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P08236

- BGLR_HUMAN

UniProt

P08236 - BGLR_HUMAN

Protein

Beta-glucuronidase

Gene

GUSB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 2 (01 May 2007)
      Previous versions | rss
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    Functioni

    Plays an important role in the degradation of dermatan and keratan sulfates.

    Catalytic activityi

    A beta-D-glucuronoside + H2O = D-glucuronate + an alcohol.

    Enzyme regulationi

    Inhibited by L-aspartic acid.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei451 – 4511Proton donor

    GO - Molecular functioni

    1. beta-glucuronidase activity Source: Reactome

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. glycosaminoglycan catabolic process Source: Reactome
    3. glycosaminoglycan metabolic process Source: Reactome
    4. hyaluronan catabolic process Source: Reactome
    5. hyaluronan metabolic process Source: Reactome
    6. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    ReactomeiREACT_120752. HS-GAG degradation.
    REACT_120996. Hyaluronan uptake and degradation.

    Protein family/group databases

    CAZyiGH2. Glycoside Hydrolase Family 2.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-glucuronidase (EC:3.2.1.31)
    Alternative name(s):
    Beta-G1
    Gene namesi
    Name:GUSB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:4696. GUSB.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. intracellular membrane-bounded organelle Source: HPA
    3. lysosomal lumen Source: Reactome
    4. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Involvement in diseasei

    Mucopolysaccharidosis 7 (MPS7) [MIM:253220]: An autosomal recessive lysosomal storage disease characterized by inability to degrade glucuronic acid-containing glycosaminoglycans. The phenotype is highly variable, ranging from severe lethal hydrops fetalis to mild forms with survival into adulthood. Most patients with the intermediate phenotype show hepatomegaly, skeletal anomalies, coarse facies, and variable degrees of mental impairment.13 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti30 – 301P → S in MPS7.
    VAR_058511
    Natural varianti38 – 381C → G in MPS7; very mild phenotype. 1 Publication
    VAR_037914
    Natural varianti52 – 521S → F in MPS7; loss of activity. 1 Publication
    VAR_037915
    Natural varianti136 – 1361G → R in MPS7. 1 Publication
    VAR_037916
    Natural varianti148 – 1481P → S in MPS7. 1 Publication
    VAR_037917
    Natural varianti150 – 1501E → K in MPS7. 1 Publication
    VAR_037918
    Natural varianti152 – 1521D → G in MPS7.
    VAR_058512
    Natural varianti176 – 1761L → F in MPS7. 4 Publications
    VAR_037920
    Natural varianti216 – 2161R → W in MPS7. 2 Publications
    VAR_003196
    Natural varianti243 – 2431L → P in MPS7.
    VAR_058513
    Natural varianti320 – 3201Y → C in MPS7. 1 Publication
    VAR_037921
    Natural varianti320 – 3201Y → S in MPS7. 1 Publication
    VAR_037922
    Natural varianti339 – 3391N → S in MPS7.
    VAR_058514
    Natural varianti350 – 3501K → N in MPS7. 1 Publication
    Corresponds to variant rs121918182 [ dbSNP | Ensembl ].
    VAR_037923
    Natural varianti351 – 3511H → Y in MPS7. 1 Publication
    Corresponds to variant rs191153460 [ dbSNP | Ensembl ].
    VAR_037924
    Natural varianti354 – 3541A → V in MPS7. 1 Publication
    VAR_003197
    Natural varianti361 – 3699Missing in MPS7.
    VAR_058515
    Natural varianti362 – 3621D → N in MPS7.
    VAR_058516
    Natural varianti364 – 3641P → L in MPS7.
    VAR_058517
    Natural varianti374 – 3741R → C in MPS7. 1 Publication
    VAR_037925
    Natural varianti382 – 3821R → C in MPS7. 2 Publications
    VAR_003198
    Natural varianti382 – 3821R → H in MPS7. 1 Publication
    VAR_037926
    Natural varianti408 – 4081P → S in MPS7. 1 Publication
    VAR_037927
    Natural varianti415 – 4151P → L in MPS7. 1 Publication
    VAR_037928
    Natural varianti435 – 4351R → P in MPS7. 1 Publication
    VAR_037929
    Natural varianti477 – 4771R → W in MPS7. 1 Publication
    VAR_037930
    Natural varianti495 – 4951Y → C in MPS7. 1 Publication
    VAR_037931
    Natural varianti508 – 5081Y → C in MPS7. 1 Publication
    VAR_037932
    Natural varianti540 – 5401E → K in MPS7.
    VAR_058518
    Natural varianti572 – 5721G → D in MPS7. 1 Publication
    VAR_037933
    Natural varianti577 – 5771R → L in MPS7; loss of activity. 1 Publication
    VAR_037934
    Natural varianti606 – 6061K → N in MPS7. 1 Publication
    VAR_037935
    Natural varianti607 – 6071G → A in MPS7.
    VAR_058519
    Natural varianti611 – 6111R → W in MPS7. 1 Publication
    VAR_003199
    Natural varianti619 – 6191A → V in MPS7. 1 Publication
    VAR_003200
    Natural varianti626 – 6261Y → H in MPS7; very mild phenotype. 1 Publication
    VAR_037936
    Natural varianti627 – 6271W → C in MPS7. 2 Publications
    VAR_003201
    Mucopolysaccharidosis type 7 is associated with non-immune hydrops fetalis, a generalized edema of the fetus with fluid accumulation in the body cavities due to non-immune causes. Non-immune hydrops fetalis is not a diagnosis in itself but a symptom, a feature of many genetic disorders, and the end-stage of a wide variety of disorders.

    Keywords - Diseasei

    Disease mutation, Mucopolysaccharidosis

    Organism-specific databases

    MIMi253220. phenotype.
    Orphaneti584. Mucopolysaccharidosis type 7.
    PharmGKBiPA29075.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 22221 PublicationAdd
    BLAST
    Chaini23 – 651629Beta-glucuronidasePRO_0000012161Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi173 – 1731N-linked (GlcNAc...)1 Publication
    Glycosylationi272 – 2721N-linked (GlcNAc...)3 Publications
    Glycosylationi420 – 4201N-linked (GlcNAc...)
    Glycosylationi631 – 6311N-linked (GlcNAc...)1 Publication

    Post-translational modificationi

    N-linked glycosylated with 3 to 4 oligosaccharide chains.3 Publications

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiP08236.
    PaxDbiP08236.
    PRIDEiP08236.

    PTM databases

    PhosphoSiteiP08236.

    Expressioni

    Gene expression databases

    ArrayExpressiP08236.
    BgeeiP08236.
    CleanExiHS_GUSB.
    GenevestigatoriP08236.

    Organism-specific databases

    HPAiHPA036322.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    BioGridi109245. 4 interactions.
    DIPiDIP-29724N.
    IntActiP08236. 3 interactions.
    MINTiMINT-4054501.
    STRINGi9606.ENSP00000302728.

    Structurei

    Secondary structure

    1
    651
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi33 – 353
    Beta strandi38 – 403
    Beta strandi43 – 497
    Beta strandi52 – 554
    Helixi57 – 604
    Helixi63 – 653
    Helixi68 – 714
    Beta strandi75 – 817
    Turni84 – 863
    Helixi90 – 934
    Beta strandi97 – 1059
    Helixi109 – 1135
    Beta strandi117 – 1248
    Beta strandi128 – 1347
    Beta strandi137 – 14711
    Beta strandi149 – 1524
    Helixi154 – 1574
    Beta strandi166 – 1738
    Beta strandi180 – 1823
    Beta strandi185 – 1884
    Turni192 – 1943
    Beta strandi200 – 2034
    Beta strandi206 – 2083
    Beta strandi218 – 23821
    Beta strandi241 – 25212
    Beta strandi256 – 2638
    Beta strandi265 – 2673
    Beta strandi269 – 28214
    Turni291 – 2933
    Beta strandi294 – 2963
    Beta strandi301 – 31111
    Beta strandi314 – 32411
    Beta strandi329 – 3313
    Beta strandi336 – 3383
    Beta strandi341 – 3433
    Beta strandi345 – 3495
    Turni355 – 3573
    Helixi363 – 37614
    Beta strandi380 – 3823
    Helixi390 – 39910
    Beta strandi402 – 4065
    Helixi415 – 4173
    Helixi420 – 43718
    Beta strandi443 – 4519
    Helixi457 – 47317
    Beta strandi479 – 4835
    Turni487 – 4893
    Helixi493 – 4953
    Beta strandi497 – 5026
    Turni505 – 5073
    Beta strandi508 – 5103
    Helixi514 – 5163
    Helixi517 – 53216
    Beta strandi536 – 5405
    Helixi559 – 57416
    Turni575 – 5806
    Beta strandi581 – 5877
    Beta strandi600 – 6045
    Helixi617 – 63115

