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

Beta-glucuronidase

Gene

GUSB

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

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)DescriptionActionsGraphical viewLength
Active sitei451Proton donor1

GO - Molecular functioni

  • beta-glucuronidase activity Source: Reactome
  • protein domain specific binding Source: AgBase
  • receptor binding Source: AgBase

GO - Biological processi

  • carbohydrate metabolic process Source: ProtInc
  • glycosaminoglycan catabolic process Source: Reactome
  • hyaluronan catabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciZFISH:HS10035-MONOMER.
ReactomeiR-HSA-2024096. HS-GAG degradation.
R-HSA-2160916. Hyaluronan uptake and degradation.
R-HSA-6798695. Neutrophil degranulation.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:4696. GUSB.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • intracellular membrane-bounded organelle Source: HPA
  • lysosomal lumen Source: Reactome
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Involvement in diseasei

Mucopolysaccharidosis 7 (MPS7)13 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:253220
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05851130P → S in MPS7. Corresponds to variant rs747792546dbSNPEnsembl.1
Natural variantiVAR_03791438C → G in MPS7; very mild phenotype. 1 Publication1
Natural variantiVAR_03791552S → F in MPS7; loss of activity. 1 Publication1
Natural variantiVAR_037916136G → R in MPS7. 1 Publication1
Natural variantiVAR_037917148P → S in MPS7. 1 PublicationCorresponds to variant rs121918177dbSNPEnsembl.1
Natural variantiVAR_037918150E → K in MPS7. 1 Publication1
Natural variantiVAR_058512152D → G in MPS7. 1
Natural variantiVAR_037920176L → F in MPS7. 4 PublicationsCorresponds to variant rs121918181dbSNPEnsembl.1
Natural variantiVAR_003196216R → W in MPS7. 2 PublicationsCorresponds to variant rs121918174dbSNPEnsembl.1
Natural variantiVAR_058513243L → P in MPS7. 1
Natural variantiVAR_037921320Y → C in MPS7. 1 Publication1
Natural variantiVAR_037922320Y → S in MPS7. 1 Publication1
Natural variantiVAR_058514339N → S in MPS7. 1
Natural variantiVAR_037923350K → N in MPS7. 1 PublicationCorresponds to variant rs121918182dbSNPEnsembl.1
Natural variantiVAR_037924351H → Y in MPS7. 1 PublicationCorresponds to variant rs191153460dbSNPEnsembl.1
Natural variantiVAR_003197354A → V in MPS7. 1 PublicationCorresponds to variant rs121918175dbSNPEnsembl.1
Natural variantiVAR_058515361 – 369Missing in MPS7. 9
Natural variantiVAR_058516362D → N in MPS7. Corresponds to variant rs398123234dbSNPEnsembl.1
Natural variantiVAR_058517364P → L in MPS7. Corresponds to variant rs771629102dbSNPEnsembl.1
Natural variantiVAR_037925374R → C in MPS7. 1 PublicationCorresponds to variant rs747572640dbSNPEnsembl.1
Natural variantiVAR_003198382R → C in MPS7. 2 PublicationsCorresponds to variant rs121918173dbSNPEnsembl.1
Natural variantiVAR_037926382R → H in MPS7. 1 Publication1
Natural variantiVAR_037927408P → S in MPS7. 1 PublicationCorresponds to variant rs779091113dbSNPEnsembl.1
Natural variantiVAR_037928415P → L in MPS7. 1 PublicationCorresponds to variant rs751025746dbSNPEnsembl.1
Natural variantiVAR_037929435R → P in MPS7. 1 Publication1
Natural variantiVAR_037930477R → W in MPS7. 1 PublicationCorresponds to variant rs774393243dbSNPEnsembl.1
Natural variantiVAR_037931495Y → C in MPS7. 1 PublicationCorresponds to variant rs121918178dbSNPEnsembl.1
Natural variantiVAR_037932508Y → C in MPS7. 1 Publication1
Natural variantiVAR_058518540E → K in MPS7. 1
Natural variantiVAR_037933572G → D in MPS7. 1 Publication1
Natural variantiVAR_037934577R → L in MPS7; loss of activity. 1 PublicationCorresponds to variant rs121918183dbSNPEnsembl.1
Natural variantiVAR_037935606K → N in MPS7. 1 Publication1
Natural variantiVAR_058519607G → A in MPS7. 1
Natural variantiVAR_003199611R → W in MPS7. 1 PublicationCorresponds to variant rs121918176dbSNPEnsembl.1
Natural variantiVAR_003200619A → V in MPS7. 1 PublicationCorresponds to variant rs121918172dbSNPEnsembl.1
Natural variantiVAR_037936626Y → H in MPS7; very mild phenotype. 1 PublicationCorresponds to variant rs777613366dbSNPEnsembl.1
Natural variantiVAR_003201627W → C in MPS7. 2 PublicationsCorresponds to variant rs121918184dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Mucopolysaccharidosis

