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This gene is a member of the immunoglobulin superfamily and encodes a protein which transmits an inhibitory signal to T cells. The protein contains a V domain, a transmembrane domain, and a cytoplasmic tail. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. The membrane-bound isoform functions as a homodimer interconnected by a disulfide bond, while the soluble isoform functions as a monomer. Mutations in this gene have been associated with insul

KIF7 is a 1,343 amino acid protein expressed in embryonic stem cells, melanotic melanoma and Jurkat T-cells. KIF7 is a member of the KIF27 subfamily of the kinesin-like protein family and contains one kinesin-motor domain. It is suggested that KIF7 may participate in the Hedgehog (Hh) signaling pathway by regulating the proteolysis and stability of GLI transcription factors. Hedgehog (Hh) signaling plays a critical role in embryonic development.

Collagens are highly conserved throughout evolution and are characterised by an uninterrupted “Glycine X Y“ triplet repeat that is a necessary part of the triple helical structure. Type I collagen (95 kDa) is found in bone, cornea, skin and tendon. Mutations in the encoding gene are associated with osteogenesis imperfecta, Ehlers Danlos syndrome, and idiopathic osteoporosis. Reciprocal translocations between chromosomes 17 and 22, where this gene and the gene for Platelet-derived growth

Collagens are highly conserved throughout evolution and are characterised by an uninterrupted “Glycine X Y“ triplet repeat that is a necessary part of the triple helical structure. Type I collagen (95 kDa) is found in bone, cornea, skin and tendon. Mutations in the encoding gene are associated with osteogenesis imperfecta, Ehlers Danlos syndrome, and idiopathic osteoporosis. Reciprocal translocations between chromosomes 17 and 22, where this gene and the gene for Platelet-derived growth

Collagens are highly conserved throughout evolution and are characterised by an uninterrupted “Glycine X Y“ triplet repeat that is a necessary part of the triple helical structure. Type I collagen (95 kDa) is found in bone, cornea, skin and tendon. Mutations in the encoding gene are associated with osteogenesis imperfecta, Ehlers Danlos syndrome, and idiopathic osteoporosis. Reciprocal translocations between chromosomes 17 and 22, where this gene and the gene for Platelet-derived growth

Collagens are highly conserved throughout evolution and are characterised by an uninterrupted “Glycine X Y“ triplet repeat that is a necessary part of the triple helical structure. Type I collagen (95 kDa) is found in bone, cornea, skin and tendon. Mutations in the encoding gene are associated with osteogenesis imperfecta, Ehlers Danlos syndrome, and idiopathic osteoporosis. Reciprocal translocations between chromosomes 17 and 22, where this gene and the gene for Platelet-derived growth