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Ubiquitin is a highly conserved protein that is covalently linked to other proteins to regulate their function and degradation. This gene encodes a member of the ubiquitin-specific protease family of cysteine proteases. The enzyme specifically cleaves ubiquitin from ubiquitin-conjugated protein substrates. The protein is found in the nucleus and cytoplasm. It functions as a co-factor of the DNA-bound androgen receptor complex, and is inhibited by a protein in the Ras-GTPase pathway. The human genome contains several pseudogenes similar to this gene. Several transcript variants, some protein-coding and others not protein-coding, have been found for this gene. [provided by RefSeq, Jan 2013].

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BECN1L1 belongs to the beclin family and may play a role in autophagy and antiviral host defense.

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BTBD1 contains a proline-rich region and a BTB/POZ domain which are typically involved in protein-protein interactions. The C-terminus of BTBD1 binds topoisomerase I and BTBD1 also interacts with TRIM5 isoform Delta. BTBD1 localizes to cytoplasmic bodies and is essential for myogenic differentiation.

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BTBD1 contains a proline-rich region and a BTB/POZ domain which are typically involved in protein-protein interactions. The C-terminus of BTBD1 binds topoisomerase I and BTBD1 also interacts with TRIM5 isoform Delta. BTBD1 localizes to cytoplasmic bodies and is essential for myogenic differentiation.

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BTBD1 contains a proline-rich region and a BTB/POZ domain which are typically involved in protein-protein interactions. The C-terminus of BTBD1 binds topoisomerase I and BTBD1 also interacts with TRIM5 isoform Delta. BTBD1 localizes to cytoplasmic bodies and is essential for myogenic differentiation.

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E3 ubiquitin-protein ligase that plays a role in the control of mitochondrial morphology. Promotes mitochondrial fragmentation and influences mitochondrial localization. Inhibits cell growth. When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugatin.

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The cell commits to dividing during the G2/M phase transition, and the timing of mitotic entry is tightly regulated to guarantee correct chromosome segregation. D53, also referred to as tumor protein D52-like 1 (TPD52L1), is a coiled-coil motif-bearing member of the D52 tumor protein family. D53 intereacts with 14-3-3, a negative regulator of the G2/M transition, in breast cancer cells. Expression of D53 is highly upregulated at the G2/M phase transition in breast cancer cell lines, and deregulated expression of this protein can adversely affect the completion of mitosis. D53 may function as a signaling intermediate and/or regulator of vesicle trafficking and cell proliferation.

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Ankyrins are membrane adaptor molecules that play important roles in coupling integral membrane proteins to the spectrin-based cytoskeleton network. Mutations of ankyrin genes can lead to severe genetic diseases, such as fatal cardiac arrhythmias and hereditary spherocytosis. ANKRD13B (ankyrin repeat domain 13B) is a 626 amino acid protein that contains two ANK repeats and three ubiquitin-interacting motif (UIM) repeats. Conserved in dog, cow, mouse and rat, ANKRD13B exists as two alternatively spliced isoforms. The gene that encodes ANKRD13B maps to human chromosome 17, which makes up over 2.5% of the human genome, with about 81 million bases encoding over 1,200 genes. Two key tumor suppressor genes are associated with chromosome 17, namely, p53 and BRCA1. Malfunction or loss of p53 expression is associated with malignant cell growth and Li-Fraumeni syndrome. BRCA1 is recognized as a genetic determinant of early onset breast cancer. Chromosome 17 is also linked to neurofibromatosis, dysregulated Schwann cell growth, Alexander disease, Birt-Hogg-Dube syndrome and Canavan disease.

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Ankyrins are membrane adaptor molecules that play important roles in coupling integral membrane proteins to the spectrin-based cytoskeleton network. Mutations of ankyrin genes can lead to severe genetic diseases, such as fatal cardiac arrhythmias and hereditary spherocytosis. ANKRD13B (ankyrin repeat domain 13B) is a 626 amino acid protein that contains two ANK repeats and three ubiquitin-interacting motif (UIM) repeats. Conserved in dog, cow, mouse and rat, ANKRD13B exists as two alternatively spliced isoforms. The gene that encodes ANKRD13B maps to human chromosome 17, which makes up over 2.5% of the human genome, with about 81 million bases encoding over 1,200 genes. Two key tumor suppressor genes are associated with chromosome 17, namely, p53 and BRCA1. Malfunction or loss of p53 expression is associated with malignant cell growth and Li-Fraumeni syndrome. BRCA1 is recognized as a genetic determinant of early onset breast cancer. Chromosome 17 is also linked to neurofibromatosis, dysregulated Schwann cell growth, Alexander disease, Birt-Hogg-Dube syndrome and Canavan disease.

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CNTD2 (cyclin N-terminal domain containing 2) is a 155 amino acid protein that contains one cyclin N-terminal domain and is encoded by a gene that maps to human chromosome 19q13.2. Chromosome 19 consists of approximately 63 million bases and makes up over 2% of human genomic DNA. Chromosome 19 is recognized for having the greatest gene density of the human chromosomes. It is the genetic home for a number of immunoglobulin superfamily members, including killer cell and leukocyte Ig-like receptors, various ICAMs, the CEACAM and PSG families, and Fc?receptors. Key genes for eye color and hair color also map to chromosome 19. Peutz-Jeghers syndrome, spinocerebellar ataxia type 6, the stroke disorder CADASIL, hypercholesterolemia and insulin-dependent diabetes have been linked to chromosome 19. Translocations with chromosome 19 and chromosome 14 can be seen in some lymphoproliferative disorders and typically involve the proto-oncogene Bcl-3.

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Ankyrins are membrane adaptor molecules that play important roles in coupling integral membrane proteins to the spectrin-based cytoskeleton network. Mutations of ankyrin genes lead to severe genetic diseases such as fatal cardiac arrhythmias and hereditary spherocytosis. ANKMY1 (ankyrin repeat and MYND domain containing 1), also known as ZMYND13 or TSAL1, is a 941 amino acid protein that contains seven ANK repeats, three MORN repeats and one MYND-type zinc finger. MORN repeats were first identified in junctophilins, cytoplasmic proteins involved in junctions between the plasma membrane and the ER/SR membrane. The presence of MORN repeats suggests that ANKMY1 may interact with the plasma membrane. The MYND domain consists of a cluster of cysteine and histidine residues, arranged with an invariant spacing to form a potential zinc-binding motif which may be involved in protein-protein interactions. Three isoforms of ANKMY1 exists due to alternative splicing events.

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Ankyrins are membrane adaptor molecules that play important roles in coupling integral membrane proteins to the spectrin-based cytoskeleton network. Mutations of ankyrin genes lead to severe genetic diseases such as fatal cardiac arrhythmias and hereditary spherocytosis. ANKLE2 (ankyrin repeat and LEM domain containing 2), also known as LEMD7, is a 938 amino acid single-pass membrane protein containing an ANK repeat and a LEM domain. Exsiting as two isoforms produced by alternative splicing events, the gene encoding ANKLE2 maps to human chromosome 12, which encodes over 1,100 genes and comprises approximately 4.5% of the human genome. Chromosome 12 is associated with a variety of diseases and afflictions, including hypochondrogenesis, achondrogenesis, Kniest dysplasia, Noonan syndrome and trisomy 12p, which causes facial developmental defects and seizure disorders.

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Possible role in EGF receptor signaling.

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Voltage-gated K+ channels in the plasma membrane control the repolarization and the frequency of action potentials in neurons, muscles and other excitable cells. The KV gene family encodes more than 30 proteins that comprise the subunits of the K+ channels, and they vary in their gating and permeation properties, subcellular distribution and expression patterns. Functional KV channels assemble as tetramers consisting of pore-forming å subunits (KV), which include the KV1, KV2, KV3 and KV4 proteins, and accessory or KV-subunits that modify the gating properties of the coexpressed KV subunits. KV∫, also known as KCNAB1 (potassium voltage-gated channel, shaker-related subfamily, beta member 1), is a 419 amino acid accessory K+ channel protein that exists as three alternatively spliced isoforms and regulates the activity of the pore-forming å subunit. It is expressed in brain, with highest levels detected in caudate nucleus, hippocampus and thalamus.

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Voltage-gated K+ channels in the plasma membrane control the repolarization and the frequency of action potentials in neurons, muscles and other excitable cells. The KV gene family encodes more than 30 proteins that comprise the subunits of the K+ channels, and they vary in their gating and permeation properties, subcellular distribution and expression patterns. Functional KV channels assemble as tetramers consisting of pore-forming å subunits (KV), which include the KV1, KV2, KV3 and KV4 proteins, and accessory or KV-subunits that modify the gating properties of the coexpressed KV subunits. KV∫, also known as KCNAB1 (potassium voltage-gated channel, shaker-related subfamily, beta member 1), is a 419 amino acid accessory K+ channel protein that exists as three alternatively spliced isoforms and regulates the activity of the pore-forming å subunit. It is expressed in brain, with highest levels detected in caudate nucleus, hippocampus and thalamus.

