Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Alpha-N-acetylglucosaminidase

Gene

NAGLU

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciZFISH:HS03153-MONOMER.
BRENDAi3.2.1.50. 2681.
ReactomeiR-HSA-2024096. 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
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:7632. NAGLU.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • lysosomal lumen Source: Reactome
  • lysosome Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Involvement in diseasei

Mucopolysaccharidosis 3B (MPS3B)14 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:252920
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05469935L → F in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication1
Natural variantiVAR_05470038R → W in MPS3B; decreases the enzyme activity markedly. 1 Publication1
Natural variantiVAR_05470148F → C in MPS3B. 1 Publication1
Natural variantiVAR_02548948F → 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 PublicationsCorresponds to variant rs104894599dbSNPEnsembl.1
Natural variantiVAR_05470269G → S in MPS3B. 1 Publication1
Natural variantiVAR_05470377V → G in MPS3B; decreases the enzyme activity markedly. 1 Publication1
Natural variantiVAR_00897979G → C in MPS3B. 2 Publications1
Natural variantiVAR_05470479G → S in MPS3B. 1 Publication1
Natural variantiVAR_05470582G → D in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication1
Natural variantiVAR_00500792Y → H in MPS3B. 1 Publication1
Natural variantiVAR_008980100H → R in MPS3B. 1 Publication1
Natural variantiVAR_005008115P → S in MPS3B. 1 PublicationCorresponds to variant rs758785463dbSNPEnsembl.1
Natural variantiVAR_054706130R → C in MPS3B; does not yield active enzyme. 2 Publications1
Natural variantiVAR_005009140Y → C in MPS3B. 6 PublicationsCorresponds to variant rs753520553dbSNPEnsembl.1
Natural variantiVAR_008981142Missing in MPS3B. 1 Publication1
Natural variantiVAR_005010153E → K in MPS3B. 2 Publications1
Natural variantiVAR_054707154I → R in MPS3B; does not yield active enzyme. 1 PublicationCorresponds to variant rs770684838dbSNPEnsembl.1
Natural variantiVAR_054708156W → C in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication1
Natural variantiVAR_054709227H → P in MPS3B. 1 PublicationCorresponds to variant rs747155746dbSNPEnsembl.1
Natural variantiVAR_054710234R → C in MPS3B. 3 PublicationsCorresponds to variant rs104894601dbSNPEnsembl.1
Natural variantiVAR_054711241V → M in MPS3B. 1 Publication1
Natural variantiVAR_054712242L → P in MPS3B; no enzyme activity. 1 Publication1
Natural variantiVAR_008982243P → L in MPS3B. 1 Publication1
Natural variantiVAR_054713246A → P in MPS3B; produces 12.7% residual enzyme activity. 1 Publication1
Natural variantiVAR_054714248H → R in MPS3B. 2 Publications1
Natural variantiVAR_054715268W → R in MPS3B. 1 Publication1
Natural variantiVAR_008983277C → F in MPS3B. 1 Publication1
Natural variantiVAR_008984280L → P in MPS3B. 1 Publication1
Natural variantiVAR_008985292G → R in MPS3B. 4 Publications1
Natural variantiVAR_054716309Y → C in MPS3B; does not yield active enzyme. 2 Publications1
Natural variantiVAR_025490314F → L in MPS3B. 1 PublicationCorresponds to variant rs104894600dbSNPEnsembl.1
Natural variantiVAR_054717334V → F in MPS3B. 1 PublicationCorresponds to variant rs749140168dbSNPEnsembl.1
Natural variantiVAR_054718335Y → C in MPS3B; decreases the enzyme activity markedly. 1 PublicationCorresponds to variant rs768918822dbSNPEnsembl.1
Natural variantiVAR_005011358P → L in MPS3B. 1 PublicationCorresponds to variant rs368687817dbSNPEnsembl.1
Natural variantiVAR_054719410F → S in MPS3B. 1 PublicationCorresponds to variant rs574688121dbSNPEnsembl.1
Natural variantiVAR_054720412G → E in MPS3B; does not yield active enzyme. 1 Publication1
