patients between 6 and 10 years of age, and death occurs typically during the second or third decade of life. Type A has been reported to be the most severe, with earlier onset and rapid progression of symptoms and shorter survival.
References
Further reading |
https://en.wikipedia.org/wiki/STIL | SCL-interrupting locus protein is a protein that in humans is encoded by the STIL gene. STIL is present in many different cell types and is essential for centriole biogenesis. This gene encodes a cytoplasmic protein implicated in regulation of the mitotic spindle checkpoint, a regulatory pathway that monitors chromosome segregation during cell division to ensure the proper distribution of chromosomes to daughter cells. The protein is phosphorylated in mitosis and in response to activation of the spindle checkpoint, and disappears when cells transition to G1 phase. It interacts with a mitotic regulator, and its expression is required to efficiently activate the spindle checkpoint.
It is proposed to regulate Cdc2 kinase activity during spindle checkpoint arrest. Chromosomal deletions that fuse this gene and the adjacent locus commonly occur in T cell leukemias, and are thought to arise through illegitimate recombination events. Multiple transcript variants encoding different isoforms have been found for this gene. Multiple types of cancer produce STIL, and its expression is linked to an increased mitotic index and cancer development. Hedgehog family-mediated signaling events are one of its associated pathways. The development and function of the nervous system are impacted by STIL. The sequence of STIL gene is highly conserved in vertebrate species .Both fetal and adult tissues express the STIL gene. Its expression levels fluctuate with the cell cycle, making it challenging to |
https://en.wikipedia.org/wiki/SIM2 | Single-minded homolog 2 is a protein that in humans is encoded by the SIM2 gene. It plays a major role in the development of the central nervous system midline as well as the construction of the face and head.
Function
SIM1 and SIM2 genes are Drosophila single-minded (sim) gene homologs. The Drosophila sim gene encodes a transcription factor that is a master regulator of neurogenesis of midline cells in the central nervous system. SIM2 maps within the so-called Down syndrome chromosomal region, specifically on the q arm of chromosome 21, band 22.2. Based on the mapping position, its potential function as transcriptional repressor and similarity to Drosophila sim, it is proposed that SIM2 may contribute to some specific Down syndrome phenotypes
Interactions
SIM2 has been shown to interact with Aryl hydrocarbon receptor nuclear translocator.
When the SIM2 gene is transfected into PC12 cells, it affects the normal cycle of cell maturation. SIM2 inhibits the expression of cyclin E, which in turn inhibits the cell's ability to pass through the G1/S checkpoint and suppresses the cell's proliferation ability. it also up-regulates the presence of p27, a growth inhibitor protein. The presence of p27 inhibits the activation of cell cycle regulatory kinases.
Disease state
There are three states of the gene: +/+, +/-, and -/-. When the gene is expressed as SIM2 -/-, it is considered disrupted and many physical malformations are seen, particularly in the craniofacial area. Indi |
https://en.wikipedia.org/wiki/SKIL | Ski-like protein is a protein that in humans is encoded by the SKIL gene.
Interactions
SKIL interacts with SKI protein, Mothers against decapentaplegic homolog 3 and Mothers against decapentaplegic homolog 2.
Protein Family
SKIL belongs to the Ski/Sno/Dac family, shared by SKI protein, Dachshund, and SKIDA1. Members of the Ski/Sno/Dac family share a domain that is roughly 100 amino acids long.
References
Further reading
Proteins
Genes on human chromosome 3 |
https://en.wikipedia.org/wiki/SNAI2 | Zinc finger protein SNAI2 is a transcription factor that in humans is encoded by the SNAI2 gene. It promotes the differentiation and migration of certain cells and has roles in initiating gastrulation.
Function
This gene encodes a member of the Snail superfamily of C2H2-type zinc finger transcription factors. The encoded protein acts as a transcriptional repressor that binds to E-box motifs and is also likely to repress E-cadherin transcription in breast carcinoma. This protein is involved in epithelial-mesenchymal transitions and has antiapoptotic activity. It regulates differentiation and migration of neural crest cells along with other genes (e.g. FOXD3, SOX9 and SOX10, BMPs) in embryonic life. Mutations in this gene may be associated with sporadic cases of neural tube defects.
SNAI2 downregulates expression of E-cadherin in premigratory neural crest cells; thus, SNAI2 induces tightly bound epithelial cells to break into a loose mesenchymal phenotype, allowing gastrulation of mesoderm in the developing embryo. Structurally similar to anti-apoptotic Ces-1 in C. elegans, SLUG is a negative regulator of productive cell death in the developing embryo and adults.
Clinical significance
Widely expressed in human tissues, SLUG is most notably absent in peripheral blood leukocytes, adult liver, and both fetal and adult brain tissues. SLUG plays a role in breast carcinoma as well as leukemia by downregulation of E-cadherin, which supports mesenchymal phenotype by shifting expr |
https://en.wikipedia.org/wiki/SPINT1 | Kunitz-type protease inhibitor 1 is an enzyme that in humans is encoded by the SPINT1 gene.
The protein encoded by this gene is a member of the Kunitz family of serine protease inhibitors. The protein is a potent inhibitor specific for HGF activator and is thought to be involved in the regulation of the proteolytic activation of HGF in injured tissues. Alternative splicing results in multiple variants encoding different isoforms.
References
Further reading
Serine protease inhibitors |
https://en.wikipedia.org/wiki/SSX2 | Protein SSX2 is a protein that in humans is encoded by the SSX2 gene.
The product of this gene belongs to the family of highly homologous synovial sarcoma, X (SSX) breakpoint proteins. These proteins may function as transcriptional repressors. They are also capable of eliciting spontaneously humoral and cellular immune responses in cancer patients, and are potentially useful targets in cancer vaccine-based immunotherapy. SSX1, SSX2 and SSX4 genes have been involved in the t(X;18) chromosomal translocation characteristically found in all synovial sarcomas. This translocation results in the fusion of the synovial sarcoma translocation gene on chromosome 18 to one of the SSX genes on chromosome X. The encoded hybrid proteins are probably responsible for transforming activity. Two transcript variants encoding distinct isoforms have been identified for this gene.
References
Further reading |
https://en.wikipedia.org/wiki/Contactin%202 | Contactin-2 is a protein that in humans is encoded by the CNTN2 gene.
Function
The protein encoded by this gene is a member of the immunoglobulin superfamily. It is a glycosylphosphatidylinositol (GPI)-anchored neuronal membrane protein that functions as a cell adhesion molecule. It may play a role in the formation of axon connections in the developing nervous system. It may also be involved in glial tumorigenesis and may provide a potential target for therapeutic intervention.
Interactions
CNTN2 has been shown to interact with CNTNAP2 and NFYB.
References
External links
Further reading |
https://en.wikipedia.org/wiki/TNNI2 | Troponin I, fast skeletal muscle is a protein that in humans is encoded by the TNNI2 gene.
The TNNI2 gene is located at 11p15.5 in the human chromosomal genome, encoding the fast twitch skeletal muscle troponin I (fsTnI). fsTnI is a 21.3 kDa protein consisting of 182 amino acids including the first methionine with an isoelectric point (pI) of 8.74. It is the inhibitory subunit of the troponin complex in fast twitch skeletal muscle fibers.
Gene evolution
Three homologous genes have evolved in vertebrates, encoding three muscle type-specific isoforms of TnI. Sequence analysis, immunological distance, and examination of evolutionarily suppressed conformational states showed that the TnI genes have evolved in close linkage with the genes encoding troponin T (TnT), another subunit of the troponin complex. The fast TnI-fast TnT gene pair represents the original TnI and TnT genes (Fig. 1). The three muscle fiber type-specific TnI-TnT gene pairs were likely originated from a TnI-like ancestor gene that presumably duplicated to form a closely linked fast TnI-like and fast TnT-like gene pair. A later duplication events resulted in emergences of a slow TnI-like and cardiac TnT-like gene pair that was further duplicated to give rise of the present-day slow TnI-cardiac TnT and cardiac TnI-slow TnT gene pairs. The seemingly scrambled ssTnI and cTnI gene pair is actually functionally related as they co-express and form troponin complex in the embryonic heart. The overlapping of enhanc |
https://en.wikipedia.org/wiki/TRIP6 | Thyroid receptor-interacting protein 6 is a protein that in humans is encoded by the TRIP6 gene.
