OGA
entrez
10724
canonical
uniprot
O60502
canonical
ensembl
ENSG00000198408
resolver
ensp
ENSP00000354850
resolver
ensp
ENSP00000409973
resolver
ensp
ENSP00000553255
resolver
ensp
ENSP00000736563
resolver
genesymbol
OGA
resolver
genesymbol_syn
HEXC
resolver
genesymbol_syn
KIAA0679
resolver
genesymbol_syn
MEA5
resolver
genesymbol_syn
MGEA5
resolver
hgnc
HGNC:7056
resolver
uniprot
B7WPB9
resolver
uniprot
D3DR79
resolver
uniprot
E9PGF9
resolver
uniprot
O75166
resolver
uniprot
Q86WV0
resolver
uniprot
Q8IV98
resolver
uniprot
Q9BVA5
resolver
uniprot
Q9HAR0
resolver
uniprot_entry
OGA_HUMAN
resolver
uniprot_sec
B7WPB9
resolver
uniprot_sec
D3DR79
resolver
uniprot_sec
E9PGF9
resolver
uniprot_sec
O75166
resolver
uniprot_sec
Q86WV0
resolver
uniprot_sec
Q8IV98
resolver
uniprot_sec
Q9BVA5
resolver
uniprot_sec
Q9HAR0
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by N-acetylglucosamine and not N-acetylgalactosamine. {ECO:0000269|PubMed:11148210}.
uniprot
proteins
amino_acid_sequence
MVQKESQATLEERESELSSNPAASAGASLEPPAAPAPGEDNPAGAGGAAVAGAAGGARRFLCGVVEGFYGRPWVMEQRKELFRRLQKWELNTYLYAPKDDYKHRMFWREMYSVEEAEQLMTLISAAREYEIEFIYAISPGLDITFSNPKEVSTLKRKLDQVSQFGCRSFALLFDDIDHNMCAADKEVFSSFAHAQVSITNEIYQYLGEPETFLFCPTEYCGTFCYPNVSQSPYLRTVGEKLLPGIEVLWTGPKVVSKEIPVESIEEVSKIIKRAPVIWDNIHANDYDQKRLFLGPYKGRSTELIPRLKGVLTNPNCEFEANYVAIHTLATWYKSNMNGVRKDVVMTDSEDSTVSIQIKLENEGSDEDIETDVLYSPQMALKLALTEWLQEFGVPHQYSSRQVAHSGAKASVVDGTPLVAAPSLNATTVVTTVYQEPIMSQGAALSGEPTTLTKEEEKKQPDEEPMDMVVEKQEETDHKNDNQILSEIVEAKMAEELKPMDTDKESIAESKSPEMSMQEDCISDIAPMQTDEQTNKEQFVPGPNEKPLYTAEPVTLEDLQLLADLFYLPYEHGPKGAQMLREFQWLRANSSVVSVNCKGKDSEKIEEWRSRAAKFEEMCGLVMGMFTRLSNCANRTILYDMYSYVWDIKSIMSMVKSFVQWLGCRSHSSAQFLIGDQEPWAFRGGLAGEFQRLLPIDGANDLFFQPPPLTPTSKVYTIRPYFPKDEASVYKICREMYDDGVGLPFQSQPDLIGDKLVGGLLSLSLDYCFVLEDEDGICGYALGTVDVTPFIKKCKISWIPFMQEKYTKPNGDKELSEAEKIMLSFHEEQEVLPETFLANFPSLIKMDIHKKVTDPSVAKSMMACLLSSLKANGSRGAFCEVRPDDKRILEFYSKLGCFEIAKMEGFPKDVVILGRSL
uniprot
proteins
ec_number
3.2.1.169
uniprot
proteins
function
FUNCTION: [Isoform 1]: Cleaves GlcNAc but not GalNAc from O-glycosylated proteins (PubMed:11148210, PubMed:11788610, PubMed:20673219, PubMed:22365600, PubMed:24088714, PubMed:28939839, PubMed:37962578). Deglycosylates a large and diverse number of proteins, such as CRYAB, ELK1, GSDMD, LMNB1 and TAB1 (PubMed:28939839, PubMed:37962578). Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrates but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro) (PubMed:20673219). Does not bind acetyl-CoA and does not have histone acetyltransferase activity (PubMed:24088714). {ECO:0000269|PubMed:11148210, ECO:0000269|PubMed:11788610, ECO:0000269|PubMed:20673219, ECO:0000269|PubMed:22365600, ECO:0000269|PubMed:24088714, ECO:0000269|PubMed:28939839, ECO:0000269|PubMed:37962578}.; FUNCTION: [Isoform 3]: Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc as substrate but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro), but has about six times lower specific activity than isoform 1. {ECO:0000269|PubMed:20673219}.
uniprot
proteins
mass_dalton
102915
uniprot
proteins
mutagenesis
MUTAGEN 69; /note="Y->K,Q: Strongly reduces affinity for glycopeptide substrates. Nearly abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:20863279, ECO:0000269|PubMed:22365600"; MUTAGEN 69; /note="Y->S: Strongly reduces affinity for glycopeptide substrates. Nearly abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:20863279, ECO:0000269|PubMed:22365600"; MUTAGEN 174; /note="D->A: Nearly abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:16533067"; MUTAGEN 175; /note="D->A: Nearly abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:16533067"; MUTAGEN 175; /note="D->N: Nearly abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:20863279"; MUTAGEN 255; /note="V->G,T: Nearly abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:20863279"; MUTAGEN 286; /note="Y->S: Nearly abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:20863279"; MUTAGEN 287; /note="D->A: Nearly abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:20863279"; MUTAGEN 413; /note="D->A: Abrogates cleavage by caspase-3."; /evidence="ECO:0000269|PubMed:18586680"; MUTAGEN 679; /note="W->N: Nearly abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:20863279
uniprot
proteins
post_translational_modification
PTM: Proteolytically cleaved by caspase-3 during apoptosis. The fragments interact with each other; cleavage does not decrease enzyme activity. {ECO:0000269|PubMed:11788610, ECO:0000269|PubMed:18586680}.
uniprot
proteins
protein_family
Glycosyl hydrolase 84 family
uniprot
proteins
pubmed
11148210
uniprot
proteins
pubmed
11341771
uniprot
proteins
pubmed
11788610
uniprot
proteins
pubmed
12168954
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16533067
uniprot
proteins
pubmed
18586680
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20673219
uniprot
proteins
pubmed
20863279
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22365600
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24088714
uniprot
proteins
pubmed
28742148
uniprot
proteins
pubmed
28939839
uniprot
proteins
pubmed
37962578
uniprot
proteins
pubmed
9734811
uniprot
proteins
pubmed
9811929
uniprot
proteins
sequence_length
916
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 3]: Nucleus {ECO:0000269|PubMed:11341771}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:11148210, ECO:0000269|PubMed:11341771, ECO:0000269|PubMed:11788610}.
uniprot
proteins