Natural variantiVAR_054721414H → R in MPS3B; no enzyme activity. 3 PublicationsCorresponds to variant rs768814260dbSNPEnsembl.1
Natural variantiVAR_054722437T → I in MPS3B. 1 Publication1
Natural variantiVAR_054723446E → K in MPS3B; no enzyme activity. 1 PublicationCorresponds to variant rs114625063dbSNPEnsembl.1
Natural variantiVAR_008986452E → K in MPS3B. 3 Publications1
Natural variantiVAR_054724455Y → C in MPS3B. 1 PublicationCorresponds to variant rs375103824dbSNPEnsembl.1
Natural variantiVAR_054725474W → G in MPS3B. 1 Publication1
Natural variantiVAR_054726482R → Q in MPS3B; no enzyme activity. 1 PublicationCorresponds to variant rs200909691dbSNPEnsembl.1
Natural variantiVAR_008987482R → W in MPS3B. 3 PublicationsCorresponds to variant rs104894596dbSNPEnsembl.1
Natural variantiVAR_054727501V → G in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication1
Natural variantiVAR_054728516P → L in MPS3B; no enzyme activity. 1 PublicationCorresponds to variant rs773054539dbSNPEnsembl.1
Natural variantiVAR_054729520R → W in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 2 Publications1
Natural variantiVAR_025491521P → L in MPS3B; accounts for approximately 6% of mutations in Australasian patients with MPS3B. 4 PublicationsCorresponds to variant rs104894595dbSNPEnsembl.1
Natural variantiVAR_054730534S → Y in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication1
Natural variantiVAR_054731560L → P in MPS3B. 1 Publication1
Natural variantiVAR_008988561L → R in MPS3B. 1 Publication1
Natural variantiVAR_025492565R → P in MPS3B; does not yield active enzyme. 3 PublicationsCorresponds to variant rs104894598dbSNPEnsembl.1
Natural variantiVAR_008989565R → Q in MPS3B. 1 PublicationCorresponds to variant rs104894598dbSNPEnsembl.1
Natural variantiVAR_025493565R → W in MPS3B; accounts for approximately 6% of the mutant alleles in Australasian patients with MPS3B. 6 PublicationsCorresponds to variant rs104894597dbSNPEnsembl.1
Natural variantiVAR_054732591L → P in MPS3B. 1 Publication1
Natural variantiVAR_054733612S → G in MPS3B. 1 PublicationCorresponds to variant rs148881970dbSNPEnsembl.1
Natural variantiVAR_054734617L → F in MPS3B. 1 Publication1
Natural variantiVAR_025494643R → C in MPS3B; accounts for approximately 20% of MPS3B alleles in a Dutch patient group. 1 PublicationCorresponds to variant rs104894594dbSNPEnsembl.1
Natural variantiVAR_005012643R → H in MPS3B. Corresponds to variant rs104894593dbSNPEnsembl.1
Natural variantiVAR_054735649W → C in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication1
Natural variantiVAR_054736650G → E in MPS3B. 1 PublicationCorresponds to variant rs527236037dbSNPEnsembl.1
Natural variantiVAR_054737658Y → F in MPS3B. 1 Publication1
Natural variantiVAR_005013664A → V in MPS3B. 1 PublicationCorresponds to variant rs746006696dbSNPEnsembl.1
Natural variantiVAR_054738674R → C in MPS3B. 2 PublicationsCorresponds to variant rs763299645dbSNPEnsembl.1
Natural variantiVAR_005014674R → H in MPS3B. 2 PublicationsCorresponds to variant rs104894590dbSNPEnsembl.1
Natural variantiVAR_054739676R → P in MPS3B. 1 Publication1
Natural variantiVAR_005015682L → R in MPS3B. 2 Publications1
Natural variantiVAR_008990705E → K in MPS3B. 2 Publications1
Charcot-Marie-Tooth disease 2V (CMT2V)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. CMT2V is an autosomal dominant sensory neuropathy with late onset. The main clinical feature is recurrent leg pain that progresses to constant painful paraesthesias in the feet and later the hands. As it evolves, some patients develop a mild sensory ataxia.
See also OMIM:616491
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_074607403I → T in CMT2V. 1 PublicationCorresponds to variant rs796052122dbSNPEnsembl.1