Function
This gene is a member of the zyxin family and encodes a protein with three LIM zinc-binding domains. This protein localizes to focal adhesion sites and along actin stress fibers. Recruitment of this protein to the plasma membrane occurs in a lysophosphatidic acid (LPA)-dependent manner and it regulates LPA-induced cell migration. Alternatively spliced variants which encode different protein isoforms have been described; however, not all variants have been fully characterized.
Interactions
TRIP6 has been shown to interact with LPAR2, BCAR1 and HOXA9.
References
Further reading
External links |
https://en.wikipedia.org/wiki/TST%20%28gene%29 | Thiosulfate sulfurtransferase is an enzyme that in humans is encoded by the TST gene.
The product of this gene is a mitochondrial matrix enzyme that is encoded by the nucleus. It may play roles in cyanide detoxification, the formation of iron-sulfur proteins, and the modification of sulfur-containing enzymes.
The gene product contains two highly conservative domains (rhodanese homology domains), suggesting these domains have a common evolutionary origin.
References
Further reading |
https://en.wikipedia.org/wiki/WIPF1 | WAS/WASL-interacting protein (WIP) is a protein that in humans is encoded by the WIPF1 gene.
Function
This gene encodes a protein that plays an important role in the organization of the actin cytoskeleton. Overexpression of WIP in mammalian cells has been shown to increase actin polymerization. The encoded protein binds to a region of Wiskott–Aldrich syndrome protein that is frequently mutated in Wiskott–Aldrich syndrome, an X-linked recessive disorder. Impairment of the interaction between these two proteins may contribute to the disease. Two transcript variants encoding the same protein have been identified for this gene. In patients lacking the WIPF1 gene WASp protein levels are depleted and WAS symptoms present.
Interactions
WIP has been shown to interact with Wiskott–Aldrich syndrome protein, N-WASp, Cortactin, NCK1, MYO1e and ITSN1. While Wiskott–Aldrich syndrome protein (WASp)is expressed only in haematopoetic cells, WIPF1 is expressed ubiquitously. The majority of the mutations causing Wiskott Aldrich Syndrome are located in the WH1 domain of WASp. These mutations affect WASp-WIPF1 binding. WIPF1 has an N-terminal profilin binding domain, two actin binding WH2 domains, a central polyproline stretch, and a C-terminal WASp Binding Domain. WASp protein is degraded in the absence of WIP; but the ubiquitously expressed WASp ortholog N-WASp remains stable in the absence of WIP.
Work in yeast
WIPF1 functions and interactions have been studied in multiple fungal sys |
https://en.wikipedia.org/wiki/SLBP | Histone RNA hairpin-binding protein or stem-loop binding protein (SLBP) is a protein that in humans is encoded by the SLBP gene.
Species distribution
SLBP has been cloned from humans, C. elegans, D. melanogaster, X. laevis, and sea urchins. The full length human protein has 270 amino acids (31 kDa) with a centrally located RNA binding domain (RBD). The 75 amino acid RBD is well conserved across species, however the remainder of SLBP is highly divergent in most organisms and not homologous to any other protein in the eukaryotic genomes.
Function
This gene encodes a protein that binds to the histone 3' UTR stem-loop structure in replication-dependent histone mRNAs. Histone mRNAs do not contain introns or polyadenylation signals, and are processed by a single endonucleolytic cleavage event downstream of the stem-loop. The stem-loop structure is essential for efficient processing of the histone pre-mRNA but this structure also controls the transport, translation and stability of histone mRNAs. SLBP expression is regulated during S-phase of the cell cycle, increasing more than 10-fold during the latter part of G1.
All SLBP proteins are capable of forming a highly stable complex with histone stem-loop RNA. Complex formation with the histone mRNA stem-loop is achieved by a novel three-helix bundle fold. SLBP proteins also recognize the tetraloop structure of the histone hairpin, the base of the stem, and the 5' flanking region. The crystal structure of human SLBP in comple |
https://en.wikipedia.org/wiki/LHX3 | LIM/homeobox protein Lhx3 is a protein that in humans is encoded by the LHX3 gene.
Function
LHX3 encodes a protein of a large protein family, members of which carry the LIM domain, a unique cysteine-rich zinc-binding domain. The encoded protein is a transcription factor that is required for pituitary development and motor neuron specification. Two transcript variants encoding distinct isoforms have been identified for this gene.
Clinical significance
Mutations in this gene have been associated with a syndrome of combined pituitary hormone deficiency and rigid cervical spine.
Interactions
LHX3 has been shown to interact with Ldb1.
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/TCL1A | T-cell leukemia/lymphoma protein 1A is a protein that in humans is encoded by the TCL1A gene.
Interactions
TCL1A has been shown to interact with AKT1 and AKT2.
References
Further reading |
https://en.wikipedia.org/wiki/Cell%20division%20cycle%207-related%20protein%20kinase | Cell division cycle 7-related protein kinase is an enzyme that in humans is encoded by the CDC7 gene. The Cdc7 kinase is involved in regulation of the cell cycle at the point of chromosomal DNA replication. The gene CDC7 appears to be conserved throughout eukaryotic evolution; this means that most eukaryotic cells have the Cdc7 kinase protein.
Function
The product encoded by this gene is predominantly localized in the nucleus and is a cell division cycle protein with kinase activity.
The protein is a serine-threonine kinase that is activated by another protein called either Dbf4 in the yeast Saccharomyces cerevisiae or ASK in mammals. The Cdc7/Dbf4 complex adds a phosphate group to the minichromosome maintenance (MCM) protein complex allowing for the initiation of DNA replication in mitosis (as explained in the Cdc7 and Replication section below).
Although expression levels of the protein appear to be constant throughout the cell cycle, the protein kinase activity appears to increase during S phase. It has been suggested that the protein is essential for initiation of DNA replication and that it plays a role in regulating cell cycle progression. Overexpression of this gene product may be associated with neoplastic transformation for some tumors. Additional transcript sizes have been detected, suggesting the presence of alternative splicing.
Cell cycle regulation
The gene, CDC7, is involved in the regulation of cell cycle because of the gene product Cdc7 kinase. The prote |
https://en.wikipedia.org/wiki/HIST2H2AC | Histone H2A type 2-C is a protein that in humans is encoded by the HIST2H2AC gene.
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene is intronless and encodes a member of the histone H2A family.
References
Further reading |
https://en.wikipedia.org/wiki/ABCG8 | ATP-binding cassette sub-family G member 8 is a protein that in humans is encoded by the ABCG8 gene.
The protein encoded by this gene is a member of the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intra-cellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the White subfamily. The protein encoded by this gene functions as a half-transporter to limit intestinal absorption and promote biliary excretion of sterols. It is expressed in a tissue-specific manner in the liver, colon, and intestine. This gene is tandemly arrayed on chromosome 2, in a head-to-head orientation with family member ABCG5. Mutations in this gene may contribute to sterol accumulation and atherosclerosis, and have been observed in patients with sitosterolemia.
Interactive pathway map
See also
ATP-binding cassette transporter
References
Further reading
External links
ATP-binding cassette transporters |
https://en.wikipedia.org/wiki/FIP1L1 | Factor interacting with PAPOLA and CPSF1 (i.e, FIP1L1; also termed Pre-mRNA 3'-end-processing factor FIP1) is a protein that in humans is encoded by the FIP1L1 gene (also known as Rhe, FIP1, and hFip1). A medically important aspect of the FIP1L1 gene is its fusion with other genes to form fusion genes which cause clonal hypereosinophilia and leukemic diseases in humans.
Gene
The human FIP1L1 gene is located on chromosome 4 at position q12 (4q12), contains 19 exons, and codes for a complete protein consisting of 594 amino acids. However, alternative splicing of its Precursor mRNA results in multiple transcript variants encoding distinct FIP1L1 protein isoforms. The FIP1L1 gene is found in a wide range of species, being designated as FIP1 in Saccharomyces cerevisiae (yeast) and fip1l1 in coho salmon as well as mice and numerous other mammalian species.
