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P54802

- ANAG_HUMAN

UniProt

P54802 - ANAG_HUMAN

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Protein

Alpha-N-acetylglucosaminidase

Gene

NAGLU

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Involved in the degradation of heparan sulfate.

Catalytic activityi

Hydrolysis of terminal non-reducing N-acetyl-D-glucosamine residues in N-acetyl-alpha-D-glucosaminides.

GO - Molecular functioni

  1. alpha-N-acetylglucosaminidase activity Source: ProtInc

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. cerebellar Purkinje cell layer development Source: Ensembl
  3. glycosaminoglycan catabolic process Source: Reactome
  4. glycosaminoglycan metabolic process Source: Reactome
  5. inner ear receptor cell development Source: Ensembl
  6. locomotor rhythm Source: Ensembl
  7. lysosome organization Source: Ensembl
  8. middle ear morphogenesis Source: Ensembl
  9. nervous system development Source: ProtInc
  10. retinal rod cell development Source: Ensembl
  11. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

ReactomeiREACT_120752. HS-GAG degradation.

Protein family/group databases

CAZyiGH89. Glycoside Hydrolase Family 89.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-N-acetylglucosaminidase (EC:3.2.1.50)
Alternative name(s):
N-acetyl-alpha-glucosaminidase
Short name:
NAG
Cleaved into the following 2 chains:
Gene namesi
Name:NAGLU
Synonyms:UFHSD1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:7632. NAGLU.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. lysosomal lumen Source: Reactome
  3. lysosome Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Involvement in diseasei