Keywords - Diseasei

Charcot-Marie-Tooth disease, Disease mutation, Mucopolysaccharidosis, Neurodegeneration, Neuropathy

Organism-specific databases

DisGeNETi4669.
MalaCardsiNAGLU.
MIMi252920. phenotype.
616491. phenotype.
OpenTargetsiENSG00000108784.
Orphaneti79270. Sanfilippo syndrome type B.
PharmGKBiPA31437.

Chemistry databases

DrugBankiDB00141. N-Acetyl-D-glucosamine.

Polymorphism and mutation databases

BioMutaiNAGLU.
DMDMi317373322.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Add BLAST23
ChainiPRO_000002072824 – 743Alpha-N-acetylglucosaminidase 82 kDa formAdd BLAST720
ChainiPRO_000002072959 – 743Alpha-N-acetylglucosaminidase 77 kDa formAdd BLAST685

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi261N-linked (GlcNAc...)Combined sources1 Publication1
Glycosylationi272N-linked (GlcNAc...)Combined sources1 Publication1
Glycosylationi435N-linked (GlcNAc...)Combined sources1 Publication1
Glycosylationi503N-linked (GlcNAc...)Combined sources1 Publication1
Glycosylationi526N-linked (GlcNAc...)Combined sources1 Publication1
Glycosylationi532N-linked (GlcNAc...)Combined sources2 Publications1

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiP54802.
MaxQBiP54802.
PaxDbiP54802.
PeptideAtlasiP54802.
PRIDEiP54802.
TopDownProteomicsiP54802.

PTM databases

iPTMnetiP54802.
PhosphoSitePlusiP54802.
UniCarbKBiP54802.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000108784.
CleanExiHS_NAGLU.
ExpressionAtlasiP54802. baseline and differential.
GenevisibleiP54802. HS.

Organism-specific databases

HPAiHPA038815.

Interactioni

Subunit structurei

Monomer and homodimer.

Protein-protein interaction databases

BioGridi110750. 23 interactors.
STRINGi9606.ENSP00000225927.

Structurei

Secondary structure

1743
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi25 – 40Combined sources16
Helixi42 – 45Combined sources4
Beta strandi48 – 52Combined sources5
Helixi54 – 56Combined sources3
Beta strandi64 – 69Combined sources6
Beta strandi75 – 81Combined sources7
Helixi82 – 95Combined sources14
Beta strandi100 – 102Combined sources3
Beta strandi105 – 107Combined sources3
Beta strandi121 – 124Combined sources4
Beta strandi128 – 132Combined sources5
Helixi137 – 140Combined sources4
Helixi147 – 159Combined sources13
Beta strandi164 – 166Combined sources3
Helixi171 – 182Combined sources12
Helixi186 – 192Combined sources7
Helixi196 – 198Combined sources3
Helixi199 – 203Combined sources5
Helixi216 – 235Combined sources20
Beta strandi239 – 243Combined sources5
Beta strandi247 – 249Combined sources3
Helixi253 – 256Combined sources4
Beta strandi262 – 264Combined sources3
Turni273 – 275Combined sources3
Beta strandi279 – 281Combined sources3
Helixi287 – 303Combined sources17
Beta strandi307 – 310Combined sources4
Helixi324 – 339Combined sources16
Beta strandi346 – 350Combined sources5
Helixi352 – 356Combined sources5
Turni358 – 360Combined sources3
Helixi363 – 370Combined sources8
Beta strandi377 – 382Combined sources6
Turni383 – 387Combined sources5
Helixi391 – 393Combined sources3
Helixi395 – 398Combined sources4
Beta strandi402 – 406Combined sources5
Helixi420 – 432Combined sources13
Beta strandi438 – 443Combined sources6
Helixi452 – 461Combined sources10
Helixi471 – 483Combined sources13
Helixi488 – 499Combined sources12
Turni500 – 502Combined sources3
Helixi516 – 518Combined sources3
Helixi533 – 545Combined sources13
Helixi547 – 550Combined sources4
Helixi554 – 584Combined sources31
Helixi588 – 600Combined sources13
Helixi602 – 610Combined sources9
Helixi614 – 616Combined sources3
Helixi618 – 628Combined sources11
Helixi632 – 646Combined sources15
Turni654 – 659Combined sources6
Helixi666 – 669Combined sources4
Helixi671 – 687Combined sources17
Helixi694 – 710Combined sources17
Helixi723 – 740Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4XWHX-ray2.32A24-743[»]
ProteinModelPortaliP54802.
SMRiP54802.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi68 – 71Poly-Gly4
Compositional biasi84 – 87Poly-Ala4

