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HUMAN:BGAL

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Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) GLB1 (synonyms: ELNR1)
Protein Name(s) Beta-galactosidase

Acid beta-galactosidase Lactase Elastin receptor 1

External Links
UniProt P16278
EMBL M22590
M27507
M27508
M34423
AK300021
AK312988
BT007147
AC112211
BC007493
CCDS CCDS43061.1
CCDS43062.1
CCDS46785.1
PIR A32688
B32688
RefSeq NP_000395.2
NP_001073279.1
NP_001129074.1
UniGene Hs.443031
PDB 3THC
3THD
3WEZ
3WF0
3WF1
3WF2
3WF3
3WF4
PDBsum 3THC
3THD
3WEZ
3WF0
3WF1
3WF2
3WF3
3WF4
ProteinModelPortal P16278
SMR P16278
BioGrid 108984
IntAct P16278
MINT MINT-3008481
STRING 9606.ENSP00000306920
BindingDB P16278
ChEMBL CHEMBL2522
CAZy GH35
PhosphoSite P16278
DMDM 215273939
MaxQB P16278
PaxDb P16278
PRIDE P16278
DNASU 2720
Ensembl ENST00000307363
ENST00000399402
ENST00000445488
GeneID 2720
KEGG hsa:2720
UCSC uc003cfh.1
uc003cfj.1
CTD 2720
GeneCards GC03M033013
GeneReviews GLB1
HGNC HGNC:4298
HPA CAB008382
HPA040610
MIM 230500
230600
230650
253010
611458
neXtProt NX_P16278
Orphanet 79255
79256
79257
309310
PharmGKB PA28709
eggNOG COG1874
HOGENOM HOG000221607
HOVERGEN HBG004841
InParanoid P16278
KO K12309
OrthoDB EOG7GXPCD
PhylomeDB P16278
TreeFam TF314816
Reactome REACT_116105
REACT_120752
REACT_121313
REACT_200874
SABIO-RK P16278
ChiTaRS GLB1
GeneWiki GLB1
GenomeRNAi 2720
NextBio 10738
PRO PR:P16278
Proteomes UP000005640
UP000005640
Bgee P16278
CleanEx HS_GLB1
ExpressionAtlas P16278
Genevestigator P16278
GO GO:0005737
GO:0070062
GO:0005794
GO:0043202
GO:0048471
GO:0004565
GO:0016936
GO:0005975
GO:0019388
GO:0006027
GO:0030203
GO:0006687
GO:0042340
GO:0042339
GO:0044281
GO:0006665
Gene3D 2.60.120.260
3.20.20.80
InterPro IPR026283
IPR008979
IPR019801
IPR013781
IPR001944
IPR017853
PANTHER PTHR23421
Pfam PF01301
PIRSF PIRSF006336
PRINTS PR00742
SUPFAM SSF49785
SSF51445
PROSITE PS01182

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

enables

GO:0004565

beta-galactosidase activity

PMID:24737316[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0042803

protein homodimerization activity

PMID:22128166[2]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P16278

F

Seeded From UniProt

complete

enables

GO:0004565

beta-galactosidase activity

PMID:25936995[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0044262

cellular carbohydrate metabolic process

PMID:11927518[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:11927518[4]

ECO:0000314

direct assay evidence used in manual assertion

C

  • part_of:(UBERON:0001621)
  • part_of:(CL:0002544)

Seeded From UniProt

complete

enables

GO:0004565

beta-galactosidase activity

PMID:11927518[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0070062

extracellular exosome

PMID:23533145[5]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0070062

extracellular exosome

PMID:19056867[6]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

part_of:(UBERON:0001088)

Seeded From UniProt

complete

part_of

GO:0005773

vacuole

PMID:21873635[7]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000602923
UniProtKB:Q9SCV3

C

Seeded From UniProt

complete

enables

GO:0004565

beta-galactosidase activity

PMID:21873635[7]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:88151
PANTHER:PTN000602923
RGD:1597145
TAIR:locus:2091496
TAIR:locus:2115310
TAIR:locus:2160649
TAIR:locus:2163951
UniProtKB:P16278
UniProtKB:Q5BFC4
ZFIN:ZDB-GENE-050410-9

F

Seeded From UniProt

complete

part_of

GO:0043231

intracellular membrane-bounded organelle

GO_REF:0000052

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005794

Golgi apparatus

GO_REF:0000052

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:1904016

response to Thyroglobulin triiodothyronine

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:D3ZUM4
ensembl:ENSRNOP00000013632