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The tripartite motif (TRIM) family of proteins are characterized by a conserved TRIM domain that includes a coiled-coil region, a B-box type zinc finger, one RING finger and three zinc-binding domains. TRIM7 (tripartite motif-containing 7), also known as RNF90 or GNIP, is a 511 amino acid protein that belongs to the TRIM family and contains one RING-type zinc finger, one B box-type zinc finger and one SPRY domain. Expressed in placenta and skeletal muscle and present at lower levels in brain, heart and pancreas, TRIM7 localizes to both the cytoplasm and the nucleus where it exists as dimers and is thought to participate in the initiation of glycogen synthesis. Multiple isoforms of TRIM7 exist due to alternative splicing events.

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Tripartite motif-containing protein 3 (TRIM3), also known as RING finger protein 22 (RNF22), RING finger protein 97 (RNF97) or brain-expressed RING finger protein (BERP), is a 744 amino acid member of the TRIM family, also known as the RING-B-box coiled-coil (RBCC) family. Members of the RBCC family have an N-terminal RING finger, followed by one or two zinc-binding domains (B-box domains), a leucine coiled-coil region and a variable C-terminal domain. Localized to cytoplasmic filaments, TRIM3 has been shown to interact with å-actinin-4 and myosin V, two proteins associated with the actin cytoskeleton. Specifically, å-actinin-4 interacts with the RBCC domain of TRIM3, and the C-terminal tail of Myosin V interacts with with the unique C-terminal ∫-propeller domain of TRIM3. These associations suggest that TRIM3 may play a role in cell motility and cargo transport. Three named isoforms of TRIM3 exist as a result of alternative splicing events.

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SH3MD2 acts as a scaffold protein, contributes to Rac-induced signal transduction such as JNKs (MAPK8 and MAPK9) activation and induces apoptosis. Within a signaling complex, it probably recruits protein kinases such as MAP3K10 or MAP3K11 which are in turn activated leading to the sequential activation of MAP2K4, MAP2K7 and JNKs (MAPK8 and MAPK9). SH3MD2 may be involved in targeting of HIV-1 GAG and GAG-POL polyproteins to the plasma membrane. This gene encodes a protein containing an N-terminus RING-finger, four SH3 domains, and a region implicated in binding of the Rho GTPase Rac. Via the RING-finger, the encoded protein has been shown to function as an ubiquitin-protein ligase involved in protein sorting at the trans-Golgi network. The encoded protein may also act as a scaffold for the c-Jun N-terminal kinase signaling pathway, facilitating the formation of a functional signaling module. There are two named isoforms.

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Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses. Known ligands include EGF, TGFA/TGF-alpha, amphiregulin, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF. Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules. May also activate the NF-kappa-B signaling cascade. Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling. Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin. Isoform 2 may act as an antagonist of EGF action.

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RSK3(Ribosomal S6 kinase 3)is a member of a family of 90-kDa ribosomal protein S6 kinases, which includes Rsk1, Rsk2 and Rsk3. These are broadly expressed serine/threonine protein kinases that are activated in response to mitogenic stimuli, including extracellular signal-regulated protein kinases Erk1 and Erk2. Rsk3 is a distinct isoform of p90Rsk that translocates to the cell nucleus, phosphorylates potential nuclear targets and may have a unique upstream activator. Several sites, such as Ser380, Thr359, Ser363 and Thr573, are important for its activation. Active Rsks appear to play a major role in transcriptional regulation by translocating to the nucleus and phosphorylating c Fos and CREB.

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Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1. In fibroblast, is required for EGF-stimulated phosphorylation of CREB1, which results in the subsequent transcriptional activation of several immediate-early genes. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the preinitiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway. Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4).

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Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1. In fibroblast, is required for EGF-stimulated phosphorylation of CREB1, which results in the subsequent transcriptional activation of several immediate-early genes. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the preinitiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway. Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4).

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The RAF family of signaling proteins has three isoforms: A RAF, RAF 1 and B RAF. These proteins are instrumental in forwarding the stimulus generated by mitogens from monomeric G proteins to the MAP kinase pathway. RAF 1 is known to be downstream of Ras and binds to it by an N terminal noncatalytic domain. This domain is conserved in A RAF and B RAF. 14-3-3 is also known to be an activator of RAFs. Activated RAF directly phosphorylates and activates MEK. A RAF is expressed at a very high concentration in urogenital and kidney tissues.