In humans, an interstitial chromosomal deletion of about 800 kilobases at 4q12 deletes the CHIC2 gene (i.e.cysteine rich hydrophobic domain 2 gene) to create an in-frame fusion of the FIP1L1 gene with the platelet-derived growth factor receptor alpha gene (PGDFRA) gene. The product of PDGFRA, platelet-derived growth factor receptor alpha (PDGFRA), is a tyrosine kinase receptor of the RTK class III. When bound by its proper ligand, Platelet-derived growth factor (PDGF), it tyrosine kinase becomes active in phosphorylating proteins that, among other functions, promote cell growth and proliferation. (The FIP1L1-PDGFRA mutation wa |
https://en.wikipedia.org/wiki/CD7 | CD7 (Cluster of Differentiation 7) is a protein that in humans is encoded by the CD7 gene.
Function
This gene encodes a transmembrane protein which is a member of the immunoglobulin superfamily. This protein is found on thymocytes and mature T cells. It plays an essential role in T-cell interactions and also in T-cell/B-cell interaction during early lymphoid development.
See also
Cluster of differentiation
DC-7
Interactions
CD7 has been shown to interact with PIK3R1.
Clinical significance
CD7 can be aberrantly expressed in refractory anaemia with excess blasts (RAEB) and may confer a worse prognosis. Also, a lack of CD7 expression could insinuate mycosis fungoides (MF) or Sezary syndrome (SS).
References
Further reading
External links
Clusters of differentiation |
https://en.wikipedia.org/wiki/CDKN2D | Cyclin-dependent kinase 4 inhibitor D is an enzyme that in humans is encoded by the CDKN2D gene.
The protein encoded by this gene is a member of the INK4 family of cyclin-dependent kinase inhibitors. This protein has been shown to form a stable complex with CDK4 or CDK6, and prevent the activation of the CDK kinases, thus function as a cell growth regulator that controls cell cycle G1 progression. The abundance of the transcript of this gene was found to oscillate in a cell-cycle dependent manner with the lowest expression at mid G1 and a maximal expression during S phase. The negative regulation of the cell cycle involved in this protein was shown to participate in repressing neuronal proliferation, as well as spermatogenesis. The expression of this gene and its protein product (p19) is observed in neurons with neurofibrillary tangles (NFTs) and it is suggested as a marker for senescent neurons. Two alternatively spliced variants of this gene, which encode an identical protein, have been reported.
Note, this protein should not be confused with p19-ARF (mouse) or the human equivalent p14ARF, which are alternative products of the CDKN2A gene.
References
Further reading
External links
Cell cycle regulators |
https://en.wikipedia.org/wiki/SPOP | Speckle-type POZ protein is a protein that in humans is encoded by the SPOP gene.
This gene encodes a protein that may modulate the transcriptional repression activities of death-associated protein 6 (DAXX), which interacts with histone deacetylase, core histones, and other histone-associated proteins. In mouse, the encoded protein binds to the putative leucine zipper domain of macroH2A1.2, a variant H2A histone that is enriched on inactivated X chromosomes. The BTB/POZ domain of this protein has been shown in other proteins to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes. Alternative splicing of this gene results in multiple transcript variants encoding the same protein.
Clinical relevance
Mutations in SPOP lead to a type of prostate tumor thought to be involved in about 15% of all prostate cancers.
References
Further reading |
https://en.wikipedia.org/wiki/SORBS2 | ArgBP2 protein, also referred to as Sorbin and SH3 domain-containing protein 2 is a protein that in humans is encoded by the SORBS2 gene. ArgBP2 belongs to the a small family of adaptor proteins having sorbin homology (SOHO) domains. ArgBP2 is highly abundant in cardiac muscle cells at sarcomeric Z-disc structures, and is expressed in other cells at actin stress fibers and the nucleus.
Structure
ArgBP2 may exist in as many as 9 unique isoforms ranging from 52 kDa to 117 kDa (492 to 1100 amino acids). ArgBP2 belongs to the a small family of adaptor proteins having sorbin homology (SOHO) domains and three SH3 domains, which regulate cell adhesion, cytoskeletal organization and growth factor signaling; other members include CAP/ponsin and vinexin. The three SH3 domains are C-terminal, a serine-threonine rich domain resides in the middle, and the sorbin homology (SoHo) domain is N-terminal. The SH3 domains interact with Arg/Abl, vinculin. The SOHO domain interacts with flotillin found in lipid rafts.
Function
The subcellular localization of this protein in epithelial and cardiac muscle cells suggests that ArgBP2 functions as an adapter protein to assemble signaling complexes in stress fibers, and that it is a potential link between Abl family kinases and the actin cytoskeleton. ArgBP2 contains several potential Abl phosphorylation sites; Arg and c-Abl represent the mammalian members of the Abelson family of non-receptor protein-tyrosine kinases. In non-muscle cells, ArgBP2 bi |
https://en.wikipedia.org/wiki/YARS | Tyrosyl-tRNA synthetase, cytoplasmic, also known as Tyrosine-tRNA ligase, is an enzyme that in humans is encoded by the YARS gene.
Living cells translate DNA sequences into RNA sequences and then into protein sequences. Proteins are chains of amino acids, such as tyrosine. As the protein grows, each amino acid is added to the end by an enzyme called transfer RNA (tRNA). Each amino acid has its own tRNA, and tyrosyl-tRNA synthetase is the tRNA that adds tyrosine to the end of a growing protein.
Aminoacyl-tRNA synthetases catalyze the aminoacylation of transfer RNA (tRNA) by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. Tyrosyl-tRNA synthetase belongs to the class I tRNA synthetase family. Cytokine activities have also been observed for the human tyrosyl-tRNA synthetase, after it is split into two parts, an N-terminal fragment that harbors the catalytic site and a C-terminal fragment found only in the mammalian enzyme. The N-terminal fragment is an interleukin-8-like cytokine, whereas the released C-terminal fragment is an EMAP II-like cytokine.
Recently, tyrosyl-tRNA synthetase has been demonstrated as the biologically and functionally significant target for resveratrol.
For a comparison of cytoplasmic human tyrosyl-tRNA synthetase with its mitochondrial counterpart and with tyrosyl-tRNA synthetases |
https://en.wikipedia.org/wiki/PRKRA | Protein kinase, interferon-inducible double stranded RNA dependent activator, also known as interferon-inducible double stranded RNA-dependent protein kinase activator A or Protein ACTivator of the interferon-induced protein kinase (PACT) is a protein that in humans is encoded by the PRKRA gene. PACT heterodimerizes with and activates protein kinase R.
PRKRA mutations have been linked to a rare form of dystonia parkinsonism.
References
Further reading |
https://en.wikipedia.org/wiki/Tankyrase | Tankyrase, also known as tankyrase 1, is an enzyme that in humans is encoded by the TNKS gene. It inhibits the binding of TERF1 to telomeric DNA.
Tankyrase attracts substantial interest in cancer research through its interaction with AXIN1 and AXIN2, which are negative regulators of pro-oncogenic β-catenin signaling. Importantly, activity in the β-catenin destruction complex can be increased by tankyrase inhibitors and thus such inhibitors are a potential therapeutic option to reduce the growth of β-catenin-dependent cancers.
Description
Tankyrase-1 is a poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking. Acts as an activator of the Wnt signaling pathway by mediating poly-ADP-ribosylation (PARylation) of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP-ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation. Also mediates PARsylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates PARsylation of TERF1, thereby contributing to the regulation of telomere length. Involved in centrosome maturation during prometaphase by mediating PARsylation of HEPACAM2/MIKI. May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles. May be involved in spindle pole assembly through PARsylation of NUMA1. Stimulates 26S proteasome acti |
https://en.wikipedia.org/wiki/HYAL2 | Hyaluronidase-2 is a multifunctional protein, previously thought to only possess acid-active hyaluronan-degrading enzymatic function. In humans it is encoded by the HYAL2 gene.
This gene encodes a protein which is similar in structure to hyaluronidases. Hyaluronidases intracellularly degrade hyaluronan, one of the major glycosaminoglycans of the extracellular matrix. Hyaluronan is thought to be involved in cell proliferation, migration and differentiation.