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BHGX-ray2.53A/B21-633[»]
    3HN3X-ray1.70A/B/D/E21-633[»]
    ProteinModelPortaliP08236.
    SMRiP08236. Positions 22-632.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08236.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 2 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3250.
    HOGENOMiHOG000120896.
    HOVERGENiHBG004843.
    InParanoidiP08236.
    KOiK01195.
    OMAiPSRECKE.
    OrthoDBiEOG7288QR.
    PhylomeDBiP08236.
    TreeFamiTF300685.

    Family and domain databases

    Gene3Di2.60.120.260. 1 hit.
    2.60.40.320. 1 hit.
    3.20.20.80. 1 hit.
    InterProiIPR008979. Galactose-bd-like.
    IPR006101. Glyco_hydro_2.
    IPR013812. Glyco_hydro_2/20_Ig-like.
    IPR023232. Glyco_hydro_2_AS.
    IPR023230. Glyco_hydro_2_CS.
    IPR006102. Glyco_hydro_2_Ig-like.
    IPR006104. Glyco_hydro_2_N.
    IPR006103. Glyco_hydro_2_TIM.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00703. Glyco_hydro_2. 1 hit.
    PF02836. Glyco_hydro_2_C. 1 hit.
    PF02837. Glyco_hydro_2_N. 1 hit.
    [Graphical view]
    PRINTSiPR00132. GLHYDRLASE2.
    SUPFAMiSSF49303. SSF49303. 1 hit.
    SSF49785. SSF49785. 1 hit.
    SSF51445. SSF51445. 1 hit.
    PROSITEiPS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
    PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P08236-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MARGSAVAWA ALGPLLWGCA LGLQGGMLYP QESPSRECKE LDGLWSFRAD    50
    FSDNRRRGFE EQWYRRPLWE SGPTVDMPVP SSFNDISQDW RLRHFVGWVW 100
    YEREVILPER WTQDLRTRVV LRIGSAHSYA IVWVNGVDTL EHEGGYLPFE 150
    ADISNLVQVG PLPSRLRITI AINNTLTPTT LPPGTIQYLT DTSKYPKGYF 200
    VQNTYFDFFN YAGLQRSVLL YTTPTTYIDD ITVTTSVEQD SGLVNYQISV 250
    KGSNLFKLEV RLLDAENKVV ANGTGTQGQL KVPGVSLWWP YLMHERPAYL 300
    YSLEVQLTAQ TSLGPVSDFY TLPVGIRTVA VTKSQFLING KPFYFHGVNK 350
    HEDADIRGKG FDWPLLVKDF NLLRWLGANA FRTSHYPYAE EVMQMCDRYG 400
    IVVIDECPGV GLALPQFFNN VSLHHHMQVM EEVVRRDKNH PAVVMWSVAN 450
    EPASHLESAG YYLKMVIAHT KSLDPSRPVT FVSNSNYAAD KGAPYVDVIC 500
    LNSYYSWYHD YGHLELIQLQ LATQFENWYK KYQKPIIQSE YGAETIAGFH 550
    QDPPLMFTEE YQKSLLEQYH LGLDQKRRKY VVGELIWNFA DFMTEQSPTR 600
    VLGNKKGIFT RQRQPKSAAF LLRERYWKIA NETRYPHSVA KSQCLENSLF 650
    T 651
    Length:651
    Mass (Da):74,732
    Last modified:May 1, 2007 - v2
    Checksum:i6BA7B1D935C9ABBD
    GO
    Isoform 2 (identifier: P08236-2) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         305-355: Missing.

