GNPTAB
entrez
79158
canonical
uniprot
Q3T906
canonical
ensembl
ENSG00000111670
resolver
ensp
ENSP00000299314
resolver
ensp
ENSP00000786188
resolver
genesymbol
GNPTAB
resolver
genesymbol_syn
GNPTA
resolver
genesymbol_syn
KIAA1208
resolver
hgnc
HGNC:29670
resolver
uniprot
A2RRQ9
resolver
uniprot
Q3ZQK2
resolver
uniprot
Q6IPW5
resolver
uniprot
Q86TQ2
resolver
uniprot
Q96N13
resolver
uniprot
Q9ULL2
resolver
uniprot_entry
GNPTA_HUMAN
resolver
uniprot_sec
A2RRQ9
resolver
uniprot_sec
Q3ZQK2
resolver
uniprot_sec
Q6IPW5
resolver
uniprot_sec
Q86TQ2
resolver
uniprot_sec
Q96N13
resolver
uniprot_sec
Q9ULL2
resolver
amino_acid_sequence
MLFKLLQRQTYTCLSHRYGLYVCFLGVVVTIVSAFQFGEVVLEWSRDQYHVLFDSYRDNIAGKSFQNRLCLPMPIDVVYTWVNGTDLELLKELQQVREQMEEEQKAMREILGKNTTEPTKKSEKQLECLLTHCIKVPMLVLDPALPANITLKDLPSLYPSFHSASDIFNVAKPKNPSTNVSVVVFDSTKDVEDAHSGLLKGNSRQTVWRGYLTTDKEVPGLVLMQDLAFLSGFPPTFKETNQLKTKLPENLSSKVKLLQLYSEASVALLKLNNPKDFQELNKQTKKNMTIDGKELTISPAYLLWDLSAISQSKQDEDISASRFEDNEELRYSLRSIERHAPWVRNIFIVTNGQIPSWLNLDNPRVTIVTHQDVFRNLSHLPTFSSPAIESHIHRIEGLSQKFIYLNDDVMFGKDVWPDDFYSHSKGQKVYLTWPVPNCAEGCPGSWIKDGYCDKACNNSACDWDGGDCSGNSGGSRYIAGGGGTGSIGVGQPWQFGGGINSVSYCNQGCANSWLADKFCDQACNVLSCGFDAGDCGQDHFHELYKVILLPNQTHYIIPKGECLPYFSFAEVAKRGVEGAYSDNPIIRHASIANKWKTIHLIMHSGMNATTIHFNLTFQNTNDEEFKMQITVEVDTREGPKLNSTAQKGYENLVSPITLLPEAEILFEDIPKEKRFPKFKRHDVNSTRRAQEEVKIPLVNISLLPKDAQLSLNTLDLQLEHGDITLKGYNLSKSALLRSFLMNSQHAKIKNQAIITDETNDSLVAPQEKQVHKSILPNSLGVSERLQRLTFPAVSVKVNGHDQGQNPPLDLETTARFRVETHTQKTIGGNVTKEKPPSLIVPLESQMTKEKKITGKEKENSRMEENAENHIGVTEVLLGRKLQHYTDSYLGFLPWEKKKYFQDLLDEEESLKTQLAYFTDSKNTGRQLKDTFADSLRYVNKILNSKFGFTSRKVPAHMPHMIDRIVMQELQDMFPEEFDKTSFHKVRHSEDMQFAFSYFYYLMSAVQPLNISQVFDEVDTDQSGVLSDREIRTLATRIHELPLSLQDLTGLEHMLINCSKMLPADITQLNNIPPTQESYYDPNLPPVTKSLVTNCKPVTDKIHKAYKDKNKYRFEIMGEEEIAFKMIRTNVSHVVGQLDDIRKNPRKFVCLNDNIDHNHKDAQTVKAVLRDFYESMFPIPSQFELPREYRNRFLHMHELQEWRAYRDKLKFWTHCVLATLIMFTIFSFFAEQLIALKRKIFPRRRIHKEASPNRIRV
uniprot
proteins
disease_involvement
DISEASE: Mucolipidosis type II (MLII) [MIM:252500]: Fatal, autosomal recessive, lysosomal storage disorder characterized by severe clinical and radiologic features, peculiar fibroblast inclusions, and no excessive mucopolysacchariduria. Congenital dislocation of the hip, thoracic deformities, hernia, and hyperplastic gums are evident soon after birth. {ECO:0000269|PubMed:16200072, ECO:0000269|PubMed:16835905, ECO:0000269|PubMed:19197337, ECO:0000269|PubMed:19617216, ECO:0000269|PubMed:19634183, ECO:0000269|PubMed:19938078, ECO:0000269|PubMed:22495880, ECO:0000269|PubMed:23566849, ECO:0000269|PubMed:23733939, ECO:0000269|PubMed:23773965, ECO:0000269|PubMed:24375680, ECO:0000269|PubMed:24798265, ECO:0000269|PubMed:25505245, ECO:0000269|PubMed:25788519, ECO:0000269|PubMed:28918368}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Mucolipidosis type III complementation group A (MLIIIA) [MIM:252600]: Autosomal recessive disease of lysosomal enzyme targeting. Clinically MLIII is characterized by restricted joint mobility, skeletal dysplasia, and short stature. Mildly coarsened facial features and thickening of the skin have been described. Cardiac valvular disease and corneal clouding may also occur. Half of the reported patients show learning disabilities or intellectual disability. {ECO:0000269|PubMed:16094673, ECO:0000269|PubMed:16465621, ECO:0000269|PubMed:16630736, ECO:0000269|PubMed:17034777, ECO:0000269|PubMed:19197337, ECO:0000269|PubMed:19617216, ECO:0000269|PubMed:19634183, ECO:0000269|PubMed:19938078, ECO:0000269|PubMed:23566849, ECO:0000269|PubMed:24045841, ECO:0000269|PubMed:24375680, ECO:0000269|PubMed:24550498, ECO:0000269|PubMed:25505245, ECO:0000269|PubMed:25788519, ECO:0000269|PubMed:28918368}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Note=Genetic variations in GNPTAB have been suggested to play a role in susceptibility to persistent stuttering. Stuttering is a common speech disorder characterized by repetitions, prolongations, and interruptions in the flow of speech. {ECO:0000269|PubMed:20147709}.