Varying functions have been described for this protein. It has been described as a lysosomal hyaluronidase which is active at a pH below 4 and specifically hydrolyzes high molecular weight hyaluronan. It has also been described as a GPI-anchored cell surface protein which does not display hyaluronidase activity but does serve as a receptor for the oncogenic virus Jaagsiekte sheep retrovirus. The gene is one of several related genes in a region of chromosome 3p21.3 associated with tumor suppression. This gene encodes two alternatively spliced transcript variants which differ only in the 5' UTR.
One study found associations between cleft lip and palate and mutations in the HYAL2 gene.
An investigation published in 2017, attributed an additional function to the Hyaluronidase 2 (HYAL2) protein. The study found interactions between HYAL2 and proteins involved in the alternative splicing of CD44 pre-mRNA. Another study published in 2020, described roles for HYAL2 in the orchestration of cytoskeletal components involved in my |
https://en.wikipedia.org/wiki/NAPA%20%28gene%29 | N-ethylmaleimide-sensitive factor Attachment Protein Alpha, also known as SNAP-α, is a SNAP protein that is involved in the intra-cellular trafficking and fusing of vesicles to target membranes in cells.
Function
The 'SNARE hypothesis' is a model explaining the process of docking and fusion of vesicles to their target membranes. According to this model, membrane proteins from the vesicle (v-SNAREs) and proteins from the target membrane (t-SNAREs) govern the specificity of vesicle targeting and docking through mutual recognition. Once the 2 classes of SNAREs bind to each other, they form a complex that recruits the general elements of the fusion apparatus, namely NSF (N-ethylmaleimide-sensitive factor) and SNAPs (soluble NSF-attachment proteins), to the site of membrane fusion, thereby forming the 20S fusion complex. Alpha- and gamma-SNAP are found in a wide range of tissues and act synergistically in intra-Golgi transport. The sequence of the predicted 295-amino acid human protein encoded by NAPA shares 37%, 60%, and 67% identity with the sequences of yeast, Drosophila, and squid alpha-SNAP, respectively. Platelets contain some of the same proteins, including NSF, p115/TAP, alpha-SNAP (this protein), gamma-SNAP, and the t-SNAREs syntaxin-2 and syntaxin-4, that are used in many vesicular transport processes in other cell types. Platelet exocytosis uses a molecular mechanism similar to that used by other secretory cells, such as neurons, although the proteins used by the pla |
https://en.wikipedia.org/wiki/EIF2S2 | Eukaryotic translation initiation factor 2 subunit 2 (eIF2β) is a protein that in humans is encoded by the EIF2S2 gene.
Function
Eukaryotic translation initiation factor 2 (eIF2) functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA and binding to a 40S ribosomal subunit. eIF2 is composed of three subunits, alpha (α), beta (β, this article), and gamma (γ), with the protein encoded by this gene representing the beta subunit. The beta subunit catalyzes the exchange of GDP for GTP, which recycles the eIF2 complex for another round of initiation.
Regulation
Both eIF2α and eIF2β expression is regulated by the NRF1 transcription factor.
See also
eIF2
References
Further reading |
https://en.wikipedia.org/wiki/CLDN6 | Claudin-6 is a protein that in humans is encoded by the CLDN6 gene. It belongs to the group of claudins. The knockout mice of mouse homolog exhibit no phenotype, indicating that claudin-6 is dispensable for normal development and homeostasis.
References
External links
Further reading |
https://en.wikipedia.org/wiki/CLDN2 | Claudin-2 is a protein that in humans is encoded by the CLDN2 gene. It belongs to the group of claudins.
Members of the claudin protein family, such as CLDN2, are expressed in an organ-specific manner and regulate the tissue-specific physiologic properties of tight junctions (Sakaguchi et al., 2002).[supplied by OMIM]
Function
Claudin-2 is expressed in cation-leaky epithelia such as that of the kidney proximal tubule. Mice that are deficient in claudin-2 have reduced reabsorption of Na+ in the proximal tubule, consistent with a role in paracellular transport.
Similar results have been obtained with cultured cells, as overexpression in claudin-2 lacking cells leads to increase of permeability for small cations.
Furthermore, claudin-2 has been shown to form paracellular channels for water.
References
External links
Further reading |
https://en.wikipedia.org/wiki/LGI1 | Leucine-rich, glioma inactivated 1, also known as LGI1, is a protein which in humans is encoded by the LGI1 gene. It may be a metastasis suppressor.
Function
The leucine-rich glioma inactivated -1 gene is rearranged as a result of translocations in glioblastoma cell lines. The protein contains a hydrophobic segment representing a putative transmembrane domain with the amino terminus located outside the cell. It also contains leucine-rich repeats with conserved cysteine-rich flanking sequences. This gene is predominantly expressed in neural tissues and its expression is reduced in low grade brain tumors and significantly reduced or absent in malignant gliomas.
Clinical significance
Since its earliest discovery, the LGI1 gene has been implicated in the control of cancer metastasis and in a predisposition to epilepsy. Following genetic linkage studies placing the hereditary form of autosomal dominant partial epilepsy with auditory features (ADPEAF) on chromosome region 10q24 mutation analysis of affected members in these families demonstrated LGI1 was a major cause of the disease.
More recently, LGI1 has been shown to be the major target of human autoantibodies which immunoprecipitate voltage-gated potassium channel complexes from mammalian brain tissue. LGI1 antibodies are found in patients with limbic encephalitis and in patients with faciobrachial dystonic seizures (FBDS). FBDS are a recently described form of epilepsy which is characterized by frequent, brief seizures |
https://en.wikipedia.org/wiki/DLG5 | Disks large homolog 5 is a protein that in humans is encoded by the DLG5 gene.
Function
This gene encodes a member of the family of discs large (DLG) homologs, a subset of the membrane-associated guanylate kinase (MAGUK) superfamily. The MAGUK proteins are composed of a catalytically inactive guanylate kinase domain, in addition to PDZ and SH3 domains, and are thought to function as scaffolding molecules at sites of cell-cell contact. The protein encoded by this gene localizes to the plasma membrane and cytoplasm, and interacts with components of adherens junctions and the cytoskeleton. It is proposed to function in the transmission of extracellular signals to the cytoskeleton and in the maintenance of epithelial cell structure. Alternative splice variants have been described but their biological nature has not been determined.
Interactions
DLG5 has been shown to interact with SORBS3.
References
Further reading |
https://en.wikipedia.org/wiki/BAG3 | BAG family molecular chaperone regulator 3 is a protein that in humans is encoded by the BAG3 gene. BAG3 is involved in chaperone-assisted selective autophagy.
Function
BAG proteins compete with Hip-1 for binding to the Hsc70/Hsp70 ATPase domain and promote substrate release. All the BAG proteins have an approximately 45-amino acid BAG domain near the C terminus but differ markedly in their N-terminal regions. The protein encoded by this gene contains a WW domain in the N-terminal region and a BAG domain in the C-terminal region. The BAG domains of BAG1, BAG2, and BAG3 interact specifically with the Hsc70 ATPase domain in vitro and in mammalian cells. All 3 proteins bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner.
Clinical significance
BAG gene has been implicated in age related neurodegenerative diseases such as Alzheimer's. It has been demonstrated that BAG1 and BAG3 regulate the proteasomal and lysosomal protein elimination pathways, respectively. It has also been shown to be a cause of familial dilated cardiomyopathy.
That BAG3 mutations are responsible for familial dilated cardiomyopathy is confirmed by another study describing 6 new molecular variants (2 missense and 4 premature Stops
). Moreover, the same publication reported that BAG3 polymorphisms are also associated with sporadic forms of the disease together with HSPB7 locus.
In muscle cells, BAG3 cooperates with the molecular chaperones Hs |
https://en.wikipedia.org/wiki/CCL4L1 | C-C motif chemokine 4-like is a protein that in humans is encoded by the CCL4L1 gene.