Mucopolysaccharidosis 3B (MPS3B) [MIM:252920]: A form of mucopolysaccharidosis type 3, an autosomal recessive lysosomal storage disease due to impaired degradation of heparan sulfate. MPS3 is characterized by severe central nervous system degeneration, but only mild somatic disease. Onset of clinical features usually occurs between 2 and 6 years; severe neurologic degeneration occurs in most patients between 6 and 10 years of age, and death occurs typically during the second or third decade of life.14 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti35 – 351L → F in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication
VAR_054699
Natural varianti38 – 381R → W in MPS3B; decreases the enzyme activity markedly. 1 Publication
VAR_054700
Natural varianti48 – 481F → C in MPS3B. 1 Publication
VAR_054701
Natural varianti48 – 481F → L in MPS3B; associated with a partially degraded polypeptide in a 16-hour chase experiment suggesting that L-48 NAGLU affects the processing and stability of the gene; some L-48 NAGLU is being correctly sorted to the lysosomal compartment. 2 Publications
VAR_025489
Natural varianti69 – 691G → S in MPS3B. 1 Publication
VAR_054702
Natural varianti77 – 771V → G in MPS3B; decreases the enzyme activity markedly. 1 Publication
VAR_054703
Natural varianti79 – 791G → C in MPS3B. 2 Publications
VAR_008979
Natural varianti79 – 791G → S in MPS3B. 1 Publication
VAR_054704
Natural varianti82 – 821G → D in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication
VAR_054705
Natural varianti92 – 921Y → H in MPS3B. 1 Publication
VAR_005007
Natural varianti100 – 1001H → R in MPS3B. 1 Publication
VAR_008980
Natural varianti115 – 1151P → S in MPS3B. 1 Publication
VAR_005008
Natural varianti130 – 1301R → C in MPS3B; does not yield active enzyme. 2 Publications
VAR_054706
Natural varianti140 – 1401Y → C in MPS3B. 6 Publications
VAR_005009
Natural varianti142 – 1421Missing in MPS3B. 1 Publication
VAR_008981
Natural varianti153 – 1531E → K in MPS3B. 2 Publications
VAR_005010
Natural varianti154 – 1541I → R in MPS3B; does not yield active enzyme. 1 Publication
VAR_054707
Natural varianti156 – 1561W → C in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication
VAR_054708
Natural varianti227 – 2271H → P in MPS3B. 1 Publication
VAR_054709
Natural varianti234 – 2341R → C in MPS3B. 3 Publications
VAR_054710
Natural varianti241 – 2411V → M in MPS3B. 1 Publication
VAR_054711
Natural varianti242 – 2421L → P in MPS3B; no enzyme activity. 1 Publication
VAR_054712
Natural varianti243 – 2431P → L in MPS3B. 1 Publication
VAR_008982
Natural varianti246 – 2461A → P in MPS3B; produces 12.7% residual enzyme activity. 1 Publication
VAR_054713
Natural varianti248 – 2481H → R in MPS3B. 2 Publications
VAR_054714
Natural varianti268 – 2681W → R in MPS3B. 1 Publication
VAR_054715
Natural varianti277 – 2771C → F in MPS3B. 1 Publication
VAR_008983
Natural varianti280 – 2801L → P in MPS3B. 1 Publication
VAR_008984
Natural varianti292 – 2921G → R in MPS3B. 4 Publications
VAR_008985
Natural varianti309 – 3091Y → C in MPS3B; does not yield active enzyme. 2 Publications
VAR_054716
Natural varianti314 – 3141F → L in MPS3B. 1 Publication
VAR_025490
Natural varianti334 – 3341V → F in MPS3B. 1 Publication
VAR_054717
Natural varianti335 – 3351Y → C in MPS3B; decreases the enzyme activity markedly. 1 Publication
VAR_054718
Natural varianti358 – 3581P → L in MPS3B. 1 Publication
VAR_005011
Natural varianti410 – 4101F → S in MPS3B. 1 Publication
VAR_054719
Natural varianti412 – 4121G → E in MPS3B; does not yield active enzyme. 1 Publication
VAR_054720
Natural varianti414 – 4141H → R in MPS3B; no enzyme activity. 3 Publications
VAR_054721
Natural varianti437 – 4371T → I in MPS3B. 1 Publication
VAR_054722
Natural varianti446 – 4461E → K in MPS3B; no enzyme activity. 1 Publication
VAR_054723
Natural varianti452 – 4521E → K in MPS3B. 3 Publications
VAR_008986
Natural varianti455 – 4551Y → C in MPS3B. 1 Publication
VAR_054724
Natural varianti474 – 4741W → G in MPS3B. 1 Publication
VAR_054725
Natural varianti482 – 4821R → Q in MPS3B; no enzyme activity. 1 Publication
Corresponds to variant rs200909691 [ dbSNP | Ensembl ].
VAR_054726
Natural varianti482 – 4821R → W in MPS3B. 3 Publications
VAR_008987
Natural varianti501 – 5011V → G in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication
VAR_054727
Natural varianti516 – 5161P → L in MPS3B; no enzyme activity. 1 Publication
VAR_054728
Natural varianti520 – 5201R → W in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 2 Publications
VAR_054729
Natural varianti521 – 5211P → L in MPS3B; accounts for approximately 6% of mutations in Australasian patients with MPS3B. 4 Publications
VAR_025491
Natural varianti534 – 5341S → Y in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication
VAR_054730
Natural varianti560 – 5601L → P in MPS3B. 1 Publication
VAR_054731
Natural varianti561 – 5611L → R in MPS3B. 1 Publication
VAR_008988
Natural varianti565 – 5651R → P in MPS3B; does not yield active enzyme. 3 Publications
VAR_025492
Natural varianti565 – 5651R → Q in MPS3B. 1 Publication
VAR_008989
Natural varianti565 – 5651R → W in MPS3B; accounts for approximately 6% of the mutant alleles in Australasian patients with MPS3B. 6 Publications
VAR_025493
Natural varianti591 – 5911L → P in MPS3B. 1 Publication
VAR_054732
Natural varianti612 – 6121S → G in MPS3B. 1 Publication
VAR_054733
Natural varianti617 – 6171L → F in MPS3B. 1 Publication
VAR_054734
Natural varianti643 – 6431R → C in MPS3B; accounts for approximately 20% of MPS3B alleles in a Dutch patient group. 1 Publication
VAR_025494
Natural varianti643 – 6431R → H in MPS3B.
VAR_005012
Natural varianti649 – 6491W → C in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication
VAR_054735
Natural varianti650 – 6501G → E in MPS3B. 1 Publication
VAR_054736
Natural varianti658 – 6581Y → F in MPS3B. 1 Publication
VAR_054737
Natural varianti664 – 6641A → V in MPS3B. 1 Publication
VAR_005013
Natural varianti674 – 6741R → C in MPS3B. 2 Publications
VAR_054738
Natural varianti674 – 6741R → H in MPS3B. 2 Publications
VAR_005014
Natural varianti676 – 6761R → P in MPS3B. 1 Publication
VAR_054739
Natural varianti682 – 6821L → R in MPS3B. 2 Publications
VAR_005015
Natural varianti705 – 7051E → K in MPS3B. 2 Publications
VAR_008990

