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mammalian protein found in Homo sapiens

Presenilins are a family of related multi-pass transmembrane proteins which constitute the catalytic subunits of the gamma-secretase intramembrane protease protein complex. They were first identified in screens for mutations causing early onset forms of familial Alzheimer's disease by Peter St George-Hyslop. Vertebrates have two presenilin genes, called PSEN1 (located on chromosome 14 in humans) that codes for presenilin 1 (PS-1) and PSEN2 (on chromosome 1 in humans) that codes for presenilin 2 (PS-2). Both genes show conservation between species, with little difference between rat and human p

group of proteins having inorganic pyrophosphatase activity

protein family

InterPro Family

class of enzyme complexes

immunoglobulin-binding protein expressed in group C and G Streptococcal bacteria

class of enzymes

mammalian protein found in Homo sapiens

Parvalbumin (PV) is a calcium-binding protein with low molecular weight (typically 9–11 kDa). In humans, it is encoded by the PVALB gene. It is a member of the albumin family; it is named for its size (parv-, from Latin '''' which means "small") and its ability to coagulate.

InterPro Family

InterPro Family

thumb|263x263px|Electron micrograph of in vitro–formed COPI-coated vesicles. Average vesicle diameter at the membrane level is 60 nm.

thumb|Stick structure of the amino acid residues in segment B54-B64 in Mabinlin II. Constructed in PyMOL (PDB 2DS2). Mabinlins are sweet-tasting proteins extracted from the seed of mabinlang (Capparis masaikai Levl.), a plant growing in Yunnan province of China. There are four homologues. Mabinlin-2 was first isolated in 1983 and characterised in 1993, and is the most extensively studied of the four. The other variants of mabinlin-1, -3 and -4 were discovered and characterised in 1994.

class of enzymes

Staphylokinase (SAK; also known as staphylococcal fibrinolysin or Müller's factor) is a protein produced by Staphylococcus aureus. It contains 136 amino acid residues and has a molecular mass of 15kDa. Synthesis of staphylokinase occurs in late exponential phase. It is similar to streptokinase.

mammalian protein found in Homo sapiens

species of fungus

class of enzymes

enzyme class, includes alll types of glycogen/starch synthases

Vacuolar-type ATPase (V-ATPase) is a highly conserved evolutionarily ancient enzyme with remarkably diverse functions in eukaryotic organisms. V-ATPases acidify a wide array of intracellular organelles and pump protons across the plasma membranes of numerous cell types. V-ATPases couple the energy of ATP hydrolysis to proton transport across intracellular and plasma membranes of eukaryotic cells. It is generally seen as the polar opposite of ATP synthase because ATP synthase is a proton channel that uses the energy from a proton gradient to produce ATP. V-ATPase however, is a proton pump that

class of cell surface receptors recognized by its pharmacological profile

large mitochondrial outer membrane translocase complex that mediates transport of proteins into mitochondrial compartments. TOM transports beta-barrel precursors across the outer membrane and the sorting and assembly machinery (SAM complex) inserts

Origin recognition complex subunit 6 is a protein that in humans is encoded by the ORC6 (ORC6L) gene.

CD72 (Cluster of Differentiation 72), also known in murine biology as Lyb-2, is a protein active in the immune system of animals. It consists of two identical halves, each of about 39-43 kD, and is a C-type lectin. Its primarily locus of expression is B-cells (from the pro-B through the mature B-cell stage), where it appears to mediate aspects of B-cell - T-cell interaction. It is a ligand for CD5.

group of transport proteins

type of enzyme

Arrestins (abbreviated Arr) are a small family of proteins important for regulating signal transduction at G protein-coupled receptors. Arrestins were first discovered in the late '80s as a part of a conserved two-step mechanism for regulating the activity of G protein-coupled receptors (GPCRs) in the visual rhodopsin system by Hermann Kühn, Scott Hall, and Ursula Wilden and in the β-adrenergic system by Martin J. Lohse and co-workers.