Function
This gene is one of several cytokine genes clustered on the q-arm of chromosome 17. Cytokines are a family of secreted proteins involved in immunoregulatory and inflammatory processes. This protein is similar to CCL4 which inhibits HIV entry by binding to the cellular receptor CCR5. The copy number of this gene varies among individuals; most individuals have 1-5 copies in the diploid genome, although rare individuals do not contain this gene at all. The human genome reference assembly contains two copies of this gene. This record represents the more centromeric gene.
References
External links
Further reading |
https://en.wikipedia.org/wiki/SLC23A2 | Solute carrier family 23 member 2 is a protein that in humans is encoded by the SLC23A2 gene.
The absorption of vitamin C into the body and its distribution to organs requires two sodium-dependent vitamin C transporters. This gene encodes one of the two required transporters and the encoded protein accounts for tissue-specific uptake of vitamin C. Previously, this gene had an official symbol of SLC23A1.
See also
Solute carrier family
References
Further reading
Solute carrier family |
https://en.wikipedia.org/wiki/ARPC1B | Actin-related protein 2/3 complex subunit 1B is a protein that in humans is encoded by the ARPC1B gene.
Function
This gene encodes one of seven subunits of the human Arp2/3 protein complex. This subunit is a member of the SOP2 family of proteins and is most similar to the protein encoded by gene ARPC1A. The similarity between these two proteins suggests that they both may function as p41 subunit of the human Arp2/3 complex that facilitates branching of actin filaments in cells. Isoforms of the p41 subunit may adapt the functions of the complex to different cell types or developmental stages. Indeed, it has recently been shown that variants of the Arp2/3 complex differ in their ability to promote actin assembly, with complexes containing ARPC1B and ARPC5L being better at this than those containing ARPC1A and ARPC5. The differing functions of ARPC1A and ARPC1B are also evident in the recent discovery of patients with severe or total ARPC1B deficiency, who have platelet and immune system abnormalities yet survive, possibly due to a compensatory up-regulation of ARPC1A expression.
Interactions
ARPC1B has been shown to interact with PAK1.
References
Further reading
External links |
https://en.wikipedia.org/wiki/FSTL3 | Follistatin-related protein 3 is a protein that in humans is encoded by the FSTL3 gene.
Follistatin-like 3 is a secreted glycoprotein of the follistatin-module-protein family. It may have a role in leukemogenesis.
References
Further reading
External links |
https://en.wikipedia.org/wiki/RGS19 | Regulator of G-protein signaling 19 is a protein that in humans is encoded by the RGS19 gene.
G proteins mediate a number of cellular processes. The protein encoded by this gene belongs to the RGS (regulators of G-protein signaling) family and specifically interacts with G protein, GAI3. This protein is a guanosine triphosphatase-activating protein that functions to down-regulate Galpha i/Galpha q-linked signaling.
Interactions
RGS19 has been shown to interact with GNAO1, GIPC1, OSTM1, GNAI1, GNAI3 and GNAZ.
References
Further reading
External links |
https://en.wikipedia.org/wiki/DLC1 | Deleted in Liver Cancer 1 also known as DLC1 and StAR-related lipid transfer protein 12 (STARD12) is a protein which in humans is encoded by the DLC1 gene.
This gene is deleted in the primary tumor of hepatocellular carcinoma. It maps to 8p22-p21.3, a region frequently deleted in solid tumors. It is suggested that this gene is a candidate tumor suppressor gene for human liver cancer, as well as for prostate, lung, colorectal, and breast cancers.
Gene
The human DLC1 gene is located on the short arm of chromosome 8 (8p21.3-22), within a region that frequently undergoes loss of heterozygosity by either genomic deletion or epigenetic silencing mechanisms in several types of solid cancers. The gene contains 14 exons and produces an mRNA transcript that is 6.3 kb in length; the second AUG present in the open reading frame is the major translational start site, and produces a polypeptide which is 1091 amino acids long.
The promoter region of the DLC1 gene contains a CpG island containing several CpG sites which can be methylated to promote gene silencing and prevent transcription.
DLC1 is frequently inactivated in human hepatocellular carcinoma, as well as some nasopharyngeal, lung, breast, prostate, kidney, colon, uterine, ovarian, and gastric cancers.
Protein structure and localization
The DLC1 protein contains four major functional domains: an N-terminal sterile α motif (SAM), a serine-rich (SR) region, a Rho-GAP domain, and a C-terminal steroidogenic acute regulatory protei |
https://en.wikipedia.org/wiki/DDX17 | Probable ATP-dependent RNA helicase DDX17 (p72) is an enzyme that in humans is encoded by the DDX17 gene.
Function
DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. This gene encodes a DEAD box protein, which is an ATPase activated by a variety of RNA species but not by dsDNA. This protein and that encoded by DDX5 gene are more closely related to each other than to any other member of the DEAD box family. Alternative splicing of this gene generates 2 transcript variants encoding different isoforms with the longer transcript reported to also initiate translation at a non-AUG (CUG) start site.
Interactions
DDX17 has been shown to interact with:
DDX5 (p68),
DHX9 (RNA Helicase A),
HDAC1,
References
Further reading
Spliceosome |
https://en.wikipedia.org/wiki/HEXIM1 | Protein HEXIM1 is a protein that in humans is encoded by the HEXIM1 gene.
Interactions
HEXIM1 has been shown to interact with Cyclin T1 and Cdk9
References
Further reading |
https://en.wikipedia.org/wiki/ANTXR1 | Anthrax toxin receptor 1 (ANTXR1 or also known asTEM8) is a protein that in humans is encoded by the ANTXR1 gene. Its molecular weight is predicted as about 63kDa.
The protein encoded by this gene is a type I transmembrane protein and is a tumor-specific endothelial marker that has been implicated in colorectal cancer. This protein has been shown to also be a docking protein or receptor for Bacillus anthracis toxin, the causative agent of the disease, anthrax. The binding of the protective antigen (PA) component, of the tripartite anthrax toxin, to this receptor protein mediates delivery of toxin components to the cytosol of cells. Once inside the cell, the other two components of anthrax toxin, edema factor (EF) and lethal factor (LF) disrupt normal cellular processes. Three alternatively spliced variants have been described.
See also
Anthrax toxin
References
External links
Further reading
Single-pass transmembrane proteins |
https://en.wikipedia.org/wiki/CGB7 | Choriogonadotropin subunit beta is a protein that in humans is encoded by the CGB7 gene.
This gene is a member of the glycoprotein hormone beta chain family and encodes the beta 7 subunit of chorionic gonadotropin (CG). Glycoprotein hormones are heterodimers consisting of a common alpha subunit and a unique beta subunit which confers biological specificity. CG is produced by the trophoblastic cells of the placenta and stimulates the ovaries to synthesize the steroids that are essential for the maintenance of pregnancy. The beta subunit of CG is encoded by 6 genes which are arranged in tandem and inverted pairs on chromosome 19q13.3 and contiguous with the luteinizing hormone beta subunit gene.
References
External links
Further reading |
https://en.wikipedia.org/wiki/ABCA2 | ATP-binding cassette sub-family A member 2 is a protein that in humans is encoded by the ABCA2 gene.
The membrane-associated protein encoded by this gene is a member of the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intracellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the ABC1 subfamily. Members of the ABC1 subfamily comprise the only major ABC subfamily found exclusively in multicellular eukaryotes. This protein is highly expressed in brain tissue and may play a role in macrophage lipid metabolism and neural development. Two transcript variants encoding different isoforms have been found for this gene.
See also
ATP-binding cassette transporter
References
Further reading
External links
ATP-binding cassette transporters |
https://en.wikipedia.org/wiki/ADH5 | Alcohol dehydrogenase class-3 is an enzyme that in humans is encoded by the ADH5 gene.
This gene encodes glutathione-dependent formaldehyde dehydrogenase or the class III alcohol dehydrogenase chi subunit, which is a member of the alcohol dehydrogenase family. Members of this family metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. Class III alcohol dehydrogenase is a homodimer composed of 2 chi subunits. It has virtually no activity for ethanol oxidation, but exhibits high activity for oxidation of long-chain primary alcohols and for oxidation of S-hydroxymethyl-glutathione, a spontaneous adduct between formaldehyde and glutathione.
