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The four human glycoprotein hormones chorionic gonadotropin (CG), luteinizing hormone (LH), follicle stimulating hormone (FSH), and thyroid stimulating hormone (TSH) are dimers consisting of alpha and beta subunits that are associated noncovalently. The alpha subunits of these hormones are identical, however, their beta chains are unique and confer biological specificity. Thyroid stimulating hormone functions in the control of thyroid structure and metabolism. The protein encoded by this ge

The protein encoded by this gene is a 36-kD water-soluble protein which carries 11-cis-retinaldehyde or 11-cis-retinal as physiologic ligands. It may be a functional component of the visual cycle. Mutations of this gene have been associated with severe rod-cone dystrophy, Bothnia dystrophy (nonsyndromic autosomal recessive retinitis pigmentosa) and retinitis punctata albescens. [provided by RefSeq, Jul 2008]

PTBP-2 is a member of the polypyrimidine tract binding family of proteins. Predominantly expressed in brain, but also found in heart and skeletal muscle, PTBP-2 localizes to the nucleus and contains four RRM (RNA recognition motif) domains. PTBP-2 functions as an RNA-binding protein associated in a complex that is involved in the regulation of exon splicing and the stabilization of mRNAs in the cytoplasm. Six isoforms exist for PTBP-2 due to alternative splicing events. Isoforms 1 and 2 (al

Luteinizing Hormone is a member of the glycoprotein hormone family. Glycoprotein hormones are heterodimers consisting of a common alpha subunit and an unique beta subunit which confers biological specificity. LH is expressed in the pituitary gland and promotes spermatogenesis and ovulation by stimulating the testes and ovaries to synthesize steroids. Mutations in the Luteinizing Hormone (LHB) gene are associated with hypogonadism which is characterized by infertility and pseudohermaphrodit

The product of this gene phosphorylates the beta-2-adrenergic receptor and appears to mediate agonist-specific desensitization observed at high agonist concentrations. This protein is an ubiquitous cytosolic enzyme that specifically phosphorylates the activated form of the beta-adrenergic and related G-protein-coupled receptors. Abnormal coupling of beta-adrenergic receptor to G protein is involved in the pathogenesis of the failing heart. [provided by RefSeq].

Hip (HSP70-interacting protein), also known as ST13 (suppression of tumorigenicity protein 13), is one of several co-chaperones that regulate activities of the HSP70 chaperone family (1,2). The homo-oligomeric protein Hip cooperates with HSP70 in protein folding by stabilizing the ADP-bound state of HSP70. Hip directly binds to the ATPase domain of HSP70 when it is converted to the ADP-bound state by proteins of the HSP40 family (3). By collaborating with other positive co-factors such as HSP40