Keywords - Diseasei

Disease mutation, Mucopolysaccharidosis

Organism-specific databases

MIMi252920. phenotype.
Orphaneti79270. Sanfilippo syndrome type B.
PharmGKBiPA31437.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Add
BLAST
Chaini24 – 743720Alpha-N-acetylglucosaminidase 82 kDa formPRO_0000020728Add
BLAST
Chaini59 – 743685Alpha-N-acetylglucosaminidase 77 kDa formPRO_0000020729Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi261 – 2611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi272 – 2721N-linked (GlcNAc...)Sequence Analysis
Glycosylationi435 – 4351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi503 – 5031N-linked (GlcNAc...)Sequence Analysis
Glycosylationi526 – 5261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi532 – 5321N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP54802.
PaxDbiP54802.
PRIDEiP54802.

PTM databases

PhosphoSiteiP54802.

Expressioni

Tissue specificityi

Liver, ovary, peripheral blood leukocytes, testis, prostate, spleen, colon, lung, placenta and kidney.

Gene expression databases

BgeeiP54802.
CleanExiHS_NAGLU.
ExpressionAtlasiP54802. baseline and differential.
GenevestigatoriP54802.

Organism-specific databases

HPAiHPA038815.

Interactioni

Subunit structurei

Monomer and homodimer.

Protein-protein interaction databases

BioGridi110750. 9 interactions.
STRINGi9606.ENSP00000225927.

Structurei

3D structure databases

ProteinModelPortaliP54802.
SMRiP54802. Positions 32-735.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi68 – 714Poly-Gly
Compositional biasi84 – 874Poly-Ala

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG86381.
GeneTreeiENSGT00390000005900.
HOGENOMiHOG000214539.
HOVERGENiHBG004225.
InParanoidiP54802.
KOiK01205.
OMAiLFPNSTM.
OrthoDBiEOG751NF0.
PhylomeDBiP54802.
TreeFamiTF300689.

