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JIP-4 is a 1,321 amino acid protein encoded by the human gene SPAG9. It contains a large N-terminal extracellular domain, a short transmembrane helical domain, and a cytoplasmic domain. There are 6 N-glycosylation sites, several phosphorylation sites for cAMP/cGMP-dependent protein kinase, protein kinase C, and casein kinase II, and 10 putative myristoylation sites. There is also a leucine zipper motif, with 6 leucine repeats, that may aid in dimerization since there is no upstream basic domain characteristic of DNA binding proteins. The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. JIP-4 is a cytoplasmic, perinuclear protein that has eight known isoforms whose expression varies by tissue and disease state.

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JIP-4 is a 1,321 amino acid protein encoded by the human gene SPAG9. It contains a large N-terminal extracellular domain, a short transmembrane helical domain, and a cytoplasmic domain. There are 6 N-glycosylation sites, several phosphorylation sites for cAMP/cGMP-dependent protein kinase, protein kinase C, and casein kinase II, and 10 putative myristoylation sites. There is also a leucine zipper motif, with 6 leucine repeats, that may aid in dimerization since there is no upstream basic domain characteristic of DNA binding proteins. The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. JIP-4 is a cytoplasmic, perinuclear protein that has eight known isoforms whose expression varies by tissue and disease state.

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Heterogeneous nuclear ribonucleoproteins (hnRNPs) are thought to be involved in pre-mRNA processing. However, its role in the regulation of gene expression is as yet poorly understood. Proteins of the heterogeneous nuclear ribonucleoparticles (hnRNP) family form a structurally diverse group of RNA binding proteins implicated in various functions. Recently, hnRNP proteins have been shown to hinder communication between factors bound to different splice sites. Conversely, several reports have described a positive role for some hnRNP proteins in pre-mRNA splicing. hnRNP-U, also termed scaffold attachment factor A (SAF-A), binds to pre-mRNA and nuclear matrix/scaffold attachment region DNA elements.

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This gene encodes a tumor suppressor protein containing transcriptional activation, DNA binding, and oligomerization domains. The encoded protein responds to diverse cellular stresses to regulate expression of target genes, thereby inducing cell cycle arrest, apoptosis, senescence, DNA repair, or changes in metabolism. Mutations in this gene are associated with a variety of human cancers, including hereditary cancers such as Li-Fraumeni syndrome. Alternative splicing of this gene and the use of alternate promoters result in multiple transcript variants and isoforms. Additional isoforms have also been shown to result from the use of alternate translation initiation codons (PMIDs: 12032546, 20937277). [provided by RefSeq, Feb 2013].

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The DnaJ family is one of the largest of all the chaperone families and has evolved with diverse cellular localization and functions. The presence of the J domain defines a protein as a member of the DnaJ family. DnaJ heat shock induced proteins are from the bacterium Escherichia coli and are under the control of the htpR regulatory protein. The DnaJ proteins play a critical role in the HSP 70 chaperone machine by interacting with HSP 70 to stimulate ATP hydrolysis. The proteins contain cysteine rich regions that are composed of zinc fingers that form a peptide binding domain responsible for the chaperone function. DnaJ proteins are important mediators of proteolysis and are involved in the regulation of protein degradation, exocytosis and endocytosis. DnaJA2 (DnaJ homolog subfamily A member 2), also known as HIRA-interacting protein 4 or cell cycle progression restoration gene 3 protein, contains one CR-type zinc finger and is a co-chaperone of HSC 70.

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The product of this gene belongs to the family of G-protein coupled receptors. This family has several receptor subtypes with different pharmacological selectivity, which overlaps in some cases, for various adenosine and uridine nucleotides. This receptor is responsive to uridine nucleotides, partially responsive to ATP, and not responsive to ADP. P2Y4 expression has been documented in blood, bone, heart, lung, pancreas, placenta, and umbilical cord.

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Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway. Somatomedin-B is a growth hormone-dependent serum factor with protease-inhibiting activity.

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This gene encodes a tumor suppressor protein containing transcriptional activation, DNA binding, and oligomerization domains. The encoded protein responds to diverse cellular stresses to regulate expression of target genes, thereby inducing cell cycle arrest, apoptosis, senescence, DNA repair, or changes in metabolism. Mutations in this gene are associated with a variety of human cancers, including hereditary cancers such as Li-Fraumeni syndrome. Alternative splicing of this gene and the use of alternate promoters result in multiple transcript variants and isoforms. Additional isoforms have also been shown to result from the use of alternate translation initiation codons (PMIDs: 12032546, 20937277). [provided by RefSeq, Feb 2013].