    Show »
    Length:600
    Mass (Da):69,142
    Checksum:i8101B66EA73520F8
    GO
    Isoform 3 (identifier: P08236-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         159-304: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:505
    Mass (Da):58,345
    Checksum:iDF74B0D5E57A9F70
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti30 – 301P → S in MPS7.
    VAR_058511
    Natural varianti38 – 381C → G in MPS7; very mild phenotype. 1 Publication
    VAR_037914
    Natural varianti52 – 521S → F in MPS7; loss of activity. 1 Publication
    VAR_037915
    Natural varianti136 – 1361G → R in MPS7. 1 Publication
    VAR_037916
    Natural varianti148 – 1481P → S in MPS7. 1 Publication
    VAR_037917
    Natural varianti150 – 1501E → K in MPS7. 1 Publication
    VAR_037918
    Natural varianti152 – 1521D → G in MPS7.
    VAR_058512
    Natural varianti152 – 1521D → N Reduced activity levels without apparent pathogenic consequences. 2 Publications
    Corresponds to variant rs149606212 [ dbSNP | Ensembl ].
    VAR_037919
    Natural varianti176 – 1761L → F in MPS7. 4 Publications
    VAR_037920
    Natural varianti216 – 2161R → W in MPS7. 2 Publications
    VAR_003196
    Natural varianti243 – 2431L → P in MPS7.
    VAR_058513
    Natural varianti320 – 3201Y → C in MPS7. 1 Publication
    VAR_037921
    Natural varianti320 – 3201Y → S in MPS7. 1 Publication
    VAR_037922
    Natural varianti339 – 3391N → S in MPS7.
    VAR_058514
    Natural varianti350 – 3501K → N in MPS7. 1 Publication
    Corresponds to variant rs121918182 [ dbSNP | Ensembl ].
    VAR_037923
    Natural varianti351 – 3511H → Y in MPS7. 1 Publication
    Corresponds to variant rs191153460 [ dbSNP | Ensembl ].
    VAR_037924
    Natural varianti354 – 3541A → V in MPS7. 1 Publication
    VAR_003197
    Natural varianti361 – 3699Missing in MPS7.
    VAR_058515
    Natural varianti362 – 3621D → N in MPS7.
    VAR_058516
    Natural varianti364 – 3641P → L in MPS7.
    VAR_058517
    Natural varianti374 – 3741R → C in MPS7. 1 Publication
    VAR_037925
    Natural varianti376 – 3761L → F.
    Corresponds to variant rs11559283 [ dbSNP | Ensembl ].
    VAR_055884
    Natural varianti382 – 3821R → C in MPS7. 2 Publications
    VAR_003198
    Natural varianti382 – 3821R → H in MPS7. 1 Publication
    VAR_037926
    Natural varianti408 – 4081P → S in MPS7. 1 Publication
    VAR_037927
    Natural varianti415 – 4151P → L in MPS7. 1 Publication
    VAR_037928
    Natural varianti435 – 4351R → P in MPS7. 1 Publication
    VAR_037929
    Natural varianti477 – 4771R → W in MPS7. 1 Publication
    VAR_037930
    Natural varianti495 – 4951Y → C in MPS7. 1 Publication
    VAR_037931
    Natural varianti508 – 5081Y → C in MPS7. 1 Publication
    VAR_037932
    Natural varianti540 – 5401E → K in MPS7.
    VAR_058518
    Natural varianti572 – 5721G → D in MPS7. 1 Publication
    VAR_037933
    Natural varianti577 – 5771R → L in MPS7; loss of activity. 1 Publication
    VAR_037934
    Natural varianti606 – 6061K → N in MPS7. 1 Publication
    VAR_037935
    Natural varianti607 – 6071G → A in MPS7.
    VAR_058519
    Natural varianti611 – 6111R → W in MPS7. 1 Publication
    VAR_003199
    Natural varianti619 – 6191A → V in MPS7. 1 Publication
    VAR_003200
    Natural varianti626 – 6261Y → H in MPS7; very mild phenotype. 1 Publication
    VAR_037936
    Natural varianti627 – 6271W → C in MPS7. 2 Publications
    VAR_003201
    Natural varianti649 – 6491L → P.3 Publications
    Corresponds to variant rs9530 [ dbSNP | Ensembl ].
    VAR_016179