Family and domain databases

InterProiIPR017853. Glycoside_hydrolase_SF.
IPR007781. NAGLU.
IPR024732. NAGLU_C.
IPR024240. NAGLU_N.
IPR024733. NAGLU_tim-barrel.
[Graphical view]
PANTHERiPTHR12872. PTHR12872. 1 hit.
PfamiPF05089. NAGLU. 1 hit.
PF12972. NAGLU_C. 1 hit.
PF12971. NAGLU_N. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P54802-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MEAVAVAAAV GVLLLAGAGG AAGDEAREAA AVRALVARLL GPGPAADFSV
60 70 80 90 100
SVERALAAKP GLDTYSLGGG GAARVRVRGS TGVAAAAGLH RYLRDFCGCH
110 120 130 140 150
VAWSGSQLRL PRPLPAVPGE LTEATPNRYR YYQNVCTQSY SFVWWDWARW
160 170 180 190 200
EREIDWMALN GINLALAWSG QEAIWQRVYL ALGLTQAEIN EFFTGPAFLA
210 220 230 240 250
WGRMGNLHTW DGPLPPSWHI KQLYLQHRVL DQMRSFGMTP VLPAFAGHVP
260 270 280 290 300
EAVTRVFPQV NVTKMGSWGH FNCSYSCSFL LAPEDPIFPI IGSLFLRELI
310 320 330 340 350
KEFGTDHIYG ADTFNEMQPP SSEPSYLAAA TTAVYEAMTA VDTEAVWLLQ
360 370 380 390 400
GWLFQHQPQF WGPAQIRAVL GAVPRGRLLV LDLFAESQPV YTRTASFQGQ
410 420 430 440 450
PFIWCMLHNF GGNHGLFGAL EAVNGGPEAA RLFPNSTMVG TGMAPEGISQ
460 470 480 490 500
NEVVYSLMAE LGWRKDPVPD LAAWVTSFAA RRYGVSHPDA GAAWRLLLRS
510 520 530 540 550
VYNCSGEACR GHNRSPLVRR PSLQMNTSIW YNRSDVFEAW RLLLTSAPSL
560 570 580 590 600
ATSPAFRYDL LDLTRQAVQE LVSLYYEEAR SAYLSKELAS LLRAGGVLAY
610 620 630 640 650
ELLPALDEVL ASDSRFLLGS WLEQARAAAV SEAEADFYEQ NSRYQLTLWG
660 670 680 690 700
PEGNILDYAN KQLAGLVANY YTPRWRLFLE ALVDSVAQGI PFQQHQFDKN
710 720 730 740
VFQLEQAFVL SKQRYPSQPR GDTVDLAKKI FLKYYPRWVA GSW
Length:743
Mass (Da):82,266
Last modified:January 11, 2011 - v2
Checksum:i6D8D6A42C7BA7CF3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti551 – 5511A → L AA sequence (PubMed:8776591)Curated
Sequence conflicti553 – 5531S → L AA sequence (PubMed:8776591)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti35 – 351L → F in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication
VAR_054699
Natural varianti38 – 381R → W in MPS3B; decreases the enzyme activity markedly. 1 Publication
VAR_054700
Natural varianti48 – 481F → C in MPS3B. 1 Publication
VAR_054701
Natural varianti48 – 481F → L in MPS3B; associated with a partially degraded polypeptide in a 16-hour chase experiment suggesting that L-48 NAGLU affects the processing and stability of the gene; some L-48 NAGLU is being correctly sorted to the lysosomal compartment. 2 Publications
VAR_025489
Natural varianti69 – 691G → S in MPS3B. 1 Publication
VAR_054702
Natural varianti77 – 771V → G in MPS3B; decreases the enzyme activity markedly. 1 Publication
VAR_054703
Natural varianti79 – 791G → C in MPS3B. 2 Publications
VAR_008979
Natural varianti79 – 791G → S in MPS3B. 1 Publication
VAR_054704
Natural varianti82 – 821G → D in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication
VAR_054705
Natural varianti92 – 921Y → H in MPS3B. 1 Publication
VAR_005007
Natural varianti100 – 1001H → R in MPS3B. 1 Publication
VAR_008980
Natural varianti115 – 1151P → S in MPS3B. 1 Publication
VAR_005008
Natural varianti130 – 1301R → C in MPS3B; does not yield active enzyme. 2 Publications
VAR_054706
Natural varianti140 – 1401Y → C in MPS3B. 6 Publications
VAR_005009
Natural varianti142 – 1421Missing in MPS3B. 1 Publication
VAR_008981
Natural varianti153 – 1531E → K in MPS3B. 2 Publications
VAR_005010
Natural varianti154 – 1541I → R in MPS3B; does not yield active enzyme. 1 Publication
VAR_054707
Natural varianti156 – 1561W → C in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication
VAR_054708
Natural varianti227 – 2271H → P in MPS3B. 1 Publication
VAR_054709
Natural varianti234 – 2341R → C in MPS3B. 3 Publications
VAR_054710
Natural varianti241 – 2411V → M in MPS3B. 1 Publication
VAR_054711
Natural varianti242 – 2421L → P in MPS3B; no enzyme activity. 1 Publication
VAR_054712
Natural varianti243 – 2431P → L in MPS3B. 1 Publication
VAR_008982