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Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodelling of blood vessels. Isoform short cleaves fibronectin and also collagen type III, but at lower rate. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells.

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Lymphotoxin beta-activated kinase which seems to be exclusively involved in the activation of NF-kappa-B and its transcriptional activity. Promotes proteolytic processing of NFKB2/P1, which leads to activation of NF-kappa-B via the non-canonical pathway. Could act in a receptor-selective manner.

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All members of the Src gene family of tyrosine kinases are characterized by a carboxy terminal domain tyrosine which is highly phosphorylated in the inactive form of the enzyme and phosphorylated to a much lesser extent when the enzyme is active. In the case of Src p60, Y527 is this tyrosine; however, a mutant form of c-Src in which Y527 is replaced by phenylalanine is transforming and displays 5- to 10-fold elevated kinase activity compared to its normal counterpart. Csk has been identified as a Src-related tyrosine kinase having both SH2 and SH3 domains and a catalytic domain but lacking sequences amino terminal to the SH3 domain as well as carboxy terminal regulatory sequences. Csk phosphorylates Src on Y527 and also downregulates Lyn, Fyn and Lck by tyrosine phosphorylation of carboxy terminal regulatory sites.

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Tumor suppressor serine/threonine-protein kinase involved in mTORC1 signaling and post-transcriptional regulation. Phosphorylates FOXO3, ERK3/MAPK6, ERK4/MAPK4, HSP27/HSPB1, p53/TP53 and RHEB. Acts as a tumor suppressor by mediating Ras-induced senescence and phosphorylating p53/TP53. Involved in post-transcriptional regulation of MYC by mediating phosphorylation of FOXO3: phosphorylation of FOXO3 leads to promote nuclear localization of FOXO3, enabling expression of miR-34b and miR-34c, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent MYC translation. Acts as a negative regulator of mTORC1 signaling by mediating phosphorylation and inhibition of RHEB. Part of the atypical MAPK signaling via its interaction with ERK3/MAPK6 or ERK4/MAPK4: the precise role of the complex formed with ERK3/MAPK6 or ERK4/MAPK4 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPK (ERK3/MAPK6 or ERK4/MAPK4), ERK3/MAPK6 (or ERK4/MAPK4) is phosphorylated and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK3/MAPK6 (or ERK4/MAPK4). Mediates phosphorylation of HSP27/HSPB1 in response to PKA/PRKACA stimulation, inducing F-actin rearrangement.

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MEF2D is a member of the myocyte-specific enhancer factor 2 (MEF2) family of transcription factors. Members of this family are involved in control of muscle and neuronal cell differentiation and development, and are regulated by class II histone deacetylases. Fusions of the encoded protein with Deleted in Azoospermia-Associated Protein 1 (DAZAP1) due to a translocation have been found in an acute lymphoblastic leukemia cell line, suggesting a role in leukemogenesis. The encoded protein may also be involved in Parkinson disease and myotonic dystrophy. Alternative splicing results in multiple transcript variants.

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MEF2D is a member of the myocyte-specific enhancer factor 2 (MEF2) family of transcription factors. Members of this family are involved in control of muscle and neuronal cell differentiation and development, and are regulated by class II histone deacetylases. Fusions of the encoded protein with Deleted in Azoospermia-Associated Protein 1 (DAZAP1) due to a translocation have been found in an acute lymphoblastic leukemia cell line, suggesting a role in leukemogenesis. The encoded protein may also be involved in Parkinson disease and myotonic dystrophy. Alternative splicing results in multiple transcript variants.

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The catenins are ubiquitously expressed, cytoplasmic proteins that associate with E-cadherin at cellular junctions. Catenin/cadherin complexes play an important role in mediating cellular adhesion. alpha T-catenin, also referred to as VR22, is a 895-amino acid protein that is most abundantally expressed in cardiomyocytes and in the peritubular myoid cells of the testis. alpha T-catenin binds to alpha E-catenin as well as to beta-catenin, and it functions to inhibit Wnt signaling. CTNNA3, the gene that encodes for alpha-T-catenin, is located on chromosome 10, and mutations in this gene show a strong correlation to late-onset Alzheimer's disease (LOAD) as well as to dilated cardiomyopathy.