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei159 – 304146Missing in isoform 3. 1 PublicationVSP_054830Add
    BLAST
    Alternative sequencei305 – 35551Missing in isoform 2. CuratedVSP_001799Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15182 mRNA. Translation: AAA52561.1.
    AK303819 mRNA. Translation: BAG64768.1.
    AK223406 mRNA. Translation: BAD97126.1.
    AC073261 Genomic DNA. Translation: AAQ96851.1.
    CH236961 Genomic DNA. Translation: EAL23740.1.
    CH471140 Genomic DNA. Translation: EAX07951.1.
    BC014142 mRNA. Translation: AAH14142.1.
    M65002 Genomic DNA. Translation: AAA52622.1.
    M10618 mRNA. Translation: AAA52621.1.
    S72462 Genomic DNA. Translation: AAD14101.1.
    CCDSiCCDS5530.1. [P08236-1]
    CCDS64665.1. [P08236-3]
    PIRiA26581.
    RefSeqiNP_000172.2. NM_000181.3. [P08236-1]
    NP_001271219.1. NM_001284290.1. [P08236-3]
    XP_005250354.1. XM_005250297.2. [P08236-2]
    UniGeneiHs.255230.

    Genome annotation databases

    EnsembliENST00000304895; ENSP00000302728; ENSG00000169919. [P08236-1]
    ENST00000421103; ENSP00000391390; ENSG00000169919. [P08236-3]
    GeneIDi2990.
    KEGGihsa:2990.
    UCSCiuc003tun.3. human. [P08236-1]

    Polymorphism databases

    DMDMi146345377.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15182 mRNA. Translation: AAA52561.1 .
    AK303819 mRNA. Translation: BAG64768.1 .
    AK223406 mRNA. Translation: BAD97126.1 .
    AC073261 Genomic DNA. Translation: AAQ96851.1 .
    CH236961 Genomic DNA. Translation: EAL23740.1 .
    CH471140 Genomic DNA. Translation: EAX07951.1 .
    BC014142 mRNA. Translation: AAH14142.1 .
    M65002 Genomic DNA. Translation: AAA52622.1 .
    M10618 mRNA. Translation: AAA52621.1 .
    S72462 Genomic DNA. Translation: AAD14101.1 .
    CCDSi CCDS5530.1. [P08236-1 ]
    CCDS64665.1. [P08236-3 ]
    PIRi A26581.
    RefSeqi NP_000172.2. NM_000181.3. [P08236-1 ]
    NP_001271219.1. NM_001284290.1. [P08236-3 ]
    XP_005250354.1. XM_005250297.2. [P08236-2 ]
    UniGenei Hs.255230.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BHG X-ray 2.53 A/B 21-633 [» ]
    3HN3 X-ray 1.70 A/B/D/E 21-633 [» ]
    ProteinModelPortali P08236.
    SMRi P08236. Positions 22-632.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109245. 4 interactions.
    DIPi DIP-29724N.
    IntActi P08236. 3 interactions.
    MINTi MINT-4054501.
    STRINGi 9606.ENSP00000302728.

    Chemistry

    ChEMBLi CHEMBL2728.

    Protein family/group databases

    CAZyi GH2. Glycoside Hydrolase Family 2.

    PTM databases

    PhosphoSitei P08236.

    Polymorphism databases

    DMDMi 146345377.

    Proteomic databases

    MaxQBi P08236.
    PaxDbi P08236.
    PRIDEi P08236.

    Protocols and materials databases

    DNASUi 2990.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000304895 ; ENSP00000302728 ; ENSG00000169919 . [P08236-1 ]
    ENST00000421103 ; ENSP00000391390 ; ENSG00000169919 . [P08236-3 ]
    GeneIDi 2990.
    KEGGi hsa:2990.
    UCSCi uc003tun.3. human. [P08236-1 ]

    Organism-specific databases

    CTDi 2990.
    GeneCardsi GC07M065425.
    H-InvDB HIX0057492.
    HGNCi HGNC:4696. GUSB.
    HPAi HPA036322.
    MIMi 253220. phenotype.
    611499. gene.
    neXtProti NX_P08236.
    Orphaneti 584. Mucopolysaccharidosis type 7.
    PharmGKBi PA29075.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3250.
    HOGENOMi HOG000120896.
    HOVERGENi HBG004843.
    InParanoidi P08236.
    KOi K01195.
    OMAi PSRECKE.
    OrthoDBi EOG7288QR.
    PhylomeDBi P08236.
    TreeFami TF300685.

    Enzyme and pathway databases

    Reactomei REACT_120752. HS-GAG degradation.
    REACT_120996. Hyaluronan uptake and degradation.

    Miscellaneous databases

    EvolutionaryTracei P08236.
    GeneWikii GUSB.
    GenomeRNAii 2990.
    NextBioi 11852.
    PROi P08236.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P08236.
    Bgeei P08236.
    CleanExi HS_GUSB.
    Genevestigatori P08236.