Natural varianti246 – 2461A → P in MPS3B; produces 12.7% residual enzyme activity. 1 Publication
VAR_054713
Natural varianti248 – 2481H → R in MPS3B. 2 Publications
VAR_054714
Natural varianti268 – 2681W → R in MPS3B. 1 Publication
VAR_054715
Natural varianti277 – 2771C → F in MPS3B. 1 Publication
VAR_008983
Natural varianti280 – 2801L → P in MPS3B. 1 Publication
VAR_008984
Natural varianti292 – 2921G → R in MPS3B. 4 Publications
VAR_008985
Natural varianti309 – 3091Y → C in MPS3B; does not yield active enzyme. 2 Publications
VAR_054716
Natural varianti314 – 3141F → L in MPS3B. 1 Publication
VAR_025490
Natural varianti334 – 3341V → F in MPS3B. 1 Publication
VAR_054717
Natural varianti335 – 3351Y → C in MPS3B; decreases the enzyme activity markedly. 1 Publication
VAR_054718
Natural varianti358 – 3581P → L in MPS3B. 1 Publication
VAR_005011
Natural varianti410 – 4101F → S in MPS3B. 1 Publication
VAR_054719
Natural varianti412 – 4121G → E in MPS3B; does not yield active enzyme. 1 Publication
VAR_054720
Natural varianti414 – 4141H → R in MPS3B; no enzyme activity. 3 Publications
VAR_054721
Natural varianti437 – 4371T → I in MPS3B. 1 Publication
VAR_054722
Natural varianti446 – 4461E → K in MPS3B; no enzyme activity. 1 Publication
VAR_054723
Natural varianti452 – 4521E → K in MPS3B. 3 Publications
VAR_008986
Natural varianti455 – 4551Y → C in MPS3B. 1 Publication
VAR_054724
Natural varianti474 – 4741W → G in MPS3B. 1 Publication
VAR_054725
Natural varianti482 – 4821R → Q in MPS3B; no enzyme activity. 1 Publication
Corresponds to variant rs200909691 [ dbSNP | Ensembl ].
VAR_054726
Natural varianti482 – 4821R → W in MPS3B. 3 Publications
VAR_008987
Natural varianti501 – 5011V → G in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication
VAR_054727
Natural varianti516 – 5161P → L in MPS3B; no enzyme activity. 1 Publication
VAR_054728
Natural varianti520 – 5201R → W in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 2 Publications
VAR_054729
Natural varianti521 – 5211P → L in MPS3B; accounts for approximately 6% of mutations in Australasian patients with MPS3B. 4 Publications
VAR_025491
Natural varianti534 – 5341S → Y in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication
VAR_054730
Natural varianti560 – 5601L → P in MPS3B. 1 Publication
VAR_054731
Natural varianti561 – 5611L → R in MPS3B. 1 Publication
VAR_008988
Natural varianti565 – 5651R → P in MPS3B; does not yield active enzyme. 3 Publications
VAR_025492
Natural varianti565 – 5651R → Q in MPS3B. 1 Publication
VAR_008989
Natural varianti565 – 5651R → W in MPS3B; accounts for approximately 6% of the mutant alleles in Australasian patients with MPS3B. 6 Publications
VAR_025493
Natural varianti591 – 5911L → P in MPS3B. 1 Publication
VAR_054732
Natural varianti612 – 6121S → G in MPS3B. 1 Publication
VAR_054733
Natural varianti617 – 6171L → F in MPS3B. 1 Publication
VAR_054734
Natural varianti643 – 6431R → C in MPS3B; accounts for approximately 20% of MPS3B alleles in a Dutch patient group. 1 Publication
VAR_025494
Natural varianti643 – 6431R → H in MPS3B.
VAR_005012
Natural varianti649 – 6491W → C in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication
VAR_054735
Natural varianti650 – 6501G → E in MPS3B. 1 Publication
VAR_054736
Natural varianti658 – 6581Y → F in MPS3B. 1 Publication
VAR_054737
Natural varianti664 – 6641A → V in MPS3B. 1 Publication
VAR_005013
Natural varianti674 – 6741R → C in MPS3B. 2 Publications
VAR_054738
Natural varianti674 – 6741R → H in MPS3B. 2 Publications
VAR_005014
Natural varianti676 – 6761R → P in MPS3B. 1 Publication
VAR_054739
Natural varianti682 – 6821L → R in MPS3B. 2 Publications
VAR_005015
Natural varianti705 – 7051E → K in MPS3B. 2 Publications
VAR_008990
Natural varianti737 – 7371R → G.6 Publications
Corresponds to variant rs86312 [ dbSNP | Ensembl ].
VAR_008991

