Human Gene COG8 (uc002ewy.2) Description and Page Index
Description: Homo sapiens component of oligomeric golgi complex 8 (COG8), mRNA. RefSeq Summary (NM_032382): This gene encodes a protein that is a component of the conserved oligomeric Golgi (COG) complex, a multiprotein complex that plays a structural role in the Golgi apparatus, and is involved in intracellular membrane trafficking and glycoprotein modification. Mutations in this gene cause congenital disorder of glycosylation, type IIh, a disease that is characterized by under-glycosylated serum proteins, and whose symptoms include severe psychomotor retardation, failure to thrive, seizures, and dairy and wheat product intolerance. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK056344.1, SRR1803613.108920.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Transcript (Including UTRs) Position: hg19 chr16:69,362,524-69,373,526 Size: 11,003 Total Exon Count: 6 Strand: - Coding Region Position: hg19 chr16:69,364,742-69,373,455 Size: 8,714 Coding Exon Count: 5
ID:COG8_HUMAN DESCRIPTION: RecName: Full=Conserved oligomeric Golgi complex subunit 8; Short=COG complex subunit 8; AltName: Full=Component of oligomeric Golgi complex 8; FUNCTION: Required for normal Golgi function (By similarity). SUBUNIT: Component of the conserved oligomeric Golgi complex which is composed of eight different subunits and is required for normal Golgi morphology and localization. SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein. DISEASE: Defects in COG8 are the cause of congenital disorder of glycosylation type 2H (CDG2H) [MIM:611182]. CDGs are a family of severe inherited diseases caused by a defect in protein N- glycosylation. They are characterized by under-glycosylated serum proteins. These multisystem disorders present with a wide variety of clinical features, such as disorders of the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions. SIMILARITY: Belongs to the COG8 family. SEQUENCE CAUTION: Sequence=AAH17492.1; Type=Erroneous initiation; Sequence=BAB15301.1; Type=Frameshift; Positions=371;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q96MW5
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.