    Family and domain databases

    Gene3Di 2.60.120.260. 1 hit.
    2.60.40.320. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR008979. Galactose-bd-like.
    IPR006101. Glyco_hydro_2.
    IPR013812. Glyco_hydro_2/20_Ig-like.
    IPR023232. Glyco_hydro_2_AS.
    IPR023230. Glyco_hydro_2_CS.
    IPR006102. Glyco_hydro_2_Ig-like.
    IPR006104. Glyco_hydro_2_N.
    IPR006103. Glyco_hydro_2_TIM.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00703. Glyco_hydro_2. 1 hit.
    PF02836. Glyco_hydro_2_C. 1 hit.
    PF02837. Glyco_hydro_2_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00132. GLHYDRLASE2.
    SUPFAMi SSF49303. SSF49303. 1 hit.
    SSF49785. SSF49785. 1 hit.
    SSF51445. SSF51445. 1 hit.
    PROSITEi PS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
    PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT PRO-649, ALTERNATIVE SPLICING.
      Tissue: Placenta.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT PRO-649.
      Tissue: Lung.
    3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1).
      Tissue: Colon.
    8. "Analysis of the 5' flanking region of the human beta-glucuronidase gene."
      Shipley J.M., Miller R.D., Wu B.M., Grubb J.H., Christensen S.G., Kyle J.W., Sly W.S.
      Genomics 10:1009-1018(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-70.
    9. "Characterization of the subunits and sugar moiety of human placental and leukemic beta-glucuronidase."
      Tanaka J., Gasa S., Sakurada K., Miyazaki T., Kasai M., Makita A.
      Biol. Chem. Hoppe-Seyler 373:57-62(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 23-32 AND 160-175.
      Tissue: Placenta.
    10. "Isolation and expression in Escherichia coli of a cDNA clone encoding human beta-glucuronidase."
      Guise K.S., Korneluk R.G., Waye J., Lamhonwah A.-M., Quan F., Palmer R., Ganschow R.E., Sly W.S., Gravel R.A.
      Gene 34:105-110(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 520-585.
      Tissue: Fibroblast.
    11. "A novel inhibitor of beta-glucuronidase: L-aspartic acid."
      Kreamer B.L., Siegel F.L., Gourley G.R.
      Pediatr. Res. 50:460-466(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INHIBITION BY L-ASPARTIC ACID.
    12. "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
      Zhang H., Li X.-J., Martin D.B., Aebersold R.
      Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-272.
    13. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-272.
      Tissue: Plasma.
    14. "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-173; ASN-272 AND ASN-631.
      Tissue: Liver.
    15. "Structure of human beta-glucuronidase reveals candidate lysosomal targeting and active-site motifs."
      Jain S., Drendel W.B., Chen Z.W., Mathews F.S., Sly W.S., Grubb J.H.
      Nat. Struct. Biol. 3:375-381(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
    16. "Mutations and polymorphisms in GUSB gene in mucopolysaccharidosis VII (Sly Syndrome)."
      Tomatsu S., Montano A.M., Dung V.C., Grubb J.H., Sly W.S.
      Hum. Mutat. 30:511-519(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON VARIANTS.
    17. "Molecular analysis of a patient with hydrops fetalis caused by beta-glucuronidase deficiency, and evidence for additional pseudogenes."
      Vervoort R., Lissens W., Liebaers I.
      Hum. Mutat. 2:443-445(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MPS7 TRP-216.
    18. "Mutational studies in a patient with the hydrops fetalis form of mucopolysaccharidosis type VII."
      Wu B.M., Sly W.S.
      Hum. Mutat. 2:446-457(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MPS7 VAL-354 AND TRP-611.
    19. "Mucopolysaccharidosis type VII: characterization of mutations and molecular heterogeneity."
      Tomatsu S., Fukuda S., Sukegawa K., Ikedo Y., Yamada S., Yamada Y., Sasaki T., Okamoto H., Kuwahara T., Yamaguchi S., Kiman T., Shintaku H., Isshiki G., Orii T.
      Am. J. Hum. Genet. 48:89-96(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MPS7 CYS-382 AND VAL-619.
