Gene Report
Basic Info
Approved Symbol |
MAN1A1
|
Approved Name |
mannosidase, alpha, class 1A, member 1 |
Location |
6q22 |
Position |
chr6:119498374-119670926, - |
External Links |
HGNC: 6821
Entrez Gene: 4121
Ensembl: ENSG00000111885
UCSC: uc003pym.1
|
No. of Studies |
0 (significant: 0; non-significant: 0; trend: 0) |
Source |
Mapped by significant region |
Gene related studies (count: 0)
Gene related SNPs (count: 0)
Gene related CNVs (count: 0)
Gene related other variant (count: 0)
Gene related regions (count: 1)
Gene related GO terms (count: 11)
Gene related KEGG pathways (count: 3)
ID |
Name |
No. of Genes in ADHDgene |
Brief Description |
hsa00510 |
N-Glycan biosynthesis |
11 |
N-glycans or asparagine-linked glycans are major constituent......
N-glycans or asparagine-linked glycans are major constituents of glycoproteins in eukaryotes. N-glycans are covalently attached to asparagine with the consensus sequence of Asn-X-Ser/Thr by an N-glycosidic bond, GlcNAc b1- Asn. Biosynthesis of N-glycans begins on the cytoplasmic face of the ER membrane with the transferase reaction of UDP-GlcNAc and the lipid-like precursor P-Dol (dolichol phosphate) to generate GlcNAc a1- PP-Dol. After sequential addition of monosaccharides by ALG glycosyltransferases [MD:M00055], the N-glycan precursor is attached by the OST (oligosaccharyltransferase) complex to the polypeptide chain that is being synthesized and translocated through the ER membrane. The protein-bound N-glycan precursor is subsequently trimmed, extended, and modified in the ER and Golgi by a complex series of reactions catalyzed by membrane-bound glycosidases and glycosyltransferases. N-glycans thus synthesized are classified into three types: high-mannose type, complex type, and hybrid type. Defects in N-glycan biosynthesis lead to a variety of human diseases known as congenital disorders of glycosylation [DS:H00118 H00119].
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|
hsa01100 |
Metabolic pathways |
237 |
|
hsa04141 |
Protein processing in endoplasmic reticulum |
26 |
The endoplasmic reticulum (ER) is a subcellular organelle wh......
The endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylated. Correctly folded proteins are packaged into transport vesicles that shuttle them to the Golgi complex. Misfolded proteins are retained within the ER lumen in complex with molecular chaperones. Proteins that are terminally misfolded bind to BiP and are directed toward degradation through the proteasome in a process called ER-associated degradation (ERAD). Accumulation of misfolded proteins in the ER causes ER stress and activates a signaling pathway called the unfolded protein response (UPR). In certain severe situations, however, the protective mechanisms activated by the UPR are not sufficient to restore normal ER function and cells die by apoptosis.
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|
Genes shared at least 5 GO terms with MAN1A1 (count: 13)
Genes shared at least 2 KEGG pathways with MAN1A1 (count: 10)
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