MAN2B1
entrez
4125
canonical
uniprot
O00754
canonical
ensembl
ENSG00000104774
resolver
ensp
ENSP00000221363
resolver
ensp
ENSP00000395473
resolver
ensp
ENSP00000528908
resolver
genesymbol
MAN2B1
resolver
genesymbol_syn
LAMAN
resolver
genesymbol_syn
MANB
resolver
hgnc
HGNC:6826
resolver
uniprot
A8K6A7
resolver
uniprot
G5E928
resolver
uniprot
O15330
resolver
uniprot
Q16680
resolver
uniprot
Q93094
resolver
uniprot
Q9BW13
resolver
uniprot_entry
A8K6A7_HUMAN
resolver
uniprot_entry
MA2B1_HUMAN
resolver
uniprot_sec
G5E928
resolver
uniprot_sec
O15330
resolver
uniprot_sec
Q16680
resolver
uniprot_sec
Q93094
resolver
uniprot_sec
Q9BW13
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by mannostatin A, swainsonine and swainsonine derivates. {ECO:0000269|PubMed:19722277, ECO:0000269|PubMed:8910458}.
uniprot
proteins
amino_acid_sequence
MGAYARASGVCARGCLDSAGPWTMSRALRPPLPPLCFFLLLLAAAGARAGGYETCPTVQPNMLNVHLLPHTHDDVGWLKTVDQYFYGIKNDIQHAGVQYILDSVISALLADPTRRFIYVEIAFFSRWWHQQTNATQEVVRDLVRQGRLEFANGGWVMNDEAATHYGAIVDQMTLGLRFLEDTFGNDGRPRVAWHIDPFGHSREQASLFAQMGFDGFFFGRLDYQDKWVRMQKLEMEQVWRASTSLKPPTADLFTGVLPNGYNPPRNLCWDVLCVDQPLVEDPRSPEYNAKELVDYFLNVATAQGRYYRTNHTVMTMGSDFQYENANMWFKNLDKLIRLVNAQQAKGSSVHVLYSTPACYLWELNKANLTWSVKHDDFFPYADGPHQFWTGYFSSRPALKRYERLSYNFLQVCNQLEALVGLAANVGPYGSGDSAPLNEAMAVLQHHDAVSGTSRQHVANDYARQLAAGWGPCEVLLSNALARLRGFKDHFTFCQQLNISICPLSQTAARFQVIVYNPLGRKVNWMVRLPVSEGVFVVKDPNGRTVPSDVVIFPSSDSQAHPPELLFSASLPALGFSTYSVAQVPRWKPQARAPQPIPRRSWSPALTIENEHIRATFDPDTGLLMEIMNMNQQLLLPVRQTFFWYNASIGDNESDQASGAYIFRPNQQKPLPVSRWAQIHLVKTPLVQEVHQNFSAWCSQVVRLYPGQRHLELEWSVGPIPVGDTWGKEVISRFDTPLETKGRFYTDSNGREILERRRDYRPTWKLNQTEPVAGNYYPVNTRIYITDGNMQLTVLTDRSQGGSSLRDGSLELMVHRRLLKDDGRGVSEPLMENGSGAWVRGRHLVLLDTAQAAAAGHRLLAEQEVLAPQVVLAPGGGAAYNLGAPPRTQFSGLRRDLPPSVHLLTLASWGPEMVLLRLEHQFAVGEDSGRNLSAPVTLNLRDLFSTFTITRLQETTLVANQLREAASRLKWTTNTGPTPHQTPYQLDPANITLEPMEIRTFLASVQWKEVDG
uniprot
proteins
disease_involvement
DISEASE: Mannosidosis, alpha B, lysosomal (MANSA) [MIM:248500]: A lysosomal storage disease characterized by accumulation of unbranched oligosaccharide chains. This accumulation is expressed histologically as cytoplasmic vacuolation predominantly in the CNS and parenchymatous organs. Depending on the clinical findings at the age of onset, a severe infantile (type I) and a mild juvenile (type II) form of alpha-mannosidosis are recognized. There is considerable variation in the clinical expression with intellectual disability, recurrent infections, impaired hearing and Hurler-like skeletal changes being the most consistent abnormalities. {ECO:0000269|PubMed:12718372, ECO:0000269|PubMed:15712269, ECO:0000269|PubMed:16919251, ECO:0000269|PubMed:17979865, ECO:0000269|PubMed:21505070, ECO:0000269|PubMed:22161967, ECO:0000269|PubMed:24353136, ECO:0000269|PubMed:26048034, ECO:0000269|PubMed:31241255, ECO:0000269|PubMed:36160623, ECO:0000269|PubMed:38243728, ECO:0000269|PubMed:38800253, ECO:0000269|PubMed:39280098, ECO:0000269|PubMed:9158146, ECO:0000269|PubMed:9758606, ECO:0000269|PubMed:9915946}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.2.1.24
uniprot
proteins
function
FUNCTION: Can hydrolyze a variety of glycan substrates containing terminal alpha-mannosidic linkages. Cleaves alpha 1,2-, alpha 1,3-, and alpha 1,6-linked mannose residues on oligosaccharides generated by N-glycoprotein degradation pathways. {ECO:0000269|PubMed:11350179, ECO:0000269|PubMed:16115860}.
uniprot
proteins
mass_dalton
113744
uniprot
proteins
post_translational_modification
PTM: First processed into 3 peptides of 70 kDa, 42 kDa (D) and 13/15 kDa (E). The 70 kDa peptide is further processed into three peptides (A, B and C). The A, B and C peptides are disulfide-linked. {ECO:0000269|PubMed:9158146}.; PTM: Heavily glycosylated. {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:8910458}.
uniprot
proteins
protein_family
Glycosyl hydrolase 38 family
uniprot
proteins
pubmed
11350179
uniprot
proteins
pubmed
12718372
uniprot
proteins
pubmed
12754519
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15712269
uniprot
proteins
pubmed
16115860
uniprot
proteins
pubmed
16919251
uniprot
proteins
pubmed
17979865
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19722277
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21505070
uniprot
proteins
pubmed
21645202
uniprot
proteins
pubmed
22161967
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24353136
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26048034
uniprot
proteins
pubmed
31241255
uniprot
proteins
pubmed
36160623
uniprot
proteins
pubmed
38243728
uniprot
proteins
pubmed
38800253
uniprot
proteins
pubmed
39280098
uniprot
proteins
pubmed
7832746
uniprot
proteins
pubmed
8166692
uniprot
proteins
pubmed
8910458
uniprot
proteins
pubmed
9158146
uniprot
proteins
pubmed
9192839
uniprot
proteins
pubmed
9758606
uniprot
proteins
pubmed
9915946
uniprot
proteins
sequence_length
1011
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome lumen {ECO:0000269|PubMed:21505070, ECO:0000269|PubMed:26048034}. Secreted {ECO:0000269|PubMed:11350179, ECO:0000269|PubMed:21505070}. Note=The protein may be secreted in an unprocessed but enzymatically active form (PubMed:11350179, PubMed:21505070). Secreted enzyme may enter cells via endocytosis (PubMed:11350179). {ECO:0000269|PubMed:11350179, ECO:0000269|PubMed:21505070}.
uniprot
proteins