Organism-specific databases

DisGeNETi2990.
MalaCardsiGUSB.
MIMi253220. phenotype.
OpenTargetsiENSG00000169919.
Orphaneti584. Mucopolysaccharidosis type 7.
PharmGKBiPA29075.

Chemistry databases

ChEMBLiCHEMBL2728.

Polymorphism and mutation databases

BioMutaiGUSB.
DMDMi146345377.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 221 PublicationAdd BLAST22
ChainiPRO_000001216123 – 651Beta-glucuronidaseAdd BLAST629

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi173N-linked (GlcNAc...)1 Publication1
Glycosylationi272N-linked (GlcNAc...)3 Publications1
Glycosylationi420N-linked (GlcNAc...)1
Glycosylationi631N-linked (GlcNAc...)1 Publication1

Post-translational modificationi

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

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiP08236.
MaxQBiP08236.
PaxDbiP08236.
PeptideAtlasiP08236.
PRIDEiP08236.

PTM databases

iPTMnetiP08236.
PhosphoSitePlusiP08236.

Expressioni

Gene expression databases

BgeeiENSG00000169919.
CleanExiHS_GUSB.
ExpressionAtlasiP08236. baseline and differential.
GenevisibleiP08236. HS.

Organism-specific databases

HPAiHPA036322.
HPA036323.

Interactioni

Subunit structurei

Homotetramer.

GO - Molecular functioni

  • protein domain specific binding Source: AgBase
  • receptor binding Source: AgBase

Protein-protein interaction databases

BioGridi109245. 10 interactors.
DIPiDIP-29724N.
IntActiP08236. 3 interactors.
MINTiMINT-4054501.
STRINGi9606.ENSP00000302728.

Chemistry databases

BindingDBiP08236.