This enzyme is an important component of cellular metabolism for the elimination of formaldehyde, a potent irritant and sensitizing agent that causes lacrymation, rhinitis, pharyngitis, and contact dermatitis.
Clinical significance
Mutations of the ADH5 gene cause AMED syndrome, an autosomal recessive digenic multisystem disorder characterized by global developmental delay with impaired intellectual development. The syndrome was first described in 2020.
References
Further reading
External links |
https://en.wikipedia.org/wiki/CKS1B | Cyclin-dependent kinases regulatory subunit 1 is a protein that in humans is encoded by the CKS1B gene.
Function
The CKS1B protein binds to the catalytic subunit of the cyclin-dependent kinases and is essential for their biological function. The CKS1B mRNA is found to be expressed in different patterns through the cell cycle in HeLa cells, which reflects a specialized role for the encoded protein.
CKS1B and CKS2 proteins have demonstrated principal roles in cell cycle regulation. Defined originally as suppressors of mutations in both fission and budding yeast Cdk1 genes, Cks molecules interact with Cdk1, Cdk2 and Cdk3. These Cdk-dependent enzyme complexes in cell cycle regulation frequently consist of Cdk molecules bound to a catalytic Cdk subunit, i.e. Cks and a regulatory cyclin subunit, such as a G1 cyclin, controlling Cdk function by directing cyclin-cdk complex activity toward specific and significant substrates. Malfunctions of cdk-dependent associations lead to defects into the entry of mitosis for cells.
Cks1 in the Cdk-independent pathway involves the recognition of substrates p27Kip1 and p21cip1 by directly associating with E3 SCFSkp2 when stimulated by certainmitogenic signals, such as TGF-β.
Clinical significance
Cks1-depleted breast cancer cells not only exhibit slowed G(1) progression, but also accumulate in G(2)-M due to blocked mitotic entry. Cdk1 expression, which is crucial for M phase entry, is drastically diminished by Cks1 depletion, and that rest |
https://en.wikipedia.org/wiki/CLCA1 | Chloride channel accessory 1 is a protein that in humans is encoded by the CLCA1 gene.
This gene encodes a member of the calcium sensitive chloride conductance protein family. To date, all members of this gene family map to the same region on chromosome 1p31-p22 and share a high degree of homology in size, sequence, and predicted structure, but differ significantly in their tissue distributions. The encoded protein is expressed as a precursor protein that is processed into two cell-surface-associated subunits, although the site at which the precursor is cleaved has not been precisely determined. The encoded protein may be involved in mediating calcium-activated chloride conductance in the intestine. Protein structure prediction methods suggest the N-terminal region of CLCA1 protein is a zinc metalloprotease.
See also
Chloride channel
References
Further reading
External links
Chloride channels |
https://en.wikipedia.org/wiki/CST4 | Cystatin-S is a protein that in humans is encoded by the CST4 gene.
The cystatin superfamily encompasses proteins that contain multiple cystatin-like sequences. Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory activity. There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins and the kininogens. The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions. The cystatin locus on chromosome 20 contains the majority of the type 2 cystatin genes and pseudogenes. This gene is located in the cystatin locus and encodes a type 2 salivary cysteine peptidase inhibitor. The protein is an S-type cystatin, based on its high level of expression in saliva, tears and seminal plasma. The specific role in these fluids is unclear but antibacterial and antiviral activity is present, consistent with a protective function.
References
External links
The MEROPS online database for peptidases and their inhibitors: I25.008
Further reading |
https://en.wikipedia.org/wiki/CTNS%20%28gene%29 | CTNS may also refer to the Center for Theology and the Natural Sciences.
CTNS is the gene that encodes the protein cystinosin in humans. Cystinosin is a lysosomal seven-transmembrane protein that functions as an active transporter for the export of cystine molecules out of the lysosome.
Mutations in CTNS are responsible for cystinosis, an autosomal recessive lysosomal storage disease.
Gene
The CTNS gene is located on the p arm of human chromosome 17, at position 13.2. It spans base pairs 3,636,468 and 3,661,542, and comprises 12 exons.
In 1995, the gene was localized to the short arm of chromosome 17. An international collaborative effort finally succeeded in isolating CTNS by positional cloning in 1998.
The CTNSN323K, CTNSK280R, and CTNSN288K mutations completely stop the movement of CySS out of the lysosome via cystinosin.[2] interestingly, CTNSN323K and CTNSK280R are related to juvenile nephropathic cystinosis while CTNSN288K mutations are found in cases with infantile nephropathic cystinosis.
Tissue distribution
The gene is expressed in the lysosomes of all organs and tissues. Cystinosin has also been found in melanosomes in melanocytes.
Structure
Cystinosin is a seven-transmembrane domain receptor embedded in the lysosomal membrane, and is a member of the lysosomal cystine transporter family of transport proteins. It comprises 367 amino acid residues, and has a molecular mass of 41738 Da. Cystinosin has seven N-glycosylation sites in the N-terminus region, spa |
https://en.wikipedia.org/wiki/DDX3X | ATP-dependent RNA helicase DDX3X is an enzyme that in humans is encoded by the DDX3X gene.
Function
DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. This gene encodes a DEAD box protein, which interacts specifically with hepatitis C virus core protein resulting a change in intracellular location. This gene has a homolog located in the nonrecombining region of the Y chromosome. The protein sequence is 91% identical between this gene and the Y-linked homolog.
Sub-cellular trafficking
DDX3X performs its functions in the cell nucleus and cytoplasm, exiting the nucleus via the exportin-1/CRM1 nuclear export pathway. It was initially reported that the DDX3X helicase domain was necessary for this interaction, while the canonical features of the trafficking pathway, namely the presence of a nuclear export signal (NES) on DDX3X and Ran-GTP binding to exportin-1, were dispensable. DDX3X binding to, and trafficking by, exportin-1 has since been shown not to require the DDX3X helicase domain and be explicitly NES- and Ran-GTP-dependent.
Role in cancer
DDX3X |
https://en.wikipedia.org/wiki/Chloride%20anion%20exchanger | Chloride anion exchanger, also known as down-regulated in adenoma (protein DRA), is a protein that in humans is encoded by the SLC26A3 gene.
Function
Protein DRA is a membrane protein in intestinal cells. It is an anion exchanger and a member of the sulfate anion transporter (SAT) family. It mediates chloride and bicarbonate exchange and additionally transports sulfate and other anions at the apical membrane, part of the plasma membrane of enterocytes. It is different from the anion exchanger that present in erythrocytes, renal tubule, and several other tissues.
The protein encoded by this gene is a transmembrane glycoprotein that functions as a sulfate transporter. It is localized to the mucosa of the lower intestinal tract, particularly to the apical membrane of columnar epithelium and some goblet cells, and is instrumental in chloride reuptake, aiding in the creation of an osmotic gradient for resorption of fluid from the lumen of the intestine.
Clinical significance
Mutations in this gene have been associated with congenital chloride diarrhoea, a treatable disease.
The congenital absence of this membrane protein results in an autosomal recessive disorder called congenital chloridorrhea or congenital chloride diarrhea (CLD).
See also
Solute carrier family
References
Further reading
Solute carrier family |
https://en.wikipedia.org/wiki/EEF1A2 | Elongation factor 1-alpha 2 is a protein that in humans is encoded by the EEF1A2 gene.
Function
This gene encodes an isoform of the alpha subunit of the elongation factor-1 complex, which is responsible for the enzymatic delivery of aminoacyl tRNAs to the ribosome. This isoform (alpha 2) is expressed in brain, heart and skeletal muscle, and the other isoform (alpha 1) is expressed in brain, placenta, lung, liver, kidney, and pancreas.
Clinical significance
This gene may be critical in the development of ovarian cancer.
Regulation
EEF1A2 is a direct target of miRNA-663 and miRNA-744.
References
Further reading
External links |
https://en.wikipedia.org/wiki/EIF2B1 | Translation initiation factor eIF-2B subunit alpha is a protein that in humans is encoded by the EIF2B1 gene.
Interactions
EIF2B1 has been shown to interact with EIF2B5.
References
Further reading |
https://en.wikipedia.org/wiki/EN2%20%28gene%29 | Homeobox protein engrailed-2 is a protein that in humans is encoded by the EN2 gene. It is a member of the engrailed gene family.
