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Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Catalyzes isomerization reactions that contribute to the biosynthesis of steroid hormones. Efficiently catalyze obligatory double-bond isomerizations of delta(5)-androstene-3,17-dione and delta(5)-pregnene-3,2-dione, precursors to testosterone and progesterone, respectively.

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The protein encoded by this gene is a member of the Fe65 protein family. It is an adaptor protein localized in the nucleus. It interacts with the Alzheimer's disease amyloid precursor protein (APP), transcription factor CP2/LSF/LBP1 and the low-density lipoprotein receptor-related protein. APP functions as a cytosolic anchoring site that can prevent the gene product's nuclear translocation. This encoded protein could play an important role in the pathogenesis of Alzheimer's disease. It is thought to regulate transcription. Also it is observed to block cell cycle progression by downregulating thymidylate synthase expression. Multiple alternatively spliced transcript variants encoding different isoforms have been described for this gene.

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Myosin is a highly conserved, ubiquitously expressed protein that interacts with Actin to generate the force for cellular movements. Conventional Myosins are hexameric proteins consisting of two heavy chain subunits, a pair of non-phosphorylatable light chain subunits and a pair of phosphorylatable light chain subunits. Three general classes of Myosin have been cloned: smooth muscle Myosins, striated muscle Myosins and non-muscle Myosins . Contractile activity in smooth muscle is regulated by the calcium/calmodulin-dependent phosphorylation of Myosin light chain (MLC) by Myosin light chain kinase. Myosin heavy chains, which are encoded by the MYH gene family, contain Actin-activated ATPase activity which generates the motor function of Myosin. Myosin heavy chains were initially isolated from a human fetal skeletal muscle and are the major determinant in the speed of contraction of skeletal muscle. Various isoforms of myosin heavy chains are differentially expressed depending on the functional activity of the muscle.

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Myosin is a highly conserved, ubiquitously expressed protein that interacts with Actin to generate the force for cellular movements. Conventional Myosins are hexameric proteins consisting of two heavy chain subunits, a pair of non-phosphorylatable light chain subunits and a pair of phosphorylatable light chain subunits. Three general classes of Myosin have been cloned: smooth muscle Myosins, striated muscle Myosins and non-muscle Myosins . Contractile activity in smooth muscle is regulated by the calcium/calmodulin-dependent phosphorylation of Myosin light chain (MLC) by Myosin light chain kinase. Myosin heavy chains, which are encoded by the MYH gene family, contain Actin-activated ATPase activity which generates the motor function of Myosin. Myosin heavy chains were initially isolated from a human fetal skeletal muscle and are the major determinant in the speed of contraction of skeletal muscle. Various isoforms of myosin heavy chains are differentially expressed depending on the functional activity of the muscle.

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Rho GTPases are GTP binding proteins that regulate a wide spectrum of cellular functions. These cellular processes include cytoskeletal rearrangements, gene transcription, cell growth and motility. Activation of Rho GTPases is under the direct control of guanine nucleotide exchange factors (GEFs). The protein encoded by this gene is a guanine nucleotide exchange factor and belongs to the Rho GTPase GFE family. Family members share a common feature, a Dbl (DH) homology domain followed by a pleckstrin (PH) homology domain. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Oct 2008].

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This gene encodes a member of the IQGAP family. The protein contains three IQ domains, one calponin homology domain, one Ras-GAP domain and one WW domain. It interacts with components of the cytoskeleton, with cell adhesion molecules, and with several signaling molecules to regulate cell morphology and motility. [provided by RefSeq, Jul 2008]

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This gene encodes a member of the IQGAP family. The protein contains three IQ domains, one calponin homology domain, one Ras-GAP domain and one WW domain. It interacts with components of the cytoskeleton, with cell adhesion molecules, and with several signaling molecules to regulate cell morphology and motility. [provided by RefSeq, Jul 2008]

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This gene encodes a member of the IQGAP family. The protein contains three IQ domains, one calponin homology domain, one Ras-GAP domain and one WW domain. It interacts with components of the cytoskeleton, with cell adhesion molecules, and with several signaling molecules to regulate cell morphology and motility. [provided by RefSeq, Jul 2008]

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Mitoferrin 2, also known as MRS3/4 (mitochondrial RNA-splicing protein 3/4 homolog), mitochondrial iron transporter 2, NPD016, MRS4L or SLC25A28 (solute carrier family 25 member 28), is a 364 amino acid multi-pass membrane protein of the mitochondrial inner membrane that mediates iron uptake. Mitoferrin 2 is thought to play a role in heme synthesis of hemoproteins and iron-sulfur cluster assembly. Ubiquitously expressed, Mitoferrin 2 is found at high levels in skeletal muscle, heart, placenta, kidney, lung, liver, brain and pancreas. Mitoferrin 2 is a member of the mitochondrial carrier family and undergoes alternative splicing events to produce four isoforms. Mitoferrin 2 contains three solcar repeats and is encoded by a gene that maps to human chromosome 10q24.2.