Structurei

Secondary structure

1651
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi33 – 35Combined sources3
Beta strandi38 – 40Combined sources3
Beta strandi43 – 49Combined sources7
Beta strandi52 – 55Combined sources4
Helixi57 – 60Combined sources4
Helixi63 – 65Combined sources3
Helixi68 – 71Combined sources4
Beta strandi75 – 81Combined sources7
Turni84 – 86Combined sources3
Helixi90 – 93Combined sources4
Beta strandi97 – 105Combined sources9
Helixi109 – 113Combined sources5
Beta strandi117 – 124Combined sources8
Beta strandi128 – 134Combined sources7
Beta strandi137 – 147Combined sources11
Beta strandi149 – 152Combined sources4
Helixi154 – 157Combined sources4
Beta strandi166 – 173Combined sources8
Beta strandi180 – 182Combined sources3
Beta strandi185 – 188Combined sources4
Turni192 – 194Combined sources3
Beta strandi200 – 203Combined sources4
Beta strandi206 – 208Combined sources3
Beta strandi218 – 238Combined sources21
Beta strandi241 – 252Combined sources12
Beta strandi256 – 263Combined sources8
Beta strandi265 – 267Combined sources3
Beta strandi269 – 282Combined sources14
Turni291 – 293Combined sources3
Beta strandi294 – 296Combined sources3
Beta strandi301 – 311Combined sources11
Beta strandi314 – 324Combined sources11
Beta strandi329 – 331Combined sources3
Beta strandi336 – 338Combined sources3
Beta strandi341 – 343Combined sources3
Beta strandi345 – 349Combined sources5
Turni355 – 357Combined sources3
Helixi363 – 376Combined sources14
Beta strandi380 – 382Combined sources3
Helixi390 – 399Combined sources10
Beta strandi402 – 406Combined sources5
Helixi415 – 417Combined sources3
Helixi420 – 437Combined sources18
Beta strandi443 – 451Combined sources9
Helixi457 – 473Combined sources17
Beta strandi479 – 483Combined sources5
Turni487 – 489Combined sources3
Helixi493 – 495Combined sources3
Beta strandi497 – 502Combined sources6
Turni505 – 507Combined sources3
Beta strandi508 – 510Combined sources3
Helixi514 – 516Combined sources3
Helixi517 – 532Combined sources16
Beta strandi536 – 540Combined sources5
Helixi559 – 574Combined sources16
Turni575 – 580Combined sources6
Beta strandi581 – 587Combined sources7
Beta strandi600 – 604Combined sources5
Helixi617 – 631Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BHGX-ray2.53A/B21-633[»]
3HN3X-ray1.70A/B/D/E21-633[»]
ProteinModelPortaliP08236.
SMRiP08236.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08236.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2024. Eukaryota.
COG3250. LUCA.
GeneTreeiENSGT00390000001752.
HOGENOMiHOG000120896.
HOVERGENiHBG004843.
InParanoidiP08236.
KOiK01195.
OMAiINFDFFN.
OrthoDBiEOG091G02MO.
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.
IPR006103. Glyco_hydro_2_cat.
IPR023230. Glyco_hydro_2_CS.
IPR006102. Glyco_hydro_2_Ig-like.
IPR006104. Glyco_hydro_2_N.
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. AlignAdd to basket

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

        10         20         30         40         50
MARGSAVAWA ALGPLLWGCA LGLQGGMLYP QESPSRECKE LDGLWSFRAD
60 70 80 90 100
FSDNRRRGFE EQWYRRPLWE SGPTVDMPVP SSFNDISQDW RLRHFVGWVW
110 120 130 140 150
YEREVILPER WTQDLRTRVV LRIGSAHSYA IVWVNGVDTL EHEGGYLPFE
160 170 180 190 200
ADISNLVQVG PLPSRLRITI AINNTLTPTT LPPGTIQYLT DTSKYPKGYF
210 220 230 240 250
VQNTYFDFFN YAGLQRSVLL YTTPTTYIDD ITVTTSVEQD SGLVNYQISV
260 270 280 290 300
KGSNLFKLEV RLLDAENKVV ANGTGTQGQL KVPGVSLWWP YLMHERPAYL
310 320 330 340 350
YSLEVQLTAQ TSLGPVSDFY TLPVGIRTVA VTKSQFLING KPFYFHGVNK
360 370 380 390 400
HEDADIRGKG FDWPLLVKDF NLLRWLGANA FRTSHYPYAE EVMQMCDRYG
410 420 430 440 450
IVVIDECPGV GLALPQFFNN VSLHHHMQVM EEVVRRDKNH PAVVMWSVAN
460 470 480 490 500
EPASHLESAG YYLKMVIAHT KSLDPSRPVT FVSNSNYAAD KGAPYVDVIC
510 520 530 540 550
LNSYYSWYHD YGHLELIQLQ LATQFENWYK KYQKPIIQSE YGAETIAGFH
560 570 580 590 600
QDPPLMFTEE YQKSLLEQYH LGLDQKRRKY VVGELIWNFA DFMTEQSPTR
610 620 630 640 650
VLGNKKGIFT RQRQPKSAAF LLRERYWKIA NETRYPHSVA KSQCLENSLF