Sequence similaritiesi

Belongs to the glycosyl hydrolase 89 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2233. Eukaryota.
ENOG410XNMK. LUCA.
GeneTreeiENSGT00390000005900.
HOGENOMiHOG000214539.
HOVERGENiHBG004225.
InParanoidiP54802.
KOiK01205.
OMAiVAKPEYM.
OrthoDBiEOG091G02QN.
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

« Hide

        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)DescriptionActionsGraphical viewLength
Sequence conflicti551A → L AA sequence (PubMed:8776591).Curated1
Sequence conflicti553S → L AA sequence (PubMed:8776591).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05469935L → F in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication1
Natural variantiVAR_05470038R → W in MPS3B; decreases the enzyme activity markedly. 1 Publication1
Natural variantiVAR_05470148F → C in MPS3B. 1 Publication1
Natural variantiVAR_02548948F → 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 PublicationsCorresponds to variant rs104894599dbSNPEnsembl.1
Natural variantiVAR_05470269G → S in MPS3B. 1 Publication1
Natural variantiVAR_05470377V → G in MPS3B; decreases the enzyme activity markedly. 1 Publication1
Natural variantiVAR_00897979G → C in MPS3B. 2 Publications1
Natural variantiVAR_05470479G → S in MPS3B. 1 Publication1
Natural variantiVAR_05470582G → D in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication1
Natural variantiVAR_00500792Y → H in MPS3B. 1 Publication1
Natural variantiVAR_008980100H → R in MPS3B. 1 Publication1
Natural variantiVAR_005008115P → S in MPS3B. 1 PublicationCorresponds to variant rs758785463dbSNPEnsembl.1
Natural variantiVAR_054706130R → C in MPS3B; does not yield active enzyme. 2 Publications1
Natural variantiVAR_005009140Y → C in MPS3B. 6 PublicationsCorresponds to variant rs753520553dbSNPEnsembl.1
Natural variantiVAR_008981142Missing in MPS3B. 1 Publication1
Natural variantiVAR_005010153E → K in MPS3B. 2 Publications1
Natural variantiVAR_054707154I → R in MPS3B; does not yield active enzyme. 1 PublicationCorresponds to variant rs770684838dbSNPEnsembl.1
Natural variantiVAR_054708156W → C in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication1
Natural variantiVAR_054709227H → P in MPS3B. 1 PublicationCorresponds to variant rs747155746dbSNPEnsembl.1
Natural variantiVAR_054710234R → C in MPS3B. 3 PublicationsCorresponds to variant rs104894601dbSNPEnsembl.1
Natural variantiVAR_054711241V → M in MPS3B. 1 Publication1
Natural variantiVAR_054712242L → P in MPS3B; no enzyme activity. 1 Publication1
Natural variantiVAR_008982243P → L in MPS3B. 1 Publication1
Natural variantiVAR_054713246A → P in MPS3B; produces 12.7% residual enzyme activity. 1 Publication1
Natural variantiVAR_054714248H → R in MPS3B. 2 Publications1
Natural variantiVAR_054715268W → R in MPS3B. 1 Publication1
Natural variantiVAR_008983277C → F in MPS3B. 1 Publication1
Natural variantiVAR_008984280L → P in MPS3B. 1 Publication1
Natural variantiVAR_008985292G → R in MPS3B. 4 Publications1
Natural variantiVAR_054716309Y → C in MPS3B; does not yield active enzyme. 2 Publications1
Natural variantiVAR_025490314F → L in MPS3B. 1 PublicationCorresponds to variant rs104894600dbSNPEnsembl.1
Natural variantiVAR_054717334V → F in MPS3B. 1 PublicationCorresponds to variant rs749140168dbSNPEnsembl.1
Natural variantiVAR_054718335Y → C in MPS3B; decreases the enzyme activity markedly. 1 PublicationCorresponds to variant rs768918822dbSNPEnsembl.1
Natural variantiVAR_005011358P → L in MPS3B. 1 PublicationCorresponds to variant rs368687817dbSNPEnsembl.1
Natural variantiVAR_074607403I → T in CMT2V. 1 PublicationCorresponds to variant rs796052122dbSNPEnsembl.1