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U43572 Genomic DNA. Translation: AAC50512.1.
U43573 mRNA. Translation: AAC50513.1.
U40846 mRNA. Translation: AAB06188.1.
L78464 mRNA. Translation: AAB36604.1.
AC067852 Genomic DNA. No translation available.
BC053991 mRNA. Translation: AAH53991.1.
CCDSiCCDS11427.1.
PIRiG02270.
RefSeqiNP_000254.2. NM_000263.3.
UniGeneiHs.50727.

Genome annotation databases

EnsembliENST00000225927; ENSP00000225927; ENSG00000108784.
GeneIDi4669.
KEGGihsa:4669.
UCSCiuc002hzv.3. human.

Polymorphism databases

DMDMi317373322.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U43572 Genomic DNA. Translation: AAC50512.1 .
U43573 mRNA. Translation: AAC50513.1 .
U40846 mRNA. Translation: AAB06188.1 .
L78464 mRNA. Translation: AAB36604.1 .
AC067852 Genomic DNA. No translation available.
BC053991 mRNA. Translation: AAH53991.1 .
CCDSi CCDS11427.1.
PIRi G02270.
RefSeqi NP_000254.2. NM_000263.3.
UniGenei Hs.50727.

3D structure databases

ProteinModelPortali P54802.
SMRi P54802. Positions 32-735.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110750. 9 interactions.
STRINGi 9606.ENSP00000225927.

Chemistry

DrugBanki DB00141. N-Acetyl-D-glucosamine.

Protein family/group databases

CAZyi GH89. Glycoside Hydrolase Family 89.

PTM databases

PhosphoSitei P54802.

Polymorphism databases

DMDMi 317373322.

Proteomic databases

MaxQBi P54802.
PaxDbi P54802.
PRIDEi P54802.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000225927 ; ENSP00000225927 ; ENSG00000108784 .
GeneIDi 4669.
KEGGi hsa:4669.
UCSCi uc002hzv.3. human.

Organism-specific databases

CTDi 4669.
GeneCardsi GC17P040687.
H-InvDB HIX0202517.
HGNCi HGNC:7632. NAGLU.
HPAi HPA038815.
MIMi 252920. phenotype.
609701. gene.
neXtProti NX_P54802.
Orphaneti 79270. Sanfilippo syndrome type B.
PharmGKBi PA31437.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG86381.
GeneTreei ENSGT00390000005900.
HOGENOMi HOG000214539.
HOVERGENi HBG004225.
InParanoidi P54802.
KOi K01205.
OMAi LFPNSTM.
OrthoDBi EOG751NF0.
PhylomeDBi P54802.
TreeFami TF300689.

Enzyme and pathway databases

Reactomei REACT_120752. HS-GAG degradation.

Miscellaneous databases

ChiTaRSi NAGLU. human.
GenomeRNAii 4669.
NextBioi 17990.
PROi P54802.
SOURCEi Search...