T
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_05851130P → S in MPS7. Corresponds to variant rs747792546dbSNPEnsembl.1
Natural variantiVAR_03791438C → G in MPS7; very mild phenotype. 1 Publication1
Natural variantiVAR_03791552S → F in MPS7; loss of activity. 1 Publication1
Natural variantiVAR_037916136G → R in MPS7. 1 Publication1
Natural variantiVAR_037917148P → S in MPS7. 1 PublicationCorresponds to variant rs121918177dbSNPEnsembl.1
Natural variantiVAR_037918150E → K in MPS7. 1 Publication1
Natural variantiVAR_058512152D → G in MPS7. 1
Natural variantiVAR_037919152D → N Reduced activity levels without apparent pathogenic consequences. 2 PublicationsCorresponds to variant rs149606212dbSNPEnsembl.1
Natural variantiVAR_037920176L → F in MPS7. 4 PublicationsCorresponds to variant rs121918181dbSNPEnsembl.1
Natural variantiVAR_003196216R → W in MPS7. 2 PublicationsCorresponds to variant rs121918174dbSNPEnsembl.1
Natural variantiVAR_058513243L → P in MPS7. 1
Natural variantiVAR_037921320Y → C in MPS7. 1 Publication1
Natural variantiVAR_037922320Y → S in MPS7. 1 Publication1
Natural variantiVAR_058514339N → S in MPS7. 1
Natural variantiVAR_037923350K → N in MPS7. 1 PublicationCorresponds to variant rs121918182dbSNPEnsembl.1
Natural variantiVAR_037924351H → Y in MPS7. 1 PublicationCorresponds to variant rs191153460dbSNPEnsembl.1
Natural variantiVAR_003197354A → V in MPS7. 1 PublicationCorresponds to variant rs121918175dbSNPEnsembl.1
Natural variantiVAR_058515361 – 369Missing in MPS7. 9
Natural variantiVAR_058516362D → N in MPS7. Corresponds to variant rs398123234dbSNPEnsembl.1
Natural variantiVAR_058517364P → L in MPS7. Corresponds to variant rs771629102dbSNPEnsembl.1
Natural variantiVAR_037925374R → C in MPS7. 1 PublicationCorresponds to variant rs747572640dbSNPEnsembl.1
Natural variantiVAR_055884376L → F.Corresponds to variant rs11559283dbSNPEnsembl.1
Natural variantiVAR_003198382R → C in MPS7. 2 PublicationsCorresponds to variant rs121918173dbSNPEnsembl.1
Natural variantiVAR_037926382R → H in MPS7. 1 Publication1
Natural variantiVAR_037927408P → S in MPS7. 1 PublicationCorresponds to variant rs779091113dbSNPEnsembl.1
Natural variantiVAR_037928415P → L in MPS7. 1 PublicationCorresponds to variant rs751025746dbSNPEnsembl.1
Natural variantiVAR_037929435R → P in MPS7. 1 Publication1
Natural variantiVAR_037930477R → W in MPS7. 1 PublicationCorresponds to variant rs774393243dbSNPEnsembl.1
Natural variantiVAR_037931495Y → C in MPS7. 1 PublicationCorresponds to variant rs121918178dbSNPEnsembl.1
Natural variantiVAR_037932508Y → C in MPS7. 1 Publication1
Natural variantiVAR_058518540E → K in MPS7. 1
Natural variantiVAR_037933572G → D in MPS7. 1 Publication1
Natural variantiVAR_037934577R → L in MPS7; loss of activity. 1 PublicationCorresponds to variant rs121918183dbSNPEnsembl.1
Natural variantiVAR_037935606K → N in MPS7. 1 Publication1
Natural variantiVAR_058519607G → A in MPS7. 1
Natural variantiVAR_003199611R → W in MPS7. 1 PublicationCorresponds to variant rs121918176dbSNPEnsembl.1
Natural variantiVAR_003200619A → V in MPS7. 1 PublicationCorresponds to variant rs121918172dbSNPEnsembl.1
Natural variantiVAR_037936626Y → H in MPS7; very mild phenotype. 1 PublicationCorresponds to variant rs777613366dbSNPEnsembl.1
Natural variantiVAR_003201627W → C in MPS7. 2 PublicationsCorresponds to variant rs121918184dbSNPEnsembl.1
Natural variantiVAR_016179649L → P.3 PublicationsCorresponds to variant rs9530dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_054830159 – 304Missing in isoform 3. 1 PublicationAdd BLAST146
Alternative sequenceiVSP_001799305 – 355Missing in isoform 2. CuratedAdd BLAST51

