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acetyl-CoA + 1-[4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-s-indacene-3-propionyl-glycylamino]-beta-D-glucosamine
CoA + 1-[4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-s-indacene-3-propionyl-glycylamino]-N-acetyl-beta-D-glucosamine
i.e. fluorescent BODIPY-glucosamine
-
-
?
acetyl-CoA + 4-methylumbelliferyl beta-D-glucosaminide
?
-
substrate activity assay
-
-
?
acetyl-CoA + 4-methylumbelliferyl-alpha-D-glucosaminide
CoA + 4-methylumbelliferyl-N-acetyl-alpha-D-glucosaminide
acetyl-CoA + 4-methylumbelliferyl-beta-D-glucosaminide
CoA + 4-methylumbelliferyl-N-acetyl-beta-D-glucosaminide
acetyl-CoA + alpha-D-glucosamine
CoA + N-acetyl-alpha-D-glucosamine
-
-
-
-
?
acetyl-CoA + beta-D-glucosamine
CoA + N-acetyl-beta-D-glucosamine
acetyl-CoA + BODIPY-beta-D-glucosaminide
CoA + BODIPY-N-acetyl-beta-D-glucosaminide
-
-
-
?
acetyl-CoA + glucosamine-L-iduronic acid-D-glucosamine
?
-
reduced with NaBH4
-
-
?
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
acetyl-CoA + heparin alpha-D-glucosaminide
CoA + heparin N-acetyl-D-glucosamine
-
also acetylates di- and tetrasaccharide fragments of heparin
-
-
?
acetyl-CoA + phosphatidylethanolamine
CoA + N-acetylphosphatidylethanolamine
-
-
-
-
?
additional information
?
-
acetyl-CoA + 4-methylumbelliferyl-alpha-D-glucosaminide
CoA + 4-methylumbelliferyl-N-acetyl-alpha-D-glucosaminide
-
-
-
?
acetyl-CoA + 4-methylumbelliferyl-alpha-D-glucosaminide
CoA + 4-methylumbelliferyl-N-acetyl-alpha-D-glucosaminide
-
-
-
?
acetyl-CoA + 4-methylumbelliferyl-alpha-D-glucosaminide
CoA + 4-methylumbelliferyl-N-acetyl-alpha-D-glucosaminide
-
-
-
?
acetyl-CoA + 4-methylumbelliferyl-beta-D-glucosaminide
CoA + 4-methylumbelliferyl-N-acetyl-beta-D-glucosaminide
-
-
-
?
acetyl-CoA + 4-methylumbelliferyl-beta-D-glucosaminide
CoA + 4-methylumbelliferyl-N-acetyl-beta-D-glucosaminide
-
-
-
?
acetyl-CoA + beta-D-glucosamine
CoA + N-acetyl-beta-D-glucosamine
-
-
-
?
acetyl-CoA + beta-D-glucosamine
CoA + N-acetyl-beta-D-glucosamine
-
-
-
?
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
-
-
-
-
?
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
-
-
-
?
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
-
-
-
-
?
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
-
brings about the acetylation of glucosamine groups of heparan sulfate and heparin from which the sulfate has been removed
-
?
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
-
initial step in heparan sulfate degradation
-
?
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
mucopolysaccharidosis IIIC (MPS IIIC, or Sanfilippo C syndrome) is a lysosomal storage disorder caused by the inherited deficiency of the lysosomal membrane enzyme acetyl-coenzyme A:alpha-glucosaminide N-acetyltransferase, which leads to impaired degradation of heparan sulfate. Structural protein that transports the activated acetyl residues across the cell membrane
-
-
?
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
-
-
-
?
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
mucopolysaccharidosis IIIC (MPS IIIC, or Sanfilippo C syndrome) is a lysosomal storage disorder caused by the inherited deficiency of the lysosomal membrane enzyme acetyl-coenzyme A:alpha-glucosaminide N-acetyltransferase, which leads to impaired degradation of heparan sulfate. Structural protein that transports the activated acetyl residues across the cell membrane
-
-
?
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
-
-
-
-
?
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
-
brings about the acetylation of glucosamine groups of heparan sulfate and heparin from which the sulfate has been removed
-
?
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
-
brings about the acetylation of glucosamine groups of heparan sulfate and heparin from which the sulfate has been removed
-
?
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
-
brings about the acetylation of glucosamine groups of heparan sulfate and heparin from which the sulfate has been removed
-
?
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
-
brings about the acetylation of glucosamine groups of heparan sulfate and heparin from which the sulfate has been removed
-
?
additional information
?
-
-
enzyme deficiency leads to Sanfilippo syndrome type C, i.e. mucopolysaccharidosis III C
-
-
?
additional information
?
-
-
enzyme deficiency leads to Sanfilippo syndrome type C, i.e. mucopolysaccharidosis III C
-
-
?
additional information
?
-
-
enzyme deficiency leads to Sanfilippo syndrome type C, i.e. mucopolysaccharidosis III C
-
-
?
additional information
?
