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GORAB encodes a member of the golgin family, a group of coiled-coil proteins localized to the Golgi. Additionally we are shipping Golgin, RAB6-Interacting Antibodies (79) and Golgin, RAB6-Interacting Kits (4) and many more products for this protein.
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in the present study a de novo deletion on 1q23.3-q24.2 combined with a GORAB missense mutation leads to a distinctive phenotype with features from Gerodermia osteodysplastica and also short stature, cutis laxa, frequent fractures, facial dysmorphism, cup-shaped ears and intellectual disability
SCYL1- BP1 affects the cell cycle through increasing steady state levels of Cyclin F (show CCNF Proteins) and RRM2 (show RRM2 Proteins) proteins, thus constituting a dual regulatory circuit
rs17684886 (ZNRF1 (show ZNRF1 Proteins)) and rs599019 (COLEC12 (show COLEC12 Proteins)) are associated with diabetic retinopathy and rs6427247 (SCYL1BP1) and rs899036 (API5 (show API5 Proteins)) are associated with severe diabetic retinopathy in Chinese patients with type 2 diabetes
SCYL1-BP1 plays a critical role in the regulation of EEA1 (show EEA1 Proteins), BMPR2 (show BMPR2 Proteins) and BRCA2 (show BRCA2 Proteins) expression.
SCYL1BP1 can promote the degradation of MDM2 (show MDM2 Proteins) protein and further inhibit the G1/S transition of lung SCC (show CYP11A1 Proteins) lines. Reintroduction of SCYL1BP1 into lung SCC (show CYP11A1 Proteins) lines significantly inhibited cell proliferation, migration, invasion and tumor formation.
Data suggest that SCYL1-BP1 is a novel regulator of the MDM2 (show MDM2 Proteins)-p53 (show TP53 Proteins) feedback loop and that it may be a potential tumor suppressor.
The chemotaxis signal pathway induced by chemokines CKbeta8 (show CCL23 Proteins) and CKbeta8 (show CCL23 Proteins)-1 is mediated via the Gi/Go protein, phospholipase C (PLC (show PLC Proteins)) and protein kinase C delta (PKC delta (show PKCd Proteins)).
study supplements the limited available data on SCYL1BP1 and further establishes deficiency of this recently described golgin as the only known cause of geroderma osteodysplastica
assessment of interaction with hPirh2 (show RCHY1 Proteins)
Study demonstrates that gerodermia osteodysplastica is caused by loss-of-function mutations in SCYL1BP1, which is highly expressed in skin and osteoblasts.
The G59S mutation in p150(glued) protein abrogates the normal function of the protein and accelerates motor neuron degeneration.
This gene encodes a member of the golgin family, a group of coiled-coil proteins localized to the Golgi. The encoded protein may function in the secretory pathway. The encoded protein, which also localizes to the cytoplasm, was identified by interactions with the N-terminal kinase-like protein, and thus it may function in mitosis. Mutations in this gene have been associated with geroderma osteodysplastica. Alternatively spliced transcript variants have been described.
N-terminal kinase-like-binding protein 1
, NTKL-binding protein 1
, RAB6-interacting golgin
, SCY1-like 1 binding protein 1
, SCY1-like 1-binding protein 1
, SCYL1-binding protein 1
, dynactin 1, isoform 1; dynactin 1 (p150, Glued homolog); p150, Glued homolog; 150 kDa dynein-associated polypeptide; p150-glued