Gene expression databases

Bgeei P54802.
CleanExi HS_NAGLU.
ExpressionAtlasi P54802. baseline and differential.
Genevestigatori P54802.

Family and domain databases

InterProi IPR017853. Glycoside_hydrolase_SF.
IPR007781. NAGLU.
IPR024732. NAGLU_C.
IPR024240. NAGLU_N.
IPR024733. NAGLU_tim-barrel.
[Graphical view ]
PANTHERi PTHR12872. PTHR12872. 1 hit.
Pfami PF05089. NAGLU. 1 hit.
PF12972. NAGLU_C. 1 hit.
PF12971. NAGLU_N. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT GLY-737.
    Tissue: Testis.
  2. "Cloning and expression of the gene involved in Sanfilippo B syndrome (mucopolysaccharidosis III B)."
    Weber B., Blanch L., Clements P.R., Scott H.S., Hopwood J.J.
    Hum. Mol. Genet. 5:771-777(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION, VARIANT GLY-737.
  3. "Molecular dissection of a cosmid from a gene-rich region in 17q21 and characterization of a candidate gene for alpha-N-acetylglucosaminidase with two cDNA isoforms."
    Zhao Z., Yazdani A., Shen Y., Sun Z.S., Bailey J., Caskey C.T., Lee C.C.
    Mamm. Genome 7:686-690(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLY-737.
  4. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLY-737.
    Tissue: Skin.
  6. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-532.
    Tissue: Liver.
  7. "Genotype-phenotype correspondence in Sanfilippo syndrome type B."
    Zhao H.G., Aronovich E.L., Whitley C.B.
    Am. J. Hum. Genet. 62:53-63(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MPS3B CYS-140; CYS-455; LEU-521; GLY-612; CYS-674 AND HIS-674.
  8. Cited for: VARIANTS MPS3B HIS-92; SER-115; CYS-140; LYS-153; LEU-358; VAL-664 AND ARG-682.
  9. "Identification of 12 novel mutations in the alpha-N-acetylglucosaminidase gene in 14 patients with Sanfilippo syndrome type B (mucopolysaccharidosis type IIIB)."
    Beesley C.E., Young E.P., Vellodi A., Winchester B.G.
    J. Med. Genet. 35:910-914(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MPS3B CYS-48; CYS-140; CYS-234; ARG-268; LEU-521; TRP-565; PRO-591 AND LYS-705.
  10. "Mucopolysaccharidosis type IIIB (Sanfilippo B): identification of 18 novel alpha-N-acetylglucosaminidase gene mutations."
    Bunge S., Knigge A., Steglich C., Kleijer W.J., van Diggelen O.P., Beck M., Gal A.
    J. Med. Genet. 36:28-31(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MPS3B CYS-79; ARG-100; CYS-140; PHE-142 DEL; LEU-243; PHE-277; PRO-280; ARG-292; LYS-452; TRP-482; ARG-561; GLN-565; HIS-674 AND LYS-705, VARIANT GLY-737.
  11. "Sanfilippo type B syndrome (mucopolysaccharidosis III B): allelic heterogeneity corresponds to the wide spectrum of clinical phenotypes."
    Weber B., Guo X.-H., Kleijer W.J., van de Kamp J.J.P., Poorthuis B.J.H.M., Hopwood J.J.
    Eur. J. Hum. Genet. 7:34-44(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MPS3B LEU-48; SER-69; PRO-227; ARG-248; ARG-292; PHE-334; SER-410; ARG-414; LEU-521; PRO-560; PRO-565; TRP-565; PHE-617; CYS-643; GLU-650; CYS-674 AND PRO-676, VARIANT GLY-737.
  12. "Mucopolysaccharidosis type IIIB: characterisation and expression of wild-type and mutant recombinant alpha-N-acetylglucosaminidase and relationship with sanfilippo phenotype in an attenuated patient."
    Yogalingam G., Weber B., Meehan J., Rogers J., Hopwood J.J.
    Biochim. Biophys. Acta 1502:415-425(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MPS3B LEU-48, CHARACTERIZATION OF VARIANT MPS3B LEU-48.