    20. "Mutational analysis of a patient with mucopolysaccharidosis type VII, and identification of pseudogenes."
      Shipley J.M., Klinkenberg M., Wu B.M., Bachinsky D.R., Grubb J.H., Sly W.S.
      Am. J. Hum. Genet. 52:517-526(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MPS7 CYS-627.
    21. "Overexpression rescues the mutant phenotype of L176F mutation causing beta-glucuronidase deficiency mucopolysaccharidosis in two Mennonite siblings."
      Wu B.M., Tomatsu S., Fukuda S., Sukegawa K., Orii T., Sly W.S.
      J. Biol. Chem. 269:23681-23688(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MPS7 PHE-176, VARIANT PRO-649.
    22. "A pseudodeficiency allele (D152N) of the human beta-glucuronidase gene."
      Vervoort R., Islam M.R., Sly W., Chabas A., Wevers R., de Jong J., Liebaers I., Lissens W.
      Am. J. Hum. Genet. 57:798-804(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MPS7 PHE-176, VARIANT ASN-152, CHARACTERIZATION OF VARIANT ASN-152.
    23. "Four novel mutations in mucopolysaccharidosis type VII including a unique base substitution in exon 10 of the beta-glucuronidase gene that creates a novel 5'-splice site."
      Yamada S., Tomatsu S., Sly W.S., Islam R., Wenger D.A., Fukuda S., Sukegawa K., Orii T.
      Hum. Mol. Genet. 4:651-655(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MPS7 SER-148 AND CYS-495.
    24. "Molecular analysis of patients with beta-glucuronidase deficiency presenting as hydrops fetalis or as early mucopolysaccharidosis VII."
      Vervoort R., Islam M.R., Sly W.S., Zabot M.T., Kleijer W.J., Chabas A., Fensom A., Young E.P., Liebaers I., Lissens W.
      Am. J. Hum. Genet. 58:457-471(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MPS7 ARG-136; LYS-150; PHE-176; TRP-216; CYS-320; SER-320; TYR-351; CYS-374; CYS-382; HIS-382; PRO-435; TRP-477; CYS-508; ASP-572; ASN-606 AND CYS-627.
    25. "beta-Glucuronidase P408S, P415L mutations: evidence that both mutations combine to produce an MPS VII allele in certain Mexican patients."
      Islam M.R., Vervoort R., Lissens W., Hoo J.J., Valentino L.A., Sly W.S.
      Hum. Genet. 98:281-284(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MPS7 SER-408 AND LEU-415.
    26. "Molecular analysis of the beta-glucuronidase gene: novel mutations in mucopolysaccharidosis type VII and heterogeneity of the polyadenylation region."
      Vervoort R., Buist N.R., Kleijer W.J., Wevers R., Fryns J.P., Liebaers I., Lissens W.
      Hum. Genet. 99:462-468(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MPS7 PHE-52, CHARACTERIZATION OF VARIANT MPS7 PHE-52.
    27. "Low beta-glucuronidase enzyme activity and mutations in the human beta-glucuronidase gene in mild mucopolysaccharidosis type VII, pseudodeficiency and a heterozygote."
      Vervoort R., Gitzelmann R., Bosshard N., Maire I., Liebaers I., Lissens W.
      Hum. Genet. 102:69-78(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ASN-152, VARIANTS MPS7 GLY-38 AND HIS-626.
    28. "Mucopolysaccharidosis VII: clinical, biochemical and molecular investigation of a Brazilian family."
      Schwartz I., Silva L.R., Leistner S., Todeschini L.A., Burin M.G., Pina-Neto J.M., Islam R.M., Shah G.N., Sly W.S., Giugliani R.
      Clin. Genet. 64:172-175(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MPS7 PHE-176.
    29. "Mutational analysis in longest known survivor of mucopolysaccharidosis type VII."
      Storch S., Wittenstein B., Islam R., Ullrich K., Sly W.S., Braulke T.
      Hum. Genet. 112:190-194(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MPS7 ASN-350 AND LEU-577, CHARACTERIZATION OF VARIANT MPS7 ASN-350 LEU-577.

    Entry informationi

    Entry nameiBGLR_HUMAN
    AccessioniPrimary (citable) accession number: P08236
    Secondary accession number(s): B4E1F6
    , E9PCV0, Q549U0, Q96CL9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    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

    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 7
      Human chromosome 7: 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

    External Data

    Dasty 3