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https://en.wikipedia.org/wiki/HARS | Histidyl-tRNA synthetase (HARS) also known as histidine-tRNA ligase, is an enzyme which in humans is encoded by the HARS gene.
Function
Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a cytoplasmic enzyme which belongs to the class II family of aminoacyl tRNA synthetases. The enzyme is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. The gene is located in a head-to-head orientation with HARSL on chromosome five, where the homologous genes share a bidirectional promoter.
Clinical significance
The gene product is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis.
Interactions
HARS has been shown to interact with EEF1B2 and EEF1G.
References
Further reading |
https://en.wikipedia.org/wiki/HLA-DOA | HLA class II histocompatibility antigen, DO alpha chain is a protein that in humans is encoded by the HLA-DOA gene.
HLA-DOA belongs to the HLA class II alpha chain paralogues. HLA-DOA forms a heterodimer with HLA-DOB. The heterodimer, HLA-DO, is found in lysosomes in B cells and regulates HLA-DM-mediated peptide loading on MHC class II molecules. In comparison with classical HLA class II molecules, this gene exhibits very little sequence variation, especially at the protein level.
References
Further reading
MHC class II |
https://en.wikipedia.org/wiki/HLA-DOB | HLA class II histocompatibility antigen, DO beta chain is a protein that in humans is encoded by the HLA-DOB gene.
HLA-DOB belongs to the HLA class II beta chain paralogues. This class II molecule is a heterodimer consisting of an alpha (DOA) and a beta chain (DOB), both anchored in the membrane. It is located in intracellular vesicles. DO suppresses peptide loading of MHC class II molecules by inhibiting HLA-DM. Class II molecules are expressed in antigen presenting cells (APC: B lymphocytes, dendritic cells, macrophages). The beta chain is approximately 26-28 kDa and its gene contains 6 exons. Exon one encodes the leader peptide, exons 2 and 3 encode the two extracellular domains, exon 4 encodes the transmembrane domain and exon 5 encodes the cytoplasmic tail.
References
Further reading
MHC class II |
https://en.wikipedia.org/wiki/Equilibrative%20nucleoside%20transporter%202 | Equilibrative nucleoside transporter 2 (ENT2) is a protein that in humans is encoded by the SLC29A2 gene.
See also
Solute carrier family
Equilibrative nucleoside transporters
Nucleoside transporters
References
Further reading
Solute carrier family
Neurotransmitter transporters |
https://en.wikipedia.org/wiki/HOXB3 | Homeobox protein Hox-B3 is a protein that in humans is encoded by the HOXB3 gene.
This gene is a member of the Antp homeobox family and encodes a nuclear protein with a homeobox DNA-binding domain. It is included in a cluster of homeobox B genes located on chromosome 17. The encoded protein functions as a sequence-specific transcription factor that is involved in development. Increased expression of this gene is associated with a distinct biologic subset of acute myeloid leukemia (AML).
See also
Homeobox
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/HOXC4 | Homeobox protein Hox-C4 is a protein that in humans is encoded by the HOXC4 gene.
Function
This gene belongs to the homeobox family of genes. The homeobox genes encode a highly conserved family of transcription factors that play an important role in morphogenesis in all multicellular organisms. Mammals possess four similar homeobox gene clusters, HOXA, HOXB, HOXC and HOXD, which are located on different chromosomes and consist of 9 to 11 genes arranged in tandem. This gene, HOXC4, is one of several homeobox HOXC genes located in a cluster on chromosome 12. Three genes, HOXC5, HOXC4 and HOXC6, share a 5' non-coding exon. Transcripts may include the shared exon spliced to the gene-specific exons, or they may include only the gene-specific exons. Two alternatively spliced variants that encode the same protein have been described for HOXC4. Transcript variant one includes the shared exon, and transcript variant two includes only gene-specific exons.
See also
Homeobox
Interactions
HOXC4 has been shown to interact with Ku70.
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/HOXD9 | Homeobox protein Hox-D9 is a protein that in humans is encoded by the HOXD9 gene.
Function
This gene belongs to the homeobox family of genes. The homeobox genes encode a highly conserved family of transcription factors that play an important role in morphogenesis in all multicellular organisms. Mammals possess four similar homeobox gene clusters, HOXA, HOXB, HOXC and HOXD, located on different chromosomes, consisting of 9 to 11 genes arranged in tandem. This gene is one of several homeobox HOXD genes located at 2q31-2q37 chromosome regions. Deletions that removed the entire HOXD gene cluster or 5' end of this cluster have been associated with severe limb and genital abnormalities. The exact role of this gene has not been determined.
See also
Homeobox
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/Hippocalcin-like%20protein%201 | Hippocalcin-like protein 1 is a protein that in humans is encoded by the HPCAL1 gene.
The protein encoded by this gene is a member of the neuron-specific calcium-binding proteins family found in the retina and brain. It is highly similar to human hippocalcin protein, and nearly identical to rat and mouse hippocalcin like-1 proteins. It may be involved in the calcium-dependent regulation of rhodopsin phosphorylation, and may be of relevance to neuronal signaling in the central nervous system. There are two alternatively spliced transcript variants of this gene, with multiple polyadenylation sites.
References
Further reading
EF-hand-containing proteins |
https://en.wikipedia.org/wiki/IFIT1 | Interferon-induced protein with tetratricopeptide repeats 1 is a protein that in humans is encoded by the IFIT1 gene.
References
Further reading |
https://en.wikipedia.org/wiki/Immunoglobulin%20heavy%20constant%20alpha%201 | Immunoglobulin heavy constant alpha 1 is a immunoglobulin gene with symbol IGHA1. It encodes a constant (C) segment of Immunoglobulin A heavy chain. Immunoglobulin A is an antibody that plays a critical role in immune function in the mucous membranes. IgA shows the same typical structure of other antibody classes, with two heavy chains and two light chains, and four distinct domains: one variable region, and three variable regions. As a major class of immunoglobulin in body secretions, IgA plays a role in defending against infection, as well as preventing the access of foreign antigens to the immunologic system.
Discovery
IGHA1 was first described in detail in 1975, when the primary structure (the amino acid sequence) of IgA was elucidated through the sequencing of tryptic and chymotryptic peptides. Similarly, the primary sequence was determined independently for the alpha-2 chain of the protein in 1979. Complete nucleotide sequences for the alpha-1 heavy chain constant region and the allelic alpha-2 heavy chain regions were published in 1984, and showed the genes were contained in three exons, each of which encodes a single region of the protein domain.
Gene Location
The genes encoding IGHA1 are found on human chromosome 14. The sequence encoding IGHA1 is 1,497 nucleotides long and is found between loci 105,707,168 and 105,708,664. The annotated chromosome location is also given as 14q32.33.
Protein Structure
The Ig alpha-1 chain C region is contained on the first of t |
https://en.wikipedia.org/wiki/IGHMBP2 | DNA-binding protein SMUBP-2, also known as immunoglobulin helicase μ-binding protein 2 (IGHMBP2) and cardiac transcription factor 1 (CATF1) – is a protein that in humans is encoded by the IGHMBP2 gene.
Mutations in the IGHMBP2 gene cause distal spinal muscular atrophy type 1 (distal hereditary motor neuropathy type VI).
References
Further reading |
https://en.wikipedia.org/wiki/KCNJ3 | G protein-activated inward rectifier potassium channel 1 (GIRK-1) is encoded in the human by the gene KCNJ3.
Potassium channels are present in most mammalian cells, where they participate in a wide range of physiologic responses. The protein encoded by this gene is an integral membrane protein and inward-rectifier type potassium channel. The encoded protein, which has a greater tendency to allow potassium to flow into a cell rather than out of a cell, is controlled by G-proteins and plays an important role in regulating heartbeat. It associates with three other G-protein-activated potassium channels to form a hetero-tetrameric pore-forming complex.
Interactions
KCNJ3 has been shown to interact with KCNJ5.
See also
G protein-coupled inwardly-rectifying potassium channel
Inward-rectifier potassium ion channel
References
Further reading
External links
Ion channels |
https://en.wikipedia.org/wiki/KCNK3 | Potassium channel subfamily K member 3 is a protein that in humans is encoded by the KCNK3 gene.
This gene encodes K2P3.1, one of the members of the superfamily of potassium channel proteins containing two pore-forming P domains. K2P3.1 is an outwardly rectifying channel that is sensitive to changes in extracellular pH and is inhibited by extracellular acidification. Also referred to as an acid-sensitive potassium channel, it is activated by the anesthetics halothane and isoflurane. Although three transcripts are detected in northern blots, there is currently no sequence available to confirm transcript variants for this gene.
Interactive pathway map
Interactions
KCNK3 has been shown to interact with YWHAB and S100A10.
See also
Tandem pore domain potassium channel
References
Further reading
External links
Ion channels |
https://en.wikipedia.org/wiki/KIR3DL2 | Killer cell immunoglobulin-like receptor 3DL2 is a protein that in humans is encoded by the KIR3DL2 gene.
Killer cell immunoglobulin-like receptors (KIRs) are transmembrane glycoproteins expressed by natural killer cells and subsets of T cells. The KIR genes are polymorphic and highly homologous and they are found in a cluster on chromosome 19q13.4 within the 1 Mb leukocyte receptor complex (LRC). The gene content of the KIR gene cluster varies among haplotypes, although several "framework" genes are found in all haplotypes (KIR3DL3, KIR3DP1, KIR3DL4, KIR3DL2). The KIR proteins are classified by the number of extracellular immunoglobulin domains (2D or 3D) and by whether they have a long (L) or short (S) cytoplasmic domain. KIR proteins with the long cytoplasmic domain transduce inhibitory signals upon ligand binding via an immune tyrosine-based inhibitory motif (ITIM), while KIR proteins with the short cytoplasmic domain lack the ITIM motif and instead associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals. The ligands for several KIR proteins are subsets of HLA class I molecules; thus, KIR proteins are thought to play an important role in regulation of the immune response. This gene is one of the "framework" loci that is present on all haplotypes.