  13. "Molecular defects in the alpha-N-acetylglucosaminidase gene in Italian Sanfilippo type B patients."
    Tessitore A., Villani G.R.D., Di Domenico C., Filocamo M., Gatti R., Di Natale P.
    Hum. Genet. 107:568-576(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MPS3B PHE-35; ASP-82; CYS-140; CYS-156; CYS-234; ARG-292; GLY-501; TRP-520; TYR-534 AND CYS-649, CHARACTERIZATION OF VARIANTS MPS3B PHE-35; ASP-82; CYS-156; GLY-501; TRP-520; TYR-534 AND CYS-649.
  14. "Allelic heterogeneity in Spanish patients with Sanfilippo disease type B. Identification of eight new mutations."
    Coll M.J., Anton C., Chabas A.
    J. Inherit. Metab. Dis. 24:83-84(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MPS3B SER-79; CYS-234; GLY-474; TRP-565 AND PHE-658.
  15. "Sanfilippo syndrome in Turkey: identification of novel mutations in subtypes A and B."
    Emre S., Terzioglu M., Tokatli A., Coskun T., Ozalp I., Weber B., Hopwood J.J.
    Hum. Mutat. 19:184-185(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MPS3B LYS-153; ARG-248; ILE-437 AND ARG-682.
  16. "Molecular analysis of the alpha-N-acetylglucosaminidase gene in seven Japanese patients from six unrelated families with mucopolysaccharidosis IIIB (Sanfilippo type B), including two novel mutations."
    Tanaka A., Kimura M., Lan H.T.N., Takaura N., Yamano T.
    J. Hum. Genet. 47:484-487(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MPS3B MET-241; LEU-314; TRP-482; PRO-565 AND TRP-565.
  17. "Identification and characterisation of mutations underlying Sanfilippo syndrome type B (mucopolysaccharidosis type IIIB)."
    Lee-Chen G.J., Lin S.P., Lin S.Z., Chuang C.K., Hsiao K.T., Huang C.F., Lien W.C.
    J. Med. Genet. 39:E3-E3(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MPS3B CYS-130; ARG-154; CYS-309; GLU-412 AND TRP-565, CHARACTERIZATION OF VARIANTS MPS3B CYS-130; ARG-154; CYS-309; GLU-412 AND TRP-565.
  18. Cited for: VARIANTS MPS3B CYS-140; PRO-242; ARG-292; ARG-414; LYS-446; LYS-452; GLN-482 AND LEU-516, CHARACTERIZATION OF VARIANTS MPS3B PRO-242; ARG-414; LYS-446; GLN-482 AND LEU-516.
  19. "Sanfilippo type B syndrome: five patients with an R565P homozygous mutation in the alpha-N-acetylglucosaminidase gene from the Okinawa islands in Japan."
    Chinen Y., Tohma T., Izumikawa Y., Uehara H., Ohta T.
    J. Hum. Genet. 50:357-359(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MPS3B PRO-565.
  20. "Molecular defects in Sanfilippo syndrome type B (mucopolysaccharidosis IIIB)."
    Beesley C.E., Jackson M., Young E.P., Vellodi A., Winchester B.G.
    J. Inherit. Metab. Dis. 28:759-767(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MPS3B TRP-38; GLY-77; CYS-79; CYS-130; PRO-246; CYS-309; CYS-335; ARG-414; LYS-452; TRP-482; TRP-520; LEU-521 AND TRP-565, CHARACTERIZATION OF VARIANTS MPS3B TRP-38; GLY-77 AND CYS-335.

Entry informationi

Entry nameiANAG_HUMAN
AccessioniPrimary (citable) accession number: P54802
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 11, 2011
Last modified: October 29, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

A MPS3B mutation at position 100 was erroneously reported (PubMed:9950362) as an amino acid change from Arg to His. The right amino acid change is from His to Arg.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

External Data

Dasty 3