Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P16278 (BGAL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 165. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length677 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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: Cytoplasmperinuclear region. Note: Localized to the perinuclear area of the cytoplasm but not to lysosomes.

Involvement in disease

GM1-gangliosidosis 1 (GM1G1) [MIM:230500]: 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. GM1-gangliosidosis type 1 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. 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.36 Ref.38 Ref.39 Ref.40 Ref.42

GM1-gangliosidosis 2 (GM1G2) [MIM:230600]: A gangliosidosis 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17 Ref.18 Ref.20 Ref.30 Ref.32 Ref.35 Ref.38 Ref.40 Ref.42

GM1-gangliosidosis 3 (GM1G3) [MIM:230650]: A gangliosidosis with 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17 Ref.18 Ref.21 Ref.22 Ref.24 Ref.31 Ref.37 Ref.38 Ref.40 Ref.42

Mucopolysaccharidosis 4B (MPS4B) [MIM:253010]: 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.23 Ref.27 Ref.31 Ref.38 Ref.39 Ref.42

Sequence similarities

Belongs to the glycosyl hydrolase 35 family.

Ontologies

Keywords
   Cellular componentCytoplasm
Lysosome
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Gangliosidosis
Mucopolysaccharidosis
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

galactose catabolic process

Inferred from electronic annotation. Source: Ensembl

glycosaminoglycan catabolic process

Traceable author statement. Source: Reactome

glycosaminoglycan metabolic process

Traceable author statement. Source: Reactome

glycosphingolipid metabolic process

Traceable author statement. Source: Reactome

keratan sulfate catabolic process

Traceable author statement. Source: Reactome

keratan sulfate metabolic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

sphingolipid metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

cytoplasm

Inferred from direct assay. Source: HPA

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

lysosomal lumen

Traceable author statement. Source: Reactome

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbeta-galactosidase activity

Traceable author statement Ref.1. Source: UniProtKB

galactoside binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 15498789. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CTNNBIP1Q9NSA31EBI-989638,EBI-747082
NEU1Q995191EBI-989638,EBI-721517

Alternative products

This entry describes 3 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
Isoform 3 (identifier: P16278-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323
Propeptide24 – 285
PRO_0000012185
Chain29 – 677649Beta-galactosidase
PRO_0000012186

Sites

Active site1881Proton donor Potential
Active site2681Nucleophile Potential

Amino acid modifications

Glycosylation261N-linked (GlcNAc...) Potential
Glycosylation2471N-linked (GlcNAc...) Potential
Glycosylation4641N-linked (GlcNAc...) Ref.13 Ref.14
Glycosylation4981N-linked (GlcNAc...) Potential
Glycosylation5421N-linked (GlcNAc...) Potential
Glycosylation5451N-linked (GlcNAc...) Potential
Glycosylation5551N-linked (GlcNAc...) Ref.14

