HUMAN:GBA2

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	GBA2 (synonyms: KIAA1605)
Protein Name(s)	Non-lysosomal glucosylceramidase NLGase Beta-glucocerebrosidase 2 Beta-glucosidase 2 Glucosylceramidase 2
External Links
UniProt	Q9HCG7
EMBL	AJ309567 AB046825 AK027884 AL834306 AL133410 AL133410 AL133410 CH471071 CH471071 BC011363 AF258662
CCDS	CCDS6589.1
RefSeq	NP_065995.1
UniGene	Hs.443134
ProteinModelPortal	Q9HCG7
BioGrid	121728
IntAct	Q9HCG7
MINT	MINT-6630061
STRING	9606.ENSP00000367343
BindingDB	Q9HCG7
ChEMBL	CHEMBL3761
CAZy	GH116
PhosphoSite	Q9HCG7
DMDM	143018392
MaxQB	Q9HCG7
PaxDb	Q9HCG7
PRIDE	Q9HCG7
Ensembl	ENST00000378094 ENST00000378103
GeneID	57704
KEGG	hsa:57704
UCSC	uc003zxw.3 uc003zxy.1 uc011lpb.1
CTD	57704
GeneCards	GC09M035726
HGNC	HGNC:18986
HPA	HPA024026
MIM	609471 614409
neXtProt	NX_Q9HCG7
Orphanet	352641 320391
PharmGKB	PA38773
eggNOG	COG4354
GeneTree	ENSGT00390000010998
HOVERGEN	HBG105975
InParanoid	Q9HCG7
KO	K17108
OrthoDB	EOG7ZGX2B
PhylomeDB	Q9HCG7
TreeFam	TF313888
Reactome	REACT_116105
SABIO-RK	Q9HCG7
ChiTaRS	GBA2
GeneWiki	GBA2
GenomeRNAi	57704
NextBio	64578
PRO	PR:Q9HCG7
Proteomes	UP000005640
Bgee	Q9HCG7
CleanEx	HS_GBA2
ExpressionAtlas	Q9HCG7
Genevestigator	Q9HCG7
GO	GO:0005789 GO:0000139 GO:0016021 GO:0005886 GO:0005790 GO:0008422 GO:0004348 GO:0008206 GO:0021954 GO:0006680 GO:0016139 GO:0006687 GO:0044281 GO:0006665
InterPro	IPR008928 IPR014551 IPR024462 IPR006775
Pfam	PF04685 PF12215
PIRSF	PIRSF028944
SUPFAM	SSF48208

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0005886	plasma membrane	PMID:19577566^[1]	ECO:0000314			C	Fig 3	complete
enables	GO:0004348	glucosylceramidase activity	PMID:17080196^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006680	glucosylceramide catabolic process	PMID:17080196^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0030259	lipid glycosylation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q69ZF3	P	Seeded From UniProt	complete
involved_in	GO:0008203	cholesterol metabolic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q69ZF3	P	Seeded From UniProt	complete
part_of	GO:0090498	extrinsic component of Golgi membrane	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q69ZF3	C	Seeded From UniProt	complete
part_of	GO:0042406	extrinsic component of endoplasmic reticulum membrane	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q69ZF3	C	Seeded From UniProt	complete
part_of	GO:0019898	extrinsic component of membrane	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q69ZF3	C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q69ZF3	C	Seeded From UniProt	complete
involved_in	GO:0097035	regulation of membrane lipid distribution	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q69ZF3	P	Seeded From UniProt	complete
involved_in	GO:0031113	regulation of microtubule polymerization	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q69ZF3	P	Seeded From UniProt	complete
involved_in	GO:0030833	regulation of actin filament polymerization	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q69ZF3	P	Seeded From UniProt	complete
enables	GO:0050295	steryl-beta-glucosidase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q69ZF3	F	Seeded From UniProt	complete
involved_in	GO:0006680	glucosylceramide catabolic process	PMID:30308956^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0046527	glucosyltransferase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q69ZF3	F	Seeded From UniProt	complete
involved_in	GO:0021954	central nervous system neuron development	PMID:23332916^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0016139	glycoside catabolic process	PMID:17105727^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0016139	glycoside catabolic process	PMID:11489889^[6]	ECO:0000303	author statement without traceable support used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	PMID:17105727^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	PMID:11489889^[6]	ECO:0000303	author statement without traceable support used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0008422	beta-glucosidase activity	PMID:11489889^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0008206	bile acid metabolic process	PMID:17105727^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0016139	glycoside catabolic process	PMID:21873635^[7]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000291741 UniProtKB:Q9HCG7	P	Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	PMID:21873635^[7]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000291741 UniProtKB:Q9HCG7	C	Seeded From UniProt	complete
enables	GO:0008422	beta-glucosidase activity	PMID:21873635^[7]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000291741 UniProtKB:Q9HCG7 ZFIN:ZDB-GENE-070522-3	F	Seeded From UniProt	complete
involved_in	GO:0007417	central nervous system development	PMID:21873635^[7]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000291746 ZFIN:ZDB-GENE-070522-3	P	Seeded From UniProt	complete
involved_in	GO:0097035	regulation of membrane lipid distribution	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q69ZF3 ensembl:ENSMUSP00000030189	P	Seeded From UniProt	complete
part_of	GO:0090498	extrinsic component of Golgi membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q69ZF3 ensembl:ENSMUSP00000030189	C	Seeded From UniProt	complete
enables	GO:0050295	steryl-beta-glucosidase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q69ZF3 ensembl:ENSMUSP00000030189	F	Seeded From UniProt	complete
enables	GO:0046527	glucosyltransferase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q69ZF3 ensembl:ENSMUSP00000030189	F	Seeded From UniProt	complete
part_of	GO:0042406	extrinsic component of endoplasmic reticulum membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q69ZF3 ensembl:ENSMUSP00000030189	C	Seeded From UniProt	complete
involved_in	GO:0031113	regulation of microtubule polymerization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q69ZF3 ensembl:ENSMUSP00000030189	P	Seeded From UniProt	complete
involved_in	GO:0030833	regulation of actin filament polymerization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q69ZF3 ensembl:ENSMUSP00000030189	P	Seeded From UniProt	complete
involved_in	GO:0030259	lipid glycosylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q69ZF3 ensembl:ENSMUSP00000030189	P	Seeded From UniProt	complete
part_of	GO:0019898	extrinsic component of membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q69ZF3 ensembl:ENSMUSP00000030189	C	Seeded From UniProt	complete
involved_in	GO:0008203	cholesterol metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q69ZF3 ensembl:ENSMUSP00000030189	P	Seeded From UniProt	complete
involved_in	GO:0006680	glucosylceramide catabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q69ZF3 ensembl:ENSMUSP00000030189	P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q69ZF3 ensembl:ENSMUSP00000030189	C	Seeded From UniProt	complete
enables	GO:0004348	glucosylceramidase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q69ZF3 ensembl:ENSMUSP00000030189	F	Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR008928 InterPro:IPR012341	F	Seeded From UniProt	complete
enables	GO:0004348	glucosylceramidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR014551	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:IPR006775	F	Seeded From UniProt	complete
involved_in	GO:0006680	glucosylceramide catabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR014551	P	Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR014551	C	Seeded From UniProt	complete
enables	GO:0004348	glucosylceramidase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.2.1.45	F	Seeded From UniProt	complete
enables	GO:0050295	steryl-beta-glucosidase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.2.1.104	F	Seeded From UniProt	complete
involved_in	GO:0008206	bile acid metabolic process	PMID:11489889^[6]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005790	smooth endoplasmic reticulum	PMID:11489889^[6]	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
part_of	GO:0005886	plasma membrane	Reactome:R-HSA-1861788	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0004348	glucosylceramidase activity	Reactome:R-HSA-1861788	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006629	lipid metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0443	P	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
enables	GO:0016757	transferase activity, transferring glycosyl groups	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0328	F	Seeded From UniProt	complete
involved_in	GO:0008202	steroid metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0753	P	Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0256	C	Seeded From UniProt	complete
involved_in	GO:0006665	sphingolipid metabolic process	GO_REF:0000037 GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0746 UniPathway:UPA00222	P	Seeded From UniProt	complete
involved_in	GO:0008203	cholesterol metabolic process	GO_REF:0000037 GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0153 UniPathway:UPA00296	P	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
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C	Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F	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:0005794	Golgi apparatus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0333	C	Seeded From UniProt	complete
part_of	GO:0000139	Golgi membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0134	C	Seeded From UniProt	complete
part_of	GO:0005789	endoplasmic reticulum membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0097	C	Seeded From UniProt	complete
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Notes