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STAC2

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STAC2

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The catenins are ubiquitously expressed, cytoplasmic proteins that associate with E-cadherin at cellular junctions. Catenin/cadherin complexes play an important role in mediating cellular adhesion. alpha T-catenin, also referred to as VR22, is a 895-amino acid protein that is most abundantally expressed in cardiomyocytes and in the peritubular myoid cells of the testis. alpha T-catenin binds to alpha E-catenin as well as to beta-catenin, and it functions to inhibit Wnt signaling. CTNNA3, the gene that encodes for alpha-T-catenin, is located on chromosome 10, and mutations in this gene show a strong correlation to late-onset Alzheimer's disease (LOAD) as well as to dilated cardiomyopathy.

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Heterotrimeric G protein-coupled receptor for endocannabinoid 2-arachidonoylglycerol mediating inhibition of adenylate cyclase. May function in inflammatory response, nociceptive transmission and bone homeostasis.

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STAC2

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Heterotrimeric G protein-coupled receptor for endocannabinoid 2-arachidonoylglycerol mediating inhibition of adenylate cyclase. May function in inflammatory response, nociceptive transmission and bone homeostasis.

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Heterotrimeric G protein-coupled receptor for endocannabinoid 2-arachidonoylglycerol mediating inhibition of adenylate cyclase. May function in inflammatory response, nociceptive transmission and bone homeostasis.

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Receptor for the cytotoxic ligand TNFSF10/TRAIL. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Promotes the activation of NF-kappa-B.

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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.

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URG4 may be involved in cell cycle progression through the regulation of cyclin D1 expression. It may participate in the development of hepatocellular carcinoma (HCC) by promoting hepatocellular growth and survival. URG4 may play an important role in development of gastric cancer.

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This gene product is highly similar to Schizosaccharomyces pombe rad9, a cell cycle checkpoint protein required for cell cycle arrest and DNA damage repair in response to DNA damage. This protein is found to possess 3' to 5' exonuclease activity, which may contribute to its role in sensing and repairing DNA damage. It forms a checkpoint protein complex with RAD1 and HUS1. This complex is recruited by checkpoint protein RAD17 to the sites of DNA damage, which is thought to be important for triggering the checkpoint-signaling cascade. Use of alternative polyA sites has been noted for this gene. [provided by RefSeq].

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Neurobeachin binds to type II regulatory subunits of protein kinase A and anchors/targets them to the membrane. It may anchor the kinase to cytoskeletal and/or organelle-associated proteins. Neurobeachin, is also a neuron-specific multidomain protein of 327 kDa with a high-affinity binding site for the type II regulatory subunit of protein kinase A. Neurobeachin is peripherally associated with pleomorphic tubulovesicular endomembranes near the trans sides of Golgi stacks and throughout the cell body and cell processes. It is also found in a subpopulation of synapses, where it is concentrated at the postsynaptic plasma membrane.

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Binds to activated CDC42 but does not stimulate its GTPase activity. It associates with calmodulin. Could serve as an assembly scaffold for the organization of a multimolecular complex that would interface incoming signals to the reorganization of the actin cytoskeleton at the plasma membrane. May promote neurite outgrowth.

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Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to hepatocyte growth factor/HGF ligand. Regulates many physiological processes including proliferation, scattering, morphogenesis and survival. Ligand binding at the cell surface induces autophosphorylation of MET on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3 or the adapter GAB1. Recruitment of these downstream effectors by MET leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. The RAS-ERK activation is associated with the morphogenetic effects while PI3K/AKT coordinates prosurvival effects. During embryonic development, MET signaling plays a role in gastrulation, development and migration of muscles and neuronal precursors, angiogenesis and kidney formation. In adults, participates in wound healing as well as organ regeneration and tissue remodeling. Promotes also differentiation and proliferation of hematopoietic cells. Acts as a receptor for Listeria internalin inlB, mediating entry of the pathogen into cells.

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Chromosome 1 is the largest human chromosome spanning about 260 million base pairs and making up 8% of the human genome. There are about 3,000 genes on chromosome 1, and considering the great number of genes there are also a large number of diseases associated with chromosome 1. Notably, the rare aging disease Hutchinson-Gilford progeria is associated with the LMNA gene which encodes lamin A. When defective, the LMNA gene product can build up in the nucleus and cause characteristic nuclear blebs. The mechanism of rapidly enhanced aging is unclear and is a topic of continuing exploration. The MUTYH gene is located on chromosome 1 and is partially responsible for familial adenomatous polyposis. Stickler syndrome, Parkinsons, Gaucher disease and Usher syndrome are also associated with chromosome 1. A breakpoint has been identified in 1q which disrupts the DISC1 gene and is linked to schizophrenia. Aberrations in chromosome 1 are found in a variety of cancers including head and neck cancer, malignant melanoma and multiple myeloma. The C1orf190 gene product has been provisionally designated C1orf190 pending further characterization.