-
-
enzyme deficiency causes mucopolysaccharidosis type IIIC
-
-
?
additional information
?
-
-
enzyme is acetylated at the cytoplasmic side of the lysosome and the acetyl group is then transferred to the inside where it is used to acetylate heparan sulfate
-
-
?
additional information
?
-
-
enzyme is acetylated at the cytoplasmic side of the lysosome and the acetyl group is then transferred to the inside where it is used to acetylate heparan sulfate
-
-
?
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acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
additional information
?
-
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
-
-
-
-
?
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
-
initial step in heparan sulfate degradation
-
?
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
mucopolysaccharidosis IIIC (MPS IIIC, or Sanfilippo C syndrome) is a lysosomal storage disorder caused by the inherited deficiency of the lysosomal membrane enzyme acetyl-coenzyme A:alpha-glucosaminide N-acetyltransferase, which leads to impaired degradation of heparan sulfate. Structural protein that transports the activated acetyl residues across the cell membrane
-
-
?
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
mucopolysaccharidosis IIIC (MPS IIIC, or Sanfilippo C syndrome) is a lysosomal storage disorder caused by the inherited deficiency of the lysosomal membrane enzyme acetyl-coenzyme A:alpha-glucosaminide N-acetyltransferase, which leads to impaired degradation of heparan sulfate. Structural protein that transports the activated acetyl residues across the cell membrane
-
-
?
acetyl-CoA + heparan sulfate alpha-D-glucosaminide
CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide
-
-
-
-
?
additional information
?
-
-
enzyme deficiency leads to Sanfilippo syndrome type C, i.e. mucopolysaccharidosis III C
-
-
?
additional information
?
-
-
enzyme deficiency leads to Sanfilippo syndrome type C, i.e. mucopolysaccharidosis III C
-
-
?
additional information
?
-
-
enzyme deficiency leads to Sanfilippo syndrome type C, i.e. mucopolysaccharidosis III C
-
-
?
additional information
?
-
-
enzyme deficiency causes mucopolysaccharidosis type IIIC
-
-
?
additional information
?
-
-
enzyme is acetylated at the cytoplasmic side of the lysosome and the acetyl group is then transferred to the inside where it is used to acetylate heparan sulfate
-
-
?
additional information
?
-
-
enzyme is acetylated at the cytoplasmic side of the lysosome and the acetyl group is then transferred to the inside where it is used to acetylate heparan sulfate
-
-
?
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Genetic Diseases, Inborn
Genetic evidence for transmembrane acetylation by lysosomes.
heparan-alpha-glucosaminide n-acetyltransferase deficiency
Crosstalk between 2 organelles: Lysosomal storage of heparan sulfate causes mitochondrial defects and neuronal death in mucopolysaccharidosis III type C.
Lysosomal Storage Diseases
The first Korean case of mucopolysaccharidosis IIIC (Sanfilippo syndrome type C) confirmed by biochemical and molecular investigation.
Mucopolysaccharidoses
A genetic and clinical study of individuals with nonsyndromic retinopathy consequent upon sequence variants in HGSNAT, the gene associated with Sanfilippo C mucopolysaccharidosis.
Mucopolysaccharidoses
Analysis of the biogenesis of heparan sulfate acetyl-CoA:alpha-glucosaminide N-acetyltransferase provides insights into the mechanism underlying its complete deficiency in mucopolysaccharidosis IIIC.
Mucopolysaccharidoses
Clinical and genetic spectrum of Sanfilippo type C (MPS IIIC) disease in The Netherlands.
Mucopolysaccharidoses
Functional analysis of the HGSNAT gene in patients with mucopolysaccharidosis IIIC (Sanfilippo C Syndrome).
Mucopolysaccharidoses
Klüver-Bucy syndrome associated with a recessive variant in HGSNAT in two siblings with Mucopolysaccharidosis type IIIC (Sanfilippo C).
Mucopolysaccharidoses
Molecular characterization of Portuguese patients with mucopolysaccharidosis IIIC: two novel mutations in the HGSNAT gene.
Mucopolysaccharidoses
Mutational analysis of the HGSNAT gene in Italian patients with mucopolysaccharidosis IIIC (Sanfilippo C syndrome). Mutation in brief #959. Online.
Mucopolysaccharidoses
Non-syndromic retinitis pigmentosa due to mutations in the mucopolysaccharidosis type IIIC gene, heparan-alpha-glucosaminide N-acetyltransferase (HGSNAT).
Mucopolysaccharidoses
Protein misfolding as an underlying molecular defect in mucopolysaccharidosis III type C.
Mucopolysaccharidoses
Sanfilippo syndrome type C: deficiency of acetyl-CoA:alpha-glucosaminide N-acetyltransferase in skin fibroblasts.
Mucopolysaccharidoses
Sanfilippo syndrome type C: mutation spectrum in the heparan sulfate acetyl-CoA: alpha-glucosaminide N-acetyltransferase (HGSNAT) gene.
Mucopolysaccharidoses
The first Korean case of mucopolysaccharidosis IIIC (Sanfilippo syndrome type C) confirmed by biochemical and molecular investigation.
