Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Identification, expression, and characterization of a cDNA encoding human endoplasmic reticulum mannosidase I, the enzyme that catalyzes the first mannose trimming step in mammalian Asn-linked oligosaccharide biosynthesis.
Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis.
The specificity of the yeast and human class I ER alpha 1,2-mannosidases involved in ER quality control is not as strict previously reported.
Mechanism of class 1 (glycosylhydrolase family 47) alpha-mannosidases involved in N-glycan processing and endoplasmic reticulum quality control.
Endoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradation.
Defining the membrane proteome of NK cells.
Mannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation steps.
In vitro mannose trimming property of human ER alpha-1,2 mannosidase I.
Proteomic analysis of cerebrospinal fluid extracellular vesicles: a comprehensive dataset.
The cytoplasmic tail of human mannosidase Man1b1 contributes to catalysis-independent quality control of misfolded alpha1-antitrypsin.
-
Beyond its luminal catalytic alpha-1,2-mannosidase activity, MAN1B1/ERManI contributes to ERAD of misfolded glycoproteins (NHK and Z variants of alpha1-antitrypsin) through an unconventional, catalysis-independent pathway controlled by its evolutionarily extended N-terminal cytoplasmic tail; this tail-dependent degradation does not require the substrate's N-glycans and drives proteasomal degradation.
Mammalian ER mannosidase I resides in quality control vesicles, where it encounters its glycoprotein substrates.
Defective MAN1B1 does not hydrolyse 1,2-linked mannose (a branch)
MAN1B1 hydrolyses 1,2-linked mannose (a branch)
ER Quality Control Compartment (ERQC)
MAN1B1 hydrolyses a second 1,2-linked mannose (a branch)
MAN1B1 hydrolyses 1,2-linked mannose (c branch)
MAN1B1,EDEM2 hydrolyse 1,2-linked mannose (b branch)
Defective MAN1B1 does not hydrolyse a second 1,2-linked mannose (a branch)
Defective MAN1B1 does not hydrolyse 1,2-linked mannose (b branch)
Defective MAN1B1 does not hydrolyse 1,2-linked mannose (c branch)
Maturation of spike protein
N-glycan mannose trimming of Spike
UniProt entry Q9UKM7 (MA1B1_HUMAN), Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
-
Calcium-dependent GH47 alpha-1,2-mannosidase (EC 3.2.1.113) of the ER membrane (type II single-pass) that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B and, at high concentration, to Man5-6GlcNAc2, targeting misfolded glycoproteins for ERAD; biallelic variants cause Rafiq syndrome/MAN1B1-CDG.