Natural variations

Alternative sequence1 – 3030Missing in isoform 3.
VSP_039974
Alternative sequence83 – 244162YVPWN…VDFGT → LPGSCGQVVGSPSAQDEASP LSEWRASYNSA in isoform 2.
VSP_031241
Natural variant101P → L in GM1G1. Ref.2 Ref.3 Ref.4 Ref.5 Ref.7 Ref.28 Ref.31 Ref.36
Corresponds to variant rs7637099 [ dbSNP | Ensembl ].
VAR_008671
Natural variant491R → C in GM1G1. Ref.17
VAR_003329
Natural variant491R → H in GM1G3. Ref.37
VAR_062340
Natural variant511I → T in GM1G3. Ref.17 Ref.18
VAR_003330
Natural variant591R → C in GM1G1; protein enzymatically inactive; severe mutation. Ref.25 Ref.30 Ref.35 Ref.38 Ref.40
VAR_026129
Natural variant591R → H in GM1G1; with cardiac involvement in some patients; protein enzymatically inactive; severe mutation. Ref.25 Ref.28 Ref.30 Ref.35 Ref.38 Ref.40 Ref.42
VAR_008672
Natural variant681R → Q in GM1G2; 7.4% of wild-type enzyme activity. Ref.42
VAR_062341
Natural variant681R → W in GM1G2; no enzyme activity. Ref.32
VAR_026130
Natural variant731K → E in GM1G3. Ref.37
VAR_062342
Natural variant821T → M in GM1G3; mild phenotype. Ref.21 Ref.31 Ref.42
VAR_008673
Natural variant831Y → C in MPS4B. Ref.38
VAR_062343
Natural variant831Y → H in MPS4B; 2-5% of activity. Ref.23
VAR_008674
Natural variant1091R → W.
Corresponds to variant rs35289681 [ dbSNP | Ensembl ].
VAR_053875
Natural variant1211R → S in GM1G1. Ref.28
VAR_008675
Natural variant1231G → R in GM1G1. Ref.18
VAR_003331
Natural variant1321M → T in GM1G1; 4.3% of wild-type enzyme activity. Ref.42
VAR_062344
Natural variant1341G → V in GM1G1. Ref.40
VAR_037937
Natural variant1361P → S in GM1G1. Ref.38
VAR_062345
Natural variant1471Missing in GM1G1. Ref.40
VAR_037938
Natural variant1481R → C in GM1G3. Ref.37
VAR_062346
Natural variant1481R → S in GM1G1. Ref.22 Ref.29
VAR_013541
Natural variant1491S → F in MPS4B; 2.0% of wild-type enzyme activity. Ref.42
VAR_062347
Natural variant1511D → V in GM1G1. Ref.38
VAR_062348
Natural variant1511D → Y in GM1G1; complete lack of protein; no enzymatic activity. Ref.33 Ref.36
VAR_026131
Natural variant1551L → R in GM1G2 and GM1G3; 6.7% of wild-type enzyme activity. Ref.40 Ref.42
VAR_037939
Natural variant1621L → S in GM1G1. Ref.40
VAR_037940
Natural variant1731L → P in GM1G1. Ref.38
VAR_062349
Natural variant1841Q → R in GM1G1; no enzymatic activity. Ref.42
VAR_062350
Natural variant1901G → D in GM1G1; 3.4% of wild-type enzyme activity. Ref.42
VAR_062351
Natural variant1981D → Y in MPS4B; 17.4% of wild-type enzyme activity. Ref.42
VAR_062352
Natural variant1991Y → C in GM1G1. Ref.38
VAR_062353
Natural variant2011R → C in GM1G1 and GM1G2; 8.4% of wild-type enzyme activity; activity severely reduced in transfection with the F-436 polymorphism. Ref.17 Ref.18 Ref.32 Ref.39 Ref.42
VAR_003332
Natural variant2011R → H in GM1G2; 36.2% of wild-type enzyme activity; also in GM1G1 and a patient with a slowly progressive GM1-gangliosidosis form. Ref.26 Ref.30 Ref.35 Ref.38 Ref.39 Ref.40 Ref.42
VAR_013542
Natural variant2081R → C in GM1G1. Ref.20 Ref.28 Ref.35 Ref.40
VAR_008676
Natural variant2141D → Y in GM1G3. Ref.22
VAR_013543
Natural variant2161V → A in GM1G1. Ref.22
VAR_013544
Natural variant2391T → M in GM1G1; protein enzymatically inactive; severe mutation; causes a rapid degradation of the protein precursor. Ref.35 Ref.42
VAR_026132
Natural variant2401V → M in GM1G1. Ref.28
VAR_008677
Natural variant2551Q → H in GM1G1; 2.4% of wild-type enzyme activity. Ref.42
VAR_062354
Natural variant2631P → S in GM1G3. Ref.24
VAR_013545
Natural variant2641L → S in GM1G2. Ref.38
VAR_062355
Natural variant2661N → S in GM1G3. Ref.26
VAR_013546
Natural variant2701Y → D in GM1G3; originally classified as Morquio syndrome. Ref.31 Ref.42
VAR_013547
Natural variant2721G → D in GM1G1. Ref.38 Ref.40
VAR_038346
Natural variant2731W → L in MPS4B; 8% of activity. Ref.16 Ref.31 Ref.39 Ref.42
VAR_003333
Natural variant2811H → Y in GM1G1 and GM1G3. Ref.31 Ref.35
VAR_013548
Natural variant3161Y → C in GM1G1. Ref.18
VAR_003334
Natural variant3181N → H in GM1G1; unknown pathological significance. Ref.39
VAR_062356
Natural variant3291T → I in GM1G1; 5.0% of wild-type enzyme activity. Ref.42
VAR_062357
Natural variant3321D → E in GM1G1; 2.3% of wild-type enzyme activity. Ref.42
VAR_062358
Natural variant3321D → N in GM1G1. Ref.29
VAR_013549
Natural variant3331Y → H in GM1G2; 3.0% of wild-type enzyme activity; the mutant protein is localized in the lysosomal-endosomal compartment. Ref.42
VAR_062359
Natural variant3461K → N in GM1G1. Ref.38 Ref.42
VAR_062360
Natural variant3471Y → C in GM1G1. Ref.38
VAR_062361
Natural variant377 – 3815Missing in GM1G1.
VAR_037941
Natural variant3971P → A in MPS4B; 24.0% of wild-type enzyme activity. Ref.42
VAR_062362
Natural variant4081Q → P in MPS4B; 1.1% of wild-type enzyme activity. Ref.31 Ref.42
VAR_013550
Natural variant4201T → K in GM1G3. Ref.38
VAR_062363
Natural variant4201T → P in GM1G1. Ref.38
VAR_062364
Natural variant4221L → R in GM1G1. Ref.38
VAR_062365
Natural variant4341S → L in GM1-gangliosidosis; unclassified clinical type. Ref.40
VAR_037942
Natural variant4361L → F Seems to have a modulating action in the expression of the severity of other mutations. Ref.32 Ref.38
Corresponds to variant rs34421970 [ dbSNP | Ensembl ].
VAR_026133
Natural variant4381G → E in GM1G3 and MPS4B; mild form; 5.7% of activity. Ref.27 Ref.37 Ref.42
VAR_013551
Natural variant4411D → N in GM1G1. Ref.38
VAR_062366
Natural variant4421R → Q in GM1G1. Ref.42
VAR_062367
Natural variant4441Y → C in MPS4B. Ref.38
VAR_062368
Natural variant4571R → Q in GM1G3. Ref.18
VAR_003335
Natural variant4821R → C in MPS4B; loss of activity. Ref.23
VAR_008678
Natural variant4821R → H in MPS4B and GM1G1; loss of activity. Ref.16 Ref.19 Ref.30 Ref.35 Ref.39
VAR_003336
Natural variant4841N → K in MPS4B; mild form; 1.9% of activity. Ref.27
VAR_013552
Natural variant4911D → N in GM1G1. Ref.28
VAR_008679
Natural variant4911D → Y in GM1G1. Ref.40
VAR_037943
Natural variant4941G → C in GM1G1. Ref.16
VAR_013553
Natural variant4941G → S in MPS4B. Ref.38
VAR_062369
Natural variant5001T → A in MPS4B; mild form; 2.1% of activity. Ref.27 Ref.31 Ref.38 Ref.42
VAR_013554
Natural variant5091W → C in MPS4B; also in a patient with a slowly progressive form of GM1-gangisidosis; loss of activity. Ref.16 Ref.26 Ref.39
VAR_003337
Natural variant5211R → C in a GM1-gangliosidosis patient; mild phenotype; reduction of activity; unknown pathological significance. Ref.6 Ref.28 Ref.35 Ref.38
Corresponds to variant rs4302331 [ dbSNP | Ensembl ].
VAR_008680
Natural variant5321S → G. Ref.22 Ref.28 Ref.29 Ref.38
VAR_008681
Natural variant5491P → L in GM1G1. Ref.40
VAR_037944
Natural variant5541G → E in GM1-gangliosidosis; unclassified clinical type. Ref.40
VAR_037945
Natural variant5781K → R in GM1G1. Ref.20
VAR_008682
Natural variant5791G → D in GM1G1 and GM1G2; protein enzymatically inactive; severe mutation. Ref.30 Ref.35
VAR_013555
Natural variant5901R → C in GM1G1. Ref.38 Ref.40
VAR_037946
Natural variant5901R → H in GM1G2. Ref.20
VAR_008683
Natural variant5911Y → 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 variant5911Y → 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 variant5951R → W Reduction of activity. Ref.41
VAR_037947
Natural variant5971P → S in GM1G1; 2.1% of wild-type enzyme activity. Ref.42
VAR_062370
Natural variant6321E → G in GM1G2. Ref.20
VAR_008686