Mucopolysaccharidosis III
A genetic and clinical study of individuals with nonsyndromic retinopathy consequent upon sequence variants in HGSNAT, the gene associated with Sanfilippo C mucopolysaccharidosis.
Mucopolysaccharidosis III
Analysis of the biogenesis of heparan sulfate acetyl-CoA:alpha-glucosaminide N-acetyltransferase provides insights into the mechanism underlying its complete deficiency in mucopolysaccharidosis IIIC.
Mucopolysaccharidosis III
Clinical and genetic spectrum of Sanfilippo type C (MPS IIIC) disease in The Netherlands.
Mucopolysaccharidosis III
Crosstalk between 2 organelles: Lysosomal storage of heparan sulfate causes mitochondrial defects and neuronal death in mucopolysaccharidosis III type C.
Mucopolysaccharidosis III
Functional analysis of the HGSNAT gene in patients with mucopolysaccharidosis IIIC (Sanfilippo C Syndrome).
Mucopolysaccharidosis III
Glycosaminoglycans and mucopolysaccharidosis type III.
Mucopolysaccharidosis III
Klüver-Bucy syndrome associated with a recessive variant in HGSNAT in two siblings with Mucopolysaccharidosis type IIIC (Sanfilippo C).
Mucopolysaccharidosis III
Lysosomal N-acetyltransferase interacts with ALIX and is detected in extracellular vesicles.
Mucopolysaccharidosis III
Lysosomal storage of heparan sulfate causes mitochondrial defects, altered autophagy, and neuronal death in the mouse model of mucopolysaccharidosis III type C.
Mucopolysaccharidosis III
Molecular analysis of Sanfilippo syndrome type C in Spain: seven novel HGSNAT mutations and characterization of the mutant alleles.
Mucopolysaccharidosis III
Mutational analysis of the HGSNAT gene in Italian patients with mucopolysaccharidosis IIIC (Sanfilippo C syndrome). Mutation in brief #959. Online.
Mucopolysaccharidosis III
Mutations in TMEM76* cause mucopolysaccharidosis IIIC (Sanfilippo C syndrome).
Mucopolysaccharidosis III
Natural History of Sanfilippo Syndrome Type C in Boyacá, Colombia.
Mucopolysaccharidosis III
Neuroinflammation, mitochondrial defects and neurodegeneration in mucopolysaccharidosis III type C mouse model.
Mucopolysaccharidosis III
Non-syndromic retinitis pigmentosa due to mutations in the mucopolysaccharidosis type IIIC gene, heparan-alpha-glucosaminide N-acetyltransferase (HGSNAT).
Mucopolysaccharidosis III
Novel Direct Assay for Acetyl-CoA:?-Glucosaminide N-Acetyltransferase Using BODIPY-Glucosamine as a Substrate.
Mucopolysaccharidosis III
Polymorphic variants (p.Ser141Ser and p.Arg737Gly) at the NAGLU gene are really indicative of pseudodeficiency alleles?
Mucopolysaccharidosis III
Protein misfolding as an underlying molecular defect in mucopolysaccharidosis III type C.
Mucopolysaccharidosis III
Sanfilippo syndrome type C: deficiency of acetyl-CoA:alpha-glucosaminide N-acetyltransferase in skin fibroblasts.
Mucopolysaccharidosis III
Sanfilippo syndrome type C: mutation spectrum in the heparan sulfate acetyl-CoA: alpha-glucosaminide N-acetyltransferase (HGSNAT) gene.
Mucopolysaccharidosis III
The first Korean case of mucopolysaccharidosis IIIC (Sanfilippo syndrome type C) confirmed by biochemical and molecular investigation.
Mucopolysaccharidosis III
Update of the spectrum of mucopolysaccharidoses type III in Tunisia: identification of three novel mutations and in silico structural analysis of the missense mutations.
Neurodegenerative Diseases
Analysis of the biogenesis of heparan sulfate acetyl-CoA:alpha-glucosaminide N-acetyltransferase provides insights into the mechanism underlying its complete deficiency in mucopolysaccharidosis IIIC.
Neurodegenerative Diseases
Crosstalk between 2 organelles: Lysosomal storage of heparan sulfate causes mitochondrial defects and neuronal death in mucopolysaccharidosis III type C.
Neurodegenerative Diseases
Novel Direct Assay for Acetyl-CoA:?-Glucosaminide N-Acetyltransferase Using BODIPY-Glucosamine as a Substrate.
Retinal Degeneration
Non-syndromic retinitis pigmentosa due to mutations in the mucopolysaccharidosis type IIIC gene, heparan-alpha-glucosaminide N-acetyltransferase (HGSNAT).
Retinal Diseases
A genetic and clinical study of individuals with nonsyndromic retinopathy consequent upon sequence variants in HGSNAT, the gene associated with Sanfilippo C mucopolysaccharidosis.
Retinitis Pigmentosa
A genetic and clinical study of individuals with nonsyndromic retinopathy consequent upon sequence variants in HGSNAT, the gene associated with Sanfilippo C mucopolysaccharidosis.
Retinitis Pigmentosa
Non-syndromic retinitis pigmentosa due to mutations in the mucopolysaccharidosis type IIIC gene, heparan-alpha-glucosaminide N-acetyltransferase (HGSNAT).
Retinitis Pigmentosa
Nonsyndromic retinitis pigmentosa caused by two novel variants in the HGSNAT gene in a Chinese family.
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0.000017
-
leukocyte, substrate 4-methylumbelliferyl-alpha-D-glucosaminide + acetyl-CoA
0.000022
-
leukocyte, substrate 4-methylumbelliferyl-beta-D-glucosaminide + acetyl-CoA
0.000058
-
fibroblast, substrate 4-methylumbelliferyl-beta-D-glucosaminide + acetyl-CoA
0.000059
-
fibroblast, substrate 4-methylumbelliferyl-alpha-D-glucosaminide + acetyl-CoA
0.000673
-
lysosomal fraction
additional information
-
-
additional information
-
Sanfilippo syndrome type C patients in comparison
additional information
-
mutant A489E, relative activity 23.1%, wild-type 100%
additional information
-
mutant A615T, relative activity 54.9%, wild-type 100%
additional information
-
mutant C76F, relative activity 15.4%, wild-type 100%
additional information
-
mutant D562V, relative activity 22.0%, wild-type 100%
additional information
-
mutant E471K, relative activity 19.8%, wild-type 100%
additional information
-
mutant G262R, relative activity 17.6%, wild-type 100%
additional information
-
mutant G424S, relative activity 18.7%, wild-type 100%
additional information
-
mutant K523Q, relative activity 96.7%, wild-type 100%
additional information
-
mutant L137P, relative activity 17.6%, wild-type 100%
additional information
-
mutant M482K, relative activity 24.2%, wild-type 100%
additional information
-
mutant N273K, relative activity 18.7%, wild-type 100%
additional information
-
mutant P237Q, relative activity 108.8%, wild-type 100%
additional information
-
mutant P283L, relative activity 20.9%, wild-type 100%
additional information
-
mutant P571L, relative activity 22.0%, wild-type 100%
additional information
-
mutant R344C, relative activity 12.1%, wild-type 100%
additional information
-
mutant R344H, relative activity 14.3%, wild-type 100%
additional information
-
mutant S518F, relative activity 30.8%, wild-type 100%
additional information
-
mutant S539C, relative activity 27.5%, wild-type 100%
additional information
-
mutant S541L, relative activity 23.1%, wild-type 100%
additional information
-
mutant V481L, relative activity 114.3%, wild-type 100%
additional information
-
mutant W403C, relative activity 17.6%, wild-type 100%
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HGNAT_HUMAN
663
12
73293
Swiss-Prot
Mitochondrion (Reliability: 2)
HGNAT_MOUSE
656
12
72504
Swiss-Prot
Mitochondrion (Reliability: 4)
A0A2G9HNQ2_9LAMI
433
9
48210
TrEMBL
other Location (Reliability: 2)
A0A2G9IA79_9LAMI
273
5
30972
TrEMBL
other Location (Reliability: 4)
A0A6J8BIA9_MYTCO
610
11
69374
TrEMBL
other Location (Reliability: 5)
A0A0W0YW40_9GAMM
370
10
41992
TrEMBL
-
A0A653VY52_9FLAO
422
12
47717
TrEMBL
-
A0A396GUZ2_MEDTR
457
9
51220
TrEMBL
other Location (Reliability: 2)
A0A8B6G5X1_MYTGA
473
11
52943
TrEMBL
other Location (Reliability: 4)
A0A0W0RRE7_LEGBO
372
10
42462
TrEMBL
-
A0A0W0S971_9GAMM
372
10
42272
TrEMBL
-
A0A2G9GYE7_9LAMI
250
4
28709
TrEMBL
other Location (Reliability: 2)
A0A0W0VTV2_9GAMM
367
10
41451
TrEMBL
-
A0A0W1A7F0_9GAMM
371
10
42200
TrEMBL
-
A0A0F4HD15_LIMFE
634
0
70408
TrEMBL
-
K9W1H5_9CYAN
371
10
41494
TrEMBL
-
A0A812B9D5_SEPPH
655
9
74186
TrEMBL
other Location (Reliability: 2)
A0A2S2DTJ9_9BACT
377
9
43047
TrEMBL
-
A0A396H9R1_MEDTR
279
6
31872
TrEMBL
other Location (Reliability: 5)
A0A396JSG0_MEDTR
497
10
56285
TrEMBL
other Location (Reliability: 1)
A0A396HC80_MEDTR
502
8
57320
TrEMBL
other Location (Reliability: 1)
A0A0A8UTY8_LEGHA
382
10
42908
TrEMBL
-
A0A0B2QBJ9_GLYSO
461
9
51383
TrEMBL
other Location (Reliability: 4)
K9VMG8_9CYAN
406
9
45075
TrEMBL
-
A0A7R8HAF7_LEPSM
439
6
49388
TrEMBL
other Location (Reliability: 3)
A0A369QHV9_9BACT
416
12
44957
TrEMBL
-
G7IEH8_MEDTR
476
9
53519
TrEMBL
other Location (Reliability: 3)
K6YQM4_9ALTE
330
8
36973
TrEMBL
-