See also
Cluster of differentiation
References
Further reading
Clusters of differentiation
Immunoglobulin superfamily |
https://en.wikipedia.org/wiki/COPG2 | Coatomer subunit gamma-2 is a protein that in humans is encoded by the COPG2 gene.
Interactions
COPG2 has been shown to interact with Dopamine receptor D1 and COPB1.
References
External links
Further reading |
https://en.wikipedia.org/wiki/EIF2AK1 | Eukaryotic translation initiation factor 2-alpha kinase 1 is an enzyme that in humans is encoded by the EIF2AK1 gene.
Function
EIF2AK1 inhibits protein synthesis at the translation initiation level, in response to various stress conditions, including oxidative stress, heme deficiency, osmotic shock and heat shock. EIF2AK1 exerts its function through the phosphorylation of EIF2S1 at 'Ser-48' and 'Ser-51', thus preventing its recycling. Binds hemin forming a 1:1 complex through a cysteine thiolate and histidine nitrogenous coordination. This binding occurs with moderate affinity, allowing it to sense the heme concentration within the cell. Owing to this unique heme-sensing capacity, it plays a crucial role in shutting off protein synthesis during acute heme-deficient conditions. In red blood cells (RBCs), it controls hemoglobin synthesis ensuring a coordinated regulation of the synthesis of the heme and globin moieties of hemoglobin. Thus plays an essential protective role for RBC survival in anemias of iron deficiency. EIF2AK1 also act to moderate ER stress during acute heme-deficient conditions.
Enzymology
EIF2AK1 is a kinase, thus it catalyses the following reaction:
ATP + a protein = ADP + a phosphoprotein
EIF2AK1 is induced by acute heme depletion, that not only increases EIF2AK1 protein levels, but also stimulates kinase activity by autophosphorylation. Inhibited by the heme-degradation products biliverdin and bilirubin. Induced by oxidative stress generated by arse |
https://en.wikipedia.org/wiki/PRPF19 | Pre-mRNA-processing factor 19 is a protein that in humans is encoded by the PRPF19 gene.
In S. cerevisiae, Pso4 has pleiotropic functions in DNA recombination and in error-prone nonhomologous end-joining DNA repair.[supplied by OMIM]
Interactions
PRPF19 has been shown to interact with CDC5L.
References
Further reading |
https://en.wikipedia.org/wiki/MED4 | Mediator of RNA polymerase II transcription subunit 4 also known as mediator complex subunit 4 (MED4), a component of Mediator or vitamin D3 receptor-interacting protein complex 36 kDa component (DRIP36) is a protein that in humans is encoded by the MED4 gene.
Function
The protein encoded by this gene is a component of the vitamin D receptor-interacting protein (DRIP) complex which functions as a nuclear receptor coactivator. The DRIP complex is capable of activating nuclear receptors in a ligand-dependent manner.
Interactions
MED4 has been shown to interact with MED25.
References
Further reading |
https://en.wikipedia.org/wiki/ACP2 | Lysosomal acid phosphatase is an enzyme that in humans is encoded by the ACP2 gene.
Lysosomal acid phosphatase is composed of two subunits, alpha and beta, and is chemically and genetically distinct from red cell acid phosphatase. Lysosomal acid phosphatase 2 is a member of a family of distinct isoenzymes which hydrolyze orthophosphoric monoesters to alcohol and phosphate. Acid phosphatase deficiency is caused by mutations in the ACP2 (beta subunit) and ACP3 (alpha subunit) genes.
References
Further reading
External links
Human proteins |
https://en.wikipedia.org/wiki/ARR3 | Arrestin-C, also known as retinal cone arrestin-3, is a protein that in humans is encoded by the ARR3 gene.
See also
Arrestin
References
Further reading
External links |
https://en.wikipedia.org/wiki/ATP6V1C1 | V-type proton ATPase subunit C 1 is an enzyme that in humans is encoded by the ATP6V1C1 gene.
This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of intracellular compartments of eukaryotic cells. V-ATPase dependent acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c'', and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This gene is one of two genes that encode the V1 domain C subunit proteins and is found ubiquitously. This C subunit is analogous but not homologous to gamma subunit of F-ATPases. Previously, this gene was designated ATP6D.
In melanocytic cells ATP6V1C1 gene expression may be regulated by MITF.
References
Further reading
External links |
https://en.wikipedia.org/wiki/ATPase%2C%20H%2B%20transporting%2C%20lysosomal%20V0%20subunit%20a1 | V-type proton ATPase 116 kDa subunit a isoform 1 is an enzyme that in humans is encoded by the ATP6V0A1 gene.
This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c", and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This gene encodes one of three A subunit proteins and the encoded protein is associated with clathrin-coated vesicles. The occurrence of splice variants encoding different protein products has been reported, but the full-length natures of these transcripts have not been determined.
References
External links
Further reading |
https://en.wikipedia.org/wiki/LMO1 | Rhombotin-1 is a protein that in humans is encoded by the LMO1 gene.
LMO1 encodes a cysteine-rich, two LIM domain transcriptional regulator. It is mapped to an area of consistent chromosomal translocation in chromosome 11, disrupting it in T-cell leukemia, although more rarely than the related gene, LMO2 is disrupted.
Interactions
LMO1 has been shown to interact with GATA3 and TAL1.
References
Further reading |
https://en.wikipedia.org/wiki/MAFG | Transcription factor MafG is a bZip Maf transcription factor protein that in humans is encoded by the MAFG gene.
MafG is one of the small Maf proteins, which are basic region and leucine zipper (bZIP)-type transcription factors. The HUGO Gene Nomenclature Committee-approved gene name of MAFG is “v-maf avian musculoaponeurotic fibrosarcoma oncogene homolog G”.
Discovery
MafG was first cloned and identified in chicken in 1995 as a new member of the small Maf (sMaf) genes. MAFG has been identified in many vertebrates, including humans. There are three functionally redundant sMaf proteins in vertebrates, MafF, MafG, and MafK.
Structure
MafG has a bZIP structure that consists of a basic region for DNA binding and a leucine zipper structure for dimer formation. Similar to other sMafs, MafG lacks any canonical transcriptional activation domains.
Expression
MAFG is broadly but differentially expressed in various tissues. MAFG expression was detected in all 16 tissues examined by the human BodyMap Project, but relatively abundant in lung, lymph node, skeletal muscle and thyroid tissues. MafG gene expression is induced by oxidative stresses, such as hydrogen peroxide and electrophilic compounds. Mouse Mafg gene is induced by Nrf2-sMaf heterodimers through an antioxidant response element (ARE) at the promoter proximal region. In response to bile acids, mouse Mafg gene is induced by the nuclear receptor, FXR (Farnesoid X receptor).
Function
Because of sequence similarity, no |
https://en.wikipedia.org/wiki/ME1%20%28gene%29 | NADP-dependent malic enzyme is a protein that in humans is encoded by the ME1 gene.
This gene encodes a cytosolic, NADP-dependent enzyme that generates NADPH for fatty acid biosynthesis. The activity of this enzyme, the reversible oxidative decarboxylation of malate to pyruvate, links the glycolytic and citric acid cycles. The regulation of expression for this gene is complex. Increased expression can result from elevated levels of thyroid hormones or by higher proportions of carbohydrates in the diet.
References
Further reading |
https://en.wikipedia.org/wiki/MT1F | Metallothionein-1F is a protein that in humans is encoded by the MT1F gene.
References
Further reading |
https://en.wikipedia.org/wiki/MYBPC1 | Myosin-binding protein C, slow-type is a protein that in humans is encoded by the MYBPC1 gene.
References
Further reading |
https://en.wikipedia.org/wiki/MYCL | L-myc-1 proto-oncogene protein is a protein that in humans is encoded by the MYCL1 gene.
MYCL1 is a bHLH (basic helix-loop-helix) transcription factor implicated in lung cancer.
Interactions
MYCL1 has been shown to interact with MAX.
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/MYL3 | Myosin essential light chain (ELC), ventricular/cardiac isoform is a protein that in humans is encoded by the MYL3 gene. This cardiac ventricular/slow skeletal ELC isoform is distinct from that expressed in fast skeletal muscle (MYL1) and cardiac atrial muscle (MYL4). Ventricular ELC is part of the myosin molecule and is important in modulating cardiac muscle contraction.
Structure
Cardiac, ventricular ELC is 21.9 kDa and composed of 195 amino acids (See human MYL3 sequences features here). Cardiac ELC and the second light chain, regulatory light chain (RLC, MYL2), are non-covalently bound to IQXXXRGXXXR motifs in the 9 nm S1-S2 lever arm of the myosin head, both alpha (MYH6) and beta (MYH7) isoforms. Both light chains are members of the EF-hand superfamily of proteins, which possess helix-loop-helix motifs in two globular domains connected by an alpha-helical linker. Though EF hand motifs are specialized to bind divalent ions such as calcium, cardiac ELC does not bind calcium at physiological levels. The N-terminal region of cardiac ELC is functionally unique in that it is positively charged, being rich in Lysine residues (amino acids 4-14), with subsequent unique structure governed by proline-alanine repeats (amino acids 15-36).
Function
Studies have provided evidence for ELC as modulator of myosin crossbridge kinetics. Treating cardiac myofibrils with the lysine-rich N-terminal peptide (amino acids 5-14) evoked a supramaximal increase in cardiac myofibrillar MgATPase ac |
https://en.wikipedia.org/wiki/NOL1 | Putative ribosomal RNA methyltransferase NOP2 is an enzyme that in humans is encoded by the NOP2 gene.
The protein encoded by this gene is a nucleolar antigen expressed in proliferating cells. It is not detectable in non-proliferating normal tissue but is detectable in many human tumors.
Overexpression of p120 leads to malignant transformation of 3T3 cells while treatment with antisense p120 mRNA causes the transformed cells to revert to their original non-malignant phenotype. The p120 protein displays a dramatic increase in expression at the G1/S transition suggesting that p120 regulates the cell cycle and nucleolar activity that is required for cell proliferation.
Interactions
NOL1 has been shown to interact with MCRS1.
References
Further reading |
https://en.wikipedia.org/wiki/PFKP | Phosphofructokinase, platelet, also known as PFKP is an enzyme which in humans is encoded by the PFKP gene.
Function
The PFKP gene encodes the platelet isoform of phosphofructokinase (PFK) (ATP:D-fructose-6-phosphate-1-phosphotransferase, EC 2.7.1.11). PFK catalyzes the irreversible conversion of fructose 6-phosphate to fructose 1,6-bisphosphate and is a key regulatory enzyme in glycolysis. The PFKP gene, which maps to chromosome 10p, is also expressed in fibroblasts. See also the muscle (PFKM) and liver (PFKL) isoforms of phosphofructokinase, which map to chromosomes 12q13 and 21q22, respectively. Full tetrameric phosphofructokinase enzyme expressed in platelets can be composed of subunits P4, P3L, and P2L2.
Interactive pathway map
References
Further reading
External links |
https://en.wikipedia.org/wiki/SERPINB6 | Serpin B6 is a protein that in humans is encoded by the SERPINB6 gene.
See also
Serpin
References
Further reading
External links
The MEROPS online database for peptidases and their inhibitors: I04.011
Serine protease inhibitors |
https://en.wikipedia.org/wiki/Neuroserpin | Neuroserpin is a protein that in humans is encoded by the SERPINI1 gene.
It is associated with Familial encephalopathy with neuroserpin inclusion bodies.
Serine protease inhibitors of the serpin superfamily are involved in many cellular processes. Neuroserpin was first identified as a protein secreted from the axons of dorsal root ganglion neurons (Stoeckli et al., 1989). It is expressed in the late stages of neurogenesis during the process of synapse formation.[supplied by OMIM]
Interactions
SERPINI1 has been shown to interact with Tissue plasminogen activator.
References
Further reading
External links
The MEROPS online database for peptidases and their inhibitors: I04.025 |
https://en.wikipedia.org/wiki/PITX1 | Paired-like homeodomain 1 is a protein that in humans is encoded by the PITX1 gene.
Function
This gene encodes a member of the RIEG/PITX homeobox family, which is in the bicoid class of homeodomain proteins. Members of this family are involved in organ development and left-right asymmetry. This protein acts as a transcriptional regulator involved in basal and hormone-regulated activity of prolactin.
Clinical relevance
Mutations in this gene have been associated with autism, club foot and polydactyly in humans.
Genetic basis of pathologies
Genomic rearrangements at the PITX1 locus are associated with Liebenberg syndrome. In PITX1 Liebenberg is associated with a translocation or deletions, which cause insert promoter groups into the PITX1 locus. A missense mutation within the PITX1 locus is associated with the development of autosomal dominant clubfoot.
Interactions
PITX1 has been shown to interact with pituitary-specific positive transcription factor 1.
References
Further reading
External links
http://omim.org/entry/602149 at OMIM, holds the most up to date information on PITX1.
https://ghr.nlm.nih.gov/gene/PITX1 at the NIH, has a summary on the effects of PITX1 mutations.
Transcription factors |
https://en.wikipedia.org/wiki/PMS1 | PMS1 protein homolog 1 is a protein that in humans is encoded by the PMS1 gene.
Function
The protein encoded by this gene was identified by its homology to a yeast protein involved in DNA mismatch repair. A role for this protein in mismatch repair has not been proven. However, the protein forms heterodimers with MLH1, a DNA mismatch repair protein, and some cases of hereditary nonpolyposis colorectal cancer have been found to have mutations in this gene.
References
Further reading |
https://en.wikipedia.org/wiki/Exosome%20component%2010 | Exosome component 10, also known as EXOSC10, is a human gene, the protein product of which is part of the exosome complex and is an autoantigen is patients with certain auto immune diseases, most notably scleromyositis.
References
Further reading |
https://en.wikipedia.org/wiki/RRM2B | Ribonucleotide-diphosphate reductase subunit M2 B is an enzyme that in humans is encoded by the RRM2B gene. The gene encoding the RRM2B protein is located on chromosome 8, at position 8q23.1. The gene and its products are also known by designations MTDPS8A, MTDPS8B, and p53R2.
Function
RRM2B codes for one of two versions of the R2 subunit of ribonucleotide reductase, which generates nucleotide precursors required for DNA replication by reducing ribonucleoside diphosphates to deoxyribonucloside diphosphates. The version of R2 encoded by RRM2B is induced by p53, and is required for normal DNA repair and mtDNA synthesis in non-proliferating cells. The other form of R2 is expressed only in dividing cells.
Interactions
RRM2B has been shown to interact with Mdm2 and Ataxia telangiectasia mutated.
Clinical relevance
Abnormalities in this gene are one of the causes of mitochondrial DNA depletion syndrome (MDDS). Neonatal hypotonia, developmental delay, encephalopathy, with seizures, deafness and lactic acidosis have been associated with mutations in this gene. MDDS is fatal, with death occurring from respiratory failure in early childhood.
It has been associated with some cases of pediatric acute liver failure.
Mutations in this gene have been shown to cause progressive external ophthalmoplegia.
Increased expression of RRM2B has been correlated with gemcitabine resistance in human cholangiocarcinoma cells and may be predictive of lack of clinical benefit from gemcitabine f |
https://en.wikipedia.org/wiki/NSDHL | Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating is an enzyme that in humans is encoded by the NSDHL gene. This enzyme is localized in the endoplasmic reticulum and is involved in cholesterol biosynthesis.
Clinical significance
Mutations in the NSDHL gene are associated with CHILD syndrome which is a X-linked dominant disorder of lipid metabolism with disturbed cholesterol biosynthesis, and typically lethal in males.
References
Further reading
External links
GeneReviews/NCBI/NIH/UW entry on NSDHL related disorders including CHILD syndrome CK syndrome |
https://en.wikipedia.org/wiki/NT5C3 | Cytosolic 5'-nucleotidase 3 (NTC53), also known as cytosolic 5'-nucleotidase 3A, pyrimidine 5’-nucleotidase (PN-I or P5'NI), and p56, is an enzyme that in humans is encoded by the NT5C3, or NT5C3A, gene on chromosome 7.
This gene encodes a member of the 5'-nucleotidase family of enzymes that catalyze the dephosphorylation of nucleoside 5'-monophosphates. The encoded protein is the type 1 isozyme of pyrimidine 5' nucleotidase and catalyzes the dephosphorylation of pyrimidine 5' monophosphates. Mutations in this gene are a cause of hemolytic anemia due to uridine 5-prime monophosphate hydrolase deficiency. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene, and pseudogenes of this gene are located on the long arm of chromosomes 3 and 4. [provided by RefSeq, Mar 2012]
Structure
The NT5C3 gene consists of 10 exons and can be alternatively spliced at exon 2. Four possible isoforms have been identified, encoding proteins with lengths of 336 residues, 297 residues, 286 residues, and 285 residues. The 286-residue long isozyme is a monomeric protein containing 5 cysteine residues and no disulfide bridges or phosphate content. It has a predicted mass of 32.7 kDa and a predicted globular tertiary structure consisting of approximately 30% α-helices and 26% extended strands. This enzyme structurally resembles members of the haloacid dehalogenase (HAD) superfamily in regards to the shared α/β-Rossmann-like domain and a smaller 4-helix b |
https://en.wikipedia.org/wiki/UBR5 | E3 ubiquitin-protein ligase UBR5 is an enzyme that in humans is encoded by the UBR5 gene.
Function
This gene encodes a progestin-induced protein, which belongs to the HECT (homology to E6-AP carboxyl terminus) family. The HECT family proteins function as E3 ubiquitin-protein ligases, targeting specific proteins for ubiquitin-mediated proteolysis. This gene is localized to chromosome 8q22 which is disrupted in a variety of cancers. This gene potentially has a role in regulation of cell proliferation or differentiation.
Interactions
UBR5 has been shown to interact with:
CIB1,
Karyopherin alpha 1,
MAPK1, and
TOPBP1.
References
Further reading
External links
Ubr5 : Protein Overview : UCSD-Nature Molecule Pages |
https://en.wikipedia.org/wiki/MED15 | Mediator of RNA polymerase II transcription subunit 15, also known as Gal11, Spt13 in yeast and PCQAP, ARC105, or TIG-1 in humans is a protein encoded by the MED15 gene.
Function
MED15 is a general transcriptional cofactor of the mediator complex involved in RNA polymerase II dependent transcription, originally called Gal11 and Spt13 and found in yeast as an essential factor for Gal4 dependent transactivation by T.Fukasawa and F.Winston labs. Transcription factors Gcn4, Pho4, Msn2, Ino2, members of the Gal4 family - Gal4, Oaf1, Pdr1, and viral VP16 have been reported to interact with yeast MED15.
Most of these transcription factors share the same transactivation domain, 9aaTAD, which directly interacts with KIX domain of the MED15.
Furthermore, human MED15 cooperates in mediator complex (previously known as PC2, ARC, or DRIP) with transcription factors like VP16 and SREBP. Human SREBP regulates sterol responsive gene expression, and this regulatory action is conserved in the genetic model organism C. elegans, a roundworm (homologues MDT-15 and SBP-1). Also in C. elegans, MDT-15 is essential for the response to several stresses (fasting, heavy metal, toxin, and oxidative stress); at least in part the fasting response is conferred by interactions of MDT-15 with nuclear receptors, including NHR-49.
Gene
The MED15 gene contains stretches of trinucleotide repeats and is located in the chromosome 22 region which is deleted in DiGeorge's syndrome. Two transcript variants en |
https://en.wikipedia.org/wiki/NLK | Serine/threonine protein kinase NLK is an enzyme that in humans is encoded by the NLK gene. Its name is an abbreviation for Nemo-Like Kinase, Nemo (nmo) being the Drosophila ortholog of the mammalian NLK gene. This enzyme is a member of the Mitogen-activated protein kinase (MAPK) family, although not explicitly designated as such (it does not even have a numbered MAPK code). It is a highly divergent, atypical member of the MAPK group, lacking most features so characteristic of most mitogen-activated protein kinases (e.g. it does not have the dual phosphorylation motifs of typical MAPKs, and is not phosphorylated by any known MAP2 kinases). Its activation mechanism and downstream targets are still not well characterized.
References
Further reading
Protein kinases |
https://en.wikipedia.org/wiki/SHC3 | SHC-transforming protein 3 is a protein that in humans is encoded by the SHC3 gene.
Interactions
SHC3 has been shown to interact with RICS and TrkB.
References
Further reading |
https://en.wikipedia.org/wiki/BCL2L2 | Bcl-2-like protein 2 is a 193-amino acid protein that in humans is encoded by the BCL2L2 gene on chromosome 14 (band q11.2-q12). It was originally discovered by Leonie Gibson, Suzanne Cory and colleagues at the Walter and Eliza Hall Institute of Medical Research, who called it Bcl-w.
Function
This gene encodes a pro-survival (anti-apoptotic) member of the bcl-2 protein family, and is most similar to Bcl-xL. The proteins of this family form hetero- or homodimers and act as anti- and pro-apoptotic regulators. Expression of this gene in cells has been shown to contribute to reduced cell apoptosis under cytotoxic conditions. Studies of the related gene in mice indicated a role in the survival of NGF- and BDNF-dependent neurons. Mutation and knockout studies of the mouse gene demonstrated an essential role in adult spermatogenesis.
Clinical significance
High levels of Bcl-w are seen in many cancers, including glioblastoma, colorectal cancer, non-small-cell lung carcinoma, and breast cancer. Breast cancer patients with metastasis have higher Bcl-w than breast cancer patients only having primary tumor. Elevated levels of Bcl-w has been shown to protect neurons from cell death induced by amyloid beta. Parkinson's disease patients with a mutant PARK2 gene have elevated Bcl-w. Bcl-w has been shown to contribute to cellular senescence.
Quercetin has been shown to inhibit the PI3K/AKT pathway leading to downregulation of Bcl-w.
Interactions
BCL2L2 has been shown to interact with:
|
https://en.wikipedia.org/wiki/PTPRS | Receptor-type tyrosine-protein phosphatase S, also known as R-PTP-S, R-PTP-sigma, or PTPσ, is an enzyme that in humans is encoded by the PTPRS gene.
Function
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains an extracellular region, a single transmembrane segment and two tandem intracytoplasmic catalytic domains (D1 and D2), and thus represents a receptor-type PTP. D1 is catalytically active, while D2 is catalytically inactive. The extracellular region of this protein is composed of multiple Ig-like and fibronectin type III-like domains. Rem2 signaling affects neuronal structure and function in part by regulation of gene expression. Molecular and Cellular NeuroscienceStudies of the similar gene in mice suggested that this PTP may be involved in cell-cell interaction, primary axonogenesis, and axon guidance during embryogenesis. This PTP has been also implicated in the molecular control of adult nerve repair. Four alternatively spliced transcript variants, which encode distinct proteins, have been reported.
Clinical significance
A PTPRS protein mimetic may improve muscular and bladder control in rats with spinal cord injuries.
Interactions
PTPRS has been shown to interact with:
chondroitin sulphate proteoglycans,
PTPRD, glial-derived |
https://en.wikipedia.org/wiki/Peroxisomal%20biogenesis%20factor%202 | Peroxisomal biogenesis factor 2 is a protein that in humans is encoded by the PEX2 gene.
This gene encodes an integral peroxisomal membrane protein required for peroxisome biogenesis. The protein is thought to be involved in peroxisomal matrix protein import. Mutations in this gene result in one form of Zellweger syndrome and infantile Refsum disease. Alternative splicing results in multiple transcript variants encoding the same protein.
References
Further reading
External links
GeneReviews/NCBI/NIH/UW entry on Peroxisome Biogenesis Disorders, Zellweger Syndrome Spectrum
OMIM entries on Peroxisome Biogenesis Disorders, Zellweger Syndrome Spectrum |
https://en.wikipedia.org/wiki/RARS%20%28gene%29 | Arginyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the RARS gene.
Aminoacyl-tRNA synthetases catalyze the aminoacylation of 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. Arginyl-tRNA synthetase belongs to the class-I aminoacyl-tRNA synthetase family.
Genetics
Mutations in RARS cause hypomyelination.
Interactions
RARS (gene) has been shown to interact with QARS.
References
Further reading
External links |
https://en.wikipedia.org/wiki/RARRES3 | Retinoic acid receptor responder protein 3 is a protein that in humans is encoded by the RARRES3 gene.
Retinoids exert biologic effects such as potent growth inhibitory and cell differentiation activities and are used in the treatment of hyperproliferative dermatological diseases. These effects are mediated by specific nuclear receptor proteins that are members of the steroid and thyroid hormone receptor superfamily of transcriptional regulators. RARRES1, RARRES2, and RARRES3 are genes whose expression is upregulated by the synthetic retinoid tazarotene. RARRES3 is thought act as a tumor suppressor or growth regulator.
Interactions
RARRES3 has been shown to interact with RNF135.
References
Further reading |
https://en.wikipedia.org/wiki/RENBP | N-acylglucosamine 2-epimerase is an enzyme that in humans is encoded by the RENBP gene.
The gene product inhibits renin activity by forming a dimer with renin, a complex known as high molecular weight renin. The encoded protein contains a leucine zipper domain, which is essential for its dimerization with renin. The gene product can catalyze the interconversion of N-acetylglucosamine to N-acetylmannosamine, indicating that it is a GlcNAc 2-epimerase. Transcript variants utilizing alternative promoters have been described in the literature.
References
Further reading |
https://en.wikipedia.org/wiki/60S%20ribosomal%20protein%20L7 | 60S ribosomal protein L7 is a protein that in humans is encoded by the RPL7 gene.
Function
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 protein that is a component of the 60S subunit. The protein belongs to the L30P family of ribosomal proteins. It contains an N-terminal basic region-leucine zipper (BZIP)-like domain and the RNP consensus sub-motif RNP2. In vitro the BZIP-like domain mediates homodimerization and stable binding to DNA and RNA, with a preference for 28S rRNA and mRNA. The protein can inhibit cell-free translation of mRNAs, suggesting that it plays a regulatory role in the translation apparatus. It is located in the cytoplasm. The protein has been shown to be an autoantigen in patients with systemic autoimmune diseases, such as systemic lupus erythematosus. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.
Interactions
RPL7 has been shown to interact with ZNF7. It interacts with HIV-1 Gag protein through Zinc Finger of HIV-1 Gag.
References
Further reading
Ribosomal proteins |
https://en.wikipedia.org/wiki/60S%20ribosomal%20protein%20L11 | 60S ribosomal protein L11 is a protein that in humans is encoded by the RPL11 gene.
Function
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 protein that is a component of the 60S subunit. The protein belongs to the L5P family of ribosomal proteins. It is located in the cytoplasm. The protein probably associates with the 5S rRNA. Alternative splice variants encoding different isoforms may exist, but they have not been fully characterized. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.
Interactions
RPL11 has been shown to interact with:
BLMH,
Mdm2,
NOP53,
P16,
P53, and
Promyelocytic leukemia protein
References
Further reading
External links
GeneReviews/NCBI/NIH/UW entry on Diamond-Blackfan Anemia
Ribosomal proteins |
https://en.wikipedia.org/wiki/ERRFI1 | ERBB receptor feedback inhibitor 1 is a protein that in humans is encoded by the ERRFI1 gene.
MIG6 is a Cytoplasmic protein whose expression is upregulated with cell growth (Wick et al., 1995). It shares significant homology with the protein product of rat gene-33, which is induced during cell stress and mediates cell signaling (Makkinje et al., 2000; Fiorentino et al., 2000).
Interactions
ERRFI1 has been shown to interact with Stratifin and CDC42.
References
Further reading
External links |
https://en.wikipedia.org/wiki/CDCA8 | Borealin is a protein that in humans is encoded by the CDCA8 gene.
Function
CDCA8 is a component of a chromosomal passenger complex required for stability of the bipolar mitotic spindle.
Interactions
CDCA8 has been shown to interact with INCENP, Survivin and Aurora B kinase.
References
Further reading
External links |
https://en.wikipedia.org/wiki/POMGNT1 | Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1 is an enzyme that in humans is encoded by the POMGNT1 gene.
Function and expression
The product of the POMGNT1 gene, protein O-mannose beta-1,2-N-acetylglucosaminyltransferase (POMGnT1), participates in O-mannosyl glycan synthesis. A mutation in this gene is the cause of muscle-eye-brain disease (MIM 253280).
Transcription of the POMGNT1 gene gives rise to a 2.7 kb mRNA in different tissues, with higher expression levels in the skeletal muscle, heart, and kidney and lower levels in the brain. POMGnT1 (EC 2.4.1.101) is a protein belonging to the GT13 family of glycosyltransferases according to the Carbohydrate-Active enZYmes (CAZy) database. In humans, the main isoform of POMGnT1 contains 660 amino acids whose sequence yields a calculated molecular mass of 75,252 Da (UniProtKB Q8WZA1).
The POMGNT1 mRNA and its encoded protein is expressed in the neural retina of all mammals studied. POMGnT1 locates in the cytoplasmic fraction in the mouse retina, where it concentrates in the Golgi complex within the myoid of photoreceptor inner segments.
References
Further reading
External links
GeneReviews/NCBI/NIH/UW entry on Congenital Muscular Dystrophy Overview |
https://en.wikipedia.org/wiki/PACS1 | Phosphofurin acidic cluster sorting protein 1, also known as PACS-1, is a protein that in humans is encoded by the PACS1 gene.
Function
The PACS-1 protein has a putative role in the localization of trans-Golgi network (TGN) membrane proteins. Mouse and rat homologs have been identified and studies of the homologous rat protein indicate a role in directing TGN localization of furin by binding to the protease's phosphorylated cytosolic domain. In addition, the human protein plays a role in HIV-1 Nef-mediated downregulation of cell surface MHC-I molecules to the TGN, thereby enabling HIV-1 to escape immune surveillance.
Interactions
PACS1 has been shown to interact with Furin.
Clinical significance
A de novo mutation c.607C>T in the PACS1 gene has been shown to result in a syndromic phenotype (colloquially called PACS1 Syndrome) that is characterized by global developmental delay, intellectual disability, and specific facial features.
Prevalence and diagnosis
The first two cases were identified in early 2011 by doctors in the Netherlands. As of late 2014, there were 20 cases identified worldwide.
Diagnosis is typically done using full genome or exome sequencing. There are likely several more cases that will eventually be reported as knowledge of the mutation spreads and testing becomes more accessible.
Observed and reported traits
Individuals with the mutation have been reported to have similar facial features, such as:
Widely spaced eyes and low-set ears
Down- |
https://en.wikipedia.org/wiki/HR%20%28gene%29 | HR is a gene encoding Protein hairless.
This gene encodes a protein whose function has been linked to hair growth. A similar protein in rat functions as a transcriptional corepressor for thyroid hormone and interacts with histone deacetylases.
Human Genetics
Variations in this gene are involved in low levels of hair (baldness / alopecia / hypotrichosis) Mutations in this gene in humans have been documented in cases of autosomal recessive congenital alopecia and atrichia with papular lesions.
The protein contains a Zinc finger domain.
See also
Corepressor
References
Further reading
External links
Transcription coregulators |
https://en.wikipedia.org/wiki/SELS%20%28gene%29 | Selenoprotein S, also known as SELS, is a human gene.
This gene encodes a selenoprotein, which contains a selenocysteine (Sec) residue at its active site. The selenocysteine is encoded by the UGA codon that normally signals translation termination. The 3' UTR of selenoprotein genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. Studies suggest that this protein may regulate cytokine production, and thus play a key role in the control of the inflammatory response. Two alternatively spliced transcript variants encoding the same protein have been found for this gene.
Interactions
SELS (gene) has been shown to interact with Valosin-containing protein.
References
Further reading
Selenoproteins |
https://en.wikipedia.org/wiki/CENPJ | Centromere protein J is a protein that in humans is encoded by the CENPJ gene. It is also known as centrosomal P4.1-associated protein (CPAP). During cell division, this protein plays a structural role in the maintenance of centrosome integrity and normal spindle morphology, and it is involved in microtubule disassembly at the centrosome. This protein can function as a transcriptional coactivator in the Stat5 signaling pathway and also as a coactivator of NF-kappaB-mediated transcription, likely via its interaction with the coactivator p300/CREB-binding protein.
The Drosophila ortholog, sas-4, has been shown to be a scaffold for a cytoplasmic complex of Cnn, Asl, CP-190, tubulin and D-PLP (similar to the human proteins PCNT and AKAP9). These complexes are then anchored at the centriole to begin formation of the centrosome.
Model organisms
Model organisms have been used in the study of CENPJ function. A conditional knockout mouse line, called Cenpjtm1a(EUCOMM)Wtsi was generated as part of the International Knockout Mouse Consortium program—a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty five tests were carried out on mutant mice and thirteen significant abnormalities were observed. Homozygous mutants were subviable, had a decreased body weight, abnormal open field, body composition, X-ray imaging |
https://en.wikipedia.org/wiki/APOM | Apolipoprotein M is an apolipoprotein and member of the lipocalin protein family that in humans is encoded by the APOM gene. It is found associated with high density lipoproteins and to a lesser extent with low density lipoproteins and triglyceride-rich lipoproteins. The encoded protein is secreted through the plasma membrane but remains membrane-bound, where it is involved in lipid transport. Two transcript variants encoding two different isoforms have been found for this gene, but only one of them has been fully characterized. It lacks an external amphipathic motif and is uniquely secreted to plasma without cleavage of its terminal signal peptide. The average molecular weight is 21253 Da, and the monoisotopic molecular weight is 21239 Da.
References
Further reading
External links
Applied Research on apoM |
https://en.wikipedia.org/wiki/IL36G | Interleukin-36 gamma previously known as interleukin-1 family member 9 (IL1F9) is a protein that in humans is encoded by the IL36G gene.
Expression
IL36G is well-expressed in the epithelium of the skin, gut, and lung. In the skin IL36G is predominantly expressed in epidermal granular layer keratinocytes with little to no expression in basal layer keratinocytes.
Function
The protein encoded by this gene is a member of the interleukin-1 cytokine family. This gene and eight other interleukin-1 family genes form a cytokine gene cluster on chromosome 2. The activity of this cytokine is mediated via the interleukin-1 receptor-like 2 (IL1RL2/IL1R-rp2/IL-36 receptor), and is specifically inhibited by interleukin-36 receptor antagonist, (IL-36RA/IL1F5/IL-1 delta). Interferon-gamma, tumor necrosis factor-alpha and interleukin-1 β (IL-1β) are reported to stimulate the expression of this cytokine in keratinocytes. The expression of this cytokine in keratinocytes can also be induced by a multiple Pathogen-Associated Molecular Patterns (PAMPs). Both IL-36γ mRNA and protein have been linked to psoriasis lesions and has been used as a biomarker for differentiating between eczema and psoriasis. As with many other interleukin-1 family cytokines IL-36γ requires proteolytic cleavage of its N-terminus for full biological activity. However, unlike IL-1β the activation of IL-36γ is inflammasome-independent. IL-36γ is specifically cleaved by the endogenous protease cathepsin S as well exogen |
https://en.wikipedia.org/wiki/BCCIP | BRCA2 and CDKN1A-interacting protein is a protein that in humans is encoded by the BCCIP gene.
This gene product was isolated on the basis of its interaction with BRCA2 and p21 proteins. It is an evolutionarily conserved nuclear protein with multiple interacting domains. The N-terminal half shares moderate homology with regions of calmodulin and M-calpain, suggesting that it may also bind calcium. Functional studies indicate that this protein may be an important cofactor for BRCA2 in tumor suppression, and a modulator of CDK2 kinase activity via p21. Several transcript variants encoding different isoforms have been described for this gene.
Interactions
BCCIP has been shown to interact with BRCA2, P21, and PTPmu (PTPRM)
References
External links
Further reading |
https://en.wikipedia.org/wiki/SALL4 | Sal-like protein 4 (SALL4) is a transcription factor encoded by a member of the Spalt-like (SALL) gene family, SALL4. The SALL genes were identified based on their sequence homology to Spalt, which is a homeotic gene originally cloned in Drosophila melanogaster that is important for terminal trunk structure formation in embryogenesis and imaginal disc development in the larval stages. There are four human SALL proteins (SALL1, 2, 3, and 4) with structural homology and playing diverse roles in embryonic development, kidney function, and cancer. The SALL4 gene encodes at least three isoforms, termed A, B, and C, through alternative splicing, with the A and B forms being the most studied. SALL4 can alter gene expression changes through its interaction with many co-factors and epigenetic complexes. It is also known as a key embryonic stem cell (ESC) factor.
Structure, interaction partners, and DNA binding activity
SALL4 contains one zinc finger in its amino (N-) terminus and three clusters of zinc fingers that each coordinates zinc with two cysteines and two histidines (Cys2His2-type) that potentially confer nucleic acid binding activity. SALL4B lacks two of the zinc finger clusters found in the A isoform. Although it remains unclear which zinc finger cluster is responsible for SALL4’s DNA binding property
Different SALL family members can form hetero- or homodimers via their conserved glutamine (Q)-rich region. SALL4 has at least one canonical nuclear localization signal (NLS |
https://en.wikipedia.org/wiki/Mitochondrial%20antiviral-signaling%20protein | Mitochondrial antiviral-signaling protein (MAVS) is a protein that is essential for antiviral innate immunity. MAVS is located in the outer membrane of the mitochondria, peroxisomes, and mitochondrial-associated endoplasmic reticulum membrane (MAM). Upon viral infection, a group of cytosolic proteins will detect the presence of the virus and bind to MAVS, thereby activating MAVS. The activation of MAVS leads the virally infected cell to secrete cytokines. This induces an immune response which kills the host's virally infected cells, resulting in clearance of the virus.
Structure
MAVS is also known as IFN-β promoter stimulator I (IPS-1), caspase activation recruitment domain adaptor inducing IFN-β(CARDIF), or virus induced signaling adaptor (VISA). MAVS is encoded by a MAVS gene. MAVS is a 540 amino acid protein that consists of three components, a N terminal caspase activation recruitment domain (CARD), a proline rich domain, and a transmembrane C terminal domain (TM).
After the MAVS gene has been transcribed into RNA, ribosomes can translate the MAVS protein from two different sites. The initial translation site generates the full-length MAVS protein. The alternative translation site generates a shorter protein, termed as “miniMAVS” or short-MAVS (sMAVS). sMAVS is a 398 amino acid MAVS protein that lacks the CARD domain. This is significant because the CARD domain is where two cytosolic proteins bind to activate MAVS, signaling that there is a virus present in the cell.
|
https://en.wikipedia.org/wiki/RPTOR | Regulatory-associated protein of mTOR also known as raptor or KIAA1303 is an adapter protein that is encoded in humans by the RPTOR gene. Two mRNAs from the gene have been identified that encode proteins of 1335 (isoform 1) and 1177 (isoform 2) amino acids long.
Gene and expression
The human gene is located on human chromosome 17 with location of the cytogenic band at 17q25.3.
Location
RPTOR is highly expressed in skeletal muscle and is somewhat less present in brain, lung, small intestine, kidney, and placenta tissue. Isoform 3 is widely expressed and most highly expressed in the nasal mucosa and pituitary. The lowest levels occur in the spleen. In the cell, RPTOR is present in cytoplasm, lysosomes, and cytoplasmic granules. Amino acid availability determines RPTOR targeting to lysosomes. In stressed cells, RPTOR associates with SPAG5 and accumulates in stress granules, which significantly reduces its presence in lysosomes.
Function
RPTOR encodes part of a signaling pathway regulating cell growth which responds to nutrient and insulin levels. RPTOR is an evolutionarily conserved protein with multiple roles in the mTOR pathway. The adapter protein and mTOR kinase form a stoichiometric complex. The encoded protein also associates with eukaryotic initiation factor 4E-binding protein-1 and ribosomal protein S6 kinase. It upregulates S6 kinase, the downstream effector ribosomal protein, and it downregulates the mTOR kinase. RPTOR also has a positive role in maintaining ce |
https://en.wikipedia.org/wiki/JAM2 | Junctional adhesion molecule B is a protein that in humans is encoded by the JAM2 gene. JAM2 has also been designated as CD322 (cluster of differentiation 322).
Function
Tight junctions represent one mode of cell-to-cell adhesion in endothelial cell sheets, forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the paracellular space. The protein encoded by this immunoglobulin superfamily gene member is localized in the tight junctions between high endothelial cells. It acts as an adhesive ligand for interacting with a variety of immune cell types and may play a role in lymphocyte homing to secondary lymphoid organs.
It is purported to promote lymphocyte transendothelial migration. It might also be involved with endothelial cell polarity, by associating to cell polarity protein PARD3 (PAR-3), together with JAM3.
Interactions
JAM2 has been shown to interact with PARD3.
It also interacts with the integrin dimer VLA-4 (also called α4β1).
References
Further reading
External links
Clusters of differentiation |
https://en.wikipedia.org/wiki/Bleomycin%20hydrolase | Bleomycin hydrolase is an enzyme that in humans is encoded by the BLMH gene.
Bleomycin hydrolase (BMH) is a cytoplasmic cysteine peptidase that is highly conserved through evolution. Its biological function is hydrolysis of the reactive electrophile homocysteine thiolactone. Another of its activities is metabolic inactivation of the glycopeptide bleomycin (BLM), an essential component of combination chemotherapy regimens for cancer. The protein contains the signature active site residues of the cysteine protease papain superfamily.
Interactions
BLMH has been shown to interact with RPL29, RPL11, UBE2I and Amyloid precursor protein.
References
External links
Further reading
EC 3.4.22 |
https://en.wikipedia.org/wiki/CACNB4 | Voltage-dependent L-type calcium channel subunit beta-4 is a protein that in humans is encoded by the CACNB4 gene.
Function
This gene encodes a member of the beta subunit family, a protein in the voltage-dependent calcium channel complex. Calcium channels mediate the influx of calcium ions into the cell upon membrane polarization and consist of a complex of alpha-1, alpha-2/delta, beta, and gamma subunits in a 1:1:1:1 ratio. Various versions of each of these subunits exist, either expressed from similar genes or the result of alternative splicing. The protein described in this record plays an important role in calcium channel function by modulating G protein inhibition, increasing peak calcium current, controlling the alpha-1 subunit membrane targeting and shifting the voltage dependence of activation and inactivation. Alternate transcriptional splice variants of this gene, encoding different isoforms, have been characterized.
Clinical significance
Certain mutations in this gene have been associated with idiopathic generalized epilepsy (IGE) and juvenile myoclonic epilepsy (JME).
Interactions
CACNB4 has been shown to interact with Cav2.1.
See also
Voltage-dependent calcium channel
References
Further reading
External links
Ion channels |
https://en.wikipedia.org/wiki/40S%20ribosomal%20protein%20S13 | 40S ribosomal protein S13 is a protein that in humans is encoded by the RPS13 gene.
Function
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 protein that is a component of the 40S subunit. The protein belongs to the S15P family of ribosomal proteins. It is located in the cytoplasm. The protein has been shown to bind to the 5.8S rRNA in rat. The gene product of the E. coli ortholog (ribosomal protein S15) functions at early steps in ribosome assembly. This gene is co-transcribed with two U14 small nucleolar RNA genes, which are located in its third and fifth introns. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.
Interactions
RPS13 has been shown to interact with PDCD4.
References
Further reading
External links
Ribosomal proteins |
https://en.wikipedia.org/wiki/40S%20ribosomal%20protein%20S16 | 40S ribosomal protein S16''' is a protein that in humans is encoded by the RPS16'' 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 protein that is a component of the 40S subunit. The protein belongs to the S9P family of ribosomal proteins. It 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
Ribosomal protein S16 is one of the proteins from the small ribosomal subunit. It belongs to a ribosomal protein family that is divided into three groups based on sequence similarity:
* Eubacterial S16.
* Algal and plant chloroplast S16.
* Cyanelle S16.
* Neurospora crassa mitochondrial S24 (cyt-21).
S16 proteins have about 100 amino-acid residues. There are two paralogues in Arabidopsis thaliana, RPS16-1 (chloroplastic) and RPS16-2 (targeted to the chloroplast and the mitochondrion)
[4].
RPS16 has been shown to interact with CDC5L.
References
Further reading
Ribosomal proteins |
https://en.wikipedia.org/wiki/40S%20ribosomal%20protein%20S27 | 40S ribosomal protein S27 also known as metallopan-stimulin 1 or MPS-1 is a protein that in humans is encoded by the RPS27 gene. Metallopanstimulin is a zinc finger protein proposed to be involved DNA repair as well as oncogenesis.
Function
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 protein that is a component of the 40S subunit. The protein belongs to the S27E family of ribosomal proteins. It contains a C4-type zinc finger domain that can bind to zinc. The encoded protein has been shown to be able to bind to nucleic acid. It is located in the cytoplasm as a ribosomal component, but it has also been detected in the nucleus. Studies in rat indicate that ribosomal protein S27 is located near ribosomal protein S18 in the 40S subunit and is covalently linked to translation initiation factor eIF3. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.
Clinical significance
Its expression is increased in several types of malignancy and MPS levels have been reported to drop with treatment of some cancers. It has also been used as a target for some chemotherapies, which aim to chelate out the zinc from the zinc finger motif of the MPS, thus yielding it inactive. These therapies have shown p |
https://en.wikipedia.org/wiki/SCG5 | Neuroendocrine protein 7B2 is a protein that in humans is encoded by the SCG5 gene. The protein expressed by this gene is widely distributed in neuroendocrine tissues. It functions as a chaperone protein for the proprotein convertase PC2 by blocking the aggregation of this protein, and is required for the production of an active PC2 enzyme. It is an intrinsically disordered protein that may also function as a chaperone for other aggregating secretory proteins in addition to proPC2 (Helwig et al. 2013). 7B2 has been identified in vertebrates and in invertebrates as low as flatworms (Protein ID: AIZ72728.1) and insects. It is also called Sgne1 and Secretogranin V. In C. elegans, it was originally called e7B2 and then renamed Seven B Two (gene name sbt-1). There is a Pfam entry for this protein: Secretogranin_V (PF05281).
References
Further reading |
https://en.wikipedia.org/wiki/SH3GL1 | Endophilin-A2 is a protein that in humans is encoded by the SH3GL1 gene.
References
Further reading |
https://en.wikipedia.org/wiki/SNRPA1 | U2 small nuclear ribonucleoprotein A' is a protein that in humans is encoded by the SNRPA1 gene.
Interactions
SNRPA1 has been shown to interact with CDC5L.
References
Further reading |
https://en.wikipedia.org/wiki/SNX2 | Sorting nexin-2 is a protein that in humans is encoded by the SNX2 gene.
Function
This gene encodes a member of the sorting nexin family. Members of this family contain a phox (PX) domain, which is a phosphoinositide binding domain, and are involved in intracellular trafficking. This protein associates with formin-binding protein 17, but its function is unknown. This protein may form oligomeric complexes with family members.
Interactions
SNX2 has been shown to interact with FNBP1.
References
Further reading |
https://en.wikipedia.org/wiki/SOX5 | Transcription factor SOX-5 is a protein that in humans is encoded by the SOX5 gene.
Function
This gene encodes a member of the SOX (SRY-related HMG-box) family of transcription factors involved in the regulation of embryonic development and in the determination of the cell fate. The encoded protein may act as a transcriptional regulator after forming a protein complex with other proteins. The encoded protein may play a role in chondrogenesis. A pseudogene of this gene is located on chromosome 8. Multiple transcript variants encoding distinct isoforms have been identified for this gene.
Mutations in the SOX5 gene can cause Lamb-Shaffer syndrome.
See also
SOX genes
References
Further reading
Transcription factors |
https://en.wikipedia.org/wiki/TROVE2 | 60 kDa SS-A/Ro ribonucleoprotein is a protein that in humans is encoded by the TROVE2 gene.
References
Further reading |
https://en.wikipedia.org/wiki/ELOVL4 | Elongation of very long chain fatty acids protein 4 is a protein that in humans is encoded by the ELOVL4 gene.
ELOVL4 is a member of a large family of fatty acid elongases (ELO), that catalyzes the rate-limiting step in the elongation of long chain fatty acids (LC-FA) into very long -chain saturated (VLC-SFA) and polyunsaturated (VLC-PUFA) fatty acids, collectively known as VLC-FA (very long chain fatty acid). ELOVL4 and its products are found in the brain, skin, retina, Meibomian glands, testes and sperm. Known mutations of ELOVL4 in humans cause diseases such as Autosomal Dominant Stargardt-like Macular Dystrophy (STGD3), Spinocerebellar Ataxia-34 (SCA34), skin deformities and seizures.
See also
Stargardt disease
References
Further reading |
https://en.wikipedia.org/wiki/PHLDA2 | Pleckstrin homology-like domain family A member 2 is a protein that in humans is encoded by the PHLDA2 gene.
This gene is one of several genes in the imprinted gene domain of 11p15.5, which is considered to be an important tumor suppressor gene region. Alterations in this region may be associated with the Beckwith-Wiedemann syndrome, Wilms tumor, rhabdomyosarcoma, adrenocortical carcinoma, and lung, ovarian, and breast cancer. Studies of the mouse gene, however, which is also located in an imprinted gene domain, have shown that the product of this gene regulates placental growth.
References
Further reading |
https://en.wikipedia.org/wiki/UBE2G2 | Ubiquitin-conjugating enzyme E2 G2 is a protein that in humans is encoded by the UBE2G2 gene.
The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. The encoded protein shares 100% sequence identity with the mouse counterpart. This gene is ubiquitously expressed, with high expression seen in adult muscle. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. Ube2g2 is known to interact with a variety of other proteins, including ubiquitin, the AMFR (E3 gp78), and the SYVN1 (Hrd1 RING).
References
Further reading
External links |
https://en.wikipedia.org/wiki/UBE2V2 | Ubiquitin-conjugating enzyme E2 variant 2 is a protein that in humans is encoded by the UBE2V2 gene. Ubiquitin-conjugating enzyme E2 variant proteins constitute a distinct subfamily within the E2 protein family.
Structure
UBE2V2 has sequence similarity to other ubiquitin-conjugating enzymes but lack the conserved cysteine residue that is critical for the catalytic activity of E2s. The protein encoded by this gene also shares homology with ubiquitin-conjugating enzyme E2 variant 1 and yeast MMS2 gene product.
Function
UBE2V2 has also been implicated as an intracellular sensor of reactive electrophilic species, which are present in high levels during periods of pathogenic and/or environmental stress. The C69 residue of UBE2V2 is capable of binding with various RES. It has been shown that binding of RES to UBE2V2 promotes UBE2V2-mediated activation of Ube2N, another E2 protein that complexes with UBE2V2. Activated Ube2N has been shown to play a major role in promoting DNA-damage responses. Thus, UBE2V2 may promote genome integrity by directly sensing RES and effecting DNA damage responses. It may also be involved in the differentiation of monocytes and enterocytes.
Interactions
UBE2V2 has been shown to interact with HLTF. Although UBE2V2 itself lacks ubiquitin-conjugating activity, it can interact with different Ubiquitin-conjugating enzymes to facilitate their catalytic activities. For instance, UBE2V2 can complex with UBE2N to form a heterodimer capable of synthesizin |
https://en.wikipedia.org/wiki/UGT2B4 | UDP glucuronosyltransferase 2 family, polypeptide B4, also known as UGT2B4, is an enzyme that in humans is encoded by the UGT2B4 gene.
Function
UGT2B4 is mainly involved in the glucuronidation of hyodeoxycholic acid, a bile acid, and catechol-estrogens, such as 17-epiestriol and 4-hydroxy-estrone.
The expression of the UGT2B4 enzyme is upregulated by the farnesoid X receptor (FXR), a nuclear receptor which is activated by bile acids. These same bile acids are substrates for the UGT2B4 enzyme. Hence upregulation of UGT2B4 by activated FXR provides a mechanism for the detection, conjugation and subsequent elimination of toxic bile acids.
References
Further reading |
https://en.wikipedia.org/wiki/UCK2 | Uridine-cytidine kinase 2 (UCK2) is an enzyme that in humans is encoded by the UCK2 gene.
The protein encoded by this gene catalyzes the phosphorylation of uridine and cytidine to uridine monophosphate (UMP) and cytidine monophosphate (CMP), respectively. This is the first step in the production of the pyrimidine nucleoside triphosphates required for RNA and DNA synthesis. In addition, an allele of this gene may play a role in mediating nonhumoral immunity to Hemophilus influenzae type B.
Structure and mechanism
Uridine-cytidine kinase 2 is a tetramer with molecular mass of about 112 kDa. In the UCK2 monomer, the active site is composed of a five-stranded β-sheet, surrounded by five α-helices and a β-hairpin loop. The β-hairpin loop in particular forms a significant portion of a deep binding pocket for the uridine/cytidine substrate to moderate binding and release of substrate and products. Binding specificity for nucleosides is determined by the His-117 and Tyr-112 residues, which hydrogen bond with the 4-amino group or the 6-oxo group of cytidine and uridine, respectively. A magnesium ion is coordinated in the active site by Glu-135, Ser-34, and Asp-62. The Asp-62 residue is responsible for the catalytic activity in the enzyme active site; the acidic side chain of the Asp-62 residue deprotonates the 5’-hydroxyl group on the substrate and activates it to attack the γ-phosphorus of ATP. Structural analyses have shown that the side chain of the catalytic Asp-62 changes conf |
https://en.wikipedia.org/wiki/WNT7A | Protein Wnt-7a is a protein that in humans is encoded by the WNT7A gene.
Function
The WNT gene family consists of structurally related genes that encode secreted signaling proteins. These proteins have been implicated in oncogenesis and in several developmental processes, including regulation of cell fate and patterning during embryogenesis. This gene is a member of the WNT gene family. It encodes a protein showing 99% amino acid identity to the mouse Wnt7A protein. This gene not only guides the development of the anterior-posterior axis in the female reproductive tract but also plays a critical role in uterine smooth muscle pattering and maintenance of adult uterine function. It is also responsive to changes in the levels of sex steroid hormone in the female reproductive tract. Decreased expression of this gene in human uterine leiomyoma is found to be inversely associated with the expression of estrogen receptor alpha.
References
Further reading |
https://en.wikipedia.org/wiki/MAP3K12 | Mitogen-activated protein kinase 12 is an enzyme that in humans is encoded by the MAP3K12 gene.
Function
The protein encoded by this gene is a member of serine/threonine protein kinase family. This kinase contains a leucine-zipper domain, and is predominately expressed in neuronal cells. The phosphorylation state of this kinase in synaptic terminals was shown to be regulated by membrane depolarization via calcineurin. This kinase forms heterodimers with leucine zipper containing transcription factors, such as cAMP responsive element binding protein (CREB) and MYC, and thus may play a regulatory role in PKA or retinoic acid induced neuronal differentiation.
Interactions
MAP3K12 has been shown to interact with MAPK8IP1, MAP2K7 and MAPK8IP2.
Role in development
MAP3K12, otherwise known as DLK, can initiate coordinated signalling cascades that culminate in the phosphorylation of C-Jun N-terminal kinases or JNK. Several experiments have implicated this interaction as having a role in the developing mammalian nervous system. For example, neuronal migration and axon growth are critical components of neuronal development. DLK null mice have defects in neuronal migration, hypoplasia of several different axonal tracts and reduced axon number in various areas of the brain such as the cingulum and internal capsule. In addition, inhibition of DLK or JNK delays radial migration and disrupts the formation of the neocortex in mice. Another important function of the developing mammal |
https://en.wikipedia.org/wiki/TMPRSS3 | Transmembrane protease, serine 3 is an enzyme that in humans is encoded by the TMPRSS3 gene.
Function
This gene encodes a member of the serine protease family. The encoded protein contains a serine protease domain, a transmembrane domain, an LDL receptor class A domain, and a scavenger receptor cysteine-rich domain. Serine proteases are known to be involved in a variety of biological processes, whose malfunction often leads to human diseases and disorders. This gene was identified by its association with both congenital and childhood onset autosomal recessive deafness. This gene is expressed in fetal cochlea and many other tissues, and is thought to be involved in the development and maintenance of the inner ear or the contents of the perilymph and endolymph. This gene was also identified as a tumor associated gene that is overexpressed in ovarian tumors. Four alternatively spliced variants have been described, two of which encode identical products.
See also
Nonsyndromic deafness (DFNB8)
References
Further reading |
https://en.wikipedia.org/wiki/SMURF2 | E3 ubiquitin-protein ligase SMURF2 is an enzyme that in humans is encoded by the SMURF2 gene which is located at chromosome 17q23.3-q24.1.
Interactions
SMURF2 has been shown to interact with:
Mothers against decapentaplegic homolog 1,
Mothers against decapentaplegic homolog 2,
Mothers against decapentaplegic homolog 3,
Mothers against decapentaplegic homolog 7,
SCYE1,
SMURF1, and
Ubiquitin C.
TOP2A,
References
Further reading |
https://en.wikipedia.org/wiki/ACD%20%28gene%29 | Adrenocortical dysplasia protein homolog is a protein that in humans is encoded by the ACD gene.
Function
This gene encodes a protein that is involved in telomere function. This protein is one of six core proteins in the telosome/shelterin telomeric complex, which functions to maintain telomere length and to protect telomere ends. Through its interaction with other components, this protein plays a key role in the assembly and stabilization of this complex, and it mediates the access of telomerase to the telomere. Multiple transcript variants encoding different isoforms have been found for this gene. This gene, which is also referred to as TPP1, is distinct from the unrelated TPP1 gene on chromosome 11, which encodes tripeptidyl-peptidase I.
TPP1 is a component of the telomere-specific shelterin complex, which facilitates the replication of the double-stranded telomeric DNA tracts and protects the telomeric end from unregulated DNA repair activities. TPP1 mainly functions as a regulator of telomerase recruitment, activation, and regulation. Although TPP1 was originally described as a bridging factor between TRF1 and TRF2, which participate in a pathway with POT1 as a negative regulator of telomerase-dependent telomere length control, more recent studies suggest that TPP1 could directly promotes telomerase activity at the telomere. A part of the TPP1 oligonucleotide/oligosaccharide-binding (OB) fold named TEL patch that interacts with the catalytic subunit of telomerase, hT |
https://en.wikipedia.org/wiki/MARCKSL1 | MARCKS-related protein is a protein that in humans is encoded by the MARCKSL1 gene.
Function
This gene encodes a member of the myristoylated alanine-rich C-kinase substrate (MARCKS) family. MARCKS play a role in cytoskeletal regulation, protein kinase C signaling and calmodulin signaling. The encoded protein affects the formation of adherens junction. Alternative splicing results in multiple transcript variants.
Interactions
MARCKSL1 has been shown to interact with DCTN2 and JNK.
References
Further reading |
https://en.wikipedia.org/wiki/USP5 | Ubiquitin specific peptidase 5 is an enzyme that in humans is encoded by the USP5 gene.
Interactions
USP5 has been shown to interact with TADA3L.
References
Further reading |
https://en.wikipedia.org/wiki/USP9X | Probable ubiquitin carboxyl-terminal hydrolase FAF-X is an enzyme that in humans is encoded by the USP9X gene.
Function
This gene is a member of the peptidase C19 family and encodes a protein that is similar to ubiquitin-specific proteases. Though this gene is located on the X chromosome, it escapes X-inactivation.
Depletion of USP9X from two-cell mouse embryos halts blastocyst development and results in slower blastomere cleavage rate, impaired cell adhesion and a loss of cell polarity. It has also been implicated that USP9X is likely to influence developmental processes through signaling pathways of Notch, Wnt, EGF, and mTOR. USP9X has been recognized in studies of mouse and human stem cells involving embryonic, neural and hematopoietic stem cells. High expression is retained in undifferentiated progenitor and stem cells and decreases as differentiation continues. USP9X is a protein-coding gene that has been implicated either directly through mutations or indirectly in a number of neurodevelopmental and neurodegenerative disorders. Three mutations have been connected with X-linked intellectual disability through disrupted neuronal growth and cell migration. Neurodegenerative disorders, such as Alzheimer's, Parkinson's and Huntington's disease, have also been linked to USP9X. Specifically, USP9X has been implicated in the regulation of the phosphorylation and expression of the microtule-associated protein tau, which forms pathological aggregates in Alzheimer's and other |
https://en.wikipedia.org/wiki/RBM10 | RNA-binding motif 10 is a protein that is encoded by the RBM10 gene. This gene maps on the X chromosome at Xp11.23 in humans. RBM10 is a regulator of alternative splicing. Alternative splicing is a process associated with gene expression to produce multiple protein isoforms from a single gene, thereby creating functional diversity and cellular complexity. RBM10 influences the expression of many genes, participating in various cellular processes and pathways such as cell proliferation and apoptosis. Its mutations are associated with various human diseases such as TARP syndrome, an X-linked congenital disorder in males resulting in pre‐ or postnatal lethality, and various cancers in adults.
Gene and protein
The RBM10 gene spans ~41.6 kb and contains 24 exons. This gene is subjected to X-inactivation, in which one of the two RBM10 genes in female cells is transcriptionally silenced by heterochromatin formation.
RBM proteins constitute a large family of RNA-binding proteins (RBPs). There are 52 RBM proteins (HGNC: HUGO Gene Nomenclature Committee), each containing one to several RNA-binding domains called RNA recognition motifs (RRMs). RBM10 contains two RRMs (RRM1 and RRM2) and other domains such as two zinc fingers (ZnFs), an octamer repeat (OCRE), three nuclear localization signals (NLSs), and a glycine-rich domain (G-patch). The amino acid (aa) sequence of RBM10 is conserved among mammals. Human RBM10 isoform 1 shares 96% and 97% sequence homology with those of mice and r |
https://en.wikipedia.org/wiki/HIST1H2AK | Histone H2A type 1 is a protein that in humans is encoded by the HIST1H2AK 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. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in the small histone gene cluster on chromosome 6p22-p21.3.
References
Further reading |
https://en.wikipedia.org/wiki/HIST1H2AC | Histone H2A type 1-C is a protein that in humans is encoded by the HIST1H2AC 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. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in the large histone gene cluster on chromosome 6.
Cancer
HIST1H2AC gene has been observed progressively downregulated in Human papillomavirus-positive neoplastic keratinocytes derived from uterine cervical preneoplastic lesions at different levels of malignancy. For this reason, HIST1H2AC is likely to be associated with tumorigenesis and may be a potential prognostic marker for uterine cervical preneoplastic lesions progression.
References
Further reading |
https://en.wikipedia.org/wiki/CDC42BPA | Serine/threonine-protein kinase MRCK alpha is an enzyme that in humans is encoded by the CDC42BPA gene.
The protein encoded by this gene is a member of the Serine/Threonine protein kinase family. This kinase contains multiple functional domains. Its kinase domain is highly similar to that of the myotonic dystrophy protein kinase (DMPK). This kinase also contains a Rac interactive binding (CRIB) domain, and has been shown to bind CDC42. It may function as a CDC42 downstream effector mediating CDC42 induced peripheral actin formation, and promoting cytoskeletal reorganization. Multiple alternatively spliced transcript variants have been described, and the full-length nature of two of them has been reported.
References
External links
Further reading |
https://en.wikipedia.org/wiki/RGS5 | Regulator of G-protein signaling 5 is a protein that in humans is encoded by the RGS5 gene.
The regulator of G protein signaling (RGS) proteins are signal transduction molecules that have structural homology to SST2 of Saccharomyces cerevisiae and EGL-10 of Caenorhabditis elegans. Multiple genes homologous to SST2 are present in higher eukaryotes. RGS proteins are involved in the regulation of heterotrimeric G proteins by acting as GTPase activators.
Interactions
RGS5 has been shown to interact with GNAO1, GNAI2 and GNAI3.
References
Further reading |
https://en.wikipedia.org/wiki/KHSRP | Far upstream element-binding protein 2 is a protein that in humans is encoded by the KHSRP gene.
References
Further reading |
https://en.wikipedia.org/wiki/PLA2G4C | Cytosolic phospholipase A2 gamma is an enzyme that in humans is encoded by the PLA2G4C gene.
References
Further reading |
https://en.wikipedia.org/wiki/PPAP2A | Lipid phosphate phosphohydrolase 1 also known as phosphatidic acid phosphatase 2a is an enzyme that in humans is encoded by the PPAP2A gene.
Function
Lipid phosphate phosphohydrolase 1 is a member of the phosphatidic acid phosphatase (PAP) family. PAPs convert phosphatidic acid to diacylglycerol, and function in de novo synthesis of glycerolipids as well as in receptor-activated signal transduction mediated by phospholipase D. This protein is an integral membrane glycoprotein, and has been shown to be a surface enzyme that plays an active role in the hydrolysis and uptake of lipids from extracellular space. The expression of this gene is found to be regulated by androgen in a prostatic adenocarcinoma cell line. At least two alternatively spliced transcript variants encoding distinct isoforms have been described.
References
Further reading |
https://en.wikipedia.org/wiki/CDK13 | Cyclin dependent kinase 13 is an enzyme that in humans is encoded by the CDK13 gene.
The protein encoded by this gene is a member of the cyclin-dependent serine/threonine protein kinase family. Members of this family are well known for their essential roles as master switches in cell cycle control. Some of the cell cycle control kinases are able to phosphorylate proteins that are important for cell differentiation and apoptosis, thus provide connections between cell proliferation, differentiation, and apoptosis. Proteins of this family may also be involved in non-cell cycle-related functions, such as neurocytoskeleton dynamics. The exact function of this protein has not yet been determined. It has unusually large N- and C-termini and is ubiquitously expressed in many tissues. Two alternatively spliced variants are described.
Clinical significance
Mutations in CDK13 cause CDK13-related disorder. A 2017 study of children with rare developmental disorders found 11 children in the United Kingdom who had a fault in their CDK13 gene. This fault affected the children's communication and language skills as well as causing learning difficulties.
References
External links
Further reading
EC 2.7.11 |
https://en.wikipedia.org/wiki/EIF3B | Eukaryotic translation initiation factor 3 subunit B (eIF3b) is a protein that in humans is encoded by the EIF3B gene.
Interactions
EIF3B has been shown to interact with P70-S6 Kinase 1 and EIF3A.
See also
Eukaryotic initiation factor 3 (eIF3)
References
Further reading |
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