References

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

↑ Aureli, M et al. (2009) Activity of plasma membrane beta-galactosidase and beta-glucosidase. FEBS Lett. 583 2469-73 PubMed GONUTS page
↑ ^2.0 ^2.1 Yildiz, Y et al. (2006) Mutation of beta-glucosidase 2 causes glycolipid storage disease and impaired male fertility. J. Clin. Invest. 116 2985-94 PubMed GONUTS page
↑ Malekkou, A et al. (2018) Biochemical Characterization of the c.1780G>C Missense Mutation in Lymphoblastoid Cells from Patients with Spastic Ataxia. Int J Mol Sci 19 PubMed GONUTS page
↑ Martin, E et al. (2013) Loss of function of glucocerebrosidase GBA2 is responsible for motor neuron defects in hereditary spastic paraplegia. Am. J. Hum. Genet. 92 238-44 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 Boot, RG et al. (2007) Identification of the non-lysosomal glucosylceramidase as beta-glucosidase 2. J. Biol. Chem. 282 1305-12 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 ^6.3 ^6.4 Matern, H et al. (2001) Molecular cloning and expression of human bile acid beta-glucosidase. J. Biol. Chem. 276 37929-33 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:19577566-1] Aureli, M et al. (2009) Activity of plasma membrane beta-galactosidase and beta-glucosidase. FEBS Lett. 583 2469-73 PubMed GONUTS page

[PMID:17080196-2] 2.0 ^2.1 Yildiz, Y et al. (2006) Mutation of beta-glucosidase 2 causes glycolipid storage disease and impaired male fertility. J. Clin. Invest. 116 2985-94 PubMed GONUTS page

[PMID:30308956-3] Malekkou, A et al. (2018) Biochemical Characterization of the c.1780G>C Missense Mutation in Lymphoblastoid Cells from Patients with Spastic Ataxia. Int J Mol Sci 19 PubMed GONUTS page

[PMID:23332916-4] Martin, E et al. (2013) Loss of function of glucocerebrosidase GBA2 is responsible for motor neuron defects in hereditary spastic paraplegia. Am. J. Hum. Genet. 92 238-44 PubMed GONUTS page

[PMID:17105727-5] 5.0 ^5.1 ^5.2 Boot, RG et al. (2007) Identification of the non-lysosomal glucosylceramidase as beta-glucosidase 2. J. Biol. Chem. 282 1305-12 PubMed GONUTS page

[PMID:11489889-6] 6.0 ^6.1 ^6.2 ^6.3 ^6.4 Matern, H et al. (2001) Molecular cloning and expression of human bile acid beta-glucosidase. J. Biol. Chem. 276 37929-33 PubMed GONUTS page

[PMID:21873635-7] 7.0 ^7.1 ^7.2 ^7.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

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HUMAN:GBA2

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References

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