A0A8B6CU61_MYTGA
622
11
70040
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P6PIE0_ROSCH
478
9
53131
TrEMBL
other Location (Reliability: 3)
A0A5B7AWT9_DAVIN
444
9
49882
TrEMBL
other Location (Reliability: 4)
A0A5B7BB13_DAVIN
457
9
50436
TrEMBL
other Location (Reliability: 2)
A0A2H9ZS88_9ASPA
331
3
37368
TrEMBL
Mitochondrion (Reliability: 3)
A0A0W0VAB4_9GAMM
369
10
41597
TrEMBL
-
A0A0W0R1Y2_9GAMM
372
10
42819
TrEMBL
-
A0A0W0STE2_9GAMM
368
10
41515
TrEMBL
-
F0RGS2_CELLC
Cellulophaga lytica (strain ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 / NCIMB 1423 / VKM B-1433 / Cy l20)
361
10
40764
TrEMBL
-
A0A6J8DR10_MYTCO
475
6
53828
TrEMBL
other Location (Reliability: 1)
A0A0W0ZVV8_9GAMM
372
9
42358
TrEMBL
-
E6X8R5_CELAD
Cellulophaga algicola (strain DSM 14237 / IC166 / ACAM 630)
363
10
40697
TrEMBL
-
A0A0W0Z1U7_9GAMM
381
10
44225
TrEMBL
-
A0A073CJX3_PLAAG
371
10
41853
TrEMBL
-
A0A2I0A047_9ASPA
537
9
59888
TrEMBL
other Location (Reliability: 3)
A0A2G9IAB5_9LAMI
484
9
54909
TrEMBL
other Location (Reliability: 2)
M2W0K7_GALSU
356
7
40849
TrEMBL
other Location (Reliability: 3)
A0A369QAU3_9BACT
379
7
43621
TrEMBL
-
A0A0B2R830_GLYSO
489
9
54905
TrEMBL
other Location (Reliability: 3)
A0A5B7BBZ9_DAVIN
468
10
53074
TrEMBL
other Location (Reliability: 1)
K9QID7_9NOSO
387
10
44009
TrEMBL
-
A0A098AUK5_DESHA
237
7
26365
TrEMBL
-
A0A2G9G742_9LAMI
486
9
53513
TrEMBL
other Location (Reliability: 2)
A0A2S2DY03_9BACT
373
8
42774
TrEMBL
-
A0A0U5DPK0_STEMA
355
9
38203
TrEMBL
-
A0A0W0Y4A2_9GAMM
378
10
42724
TrEMBL
-
A0A0W0YT96_9GAMM
368
10
42212
TrEMBL
-
I1DW22_9GAMM
397
10
45027
TrEMBL
-
A0A0W0TBQ9_9GAMM
379
10
43285
TrEMBL
-
D2QUS7_SPILD
Spirosoma linguale (strain ATCC 33905 / DSM 74 / LMG 10896)
381
9
42603
TrEMBL
-
A0A5B6ZXG6_DAVIN
149
4
17029
TrEMBL
Secretory Pathway (Reliability: 3)
A0A812BAR1_SEPPH
692
10
78700
TrEMBL
other Location (Reliability: 2)
M5CRH9_STEMA
355
9
38294
TrEMBL
-
A0A0W0XYT7_9GAMM
377
10
41867
TrEMBL
-
A0A2P6PKW2_ROSCH
421
9
47300
TrEMBL
other Location (Reliability: 1)
A0A2P6RB41_ROSCH
516
10
58173
TrEMBL
other Location (Reliability: 2)
A0A5B6ZUT7_DAVIN
510
10
57014
TrEMBL
Mitochondrion (Reliability: 5)
A0A098GF91_TATMI
379
10
43194
TrEMBL
-
A0A2G9HYP2_9LAMI
484
9
54952
TrEMBL
other Location (Reliability: 2)
D2QUR2_SPILD
Spirosoma linguale (strain ATCC 33905 / DSM 74 / LMG 10896)
364
10
40168
TrEMBL
-
A0A0W0WV41_9GAMM
378
10
43114
TrEMBL
-
A0A0B2QY57_GLYSO
463
9
51605
TrEMBL
other Location (Reliability: 3)
K6YIY7_9ALTE
365
10
41300
TrEMBL
-
A0A1G4GAZ4_9BACT
372
10
42260
TrEMBL
-
K6Y4R3_9ALTE
366
10
40827
TrEMBL
-
A0A0W1A1C5_9GAMM
381
10
43599
TrEMBL
-
A0A0W0TNF3_9GAMM
390
10
43617
TrEMBL
-
A0A8B6DUQ1_MYTGA
819
12
93179
TrEMBL
other Location (Reliability: 2)
A0A8B6DX20_MYTGA
614
11
69677
TrEMBL
Secretory Pathway (Reliability: 3)
A0A2I0B3N2_9ASPA
488
9
54681
TrEMBL
other Location (Reliability: 1)
M2WYL4_GALSU
351
7
40282
TrEMBL
other Location (Reliability: 5)
A0A0W0WBT9_9GAMM
378
10
42890
TrEMBL
-
A0A2G9GYF7_9LAMI
489
9
55532
TrEMBL
other Location (Reliability: 2)
A0A0W0XIP7_9GAMM
382
10
42837
TrEMBL
-
A0A396J3S6_MEDTR
416
9
46398
TrEMBL
other Location (Reliability: 2)
A0A396HBA0_MEDTR
221
4
25040
TrEMBL
other Location (Reliability: 1)
A0A2P6QZW3_ROSCH
475
9
52292
TrEMBL
other Location (Reliability: 1)
A0A2H9ZW75_9ASPA
457
9
50708
TrEMBL
other Location (Reliability: 4)
A0A2G9GV58_9LAMI
462
9
51028
TrEMBL
other Location (Reliability: 3)
F4A0F0_MAHA5
Mahella australiensis (strain DSM 15567 / CIP 107919 / 50-1 BON)
368
10
41327
TrEMBL
-
M5D4A0_STEMA
355
9
38391
TrEMBL
-
A0A0W0YYB3_LEGSP
386
10
43684
TrEMBL
-
A0A7R8GYV1_LEPSM
447
6
51317
TrEMBL
other Location (Reliability: 4)
A0A0W0TQT4_LEGER
372
10
41186
TrEMBL
-
A0A2I0ASB5_9ASPA
501
9
57111
TrEMBL
other Location (Reliability: 3)
A0A0W0ZGB4_9GAMM
372
10
42138
TrEMBL
-
A0A0W0UA35_9GAMM
373
10
42084
TrEMBL
-
G7KXJ3_MEDTR
467
9
52760
TrEMBL
other Location (Reliability: 2)
A0A2P6R755_ROSCH
467
9
52939
TrEMBL
other Location (Reliability: 2)
A0A2G9G995_9LAMI
461
9
51076
TrEMBL
other Location (Reliability: 3)
B8L902_9GAMM
355
9
38303