Function
Homeobox-containing genes are thought to have a role in controlling development. In Drosophila, the 'engrailed' (en) gene plays an important role during development in segmentation, where it is required for the formation of posterior compartments. Different mutations in the mouse homologs, En1 and En2, produced different developmental defects that frequently are lethal. The human engrailed homologs 1 and 2 encode homeodomain-containing proteins and have been implicated in the control of pattern formation during development of the central nervous system.
Description
The Engrailed-2 gene encodes for the Engrailed-2 homeobox transcription factor. The signaling molecule, fibroblast growth factor 8 (FGF8), controls the expression of the En2 gene. The isthmus organizer expresses varying concentrations of FGF8 that influence the En2 transcription factor. En2 transcription factor is involved in patterning the midbrain of the central nervous system during embryonic development. Specifically, it is required for proper positioning of folia in the developing hemispheres. It continues to regulate foliation throughout nervous system development. En2 patterns cerebellum foliation in the mediolateral axis. Several birth defects can arise from inadequate or abnormal En2 expression. Scientists use a mice model to study the effects of En2 knockout allel |
https://en.wikipedia.org/wiki/EPHA7 | Ephrin type-A receptor 7 is a protein that in humans is encoded by the EPHA7 gene.
This gene belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family. EPH and EPH-related receptors have been implicated in mediating developmental events, particularly in the nervous system. Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands.
References
Further reading
Tyrosine kinase receptors |
https://en.wikipedia.org/wiki/FBLN2 | Fibulin-2 is a protein that in humans is encoded by the FBLN2 gene.
This gene encodes an extracellular matrix protein, which belongs to the fibulin family. This protein binds various extracellular ligands and calcium. It may play a role during organ development, in particular, during the differentiation of heart, skeletal and neuronal structures. Alternatively spliced transcript variants encoding different isoforms have been identified.
Its role as a biomarker for meningiomas (a common tumour affecting the central nervous system) was recently described where a blood test can predict whether patients have a grade II meningiomas (poor outcome) and not a grade I meningioma (better outcome), without the need for a surgical biopsy.
Interactions
FBLN2 has been shown to interact with Laminin, alpha 1, Laminin, alpha 5 and Perlecan.
References
Further reading |
https://en.wikipedia.org/wiki/FGF9 | Glia-activating factor is a protein that in humans is encoded by the FGF9 gene.
Function
The protein encoded by this gene is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein was isolated as a secreted factor that exhibits a growth-stimulating effect on cultured glial cells. In nervous system, this protein is produced mainly by neurons and may be important for glial cell development. Expression of the mouse homolog of this gene was found to be dependent on Sonic hedgehog (Shh) signaling. Mice lacking the homolog gene displayed a male-to-female sex reversal phenotype, which suggested a role in testicular embryogenesis. This gene is involved in the patterning of sex determination, lung development, and skeletal development.
Sex determination
FGF9 has also been shown to play a vital role in male sex development. FGF9’s role in sex determination begins with its expression in the bi-potent gonads for both females and males. Once activated by SOX9, it is responsible for forming a feedforward loop with Sox9, increasing the levels of both genes. It forms a positive feedback loop upregulating SOX9, while simultaneously inactivating the female Wnt4 signaling pathway.
Lung development
In lung development, FGF9 is expressed in the mes |
https://en.wikipedia.org/wiki/GNB5 | Guanine nucleotide-binding protein subunit beta-5 is a protein that in humans is encoded by the GNB5 gene. Alternatively spliced transcript variants encoding different isoforms exist.
Function
Heterotrimeric guanine nucleotide-binding proteins (G proteins), which integrate signals between receptors and effector proteins, are composed of an alpha, a beta, and a gamma subunit. These subunits are encoded by families of related genes. This gene encodes a beta subunit. Beta subunits are important regulators of alpha subunits, as well as of certain signal transduction receptors and effectors.
GNB5 has been shown to differentially control RGS protein stability and membrane anchor binding, and therefore is involved in the control of complex neuronal G protein signaling pathways.
Interactions
GNB5 has been shown to interact with:
GNG7,
GNG13,
RGS7 and
RGS9.
References
Further reading |
https://en.wikipedia.org/wiki/PRDX3 | Thioredoxin-dependent peroxide reductase, mitochondrial is an enzyme that in humans is encoded by the PRDX3 gene. It is a member of the peroxiredoxin family of antioxidant enzymes.
Function
This gene encodes a protein with antioxidant function and is localized in the mitochondrion. This gene shows significant nucleotide sequence similarity to the gene coding for the C22 subunit of Salmonella typhimurium alkylhydroperoxide reductase. Expression of this gene product in E. coli deficient in the C22-subunit gene rescued resistance of the bacteria to alkylhydroperoxide. The human and mouse genes are highly conserved, and they map to the regions syntenic between mouse and human chromosomes. Sequence comparisons with recently cloned mammalian homologues suggest that these genes consist of a family that is responsible for regulation of cellular proliferation, differentiation, and antioxidant functions. Two transcript variants encoding two different isoforms have been found for this gene.
Interactions
PRDX3 has been shown to interact with MAP3K13.
Clinical significance
It has been demonstrated that serum peroxiredoxin 3 can be a valuable biomarker for the diagnosis and assessment of hepatocellular carcinoma It has been shown that peroxiredoxin proteins protect MCF-7 breast cancer cells against doxorubicin-mediated toxicity. Additionally, it has been shown that peroxiredoxin 3 is overexpressed in prostate cancer and promotes cancer cell survival by defending cells against the |
https://en.wikipedia.org/wiki/SF3A3 | Splicing factor 3A subunit 3 is a protein that in humans is encoded by the SF3A3 gene.
This gene encodes subunit 3 of the splicing factor 3a protein complex. The splicing factor 3a heterotrimer includes subunits 1, 2 and 3 and is necessary for the in vitro conversion of 15S U2 snRNP into an active 17S particle that performs pre-mRNA splicing. Subunit 3 interacts with subunit 1 through its amino-terminus while the zinc finger domain of subunit 3 plays a role in its binding to the 15S U2 snRNP. This gene has a pseudogene on chromosome 20.
Interactions
SF3A3 has been shown to interact with SF3A1.
References
Further reading |
https://en.wikipedia.org/wiki/MAPRE2 | Microtubule-associated protein RP/EB family member 2 is a protein that in humans is encoded by the MAPRE2 gene.
Function
The protein encoded by this gene shares significant homology to the adenomatous polyposis coli (APC) protein-binding EB1 gene family. The function of this protein is unknown; however, its homology suggests involvement in tumorigenesis of colorectal cancers and proliferative control of normal cells. This gene may belong to the intermediate/early gene family, involved in the signal transduction cascade downstream of the TCR.
Interactions
MAPRE2 has been shown to interact with APC.
References
Further reading |
https://en.wikipedia.org/wiki/PTP4A3 | Protein tyrosine phosphatase type IVA 3 is an enzyme that in humans is encoded by the PTP4A3 gene.
The protein encoded by this gene belongs to a small class of prenylated protein tyrosine phosphatases (PTPs). PTPs are cell signaling molecules that play regulatory roles in a variety of cellular processes. This class of PTPs contain a PTP domain and a characteristic C-terminal prenylation motif. Studies of this class of PTPs in mice demonstrated that they were prenylated proteins in vivo, which suggested their association with cell plasma membrane. Overexpression of this gene in mammalian cells was reported to inhibit angiotensin-II induced cell calcium mobilization and promote cell growth. Two alternatively spliced variants exist.
References
Further reading |
https://en.wikipedia.org/wiki/TREX1 | Three prime repair exonuclease 1 is an enzyme that in humans is encoded by the TREX1 gene.
Function
This gene encodes the major 3'->5' DNA exonuclease in human cells. The protein is a non-processive exonuclease that may serve a proofreading function for a human DNA polymerase. It is also a component of the SET complex, and acts to rapidly degrade 3' ends of nicked DNA during granzyme A-mediated cell death. Mutations in this gene result in Aicardi-Goutieres syndrome, chilblain lupus, RVCL (Retinal Vasculopathy with Cerebral Leukodystrophy), and Cree encephalitis. Multiple transcript variants encoding different isoforms have been found for this gene.