Calponin is a calcium binding protein. Calponin tonically inhibits the ATPase activity of myosin in smooth muscle. Phosphorylation of calponin by a protein kinase, which is dependent upon calcium binding to calmodulin, releases the calponin's inhibition of the smooth muscle ATPase.

glycoprotein spike on a viral capsid or viral envelope

class of enzymes

class of enzymes

InterPro Family

protein family

InterPro Family

class of enzymes

class of enzymes

class of enzymes

secretoglobin protein

Perilipin, also known as lipid droplet-associated protein, perilipin 1, or PLIN, is a protein that, in humans, is encoded by the PLIN gene. The perilipins are a family of proteins that associate with the surface of lipid droplets. Phosphorylation of perilipin is essential for the mobilization of fats in adipose tissue.

mammalian protein found in Homo sapiens

class of enzymes

InterPro Family

class of enzymes

InterPro Family

thumb|right | alt=Visualization of the CD58 crystallized protein from the PDB identifier 1CCZ | Visualization of the CD58 crystallized protein from the PDB identifier 1CCZ CD58, or lymphocyte function-associated antigen 3 (LFA-3), is a cell adhesion molecule expressed on Antigen Presenting Cells (APCs), particularly macrophages, and other tissue cells.

Chemokine (C-C motif) ligand 14 (CCL14) is a small cytokine belonging to the CC chemokine family. It is also commonly known as HCC-1. It is produced as a protein precursor that is processed to generate a mature active protein containing 74 amino acids that and is 46% identical in amino acid composition to CCL3 and CCL4. This chemokine is expressed in various tissues including spleen, bone marrow, liver, muscle, and gut. CCL14 activates monocytes, but does not induce their chemotaxis. Human CCL14 is located on chromosome 17 within a cluster of other chemokines belonging to the CC family.

integrin complex found on platelets

InterPro Family

class of enzymes

class of enzymes

Serratiopeptidase (Serratia E-15 protease, also known as serralysin, serrapeptase, serratiapeptase, serratia peptidase, serratio peptidase, or serrapeptidase) is a proteolytic enzyme (protease) produced by enterobacterium Serratia sp. E-15, now known as Serratia marcescens ATCC 21074. This microorganism was originally isolated in the late 1960s from silkworm (Bombyx mori L.) intestine. Serratiopeptidase is present in the silkworm intestine and allows the emerging moth to dissolve its cocoon. Serratiopeptase is produced by purification from culture of Serratia E-15 bacteria. It is a member of t

group of anti-viral cytokines

Semaphorins are a class of secreted and membrane proteins that were originally identified as axonal growth cone guidance molecules. They primarily act as short-range inhibitory signals and signal through multimeric receptor complexes. Semaphorins are usually cues to deflect axons from inappropriate regions, especially important in the neural system development. The major class of proteins that act as their receptors are called plexins, with neuropilins as their co-receptors in many cases. The main receptors for semaphorins are plexins, which have established roles in regulating Rho-family GTPa

mammalian protein found in Homo sapiens

cell surface protein binding somatostatin and triggering intracellular changes

thumb | right | alt=Visualization of the CCL23 crystallized protein from PDB identifier 1G91 | Visualization of the CCL23 crystallized protein from PDB identifier 1G91 Chemokine (C-C motif) ligand 23 (CCL23) is a small cytokine belonging to the CC chemokine family that is also known as Macrophage inflammatory protein 3 (MIP-3) and Myeloid progenitor inhibitory factor 1 (MPIF-1). CCL23 is predominantly expressed in lung and liver tissue, but is also found in bone marrow and placenta. It is also expressed in some cell lines of myeloid origin. CCL23 is highly chemotactic for resting T cells and m

ATP-binding protein sequence motifs

thumb|left|Domain structure of formin proteins across phyla.

class of enzymes