TrEMBL
-
A0A0W0UNE1_9GAMM
368
10
41194
TrEMBL
-
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A489E
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
A615T
-
mutant represents a rare polymorphism which has no effect on the activity, processing and targeting of the enzyme
C123S
mutation within the lysosomal luminal loops, complete loss of activity. Mutants does not undergo intralysosomal maturation and does not form the mature oligomer
C151S
mutation within the lysosomal luminal loops, complete loss of activity. Mutants does not undergo intralysosomal maturation
C305S
mutation within the predicted cytosolic luminal loops, no loss of activity
C308S
mutation within the predicted cytosolic luminal loops, no loss of activity
C374S
mutation within the predicted cytosolic luminal loops, no loss of activity
C434S
mutation within the lysosomal luminal loops, complete loss of activity. Mutants does not undergo intralysosomal maturation and does not form the mature oligomer
C79S
mutation within the lysosomal luminal loops, complete loss of activity. Mutants does not undergo intralysosomal maturation
D562V
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
E471K
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
G262R
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
G424S
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
H269A
complete loss of enzymic activity, intralysosomal processing is retained
H451A
complete loss of enzymic activity, no processing observed
H605A
complete loss of enzymic activity, no processing observed
K523Q
-
mutant represents a rare polymorphism which has no effect on the activity, processing and targeting of the enzyme
L137P
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
L208A/I209A
mutation in a predicted dileucine targeting motif, mutant displays both lysosomal and plasma membrane localization
M482K
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
N273K
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
P237Q
-
mutant represents a rare polymorphism which has no effect on the activity, processing and targeting of the enzyme
P283L
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
P571L
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
R344C
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
R344H
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
S518F
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
S539C
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
S541L
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
V481L
-
mutant represents a rare polymorphism which has no effect on the activity, processing and targeting of the enzyme
W403C
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
C76F
-
missense mutant, mutation causes misfolding of the enzyme, which is abnormally glycosylated and not targeted to the lysosome, but retained in the endoplasmic reticulum
C76F
mutation within the lysosomal luminal loops, complete loss of activity. Mutants does not undergo intralysosomal maturation
additional information
-
c.1-1925_118+296del, mutation, 2339-bp deletion including exon 1
additional information
-
c.1030C>T, missense mutation, predicted effect on protein, p.R344C
additional information
-
c.1209G>T, missense mutation, predicted effect on protein, p.W403C
additional information
-
c.1250+1G>A, splicing site mutation, intron 12
additional information
-
c.1250+2T>C, splicing site mutation, intron 12
additional information
-
c.1271dupG, mutation, predicted effect on protein, p.I425HfsX45
additional information
-
c.1411G>A, missense mutation, predicted effect on protein, p.E471K
additional information
-
c.1441G>T, polymorphism, predicted effect on protein, p.V481L
additional information
-
c.1457G>A, missense mutation, predicted effect on protein, p.G486E
additional information
-
c.1466C>A, missense mutation, predicted effect on protein, p.A489E
additional information
-
c.1516C>T, nonsense mutation, predicted effect on protein, p.R506X, premature termination codon
additional information
-
c.1542+4dupA, splicing site mutation, intron 15