Natural variantiVAR_054719410F → S in MPS3B. 1 PublicationCorresponds to variant rs574688121dbSNPEnsembl.1
Natural variantiVAR_054720412G → E in MPS3B; does not yield active enzyme. 1 Publication1
Natural variantiVAR_054721414H → R in MPS3B; no enzyme activity. 3 PublicationsCorresponds to variant rs768814260dbSNPEnsembl.1
Natural variantiVAR_054722437T → I in MPS3B. 1 Publication1
Natural variantiVAR_054723446E → K in MPS3B; no enzyme activity. 1 PublicationCorresponds to variant rs114625063dbSNPEnsembl.1
Natural variantiVAR_008986452E → K in MPS3B. 3 Publications1
Natural variantiVAR_054724455Y → C in MPS3B. 1 PublicationCorresponds to variant rs375103824dbSNPEnsembl.1
Natural variantiVAR_054725474W → G in MPS3B. 1 Publication1
Natural variantiVAR_054726482R → Q in MPS3B; no enzyme activity. 1 PublicationCorresponds to variant rs200909691dbSNPEnsembl.1
Natural variantiVAR_008987482R → W in MPS3B. 3 PublicationsCorresponds to variant rs104894596dbSNPEnsembl.1
Natural variantiVAR_054727501V → G in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication1
Natural variantiVAR_054728516P → L in MPS3B; no enzyme activity. 1 PublicationCorresponds to variant rs773054539dbSNPEnsembl.1
Natural variantiVAR_054729520R → W in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 2 Publications1
Natural variantiVAR_025491521P → L in MPS3B; accounts for approximately 6% of mutations in Australasian patients with MPS3B. 4 PublicationsCorresponds to variant rs104894595dbSNPEnsembl.1
Natural variantiVAR_054730534S → Y in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication1
Natural variantiVAR_054731560L → P in MPS3B. 1 Publication1
Natural variantiVAR_008988561L → R in MPS3B. 1 Publication1
Natural variantiVAR_025492565R → P in MPS3B; does not yield active enzyme. 3 PublicationsCorresponds to variant rs104894598dbSNPEnsembl.1
Natural variantiVAR_008989565R → Q in MPS3B. 1 PublicationCorresponds to variant rs104894598dbSNPEnsembl.1
Natural variantiVAR_025493565R → W in MPS3B; accounts for approximately 6% of the mutant alleles in Australasian patients with MPS3B. 6 PublicationsCorresponds to variant rs104894597dbSNPEnsembl.1
Natural variantiVAR_054732591L → P in MPS3B. 1 Publication1
Natural variantiVAR_054733612S → G in MPS3B. 1 PublicationCorresponds to variant rs148881970dbSNPEnsembl.1
Natural variantiVAR_054734617L → F in MPS3B. 1 Publication1
Natural variantiVAR_025494643R → C in MPS3B; accounts for approximately 20% of MPS3B alleles in a Dutch patient group. 1 PublicationCorresponds to variant rs104894594dbSNPEnsembl.1
Natural variantiVAR_005012643R → H in MPS3B. Corresponds to variant rs104894593dbSNPEnsembl.1
Natural variantiVAR_054735649W → C in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type. 1 Publication1
Natural variantiVAR_054736650G → E in MPS3B. 1 PublicationCorresponds to variant rs527236037dbSNPEnsembl.1
Natural variantiVAR_054737658Y → F in MPS3B. 1 Publication1
Natural variantiVAR_005013664A → V in MPS3B. 1 PublicationCorresponds to variant rs746006696dbSNPEnsembl.1
Natural variantiVAR_054738674R → C in MPS3B. 2 PublicationsCorresponds to variant rs763299645dbSNPEnsembl.1
Natural variantiVAR_005014674R → H in MPS3B. 2 PublicationsCorresponds to variant rs104894590dbSNPEnsembl.1
Natural variantiVAR_054739676R → P in MPS3B. 1 Publication1
Natural variantiVAR_005015682L → R in MPS3B. 2 Publications1
Natural variantiVAR_008990705E → K in MPS3B. 2 Publications1
Natural variantiVAR_008991737R → G.6 PublicationsCorresponds to variant rs86312dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4XWHX-ray2.32A24-743[»]
ProteinModelPortaliP54802.
SMRiP54802.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110750. 23 interactors.
STRINGi9606.ENSP00000225927.