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Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1. In fibroblast, is required for EGF-stimulated phosphorylation of CREB1 and histone H3 at 'Ser-10', which results in the subsequent transcriptional activation of several immediate-early genes. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the preinitiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway. Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4).

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Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1. In fibroblast, is required for EGF-stimulated phosphorylation of CREB1 and histone H3 at 'Ser-10', which results in the subsequent transcriptional activation of several immediate-early genes. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the preinitiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway. Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4).

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The protein encoded by this gene is a small GTPase of the Rho-subfamily, which regulates signaling pathways that control diverse cellular functions including cell morphology, migration, endocytosis and cell cycle progression. This protein is highly similar to Saccharomyces cerevisiae Cdc 42, and is able to complement the yeast cdc42-1 mutant. The product of oncogene Dbl was reported to specifically catalyze the dissociation of GDP from this protein. This protein could regulate actin polymerization through its direct binding to Neural Wiskott-Aldrich syndrome protein (N-WASP), which subsequently activates Arp2/3 complex. Alternative splicing of this gene results in multiple transcript variants. Pseudogenes of this gene have been identified on chromosomes 3, 4, 5, 7, 8 and 20. [provided by RefSeq, Apr 2013].

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mTOR controls cell growth, in part by regulating p70 S6 kinase alpha (p70alpha) and eukaryotic initiation factor 4E binding protein 1 (4EBP1). Raptor is a 150 kDa mTOR binding protein that also binds 4EBP1 and p70alpha. The binding of Raptor to mTOR is necessary for the mTOR-catalyzed phosphorylation of 4EBP1 in vitro, and it strongly enhances the mTOR kinase activity toward p70alpha. Rapamycin or amino acid withdrawal increases, whereas insulin strongly inhibits, the recovery of 4EBP1 and raptor on 7-methyl-GTP Sepharose. Partial inhibition of raptor expression by RNA interference (RNAi) reduces mTOR-catalyzed 4EBP1 phosphorylation in vitro. RNAi of C. elegans raptor yields an array of phenotypes that closely resemble those produced by inactivation of Ce-TOR. Thus, raptor is an essential scaffold for the mTOR-catalyzed phosphorylation of 4EBP1 and mediates TOR action in vivo.

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Nuclear MarkerRb is a tumor suppressor gene which functions as a negative regulator of the cell cycle by interacting with transcription factors including E2F1, PU1, ATF2, UBF, Elf1 and cAbl. This ability of Rb to alter transcription is regulated by phosphorylation catalyzed by the cyclin dependent protein kinases (cdks). Rb is phosphorylated on serine and threonine, but not on tyrosine residues. It forms a complex with SV40 large T antigen, adenovirus E1A, and human papilloma virus 16E. Rb protein may act by regulating transcription and loss of its function leads to uncontrolled cell growth. Aberrations in the Rb gene have been implicated in cancers of breast, colon, prostate, kidney, nasopharynx, and leukemia.

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Nuclear MarkerRb is a tumor suppressor gene which functions as a negative regulator of the cell cycle by interacting with transcription factors including E2F1, PU1, ATF2, UBF, Elf1 and cAbl. This ability of Rb to alter transcription is regulated by phosphorylation catalyzed by the cyclin dependent protein kinases (cdks). Rb is phosphorylated on serine and threonine, but not on tyrosine residues. It forms a complex with SV40 large T antigen, adenovirus E1A, and human papilloma virus 16E. Rb protein may act by regulating transcription and loss of its function leads to uncontrolled cell growth. Aberrations in the Rb gene have been implicated in cancers of breast, colon, prostate, kidney, nasopharynx, and leukemia.

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Rb is a tumor suppressor gene which functions as a negative regulator of the cell cycle by interacting with transcription factors including E2F1, PU1, ATF2, UBF, Elf1 and cAbl. This ability of Rb to alter transcription is regulated by phosphorylation catalyzed by the cyclin dependent protein kinases (cdks). Rb is phosphorylated on serine and threonine, but not on tyrosine residues. It forms a complex with SV40 large T antigen, adenovirus E1A, and human papilloma virus 16E. Rb protein may act by regulating transcription and loss of its function leads to uncontrolled cell growth. Aberrations in the Rb gene have been implicated in cancers of breast, colon, prostate, kidney, nasopharynx, and leukemia.