additional information
-
c.1553C>T, missense mutation, predicted effect on protein, p.S518F
additional information
-
c.1622C>T, missense mutation, predicted effect on protein, p.S541L
additional information
-
c.1674C>G, nonsense mutation, predicted effect on protein, p.Y558X, premature termination codon
additional information
-
c.1843G>A, polymorphism, predicted effect on protein, p.A615T
additional information
-
c.410T>C, missense mutation, predicted effect on protein, p.L137P
additional information
-
c.493+1G>A, splicing site mutation, intron 4
additional information
-
c.641delG, mutation, predicted effect on protein, p.Gly214AspfsX62
additional information
-
c.739delA, mutation, predicted effect on protein, p.R247GfsX29
additional information
-
c.744-2A>G, splicing site mutation, intron 7
additional information
-
c.848C>T, missense mutation, predicted effect on protein, p.P283L
additional information
-
c.852-1G>A, splicing site mutation, intron 9
additional information
-
c.887C>A, nonsense mutation, predicted effect on protein, p.S296X, premature termination codon
additional information
deletion of 12 residues at the C terminus of the enzyme, del624-635, leads to localization of the protein to the plasma membrane, in contrast to the lysosomal localization of wild-type enzyme. Mutant protein does not show maturation and has no enzymic activity
additional information
-
deletion of 12 residues at the C terminus of the enzyme, del624-635, leads to localization of the protein to the plasma membrane, in contrast to the lysosomal localization of wild-type enzyme. Mutant protein does not show maturation and has no enzymic activity
additional information
mutation of a putative LYPXnL-based binding site within HGSNAT for the V-domain of ALIX ablates association of HGSNAT with ALIX, posttranslational maturation, and transport through the endolysosomal network
additional information
-
mutation of a putative LYPXnL-based binding site within HGSNAT for the V-domain of ALIX ablates association of HGSNAT with ALIX, posttranslational maturation, and transport through the endolysosomal network
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Klein, U.; Kresse, H.; Von Figura, K.
Sanfilippo syndrome type C: deficiency of acetyl-CoA: alpha-glucosaminide N-acetyltransferase in skin fibroblasts
Proc. Natl. Acad. Sci. USA
75
5185-5189
1978
Homo sapiens
brenda
Pohlmann, R.; Klein, U.; Fromme, H.G.; Von Figura, K.
Localisation of acetyl-CoA: alpha-glucosaminide N-acetyltransferase in microsomes and lysosomes of rat liver
Hoppe-Seyler's Z. Physiol. Chem.
362
1199-1207
1981
Rattus norvegicus
brenda
Bame, K.J.; Rome, L.H.
Acetyl-CoA: alpha-glucosaminide N-acetyltransferase from rat liver
Methods Enzymol.
138
607-611
1987
Rattus norvegicus
brenda
Bame, K.J.; Rome, L.H.
Acetyl-coenzyme A:alpha-glucosaminide N-acetyltransferase. Evidence for an active site histidine residue
J. Biol. Chem.
261
10127-10132
1986
Rattus norvegicus
brenda
Bame, K.J.; Rome, L.H.
Acetyl coenzyme A:alpha-glucosaminide N-acetyltransferase. Evidence for a transmembrane acetylation mechanism
J. Biol. Chem.
260
11293-11299
1985
Rattus norvegicus
brenda
Reynertson, R.; Campbell, P.; Ford, J.D.; Jacobsson, I.; Roden, L.; Thompson, J.N.
New oligosaccharides from heparin and heparan sulfate and their use as substrates for heparin-degrading enzymes
J. Biol. Chem.
258
7449-7459
1983
Homo sapiens
brenda
Meikle, P.J.; Whittle, A.M.; Hopwood, J.J.
Human acetyl-coenzyme A:alpha-glucosaminide N-acetyltransferase. Kinetic characterization and mechanistic interpretation
Biochem. J.
308
327-333
1995
Homo sapiens
-
brenda
Voznyi, Y.V.; Karpova, E.A.; Dudukina, T.V.; Tsvetkova, I.V.; Boer, A.M.; Janse, H.C.; van Diggelen, O.P.
A fluorometric enzyme assay for the diagnosis of Sanfilippo disease C (MPS III C)
J. Inherit. Metab. Dis.
16
465-472
1993
Homo sapiens
brenda
Taute, A.; Watzig, K.; Simons, B.; Lohaus, C.; Meyer, H.E.; Hasilik, A.
Presence of detergent-resistant microdomains in lysosomal membranes
Biochem. Biophys. Res. Commun.