Chemistry databases

DrugBankiDB00141. N-Acetyl-D-glucosamine.

Protein family/group databases

CAZyiGH89. Glycoside Hydrolase Family 89.

PTM databases

iPTMnetiP54802.
PhosphoSitePlusiP54802.
UniCarbKBiP54802.

Polymorphism and mutation databases

BioMutaiNAGLU.
DMDMi317373322.

Proteomic databases

EPDiP54802.
MaxQBiP54802.
PaxDbiP54802.
PeptideAtlasiP54802.
PRIDEiP54802.
TopDownProteomicsiP54802.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000225927; ENSP00000225927; ENSG00000108784.
GeneIDi4669.
KEGGihsa:4669.
UCSCiuc002hzv.4. human.

Organism-specific databases

CTDi4669.
DisGeNETi4669.
GeneCardsiNAGLU.
H-InvDBHIX0202517.
HGNCiHGNC:7632. NAGLU.
HPAiHPA038815.
MalaCardsiNAGLU.
MIMi252920. phenotype.
609701. gene.
616491. phenotype.
neXtProtiNX_P54802.
OpenTargetsiENSG00000108784.
Orphaneti79270. Sanfilippo syndrome type B.
PharmGKBiPA31437.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2233. Eukaryota.
ENOG410XNMK. LUCA.
GeneTreeiENSGT00390000005900.
HOGENOMiHOG000214539.
HOVERGENiHBG004225.
InParanoidiP54802.
KOiK01205.
OMAiVAKPEYM.
OrthoDBiEOG091G02QN.
PhylomeDBiP54802.
TreeFamiTF300689.

Enzyme and pathway databases

BioCyciZFISH:HS03153-MONOMER.
BRENDAi3.2.1.50. 2681.
ReactomeiR-HSA-2024096. HS-GAG degradation.

Miscellaneous databases

ChiTaRSiNAGLU. human.
GenomeRNAii4669.
PROiP54802.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000108784.
CleanExiHS_NAGLU.
ExpressionAtlasiP54802. baseline and differential.
GenevisibleiP54802. HS.

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.
ProtoNetiSearch...

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: November 30, 2016
This is version 161 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

3D-structure, 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
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.