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
NP_001280033.1. NM_001293104.1.
NP_001280034.1. NM_001293105.1.
XP_005250354.1. XM_005250297.3. [P08236-2]
UniGeneiHs.255230.

Genome annotation databases

EnsembliENST00000304895; ENSP00000302728; ENSG00000169919. [P08236-1]
ENST00000421103; ENSP00000391390; ENSG00000169919. [P08236-3]
GeneIDi2990.
KEGGihsa:2990.
UCSCiuc003tun.4. human. [P08236-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
NP_001280033.1. NM_001293104.1.
NP_001280034.1. NM_001293105.1.
XP_005250354.1. XM_005250297.3. [P08236-2]
UniGeneiHs.255230.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BHGX-ray2.53A/B21-633[»]
3HN3X-ray1.70A/B/D/E21-633[»]
ProteinModelPortaliP08236.
SMRiP08236.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109245. 10 interactors.
DIPiDIP-29724N.
IntActiP08236. 3 interactors.
MINTiMINT-4054501.
STRINGi9606.ENSP00000302728.

Chemistry databases

BindingDBiP08236.
ChEMBLiCHEMBL2728.

Protein family/group databases

CAZyiGH2. Glycoside Hydrolase Family 2.

PTM databases

iPTMnetiP08236.
PhosphoSitePlusiP08236.

Polymorphism and mutation databases

BioMutaiGUSB.
DMDMi146345377.

Proteomic databases

EPDiP08236.
MaxQBiP08236.
PaxDbiP08236.
PeptideAtlasiP08236.
PRIDEiP08236.

Protocols and materials databases

DNASUi2990.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000304895; ENSP00000302728; ENSG00000169919. [P08236-1]
ENST00000421103; ENSP00000391390; ENSG00000169919. [P08236-3]
GeneIDi2990.
KEGGihsa:2990.
UCSCiuc003tun.4. human. [P08236-1]

Organism-specific databases

CTDi2990.
DisGeNETi2990.
GeneCardsiGUSB.
H-InvDBHIX0057492.
HGNCiHGNC:4696. GUSB.
HPAiHPA036322.
HPA036323.
MalaCardsiGUSB.
MIMi253220. phenotype.
611499. gene.
neXtProtiNX_P08236.
OpenTargetsiENSG00000169919.
Orphaneti584. Mucopolysaccharidosis type 7.
PharmGKBiPA29075.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2024. Eukaryota.
COG3250. LUCA.
GeneTreeiENSGT00390000001752.
HOGENOMiHOG000120896.
HOVERGENiHBG004843.
InParanoidiP08236.
KOiK01195.
OMAiINFDFFN.
OrthoDBiEOG091G02MO.
PhylomeDBiP08236.
TreeFamiTF300685.

Enzyme and pathway databases

BioCyciZFISH:HS10035-MONOMER.
ReactomeiR-HSA-2024096. HS-GAG degradation.
R-HSA-2160916. Hyaluronan uptake and degradation.
R-HSA-6798695. Neutrophil degranulation.

Miscellaneous databases

ChiTaRSiGUSB. human.
EvolutionaryTraceiP08236.
GeneWikiiGUSB.
GenomeRNAii2990.
PROiP08236.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000169919.
CleanExiHS_GUSB.
ExpressionAtlasiP08236. baseline and differential.
GenevisibleiP08236. HS.

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.
IPR006103. Glyco_hydro_2_cat.
IPR023230. Glyco_hydro_2_CS.
IPR006102. Glyco_hydro_2_Ig-like.
IPR006104. Glyco_hydro_2_N.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 183 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

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.