298
5-9
2002
Homo sapiens
brenda
Gerber, S.A.; Turecek, F.; Gelb, M.H.
Design and synthesis of substrate and internal standard conjugates for profiling enzyme activity in the Sanfilippo syndrome by affinity chromatography/electrospray ionization mass spectrometry
Bioconjug. Chem.
12
603-615
2001
Homo sapiens
brenda
Nelson, K.; Melville, E.L.; Meikle, P.J.; Anson, D.S.
Immortalisation of a mucopolysaccharidosis type IIIC fibroblast cell line via expression of SV40 T antigen
Cell Biol. Int.
27
567-570
2003
Homo sapiens
brenda
Hrebicek, M.; Mrazova, L.; Seyrantepe, V.; Durand, S.; Roslin, N.M.; Noskova, L.; Hartmannova, H.; Ivanek, R.; Cizkova, A.; Poupetova, H.; Sikora, J.; Urinovska, J.; Stranecky, V.; Zeman, J.; Lepage, P.; Roquis, D.; Verner, A.; Ausseil, J.; Beesley, C.E.; Maire, I.; Poorthuis, B.J.; van de Kamp, J.
Mutations in TMEM76* cause mucopolysaccharidosis IIIC (Sanfilippo C syndrome)
Am. J. Hum. Genet.
79
807-819
2006
Mus musculus (Q3UDW8), Mus musculus, Homo sapiens (Q68CP4), Homo sapiens
brenda
Ausseil, J.; Landry, K.; Seyrantepe, V.; Trudel, S.; Mazur, A.; Lapointe, F.; Pshezhetsky, A.V.
An acetylated 120-kDa lysosomal transmembrane protein is absent from mucopolysaccharidosis IIIC fibroblasts: a candidate molecule for MPS IIIC
Mol. Genet. Metab.
87
22-31
2006
Homo sapiens (Q68CP4)
brenda
Feldhammer, M.; Durand, S.; Mrazova, L.; Boucher, R.M.; Laframboise, R.; Steinfeld, R.; Wraith, J.E.; Michelakakis, H.; van Diggelen, O.P.; Hrebicek, M.; Kmoch, S.; Pshezhetsky, A.V.
Sanfilippo syndrome type C: mutation spectrum in the heparan sulfate acetyl-CoA: alpha-glucosaminide N-acetyltransferase (HGSNAT) gene
Hum. Mutat.
30
918-925
2009
Homo sapiens
brenda
Feldhammer, M.; Durand, S.; Pshezhetsky, A.V.
Protein misfolding as an underlying molecular defect in mucopolysaccharidosis III type C
PLoS ONE
4
e7434
2009
Homo sapiens
brenda
Durand, S.; Feldhammer, M.; Bonneil, E.; Thibault, P.; Pshezhetsky, A.V.
Analysis of the biogenesis of heparan sulfate acetyl-CoA:alpha-glucosaminide N-acetyltransferase provides insights into the mechanism underlying its complete deficiency in mucopolysaccharidosis IIIC
J. Biol. Chem.
285
31233-31242
2010
Homo sapiens (Q68CP4), Homo sapiens
brenda
Haer-Wigman, L.; Newman, H.; Leibu, R.; Bax, N.M.; Baris, H.N.; Rizel, L.; Banin, E.; Massarweh, A.; Roosing, S.; Lefeber, D.J.; Zonneveld-Vrieling, M.N.; Isakov, O.; Shomron, N.; Sharon, D.; Den Hollander, A.I.; Hoyng, C.B.; Cremers, F.P.; Ben-Yosef, T.
Non-syndromic retinitis pigmentosa due to mutations in the mucopolysaccharidosis type IIIC gene, heparan-alpha-glucosaminide N-acetyltransferase (HGSNAT)
Hum. Mol. Genet.
24
3742-3751
2015
Homo sapiens (Q68CP4), Homo sapiens
brenda
Choi, Y.; Tuzikov, A.B.; Ovchinnikova, T.V.; Bovin, N.V.; Pshezhetsky, A.V.
Novel direct assay for acetyl-CoA:alpha-glucosaminide N-acetyltransferase using BODIPY-glucosamine as a substrate
JIMD Rep.
28
11-18
2015
Homo sapiens (Q68CP4), Homo sapiens
brenda
Fedele, A.O.; Isenmann, S.; Kamei, M.; Snel, M.F.; Trim, P.J.; Proud, C.G.; Hopwood, J.J.
Lysosomal N-acetyltransferase interacts with ALIX and is detected in extracellular vesicles
Biochim. Biophys. Acta
1865
1451-1464
2018
Homo sapiens (Q68CP4), Homo sapiens
brenda
Choi, Y.; Tuzikov, A.; Ovchinnikova, T.; Bovin, N.; Pshezhetsky, A.
Novel direct assay for acetyl-CoA alpha-glucosaminide N-acetyltransferase using BODIPY-glucosamine as a substrate
JIMD Rep.
28
11-18
2016
Homo sapiens (Q68CP4), Homo sapiens
brenda