uniprot
proteins
ec_number
2.7.8.17
uniprot
proteins
function
FUNCTION: Catalyzes the formation of mannose 6-phosphate (M6P) markers on high mannose type oligosaccharides in the Golgi apparatus. M6P residues are required to bind to the M6P receptors (MPR), which mediate the vesicular transport of lysosomal enzymes to the endosomal/prelysosomal compartment. {ECO:0000269|PubMed:19955174, ECO:0000269|PubMed:23733939, ECO:0000269|PubMed:28918368}.
uniprot
proteins
mass_dalton
143622
uniprot
proteins
mutagenesis
MUTAGEN 346; /note="I->A: Partially cleaved by MBTPS1."; /evidence="ECO:0000269|PubMed:25788519"; MUTAGEN 357; /note="W->A: Abolishes proteolytic cleavage by MBTPS1."; /evidence="ECO:0000269|PubMed:25788519"; MUTAGEN 925; /note="R->A: Abolishes proteolytic cleavage by MBTPS1."; /evidence="ECO:0000269|PubMed:21719679"; MUTAGEN 927; /note="L->A: Abolishes proteolytic cleavage by MBTPS1."; /evidence="ECO:0000269|PubMed:21719679"; MUTAGEN 928; /note="K->A: Abolishes proteolytic cleavage by MBTPS1."; /evidence="ECO:0000269|PubMed:21719679
uniprot
proteins
post_translational_modification
PTM: The alpha- and beta-subunits are generated by a proteolytic cleavage by MBTPS1 protease at the Lys-928-Asp-929 bond. {ECO:0000269|PubMed:21719679, ECO:0000269|PubMed:24375680, ECO:0000269|PubMed:25788519, ECO:0000269|PubMed:28918368}.
uniprot
proteins
protein_family
Stealth family
uniprot
proteins
pubmed
10574462
uniprot
proteins
pubmed
12168954
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16094673
uniprot
proteins
pubmed
16120602
uniprot
proteins
pubmed
16200072
uniprot
proteins
pubmed
16299590
uniprot
proteins
pubmed
16465621
uniprot
proteins
pubmed
16630736
uniprot
proteins
pubmed
16835905
uniprot
proteins
pubmed
17034777
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19197337
uniprot
proteins
pubmed
19617216
uniprot
proteins
pubmed
19634183
uniprot
proteins
pubmed
19938078
uniprot
proteins
pubmed
19955174
uniprot
proteins
pubmed
20147709
uniprot
proteins
pubmed
21719679
uniprot
proteins
pubmed
22495880
uniprot
proteins
pubmed
23566849
uniprot
proteins
pubmed
23733939
uniprot
proteins
pubmed
23773965
uniprot
proteins
pubmed
24045841
uniprot
proteins
pubmed
24375680
uniprot
proteins
pubmed
24550498
uniprot
proteins
pubmed
24767253
uniprot
proteins
pubmed
24798265
uniprot
proteins
pubmed
25505245
uniprot
proteins
pubmed
25788519
uniprot
proteins
pubmed
27535533
uniprot
proteins
pubmed
28918368
uniprot
proteins
pubmed
36074821
uniprot
proteins
sequence_length
1256
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [N-acetylglucosamine-1-phosphotransferase subunit alpha]: Golgi apparatus membrane {ECO:0000269|PubMed:16120602, ECO:0000269|PubMed:16200072, ECO:0000269|PubMed:21719679, ECO:0000269|PubMed:23733939, ECO:0000269|PubMed:24375680, ECO:0000269|PubMed:25788519, ECO:0000269|PubMed:28918368}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [N-acetylglucosamine-1-phosphotransferase subunit beta]: Golgi apparatus membrane {ECO:0000269|PubMed:16120602, ECO:0000269|PubMed:16200072, ECO:0000269|PubMed:21719679, ECO:0000269|PubMed:23733939, ECO:0000269|PubMed:24375680, ECO:0000269|PubMed:28918368}; Single-pass type II membrane protein {ECO:0000305}.
uniprot
proteins
transmembrane_region
TRANSMEM 22..42; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1215..1235; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins