Reviewed, UniProtKB/Swiss-Prot P16278 (BGAL_HUMAN)

Names and origin

Protein names

Recommended name:
    Beta-galactosidase
    EC=3.2.1.23
Alternative name(s):
    Acid beta-galactosidase
      Short name=Lactase
    Elastin receptor 1

Gene names

Name:	GLB1
Synonyms:	ELNR1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	677 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans. Ref.9 Isoform 2 has no beta-galactosidase catalytic activity, but plays functional roles in the formation of extracellular elastic fibers (elastogenesis) and in the development of connective tissue. Seems to be identical to the elastin-binding protein (EBP), a major component of the non-integrin cell surface receptor expressed on fibroblasts, smooth muscle cells, chondroblasts, leukocytes, and certain cancer cell types. In elastin producing cells, associates with tropoelastin intracellularly and functions as a recycling molecular chaperone which facilitates the secretions of tropoelastin and its assembly into elastic fibers. Ref.9
Catalytic activity	Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
Subcellular location	Isoform 1: Lysosome. Isoform 2: Cytoplasm › perinuclear region. Note: Localized to the perinuclear area of the cytoplasm but not to lysosomes.
Involvement in disease	Defects in GLB1 are the cause of GM1-gangliosidosis type 1 (GM1G1) [MIM:230500]; also known as infantile GM1-gangliosidosis. GM1-gangliosidosis is an autosomal recessive lysosomal storage disease marked by the accumulation of GM1 gangliosides, glycoproteins and keratan sulfate primarily in neurons of the central nervous system. GM1G1 is characterized by onset within the first three months of life, central nervous system degeneration, coarse facial features, hepatosplenomegaly, skeletal dysmorphology reminiscent of Hurler syndrome, and rapidly progressive psychomotor deterioration. Urinary oligosaccharide levels are high. It leads to death usually between the first and second year of life. Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.22 Ref.25 Ref.28 Ref.29 Ref.30 Ref.33 Ref.35 Ref.40 Defects in GLB1 are the cause of GM1-gangliosidosis type 2 (GM1G2) [MIM:230600]; also known as late infantile/juvenile GM1-gangliosidosis. GM1G2 is characterized by onset between ages 1 and 5. The main symptom is locomotor ataxia, ultimately leading to a state of decerebration with epileptic seizures. Patients do not display the skeletal changes associated with the infantile form, but they nonetheless excrete elevated amounts of beta-linked galactose-terminal oligosaccharides. Inheritance is autosomal recessive. Defects in GLB1 are the cause of GM1-gangliosidosis type 3 (GM1G3) [MIM:230650]; also known as adult or chronic GM1-gangliosidosis. GM1G3 is characterized by a variable phenotype. Patients show mild skeletal abnormalities, dysarthria, gait disturbance, dystonia and visual impairment. Visceromegaly is absent. Intellectual deficit can initially be mild or absent but progresses over time. Inheritance is autosomal recessive. Defects in GLB1 are the cause of mucopolysaccharidosis type 4B (MPS4B) [MIM:253010]; also known as Morquio syndrome B. MPS4B is a form of mucopolysaccharidosis type 4, an autosomal recessive lysosomal storage disease characterized by intracellular accumulation of keratan sulfate and chondroitin-6-sulfate. Key clinical features include short stature, skeletal dysplasia, dental anomalies, and corneal clouding. Intelligence is normal and there is no direct central nervous system involvement, although the skeletal changes may result in neurologic complications. There is variable severity, but patients with the severe phenotype usually do not survive past the second or third decade of life. Ref.16 Ref.31 Ref.23 Ref.27
Sequence similarities	Belongs to the glycosyl hydrolase 35 family.

Ontologies

Keywords
Cellular component	Cytoplasm Lysosome
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Gangliosidosis
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein Zymogen
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	beta-galactosidase activity Ref.1 Traceable author statement. Source: UniProtKB cation binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CTNNBIP1	Q9NSA3	1	EBI-989638,EBI-747082
NEU1	Q99519	1	EBI-989638,EBI-721517

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P16278-1)

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.

Isoform 2 (identifier: P16278-2)

Also known as: Beta-galactosidase-related protein; Beta-galactosidase-like protein; S-Gal; Elastin-binding protein; EBP;

The sequence of this isoform differs from the canonical sequence as follows:
     83-244: YVPWNFHEPW...GLYTTVDFGT → LPGSCGQVVGSPSAQDEASPLSEWRASYNSA

Note: Localized to the perinuclear area of the cytoplasm but not to lysosomes.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23
	Propeptide	24 – 28	5			PRO_0000012185
	Chain	29 – 677	649	Beta-galactosidase		PRO_0000012186
Sites
	Active site	188	1	Proton donor Potential
	Active site	268	1	Nucleophile Potential
Amino acid modifications
	Glycosylation	26	1	N-linked (GlcNAc...) Potential
	Glycosylation	247	1	N-linked (GlcNAc...) Potential
	Glycosylation	464	1	N-linked (GlcNAc...) Ref.13 Ref.15
	Glycosylation	498	1	N-linked (GlcNAc...) Potential
	Glycosylation	542	1	N-linked (GlcNAc...) Potential
	Glycosylation	545	1	N-linked (GlcNAc...) Potential
	Glycosylation	555	1	N-linked (GlcNAc...) Ref.15
Natural variations
	Alternative sequence	83 – 244	162	YVPWN…VDFGT → LPGSCGQVVGSPSAQDEASP LSEWRASYNSA in isoform 2.		VSP_031241
	Natural variant	10	1	P → L in GM1G1. dbSNP rs7637099.		VAR_008671
	Natural variant	49	1	R → C in GM1G1. Ref.17		VAR_003329
	Natural variant	49	1	R → H in GM1G3.		VAR_062340
	Natural variant	51	1	I → T in GM1G3. Ref.17 Ref.18		VAR_003330
	Natural variant	59	1	R → C in GM1G1; protein enzymatically inactive; severe mutation. Ref.25 Ref.30 Ref.35 Ref.40		VAR_026129
	Natural variant	59	1	R → H in GM1G1; with cardiac involvement in some patients; protein enzymatically inactive; severe mutation. Ref.25 Ref.28 Ref.30 Ref.35 Ref.40		VAR_008672
	Natural variant	68	1	R → Q in GM1G2; 7.4% of wild-type enzyme activity.		VAR_062341
	Natural variant	68	1	R → W in GM1G2; no enzyme activity. Ref.32		VAR_026130
	Natural variant	73	1	K → E in GM1G3.		VAR_062342
	Natural variant	82	1	T → M in GM1G3; mild phenotype. Ref.21 Ref.31		VAR_008673
	Natural variant	83	1	Y → C in MPS4B.		VAR_062343
	Natural variant	83	1	Y → H in MPS4B; 2-5% of activity. Ref.23		VAR_008674
	Natural variant	109	1	R → W: dbSNP rs35289681.		VAR_053875
	Natural variant	121	1	R → S in GM1G1. Ref.28		VAR_008675
	Natural variant	123	1	G → R in GM1G1.		VAR_003331
	Natural variant	132	1	M → T in GM1G1; 4.3% of wild-type enzyme activity.		VAR_062344
	Natural variant	134	1	G → V in GM1G1. Ref.40		VAR_037937
	Natural variant	136	1	P → S in GM1G1.		VAR_062345
	Natural variant	147	1	Missing in GM1G1.		VAR_037938
	Natural variant	148	1	R → C in GM1G3.		VAR_062346
	Natural variant	148	1	R → S in GM1G1. Ref.22 Ref.29		VAR_013541
	Natural variant	149	1	S → F in MPS4B; 2.0% of wild-type enzyme activity.		VAR_062347
	Natural variant	151	1	D → V in GM1G1.		VAR_062348
	Natural variant	151	1	D → Y in GM1G1; complete lack of protein; no enzymatic activity. Ref.33		VAR_026131
	Natural variant	155	1	L → R in GM1G2 and GM1G3; 6.7% of wild-type enzyme activity.		VAR_037939
	Natural variant	162	1	L → S in GM1G1. Ref.40		VAR_037940
	Natural variant	173	1	L → P in GM1G1.		VAR_062349
	Natural variant	184	1	Q → R in GM1G1; no enzymatic activity.		VAR_062350
	Natural variant	190	1	G → D in GM1G1; 3.4% of wild-type enzyme activity.		VAR_062351
	Natural variant	198	1	D → Y in MPS4B; 17.4% of wild-type enzyme activity.		VAR_062352
	Natural variant	199	1	Y → C in GM1G1.		VAR_062353
	Natural variant	201	1	R → C in GM1G1 and GM1G2; 8.4% of wild-type enzyme activity; activity severely reduced in transfection with the F-436 polymorphism.		VAR_003332
	Natural variant	201	1	R → H in GM1G2; 36.2% of wild-type enzyme activity; also in GM1G1 and a patient with a slowly progressive GM1-gangliosidosis form.		VAR_013542
	Natural variant	208	1	R → C in GM1G1. Ref.20 Ref.28 Ref.35 Ref.40		VAR_008676
	Natural variant	214	1	D → Y in GM1G3. Ref.22		VAR_013543
	Natural variant	216	1	V → A in GM1G1. Ref.22		VAR_013544
	Natural variant	239	1	T → M in GM1G1; protein enzymatically inactive; severe mutation; causes a rapid degradation of the protein precursor. Ref.35		VAR_026132
	Natural variant	240	1	V → M in GM1G1. Ref.28		VAR_008677
	Natural variant	255	1	Q → H in GM1G1; 2.4% of wild-type enzyme activity.		VAR_062354
	Natural variant	263	1	P → S in GM1G3. Ref.24		VAR_013545
	Natural variant	264	1	L → S in GM1G2.		VAR_062355
	Natural variant	266	1	N → S in GM1G3. Ref.26		VAR_013546
	Natural variant	270	1	Y → D in GM1G3; originally classified as Morquio syndrome. Ref.31		VAR_013547
	Natural variant	272	1	G → D in GM1G1. Ref.40		VAR_038346
	Natural variant	273	1	W → L in MPS4B; 8% of activity. Ref.16 Ref.31		VAR_003333
	Natural variant	281	1	H → Y in GM1G1 and GM1G3. Ref.35 Ref.31		VAR_013548
	Natural variant	316	1	Y → C in GM1G1. Ref.18		VAR_003334
	Natural variant	318	1	N → H in GM1G1; uncertain pathogenicity.		VAR_062356
	Natural variant	329	1	T → I in GM1G1; 5.0% of wild-type enzyme activity.		VAR_062357
	Natural variant	332	1	D → E in GM1G1; 2.3% of wild-type enzyme activity.		VAR_062358
	Natural variant	332	1	D → N in GM1G1. Ref.29		VAR_013549
	Natural variant	333	1	Y → H in GM1G2; 3.0% of wild-type enzyme activity; the mutant protein is localized in the lysosomal-endosomal compartment.		VAR_062359
	Natural variant	346	1	K → N in GM1G1.		VAR_062360
	Natural variant	347	1	Y → C in GM1G1.		VAR_062361
	Natural variant	377 – 381	5	Missing in GM1G1.		VAR_037941
	Natural variant	397	1	P → A in MPS4B; 24.0% of wild-type enzyme activity.		VAR_062362
	Natural variant	408	1	Q → P in MPS4B; 1.1% of wild-type enzyme activity.		VAR_013550
	Natural variant	420	1	T → K in GM1G3.		VAR_062363
	Natural variant	420	1	T → P in GM1G1.		VAR_062364
	Natural variant	422	1	L → R in GM1G1.		VAR_062365
	Natural variant	434	1	S → L in GM1-gangliosidosis; unclassified clinical type. Ref.40		VAR_037942
	Natural variant	436	1	L → F Seems to have a modulating action in the expression of the severity of other mutations. dbSNP rs34421970.		VAR_026133
	Natural variant	438	1	G → E in GM1G3 and MPS4B; mild form; 5.7% of activity.		VAR_013551
	Natural variant	441	1	D → N in GM1G1.		VAR_062366
	Natural variant	442	1	R → Q in GM1G1.		VAR_062367
	Natural variant	444	1	Y → C in MPS4B.		VAR_062368
	Natural variant	457	1	R → Q in GM1G3.		VAR_003335
	Natural variant	482	1	R → C in MPS4B; loss of activity. Ref.23		VAR_008678
	Natural variant	482	1	R → H in MPS4B and GM1G1; loss of activity. Ref.16 Ref.19 Ref.30 Ref.35		VAR_003336
	Natural variant	484	1	N → K in MPS4B; mild form; 1.9% of activity. Ref.27		VAR_013552
	Natural variant	491	1	D → N in GM1G1. Ref.28		VAR_008679
	Natural variant	491	1	D → Y in GM1G1. Ref.40		VAR_037943
	Natural variant	494	1	G → C in GM1G1. Ref.16		VAR_013553
	Natural variant	494	1	G → S in MPS4B.		VAR_062369
	Natural variant	500	1	T → A in MPS4B; mild form; 2.1% of activity. Ref.31 Ref.27		VAR_013554
	Natural variant	509	1	W → C in MPS4B; also in a patient with a slowly progressive form of GM1-gangisidosis; loss of activity. Ref.16 Ref.26		VAR_003337
	Natural variant	521	1	R → C in a GM1-gangliosidosis patient; mild phenotype; reduction of activity; could be a polymorphism. dbSNP rs4302331. Ref.28 Ref.35 Ref.6		VAR_008680
	Natural variant	532	1	S → G		VAR_008681
	Natural variant	549	1	P → L in GM1G1. Ref.40		VAR_037944
	Natural variant	554	1	G → E in GM1-gangliosidosis; unclassified clinical type. Ref.40		VAR_037945
	Natural variant	578	1	K → R in GM1G1. Ref.20		VAR_008682
	Natural variant	579	1	G → D in GM1G1 and GM1G2; protein enzymatically inactive; severe mutation. Ref.30 Ref.35		VAR_013555
	Natural variant	590	1	R → C in GM1G1. Ref.40		VAR_037946
	Natural variant	590	1	R → H in GM1G2. Ref.20		VAR_008683
	Natural variant	591	1	Y → C in GM1G1; with cardiac involvement in some patients; protein enzymatically inactive; severe mutation; causes a rapid degradation of the protein precursor. Ref.25 Ref.30 Ref.35		VAR_008684
	Natural variant	591	1	Y → N in GM1G1; with cardiac involvement in some patients; protein enzymatically inactive; severe mutation; causes a rapid degradation of the protein precursor. Ref.25 Ref.30 Ref.35		VAR_008685
	Natural variant	595	1	R → W Reduction of activity. Ref.41		VAR_037947
	Natural variant	597	1	P → S in GM1G1; 2.1% of wild-type enzyme activity.		VAR_062370
	Natural variant	632	1	E → G in GM1G2. Ref.20		VAR_008686
Experimental info
	Sequence conflict	201	1	R → A in AAA51822. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 25, 2008. Version 2. Checksum: 74421586B1BCFECA	FASTA	677	76,075
	10 20 30 40 50 60 MPGFLVRILP LLLVLLLLGP TRGLRNATQR MFEIDYSRDS FLKDGQPFRY ISGSIHYSRV 70 80 90 100 110 120 PRFYWKDRLL KMKMAGLNAI QTYVPWNFHE PWPGQYQFSE DHDVEYFLRL AHELGLLVIL 130 140 150 160 170 180 RPGPYICAEW EMGGLPAWLL EKESILLRSS DPDYLAAVDK WLGVLLPKMK PLLYQNGGPV 190 200 210 220 230 240 ITVQVENEYG SYFACDFDYL RFLQKRFRHH LGDDVVLFTT DGAHKTFLKC GALQGLYTTV 250 260 270 280 290 300 DFGTGSNITD AFLSQRKCEP KGPLINSEFY TGWLDHWGQP HSTIKTEAVA SSLYDILARG 310 320 330 340 350 360 ASVNLYMFIG GTNFAYWNGA NSPYAAQPTS YDYDAPLSEA GDLTEKYFAL RNIIQKFEKV 370 380 390 400 410 420 PEGPIPPSTP KFAYGKVTLE KLKTVGAALD ILCPSGPIKS LYPLTFIQVK QHYGFVLYRT 430 440 450 460 470 480 TLPQDCSNPA PLSSPLNGVH DRAYVAVDGI PQGVLERNNV ITLNITGKAG ATLDLLVENM 490 500 510 520 530 540 GRVNYGAYIN DFKGLVSNLT LSSNILTDWT IFPLDTEDAV RSHLGGWGHR DSGHHDEAWA 550 560 570 580 590 600 HNSSNYTLPA FYMGNFSIPS GIPDLPQDTF IQFPGWTKGQ VWINGFNLGR YWPARGPQLT 610 620 630 640 650 660 LFVPQHILMT SAPNTITVLE LEWAPCSSDD PELCAVTFVD RPVIGSSVTY DHPSKPVEKR 670 LMPPPPQKNK DSWLDHV
	Isoform 2 (Beta-galactosidase-related protein) (Beta-galactosidase-like protein) (S-Gal) (Elastin-binding protein) (EBP) [UniParc] [UniParc]. Checksum: 2EC2BBA4F39E966C	FASTA	546	60,536
	10 20 30 40 50 60 MPGFLVRILP LLLVLLLLGP TRGLRNATQR MFEIDYSRDS FLKDGQPFRY ISGSIHYSRV 70 80 90 100 110 120 PRFYWKDRLL KMKMAGLNAI QTLPGSCGQV VGSPSAQDEA SPLSEWRASY NSAGSNITDA 130 140 150 160 170 180 FLSQRKCEPK GPLINSEFYT GWLDHWGQPH STIKTEAVAS SLYDILARGA SVNLYMFIGG 190 200 210 220 230 240 TNFAYWNGAN SPYAAQPTSY DYDAPLSEAG DLTEKYFALR NIIQKFEKVP EGPIPPSTPK 250 260 270 280 290 300 FAYGKVTLEK LKTVGAALDI LCPSGPIKSL YPLTFIQVKQ HYGFVLYRTT LPQDCSNPAP 310 320 330 340 350 360 LSSPLNGVHD RAYVAVDGIP QGVLERNNVI TLNITGKAGA TLDLLVENMG RVNYGAYIND 370 380 390 400 410 420 FKGLVSNLTL SSNILTDWTI FPLDTEDAVR SHLGGWGHRD SGHHDEAWAH NSSNYTLPAF 430 440 450 460 470 480 YMGNFSIPSG IPDLPQDTFI QFPGWTKGQV WINGFNLGRY WPARGPQLTL FVPQHILMTS 490 500 510 520 530 540 APNTITVLEL EWAPCSSDDP ELCAVTFVDR PVIGSSVTYD HPSKPVEKRL MPPPPQKNKD SWLDHV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, sequencing, and expression of cDNA for human beta-galactosidase." Oshima A., Tsuji A., Nagao Y., Sakuraba H., Suzuki Y. Biochem. Biophys. Res. Commun. 157:238-244(1988) [PubMed: 3143362] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Placenta.
[2]	"Alternative splicing of beta-galactosidase mRNA generates the classic lysosomal enzyme and a beta-galactosidase-related protein." Morreau H., Galjart N.J., Gillemans N., Willemsen R., van der Horst G.T.J., D'Azzo A. J. Biol. Chem. 264:20655-20663(1989) [PubMed: 2511208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PARTIAL PROTEIN SEQUENCE, VARIANT LEU-10. Tissue: Testis.
[3]	"Isolation, characterization, and mapping of a human acid beta-galactosidase cDNA." Yamamoto Y., Hake C.A., Martin B.M., Kretz K.A., Ahern-Rindell A.J., Naylor S.L., Mudd M., O'Brien J.S. DNA Cell Biol. 9:119-127(1990) [PubMed: 2111707] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LEU-10.
[4]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-10.
[6]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed: 16641997] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT CYS-521.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-10. Tissue: Colon.
[8]	"The 67-kD elastin/laminin-binding protein is related to an enzymatically inactive, alternatively spliced form of beta-galactosidase." Hinek A., Rabinovitch M., Keeley F., Okamura-Oho Y., Callahan J. J. Clin. Invest. 91:1198-1205(1993) [PubMed: 8383699] [Abstract] Cited for: DOMAIN ELASTIN/LAMININ BINDING.
[9]	"Biological roles of the non-integrin elastin/laminin receptor." Hinek A. Biol. Chem. 377:471-480(1996) [PubMed: 8922281] [Abstract] Cited for: FUNCTION (ISOFORM 2).
[10]	"The 67-kDa enzymatically inactive alternatively spliced variant of beta-galactosidase is identical to the elastin/laminin-binding protein." Privitera S., Prody C.A., Callahan J.W., Hinek A. J. Biol. Chem. 273:6319-6326(1998) [PubMed: 9497360] [Abstract] Cited for: IDENTITY OF BETA-GALACTOSIDASE-RELATED PROTEIN WITH EBP.
[11]	"Molecular basis of GM1 gangliosidosis and Morquio disease, type B. Structure-function studies of lysosomal beta-galactosidase and the non-lysosomal beta-galactosidase-like protein." Callahan J.W. Biochim. Biophys. Acta 1455:85-103(1999) [PubMed: 10571006] [Abstract] Cited for: REVIEW.
[12]	"Impaired elastic-fiber assembly by fibroblasts from patients with either Morquio B disease or infantile GM1-gangliosidosis is linked to deficiency in the 67-kD spliced variant of beta-galactosidase." Hinek A., Zhang S., Smith A.C., Callahan J.W. Am. J. Hum. Genet. 67:23-36(2000) [PubMed: 10841810] [Abstract] Cited for: ELASTIC-FIBER ASSEMBLY STUDIES.
[13]	"Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach." Lewandrowski U., Moebius J., Walter U., Sickmann A. Mol. Cell. Proteomics 5:226-233(2006) [PubMed: 16263699] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-464, MASS SPECTROMETRY. Tissue: Platelet.
[14]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[15]	"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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-464 AND ASN-555, MASS SPECTROMETRY. Tissue: Liver.
[16]	"Human beta-galactosidase gene mutations in morquio B disease." Oshima A., Yoshida K., Shimmoto M., Fukuhara Y., Sakuraba H., Suzuki Y. Am. J. Hum. Genet. 49:1091-1093(1991) [PubMed: 1928092] [Abstract] Cited for: VARIANTS MPS4B LEU-273; HIS-482 AND CYS-509, VARIANT GM1G1 CYS-494.
[17]	"GM1-gangliosidosis (genetic beta-galactosidase deficiency): identification of four mutations in different clinical phenotypes among Japanese patients." Nishimoto J., Nanba E., Inui K., Okada S., Suzuki K. Am. J. Hum. Genet. 49:566-574(1991) [PubMed: 1909089] [Abstract] Cited for: VARIANT GM1G1 CYS-49, VARIANT GM1G3 THR-51, VARIANT GM1G2 CYS-201.
[18]	"Human beta-galactosidase gene mutations in GM1-gangliosidosis: a common mutation among Japanese adult/chronic cases." Yoshida K., Oshima A., Shimmoto M., Fukuhara Y., Sakuraba H., Yanagisawa N., Suzuki Y. Am. J. Hum. Genet. 49:435-442(1991) [PubMed: 1907800] [Abstract] Cited for: VARIANTS GM1G3 THR-51 AND GLN-457, VARIANTS GM1G1 ARG-123 AND CYS-316, VARIANT GM1G2 CYS-201.
[19]	"A homozygous missense arginine to histidine substitution at position 482 of the beta-galactosidase in an Italian infantile GM1-gangliosidosis patient." Mosna G., Fattore S., Tubiello G., Brocca S., Trubia M., Gianazza E., Gatti R., Danesino C., Minelli A., Piantanida M. Hum. Genet. 90:247-250(1992) [PubMed: 1487238] [Abstract] Cited for: VARIANT GM1G1 HIS-482.
[20]	"Mutations in acid beta-galactosidase cause GM1-gangliosidosis in American patients." Boustany R.-M.N., Qian W.-H., Suzuki K. Am. J. Hum. Genet. 53:881-888(1993) [PubMed: 8213816] [Abstract] Cited for: VARIANTS GM1G1 CYS-208 AND ARG-578, VARIANTS GM1G2 HIS-590 AND GLY-632.
[21]	"Mutations in the lysosomal beta-galactosidase gene that cause the adult form of GM1 gangliosidosis." Chakraborty S., Rafi M.A., Wenger D.A. Am. J. Hum. Genet. 54:1004-1013(1994) [PubMed: 8198123] [Abstract] Cited for: VARIANT GM1G3 MET-82.
[22]	"Novel missense mutations in beta-glactosidase that result in GM1-gangliosidosis." Hilson W.L., Okamura-Oho Y., Zhang S., Clarke J.T.R., Mahuran D., Callahan J.W. Am. J. Hum. Genet. 55:A223-A223(1994) Cited for: VARIANTS GM1G1 SER-148 AND ALA-216, VARIANT GM1G3 TYR-214, VARIANT GLY-532.
[23]	"Clinical and molecular analysis of a Japanese boy with Morquio B disease." Ishii N., Oohira T., Oshima A., Sakuraba H., Endo F., Matsuda I., Sukegawa K., Orii T., Suzuki Y. Clin. Genet. 48:103-108(1995) [PubMed: 7586649] [Abstract] Cited for: VARIANTS MPS4B HIS-83 AND CYS-482.
[24]	"Beta-galactosidase deficiency (beta-galactosidosis): GM1 gangliosidosis and Morquio B disease." Suzuki Y., Sakuraba H., Oshima A. (In) Scriver C.R., Beaudet A.L., Sly W.S., Valle D. (eds.); The metabolic and molecular bases of inherited disease, pp.2787-2823, McGraw-Hill Publishing Co., New York (1995) Cited for: VARIANT GM1G3 SER-263.
[25]	"Identification of new mutations in six Italian patients affected by a variant form of infantile GM1-gangliosidosis with severe cardiomyopathy." Morrone A., Bardelli T., Donati M.A., Giorgi M., Di Rocco R., Gatti R., Taddeucci G., Ricci R., D'Azzo A., Zammarchi E. Am. J. Hum. Genet. 61:A258-A258(1997) Cited for: VARIANTS GM1G1 HIS-59; ASN-591 AND CYS-591.
[26]	"Beta-Galactosidase gene mutations in patients with slowly progressive GM1 gangliosidosis." Kaye E.M., Shalish C., Livermore J., Taylor H.A., Stevenson R.E., Breakefield X.O. J. Child Neurol. 12:242-247(1997) [PubMed: 9203065] [Abstract] Cited for: VARIANTS SLOWLY PROGRESSIVE GM1-GANGLIOSIDOSIS HIS-201; SER-266 AND CYS-509.
[27]	"Novel mutations (Asn 484 Lys, Thr 500 Ala, Gly 438 Glu) in Morquio B disease." Bagshaw R.D., Zhang S., Hinek A., Skomorowski M.-A., Whelan D., Clarke J.T.R., Callahan J.W. Biochim. Biophys. Acta 1588:247-253(2002) [PubMed: 12393180] [Abstract] Cited for: VARIANTS MPS4B GLU-438; LYS-484 AND ALA-500.
[28]	"Six novel beta-galactosidase gene mutations in Brazilian patients with GM1-gangliosidosis." Silva C.M.D., Severini M.H., Sopelsa A., Coelho J.C., Zaha A., d'Azzo A., Giugliani R. Hum. Mutat. 13:401-409(1999) [PubMed: 10338095] [Abstract] Cited for: VARIANTS GM1G1 HIS-59; SER-121; CYS-208; MET-240 AND ASN-491, VARIANTS LEU-10; CYS-521 AND GLY-532.
[29]	"Characterization of beta-galactosidase mutations Asp332-->Asn and Arg148-->Ser, and a polymorphism, Ser532-->Gly, in a case of GM1 gangliosidosis." Zhang S., Bagshaw R., Hilson W., Oho Y., Hinek A., Clarke J.T.R., Hinek A., Callahan J.W. Biochem. J. 348:621-632(2000) [PubMed: 10839995] [Abstract] Cited for: VARIANTS GM1G1 SER-148 AND ASN-332, VARIANT GLY-532.
[30]	"Beta-galactosidase gene mutations affecting the lysosomal enzyme and the elastin-binding protein in GM1-gangliosidosis patients with cardiac involvement." Morrone A., Bardelli T., Donati M.A., Giorgi M., Di Rocco M., Gatti R., Parini R., Ricci R., Taddeucci G., D'Azzo A., Zammarchi E. Hum. Mutat. 15:354-366(2000) [PubMed: 10737981] [Abstract] Cited for: VARIANTS GM1G1 HIS-59; HIS-482; ASN-591 AND CYS-591, VARIANTS GM1G2 HIS-201 AND ASP-579.
[31]	"Mutation analyses in 17 patients with deficiency in acid beta-galactosidase: three novel point mutations and high correlation of mutation W273L with Morquio disease type B." Paschke E., Milos I., Kreimer-Erlacher H., Hoefler G., Beck M., Hoeltzenbein M., Kleijer W., Levade T., Michelakakis H., Radeva B. Hum. Genet. 109:159-166(2001) [PubMed: 11511921] [Abstract] Cited for: VARIANTS MPS4B LEU-273; PRO-408 AND ALA-500, VARIANTS GM1G3 MET-82; ASP-270 AND TYR-281, VARIANT LEU-10.
[32]	"Modulating action of the new polymorphism L436F detected in the GLB1 gene of a type-II GM1 gangliosidosis patient." Caciotti A., Bardelli T., Cunningham J., D'Azzo A., Zammarchi E., Morrone A. Hum. Genet. 113:44-50(2003) [PubMed: 12644936] [Abstract] Cited for: VARIANTS GM1G2 TRP-68 AND CYS-201, CHARACTERIZATION OF VARIANTS GM1G2 TRP-68 AND CYS-201, VARIANT PHE-436, MODULATING ACTION OF VARIANT PHE-436.
[33]	"Four novel mutations in patients from the Middle East with the infantile form of GM1-gangliosidosis." Georgiou T., Drousiotou A., Campos Y., Caciotti A., Sztriha L., Gururaj A., Ozand P., Zammarchi E., Morrone A., D'Azzo A. Hum. Mutat. 24:352-352(2004) [PubMed: 15365997] [Abstract] Cited for: VARIANT GM1G1 TYR-151, CHARACTERIZATION OF VARIANT GM1G1 TYR-151.
[34]	Erratum Georgiou T., Drousiotou A., Campos Y., Caciotti A., Sztriha L., Gururaj A., Ozand P., Zammarchi E., Morrone A., D'Azzo A. Hum. Mutat. 24:536-537(2004)
[35]	"Role of beta-galactosidase and elastin binding protein in lysosomal and nonlysosomal complexes of patients with GM1-gangliosidosis." Caciotti A., Donati M.A., Boneh A., d'Azzo A., Federico A., Parini R., Antuzzi D., Bardelli T., Nosi D., Kimonis V., Zammarchi E., Morrone A. Hum. Mutat. 25:285-292(2005) [PubMed: 15714521] [Abstract] Cited for: VARIANTS GM1G1 HIS-59; CYS-59; CYS-208; MET-239; TYR-281; HIS-482; ASP-579; ASN-591 AND CYS-591, VARIANT GM1G2 HIS-201, VARIANT CYS-521, CHARACTERIZATION OF VARIANTS GM1G1 HIS-59; CYS-59; CYS-208; MET-239; TYR-281; HIS-482; ASP-579; ASN-591 AND CYS-591, CHARACTERIZATION OF VARIANT GM1G2 HIS-201, CHARACTERIZATION OF VARIANT CYS-521.
[36]	"Magnetic resonance imaging findings and novel mutations in GM1 gangliosidosis." Gururaj A., Sztriha L., Hertecant J., Johansen J.G., Georgiou T., Campos Y., Drousiotou A., d'Azzo A. J. Child Neurol. 20:57-60(2005) [PubMed: 15791924] [Abstract] Cited for: VARIANTS GM1G1 LEU-10 AND TYR-151.
[37]	"Dystonia and parkinsonism in GM1 type 3 gangliosidosis." Roze E., Paschke E., Lopez N., Eck T., Yoshida K., Maurel-Ollivier A., Doummar D., Caillaud C., Galanaud D., Billette de Villemeur T., Vidailhet M., Roubergue A. Mov. Disord. 20:1366-1369(2005) [PubMed: 15986423] [Abstract] Cited for: VARIANTS GM1G3 HIS-49; GLU-73; CYS-148 AND GLU-438.
[38]	"Twenty-one novel mutations in the GLB1 gene identified in a large group of GM1-gangliosidosis and Morquio B patients: possible common origin for the prevalent p.R59H mutation among Gypsies." Santamaria R., Chabas A., Coll M.J., Miranda C.S., Vilageliu L., Grinberg D. Hum. Mutat. 27:1060-1060(2006) [PubMed: 16941474] [Abstract] Cited for: VARIANTS GM1G1 CYS-59; HIS-59; SER-136; VAL-151; PRO-173; CYS-199; ASP-272; ASN-346; CYS-347; PRO-420; ARG-422; ASN-441 AND CYS-590, VARIANT GM1G2 SER-264, VARIANTS GM1G3 HIS-201 AND LYS-420, VARIANTS MPS4B CYS-83; CYS-444; SER-494 AND ALA-500, VARIANTS PHE-436; CYS-521 AND GLY-532.
[39]	"Elastogenesis in cultured dermal fibroblasts from patients with lysosomal beta-galactosidase, protective protein/cathepsin A and neuraminidase-1 deficiencies." Tatano Y., Takeuchi N., Kuwahara J., Sakuraba H., Takahashi T., Takada G., Itoh K. J. Med. Invest. 53:103-112(2006) [PubMed: 16538002] [Abstract] Cited for: VARIANTS MPS4B LEU-273; HIS-482 AND CYS-509, VARIANTS GM1G1 CYS-201; HIS-201 AND HIS-318.
[40]	"Identification of 14 novel GLB1 mutations, including five deletions, in 19 patients with GM1 gangliosidosis from South America." Santamaria R., Blanco M., Chabas A., Grinberg D., Vilageliu L. Clin. Genet. 71:273-279(2007) [PubMed: 17309651] [Abstract] Cited for: VARIANTS GM1G1 CYS-59; HIS-59; VAL-134; LEU-147 DEL; SER-162; CYS-208; ASP-272; 377-VAL--LYS-381 DEL; TYR-491; LEU-549 AND CYS-590, VARIANT GM1G2 HIS-201, VARIANT GM1G3 ARG-155, VARIANTS GM1-GANGLIOSIDOSIS LEU-434 AND GLU-554.
[41]	"Identification of a novel pseudodeficiency allele in the GLB1 gene in a carrier of GM1 gangliosidosis." Gort L., Santamaria R., Grinberg D., Vilageliu L., Chabas A. Clin. Genet. 72:109-111(2007) [PubMed: 17661814] [Abstract] Cited for: VARIANT TRP-595, CHARACTERIZATION OF VARIANT TRP-595.
[42]	"GM1 gangliosidosis and Morquio B disease: expression analysis of missense mutations affecting the catalytic site of acid beta-galactosidase." Hofer D., Paul K., Fantur K., Beck M., Buerger F., Caillaud C., Fumic K., Ledvinova J., Lugowska A., Michelakakis H., Radeva B., Ramaswami U., Plecko B., Paschke E. Hum. Mutat. 30:1214-1221(2009) [PubMed: 19472408] [Abstract] Cited for: VARIANTS GM1G1 HIS-59; THR-132; ARG-184; ASP-190; CYS-201; HIS-201; MET-239; HIS-255; ILE-329; GLU-332; ASN-346; GLN-442 AND SER-597, VARIANTS GM1G2 GLN-68; ARG-155 AND HIS-333, VARIANTS GM1G3 MET-82; ASP-270 AND GLU-438, VARIANTS MPS4B PHE-149; TYR-198; LEU-273; ALA-397; PRO-408 AND ALA-500, CHARACTERIZATION OF VARIANTS GM1G1 THR-132; ARG-184; ASP-190; CYS-201; HIS-201; HIS-255; ILE-329; GLU-332 AND SER-597, CHARACTERIZATION OF VARIANTS GM1G2 GLN-68; ARG-155 AND HIS-333, CHARACTERIZATION OF VARIANTS GM1G3 ASP-270 AND GLU-438, CHARACTERIZATION OF VARIANTS MPS4B PHE-149; TYR-198; LEU-273; ALA-397; PRO-408 AND ALA-500.
+	Additional computationally mapped references.

Web resources

GeneReviews

Wikipedia

Beta-galactosidase entry

Cross-references

Sequence databases
EMBL GenBank DDBJ	M22590 mRNA. Translation: AAA51822.1. M27507 mRNA. Translation: AAA51819.1. M27508 mRNA. Translation: AAA35599.1. M34423 mRNA. Translation: AAA51823.1. AK312988 mRNA. Translation: BAG35825.1. BT007147 mRNA. Translation: AAP35811.1. AC112211 Genomic DNA. No translation available. BC007493 mRNA. Translation: AAH07493.1.
IPI	IPI00441344. IPI00441550.
PIR	A32611. A32688. B32688.
RefSeq	NP_000395.2. NP_001073279.1. NP_001129074.1.
UniGene	Hs.443031
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P16278. 3 interactions.
STRING	P16278.
Protein family/group databases
CAZy	GH35. Glycoside Hydrolase Family 35.
PTM databases
PhosphoSite	P16278.
Proteomic databases
PRIDE	P16278.
Genome annotation databases
Ensembl	ENST00000307363; ENSP00000306920; ENSG00000170266; Homo sapiens. [Genome view]
GeneID	2720.
KEGG	hsa:2720.
UCSC	uc003cfj.1. human.
Organism-specific databases
CTD	2720.
GeneCards	GC03M033013.
H-InvDB	HIX0003151.
HGNC	HGNC:4298. GLB1.
HPA	CAB008382.
MIM	230500. phenotype. 230600. phenotype. 230650. phenotype. 253010. phenotype. 611458. gene.
Orphanet	79255. Gangliosidosis GM1, type 1. 79257. Gangliosidosis GM1, type 3. 354. GM1 gangliosidosis. 582. Mucopolysaccharidosis type 4.
PharmGKB	PA28709.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG13199.
HOVERGEN	P16278.
InParanoid	P16278.
Enzyme and pathway databases
BRENDA	3.2.1.23. 247.
Gene expression databases
ArrayExpress	P16278.
Bgee	P16278.
CleanEx	HS_GLB1.
Genevestigator	P16278.
GermOnline	ENSG00000170266. Homo sapiens.
Family and domain databases
InterPro	IPR019801. Glyco_hydro_35_CS. IPR017853. Glyco_hydro_catalytic_core. IPR013781. Glyco_hydro_sg_catalytic. IPR001944. Glycoside_Hdrlase_35. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PANTHER	PTHR23421. Glyco_hydro_35. 1 hit.
Pfam	PF01301. Glyco_hydro_35. 1 hit. [Graphical view]
PRINTS	PR00742. GLHYDRLASE35.
PROSITE	PS01182. GLYCOSYL_HYDROL_F35. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	10738.
SOURCE	Search...

Entry information

Entry name

BGAL_HUMAN

Accession

Primary (citable) accession number: P16278
Secondary accession number(s): B2R7H8, P16279

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	November 25, 2008
Last modified:	February 9, 2010
This is version 119 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.