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E2-like enzyme which forms an intermediate with UFM1 via a thioester linkage.

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Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. It is the terminal component of a respiratory chain that transfers single electrons from cytoplasmic NADPH across the plasma membrane to molecular oxygen on the exterior. Also functions as a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes. It participates in the regulation of cellular pH and is blocked by zinc.

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CD1a is a non polymorphic MHC Class 1 related cell surface glycoprotein, expressed in association with Beta 2 microglobulin. CD1a is expressed by cortical thymocytes, Langerhan's cells and by interdigitating cells. CD1a is also expressed by some malignancies of T cell lineage and in histiocytosis X.

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CD1a is a non polymorphic MHC Class 1 related cell surface glycoprotein, expressed in association with Beta 2 microglobulin. CD1a is expressed by cortical thymocytes, Langerhan's cells and by interdigitating cells. CD1a is also expressed by some malignancies of T cell lineage and in histiocytosis X.

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The protein encoded by this gene is a member of the MAP kinase family. MAP kinases, also known as extracellular signal-regulated kinases (ERKs), act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. The activation of this kinase requires its phosphorylation by upstream kinases. Upon activation, this kinase translocates to the nucleus of the stimulated cells, where it phosphorylates nuclear targets. Two alternatively spliced transcript variants encoding the same protein, but differing in the UTRs, have been reported for this gene.

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Has a strict specificity for hydrolysis of asparaginyl bonds. Can also cleave aspartyl bonds slowly, especially under acidic conditions. Required for normal lysosomal protein degradation in renal proximal tubules. Required for normal degradation of internalized EGFR. Plays a role in the regulation of cell proliferation via its role in EGFR degradation (By similarity). May be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system.

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Epoxide hydrolase that catalyzes the final step in the biosynthesis of the proinflammatory mediator leukotriene B4. Has also aminopeptidase activity.

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Converts noradrenaline to adrenaline.

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Spo11 is a type II topoisomerase that is thought to generate the chromosome breaks that initiate meiotic recombination. The Spo11 protein initiates meiotic recombination by generating DNA double-strand breaks (DSBs) and is required for meiotic synapsis in S. cerevisiae. The DSBs are located mostly in promoter regions, where the chromatin is in an open configuration, and cluster in domains along the chromosome. Expression of the Spo11 is detected mainly in the testis, in agreement with its predicted function in the initiation of meiotic recombination. Disruption of Spo11 leads to severe gonadal abnormalities from defective meiosis and results in infertility.

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Phosphorylated upon DNA damage, probably by ATM or ATR.

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Binds VLDL and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits. Binding to Reelin induces tyrosine phosphorylation of Dab1 and modulation of Tau phosphorylation (By similarity).

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Binds VLDL and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits. Binding to Reelin induces tyrosine phosphorylation of Dab1 and modulation of Tau phosphorylation (By similarity).

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Palmitoylates sex steroid hormone receptors, including ESR1, PGR and AR, thereby regulating their targeting to the plasma membrane. This affects rapid intracellular signaling by sex hormones via ERK and AKT kinases and the generation of cAMP, but does not affect that mediated by their nuclear receptor (By similarity).

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Palmitoylates sex steroid hormone receptors, including ESR1, PGR and AR, thereby regulating their targeting to the plasma membrane. This affects rapid intracellular signaling by sex hormones via ERK and AKT kinases and the generation of cAMP, but does not affect that mediated by their nuclear receptor (By similarity).

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Palmitoylates sex steroid hormone receptors, including ESR1, PGR and AR, thereby regulating their targeting to the plasma membrane. This affects rapid intracellular signaling by sex hormones via ERK and AKT kinases and the generation of cAMP, but does not affect that mediated by their nuclear receptor (By similarity).

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Receptor for TNFSF9/4-1BBL. Possibly active during T cell activation.

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Receptor for TNFSF9/4-1BBL. Possibly active during T cell activation.

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This protein is part of the THO complex (THOC). The THO complex is recruited to transcribed genes and travels with the RNA polymerase during elongation. It may physically link proteins that function in transcription and in RNA export and RNA processing.

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Required for the relief of p53-dependent checkpoint mediated cell cycle arrest. Binds to and dephosphorylates 'Ser-15' of TP53 and 'Ser-345' of CHEK1 which contributes to the functional inactivation of these proteins.

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Required for the relief of p53-dependent checkpoint mediated cell cycle arrest. Binds to and dephosphorylates 'Ser-15' of TP53 and 'Ser-345' of CHEK1 which contributes to the functional inactivation of these proteins.

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This protein is part of the THO complex (THOC). The THO complex is recruited to transcribed genes and travels with the RNA polymerase during elongation. It may physically link proteins that function in transcription and in RNA export and RNA processing.