Clinical relevance
Mutations within the TREX1 gene cause familial chilblain lupus. The TREX1 polymorphisms confer susceptibility to systemic lupus erythematosus. Missense mutations of the TREX1 gene significantly downregulate its exonucleolytic capacity and result in the accumulation of nucleic acids. The build-up of the nucleic acids within the cytoplasm stimulates type-I interferon responses that could trigger autoimmune responses. The region containing the TREX1 gene (3p21.31) has been linked to COVID-19 severity in a recent genome-wide association study. This might explain the occurrence of chilblain like lesions in patients infected with SARS-CoV-2.
TREX1 helps HIV‑1 to evade cytosolic sensing by degrading viral cDNA in the cytoplasm
Mutations in TREX1 can give cause failure to appropriately remove ribonucleotides misin |
https://en.wikipedia.org/wiki/CCT5%20%28gene%29 | T-complex protein 1 subunit epsilon is a protein that in humans is encoded by the CCT5 gene.
Function
This gene encodes a molecular chaperone that is member of the TRiC complex. This complex consists of two identical stacked rings, each containing eight different proteins. Unfolded polypeptides enter the central cavity of the complex and are folded in an ATP-dependent manner. The complex folds various proteins, including actin and tubulin. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized.
Interactions
CCT5 (gene) has been shown to interact with PPP4C.
References
External links
Further reading |
https://en.wikipedia.org/wiki/ASCC3L1 | U5 small nuclear ribonucleoprotein 200 kDa helicase is an enzyme that in humans is encoded by the SNRNP200 gene.
References
External links
Further reading
Spliceosome |
https://en.wikipedia.org/wiki/FNBP1 | Formin-binding protein 1 is a protein that in humans is encoded by the FNBP1 gene.
Function
The protein encoded by this gene is a member of the formin-binding-protein family. The protein contains an N-terminal Fer/Cdc42-interacting protein 4 (CIP4) homology (FCH) domain followed by a coiled-coil domain, a proline-rich motif, a second coiled-coil domain, a Rho family protein-binding domain (RBD), and a C-terminal SH3 domain. This protein binds sorting nexin 2 (SNX2), tankyrase (TNKS), and dynamin; an interaction between this protein and formin has not been demonstrated yet in human.
Interactions
FNBP1 has been shown to interact with:
AKAP9,
DNM1,
Fas ligand
SNX2, and
TNKS.
References
Further reading |
https://en.wikipedia.org/wiki/NFASC | Neurofascin is a protein that in humans is encoded by the NFASC gene.
Function
Neurofascin is an L1 family immunoglobulin cell adhesion molecule (see L1CAM) involved in axon subcellular targeting and synapse formation during neural development.
Clinical importance
A homozygous mutation causing loss of Nfasc155 causes severe congenital hypotonia, contractures of fingers and toes and no reaction to touch or pain.
References
Further reading
Human proteins |
https://en.wikipedia.org/wiki/HIST3H2BB | Histone H2B type 3-B is a protein that in humans is encoded by the HIST3H2BB gene.
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 base pairs (bp) of DNA wrapped around a histone octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fiber is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. This gene is intronless and encodes a member of the histone H2B family. Transcripts from this gene contain a palindromic termination element.
References
Further reading |
https://en.wikipedia.org/wiki/FYB | FYN binding protein (FYB-120/130), also known as FYB, ADAP (Adhesion and degranulation-promoting adapter protein), and SLAP-130 (SLP-76-associated phosphoprotein) is a protein that is encoded by the FYB gene in humans. The protein is expressed in T cells, monocytes, mast cells, macrophages, NK cells, but not B cells. FYB is a multifunctional protein involved in post-activation T cell signaling, lymphocyte cytokine production, cell adhesion, and actin remodeling.
Structure
Two isoforms of FYB with different lengths of 120 and 130 kDa (FYB-120 and FYB-130) exist. The 130kDa version has an extra insertion of 46 amino acids and is preferentially expressed in peripheral T cells. The FYB protein has a variety of binding domains: a non-structured N-terminal region, a proline-rich region, two SH3 domains, a FPPP-motif which binds the ENA/VASP protein family, and other tyrosine-based signaling motifs.
Function
FYB is critical for activation and proliferation of T-helper cells (CD4+) and required for chemokine signal transduction in T-helper cells and cytotoxic T cells (CD8+).
FYB regulates cytokine production in T cells as well as in activated NK cells through the FYN-ADAP axis. In T cells, after TCR stimulation, a unique region of FYB, pYDGI, allows phosphorylation of the protein by FYN. After being phosphorylated, ADAP can bind to Carma1, causing NF-κB translocation into the nucleus and cytokine production.
In mast cells, FYB regulates cell adhesion as well as degranulation. I |
https://en.wikipedia.org/wiki/GFPT1 | Glucosamine—fructose-6-phosphate aminotransferase isomerizing 1 is an enzyme that in humans is encoded by the GFPT1 gene.
Glutamine-fructose-6-phosphate transaminase 1 is the first and rate-limiting enzyme of the hexosamine pathway. GFAT controls the flux of glucose into the hexosamine pathway and catalyzes the formation of glucosamine 6-phosphate.
References
Further reading |
https://en.wikipedia.org/wiki/GCLM | Glutamate-cysteine ligase regulatory subunit is an enzyme that in humans is encoded by the GCLM gene.
Glutamate-cysteine ligase, also known as gamma-glutamylcysteine synthetase, is the first rate limiting enzyme of glutathione synthesis. The enzyme consists of two subunits, a heavy catalytic subunit and a light regulatory subunit. Gamma glutamylcysteine synthetase deficiency has been implicated in some forms of hemolytic anemia.
References
Further reading |
https://en.wikipedia.org/wiki/HABP2 | Hyaluronan-binding protein 2 also known as factor VII activating protease (FSAP) is a protein that in humans is encoded by the HABP2 gene.
The protein encoded by this gene is an extracellular serine protease which binds hyaluronic acid. It is involved in cell adhesion. The protein is synthesized as a single chain, but then undergoes an autoproteolytic event to form the functional heterodimer. Further autoproteolysis leads to smaller, inactive peptides. Two transcript variants utilizing alternative polyA sites exist for this gene.
References
Further reading |
https://en.wikipedia.org/wiki/HAGH | Hydroxyacylglutathione hydrolase, mitochondrial is an enzyme that in humans is encoded by the HAGH gene.
The enzyme encoded by this gene is classified as a thiolesterase and is responsible for the hydrolysis of S-lactoyl-glutathione to reduced glutathione and D-lactate.
References
Further reading |
https://en.wikipedia.org/wiki/Hyaluronan-mediated%20motility%20receptor | Hyaluronan-mediated motility receptor (HMMR), also known as RHAMM (Receptor for Hyaluronan Mediated Motility) is a protein which in humans is encoded by the HMMR gene. RHAMM recently has been also designated CD168 (cluster of differentiation 168).
Function
RHAMM was originally discovered as a soluble protein that altered migratory cell behavior and bound to hyaluronan. RHAMM is less well studied than the main hyaluronan (HA) receptor, CD44. In contrast to CD44 and other cell-surface receptors which contain the classical membrane spanning domain and signal sequence for secretion from the endoplasmic reticulum / Golgi complex, RHAMM does not contain a membrane spanning domain nor does the mRNA transcript contain a signal sequence. RHAMM is localized inside the cell and is unconventionally exported to the cell surface in response to certain defined stimuli such as wounding and cytokines including TGF-β. The precise unconventional export mechanism for transporting RHAMM to the extracellular space is still unclear but may involve transport channels or proteins, flippase activity, or exocytosis, similar to other non-conventionally exported cell surface proteins such as BFGF1,2 and epimorphin.
Intracellularly, RHAMM associates with microtubules and, working with BRCA1 and BARD1, plays a role in the regulation of mitosis, and in maintaining mitotic spindle integrity. RHAMM also binds directly with ERK1 and forms complexes with ERK1,2 and MEK1, suggesting a role as a scaffold pro |
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