Experimental info

Sequence conflict891H → Y in BAH13196. Ref.4
Sequence conflict2011R → A in AAA51822. Ref.1

Secondary structure

................................................................................................................... 677
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 74421586B1BCFECA

FASTA67776,075
        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 

« Hide

Isoform 2 (Beta-galactosidase-related protein) (Beta-galactosidase-like protein) (S-Gal) (Elastin-binding protein) (EBP) [UniParc] [UniParc].

Checksum: 2EC2BBA4F39E966C
Show »

FASTA54660,536
Isoform 3 [UniParc].

Checksum: 1D57AD9A29CF9DA6
Show »

FASTA64772,751

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] (ISOFORMS 1 AND 3), VARIANT LEU-10.
[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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-464.
Tissue: Platelet.
[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-464 AND ASN-555.
Tissue: Liver.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: VARIANT GM1G3 MET-82.
[22]"Novel missense mutations in beta-galactosidase 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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

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.
AK300021 mRNA. Translation: BAH13196.1.
AK312988 mRNA. Translation: BAG35825.1.
BT007147 mRNA. Translation: AAP35811.1.
AC112211 Genomic DNA. No translation available.
BC007493 mRNA. Translation: AAH07493.1.
CCDSCCDS43061.1. [P16278-1]
CCDS43062.1. [P16278-3]
CCDS46785.1. [P16278-2]
PIRA32611. A32688.
B32688.
RefSeqNP_000395.2. NM_000404.2. [P16278-1]
NP_001073279.1. NM_001079811.1. [P16278-3]
NP_001129074.1. NM_001135602.1. [P16278-2]
UniGeneHs.443031.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3THCX-ray1.80A/B/C/D24-677[»]
3THDX-ray1.79A/B/C/D24-677[»]
3WEZX-ray2.11A/B/C/D24-677[»]
3WF0X-ray2.20A/B/C/D24-677[»]
3WF1X-ray2.00A/B/C/D24-677[»]
3WF2X-ray2.30A/B/C/D24-677[»]
3WF3X-ray2.15A/B/C/D24-677[»]
3WF4X-ray2.30A/B/C/D24-677[»]
ProteinModelPortalP16278.
SMRP16278. Positions 29-647.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108984. 11 interactions.
IntActP16278. 9 interactions.
MINTMINT-3008481.
STRING9606.ENSP00000306920.

Chemistry

BindingDBP16278.
ChEMBLCHEMBL2522.

Protein family/group databases

CAZyGH35. Glycoside Hydrolase Family 35.

PTM databases

PhosphoSiteP16278.

Polymorphism databases

DMDM215273939.

Proteomic databases

MaxQBP16278.
PaxDbP16278.
PRIDEP16278.

Protocols and materials databases

DNASU2720.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000307363; ENSP00000306920; ENSG00000170266.
ENST00000399402; ENSP00000382333; ENSG00000170266.
ENST00000445488; ENSP00000393377; ENSG00000170266.
GeneID2720.
KEGGhsa:2720.
UCSCuc003cfh.1. human. [P16278-1]
uc003cfj.1. human. [P16278-2]

Organism-specific databases

CTD2720.
GeneCardsGC03M033013.
GeneReviewsGLB1.
HGNCHGNC:4298. GLB1.
HPACAB008382.
HPA040610.
MIM230500. phenotype.
230600. phenotype.
230650. phenotype.
253010. phenotype.
611458. gene.
neXtProtNX_P16278.
Orphanet79255. GM1 gangliosidosis type 1.
79256. GM1 gangliosidosis type 2.
79257. GM1 gangliosidosis type 3.
309310. Mucopolysaccharidosis type 4B.
PharmGKBPA28709.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1874.
HOGENOMHOG000221607.
HOVERGENHBG004841.
InParanoidP16278.
KOK12309.
OrthoDBEOG7GXPCD.
PhylomeDBP16278.
TreeFamTF314816.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
REACT_17015. Metabolism of proteins.
SABIO-RKP16278.

Gene expression databases

ArrayExpressP16278.
BgeeP16278.
CleanExHS_GLB1.
GenevestigatorP16278.

Family and domain databases

Gene3D2.60.120.260. 1 hit.
3.20.20.80. 1 hit.
InterProIPR026283. B-gal_1-like.
IPR008979. Galactose-bd-like.
IPR019801. Glyco_hydro_35_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR001944. Glycoside_Hdrlase_35.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR23421. PTHR23421. 1 hit.
PfamPF01301. Glyco_hydro_35. 1 hit.
[Graphical view]
PIRSFPIRSF006336. B-gal. 1 hit.
PRINTSPR00742. GLHYDRLASE35.
SUPFAMSSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEPS01182. GLYCOSYL_HYDROL_F35. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGLB1. human.
GeneWikiGLB1.
GenomeRNAi2720.
NextBio10738.
PROP16278.
SOURCESearch...

Entry information

Entry nameBGAL_HUMAN
AccessionPrimary (citable) accession number: P16278
Secondary accession number(s): B2R7H8, B7Z6B0, P16279
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 165 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries