Membrane proteins are common proteins that are part of, or interact with, biological membranes. Membrane proteins fall into several broad categories depending on their location. Integral membrane proteins are a permanent part of a cell membrane and can either penetrate the membrane (transmembrane) or associate with one or the other side of a membrane. Peripheral membrane proteins are transiently associated with the cell membrane.
Topology of a transmembrane protein refers to locations of N- and C-termini of membrane-spanning polypeptide chain with respect to the inner or outer sides of the biological membrane occupied by the protein.
A signal peptide is a short peptide present at the N-terminus of most newly synthesized proteins that are destined toward the secretory pathway. These proteins include those that reside either inside certain organelles, secreted from the cell, or inserted into most cellular membranes. Although most type I membrane-bound proteins have signal peptides, most type II and multi-spanning membrane-bound proteins are targeted to the secretory pathway by their first transmembrane domain, which biochemically resembles a signal sequence except that it is not cleaved. They are a kind of target peptide.
The SH2domain is a structurally conserved protein domain contained within the Src oncoprotein and in many other intracellular signal-transducing proteins. SH2 domains bind to phosphorylated tyrosine residues on other proteins, modifying the function or activity of the SH2-containing protein. The SH2 domain may be considered the prototypical modular protein-protein interaction domain, allowing the transmission of signals controlling a variety of cellular functions. SH2 domains are especially common in adaptor proteins that aid in the signal transduction of receptor tyrosine kinase pathways.
Søren Brunak is a Danish biological and physical scientist working in bioinformatics, systems biology, and medical informatics. He is a professor of Disease Systems Biology at the University of Copenhagen and professor of bioinformatics at the Technical University of Denmark. As Research Director at the Novo Nordisk Foundation Center for Protein Research at the University of Copenhagen Medical School, he leads a research effort where molecular-level systems biology data are combined with phenotypic data from the healthcare sector, such as electronic patient records, registry information, and biobank questionnaires. A major aim is to understand the network biology basis for time-ordered comorbidities and discriminate between treatment-related disease correlations and other comorbidities in disease trajectories. Søren Brunak also holds a position as a Medical Informatics Officer at Rigshospitalet, the Capital Region of Denmark.
Carbohydrate kinase domain containing protein, encoded by CARKD gene, is a human protein of unknown function. The CARKD gene encodes proteins with a predicted mitochondrial propeptide (mCARKD), a signal peptide (spCARKD) or neither of them (cCARKD). Confocal microscopy analysis of transfected CHO cells indicated that cCARKD remains in the cytosol, whereas mCARKD and spCARKD are targeted to the mitochondria and the endoplasmic reticulum respectively. The protein is conserved throughout many species, and has predicted orthologs through eukaryotes, bacteria, and archea.
Neuroblastoma breakpoint family, member 15, also known as NBPF15, is a protein which in humans is encoded by the NBPF15 gene. The gene is 18762 bp long, with mRNA that is 3837 bp long. The gene is located on chromosome 1q21.1. Its sub-cellular location is predicted to be in the nucleus and cytoplasm. It contains what is known as the NBPF repeat, which is a two-exon stretch of sequence that is characteristic of all 21 members of the NBPF gene family. The repeat is considered the ancestral exons, and the NBPF family has been linked to primate evolution.
Transmembrane protein 126B is a protein that in humans is encoded by the TMEM126B gene. TMEM126B is a mitochondrial transmembrane protein which is a component of the mitochondrial complex I assembly complex. The TMEM126B gene is conserved in mammals. The encoded protein serves as an assembly factor that is required for formation of the membrane arm of the complex. It interacts with NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 13. Naturally occurring mutations in this gene are associated with isolated complex I deficiency. A pseudogene of this gene has been defined on chromosome 9.
KIAA0090 is a human gene coding for a protein of unknown function. KIAA0090 has two aliases OTTHUMP00000002581 and RP1-43E13.1. The gene codes for multiple transcript variants which can localize to different subcellular compartments. KIAA0090 interacts with multiple effector proteins. KIAA0090 contains a conserved COG1520 WD40 like repeat domain thought to be the method of such interaction.
The ISCB Accomplishment by a Senior Scientist Award is an annual prize awarded by the International Society for Computational Biology for contributions to the field of computational biology.
TMEM106A is a gene that encodes the transmembrane protein 106A (TMEM106A) in Homo sapiens. It is located at 17q21.31 on the plus strand next to cancer-related genes NBR1 and BRCA1. The TMEM106A gene contains a domain of unknown function, DUF1356.
In molecular biology, protein fold classes are broad categories of protein tertiary structure topology. They describe groups of proteins that share similar amino acid and secondary structure proportions. Each class contains multiple, independent protein superfamilies.
Alfonso Valencia is a Spanish biologist, ICREA Professor, current director of the Life Sciences department at Barcelona Supercomputing Center., of Spanish National Bioinformatics Institute (INB-ISCIII), and coordinator of the data pillar of the Spanish Personalised Medicine initiative, IMPaCT. From 2015-2018, he was President of the International Society for Computational Biology.
CXorf66 also known as Chromosome X Open Reading Frame 66, is a 361aa protein in humans that is encoded by the CXorf66 gene. The protein encoded is predicted to be a type 1 transmembrane protein; however, its exact function is currently unknown.
Stephen H. White is an American Biophysicist, academic, and author. He is a Professor Emeritus of Physiology and Biophysics at the University of California, Irvine.
Leucine-Rich Single-Pass Membrane Protein 1 (LSMEM1) is a protein that, in humans, is encoded by the LSMEM1 gene.
Leucine rich repeat containing 24 is a protein that, in humans, is encoded by the LRRC24 gene. The protein is represented by the official symbol LRRC24, and is alternatively known as LRRC14OS. The function of LRRC24 is currently unknown. It is a member of the leucine-rich repeat (LRR) superfamily of proteins.
Hanah Margalit is a Professor in the faculty of medicine at the Hebrew University of Jerusalem. Her research combines bioinformatics, computational biology and systems biology, specifically in the fields of gene regulation in bacteria and eukaryotes.
Shuguang Zhang is an American biochemist. He is at the MIT Media Lab's Laboratory for Molecular Architecture. Shuguang Zhang's research focuses on designs of biological molecules, particularly proteins and peptides. He has published over 170 scientific papers, which have cumulatively been cited over 35,000 times with an h-index of 88. On the “Updated science-wide author databases of standardizes citation indicators”, he is ranked 18th worldwide in the field of Biomedical Engineering. Zhang is also a co-founder and board member of Molecular Frontiers Foundation, which organizes annual Molecular Frontiers Symposia in Sweden and around the world. The selected winners are awarded Molecular Frontiers Inquiry Prize.