P

Seeded From UniProt

complete

involved_in

GO:0051413

response to cortisone

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:D3ZUM4
ensembl:ENSRNOP00000013632

P

Seeded From UniProt

complete

involved_in

GO:0019388

galactose catabolic process

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:D3ZUM4
ensembl:ENSRNOP00000013632

P

Seeded From UniProt

complete

enables

GO:0016936

galactoside binding

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:D3ZUM4
ensembl:ENSRNOP00000013632

F

Seeded From UniProt

complete

part_of

GO:0005764

lysosome

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:D3ZUM4
ensembl:ENSRNOP00000013632

C

Seeded From UniProt

complete

enables

GO:0004565

beta-galactosidase activity

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:D3ZUM4
ensembl:ENSRNOP00000013632

F

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P23780
ensembl:ENSMUSP00000055803

F

Seeded From UniProt

complete

part_of

GO:0005615

extracellular space

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P23780
ensembl:ENSMUSP00000055803

C

Seeded From UniProt

complete

enables

GO:0004565

beta-galactosidase activity

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P23780
ensembl:ENSMUSP00000055803

F

Seeded From UniProt

complete

enables

GO:0004553

hydrolase activity, hydrolyzing O-glycosyl compounds

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001944
InterPro:IPR019801

F

Seeded From UniProt

complete

enables

GO:0004565

beta-galactosidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR026283

F

Seeded From UniProt

complete

involved_in

GO:0005975

carbohydrate metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001944
InterPro:IPR019801

P

Seeded From UniProt

complete

enables

GO:0004565

beta-galactosidase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.2.1.23

F

Seeded From UniProt

complete

enables

GO:0004565

beta-galactosidase activity

PMID:3143362[8]
PMID:3143362[8]

ECO:0000304

author statement supported by traceable reference used in manual assertion


F

Seeded From UniProt

complete

part_of

GO:1904813

ficolin-1-rich granule lumen

Reactome:R-HSA-6800434

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0043312

neutrophil degranulation

Reactome:R-HSA-6798695

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0043202

lysosomal lumen

Reactome:R-HSA-4084999
Reactome:R-HSA-2090079
Reactome:R-HSA-1630306
Reactome:R-HSA-1606312
Reactome:R-HSA-1605724
Reactome:R-HSA-1605624

ECO:0000304

author statement supported by traceable reference used in manual assertion






C

Seeded From UniProt

complete

involved_in

GO:0042340

keratan sulfate catabolic process

Reactome:R-HSA-2022857

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0035578

azurophil granule lumen

Reactome:R-HSA-6798751

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006687

glycosphingolipid metabolic process

Reactome:R-HSA-1660662

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006027

glycosaminoglycan catabolic process

Reactome:R-HSA-2024096

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

Reactome:R-HSA-6800434
Reactome:R-HSA-6798751

ECO:0000304

author statement supported by traceable reference used in manual assertion


C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963

C

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

involved_in

GO:0008152

metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0326

P

Seeded From UniProt

complete

part_of

GO:0005764

lysosome

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0458
UniProtKB-SubCell:SL-0158

C

Seeded From UniProt

complete

enables

GO:0016798

hydrolase activity, acting on glycosyl bonds

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0326

F

Seeded From UniProt

complete

part_of

GO:0048471

perinuclear region of cytoplasm

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0198

C

Seeded From UniProt

complete

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Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ Suzuki, H et al. (2014) Structural basis of pharmacological chaperoning for human β-galactosidase. J. Biol. Chem. 289 14560-8 PubMed GONUTS page
  2. ↑ Ohto, U et al. (2012) Crystal structure of human β-galactosidase: structural basis of Gm1 gangliosidosis and morquio B diseases. J. Biol. Chem. 287 1801-12 PubMed GONUTS page
  3. ↑ Bidchol, AM et al. (2015) Recurrent and novel GLB1 mutations in India. Gene 567 173-81 PubMed GONUTS page
  4. ↑ 4.0 4.1 4.2 Minamino, T et al. (2002) Endothelial cell senescence in human atherosclerosis: role of telomere in endothelial dysfunction. Circulation 105 1541-4 PubMed GONUTS page
  5. ↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
  6. ↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
  7. ↑ 7.0 7.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  8. ↑ 8.0 8.1 Oshima, A et al. (1988) Cloning, sequencing, and expression of cDNA for human beta-galactosidase. Biochem. Biophys. Res. Commun. 157 238-44 PubMed GONUTS page
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