dbPTM

BGAL_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BGAL_HUMAN
UniProt AC	P16278
Protein Name	Beta-galactosidase
Gene Name	GLB1
Organism	Homo sapiens (Human).
Sequence Length	677
Subcellular Localization	Isoform 1: Lysosome . Isoform 2: Cytoplasm, perinuclear region . Localized to the perinuclear area of the cytoplasm but not to lysosomes.
Protein Description	Isoform 1: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.; 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..
Protein Sequence	MPGFLVRILPLLLVLLLLGPTRGLRNATQRMFEIDYSRDSFLKDGQPFRYISGSIHYSRVPRFYWKDRLLKMKMAGLNAIQTYVPWNFHEPWPGQYQFSEDHDVEYFLRLAHELGLLVILRPGPYICAEWEMGGLPAWLLEKESILLRSSDPDYLAAVDKWLGVLLPKMKPLLYQNGGPVITVQVENEYGSYFACDFDYLRFLQKRFRHHLGDDVVLFTTDGAHKTFLKCGALQGLYTTVDFGTGSNITDAFLSQRKCEPKGPLINSEFYTGWLDHWGQPHSTIKTEAVASSLYDILARGASVNLYMFIGGTNFAYWNGANSPYAAQPTSYDYDAPLSEAGDLTEKYFALRNIIQKFEKVPEGPIPPSTPKFAYGKVTLEKLKTVGAALDILCPSGPIKSLYPLTFIQVKQHYGFVLYRTTLPQDCSNPAPLSSPLNGVHDRAYVAVDGIPQGVLERNNVITLNITGKAGATLDLLVENMGRVNYGAYINDFKGLVSNLTLSSNILTDWTIFPLDTEDAVRSHLGGWGHRDSGHHDEAWAHNSSNYTLPAFYMGNFSIPSGIPDLPQDTFIQFPGWTKGQVWINGFNLGRYWPARGPQLTLFVPQHILMTSAPNTITVLELEWAPCSSDDPELCAVTFVDRPVIGSSVTYDHPSKPVEKRLMPPPPQKNKDSWLDHV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
21	Phosphorylation	VLLLLGPTRGLRNAT HHHHHCCCCCHHHHH	35.25	-
26	N-linked_Glycosylation	GPTRGLRNATQRMFE CCCCCHHHHHHHHEE	53.00	UniProtKB CARBOHYD
28	Phosphorylation	TRGLRNATQRMFEID CCCHHHHHHHHEEEE	21.91	27732954
37	Phosphorylation	RMFEIDYSRDSFLKD HHEEEECCCHHHCCC	26.34	30266825
40	Phosphorylation	EIDYSRDSFLKDGQP EEECCCHHHCCCCCE	31.22	30266825
43 (in isoform 2)	Ubiquitination	-	58.78	21906983
43 (in isoform 1)	Ubiquitination	-	58.78	21890473
43	Methylation	YSRDSFLKDGQPFRY CCCHHHCCCCCEEEE	58.78	-
43	Ubiquitination	YSRDSFLKDGQPFRY CCCHHHCCCCCEEEE	58.78	2190698
57	Phosphorylation	YISGSIHYSRVPRFY EEECCCCCCCCCCHH	9.12	-
58	Phosphorylation	ISGSIHYSRVPRFYW EECCCCCCCCCCHHH	16.79	-
85	Phosphorylation	NAIQTYVPWNFHEPW CHHHHCCCCCCCCCC	15.18	-
88	Phosphorylation	QTYVPWNFHEPWPGQ HHCCCCCCCCCCCCC	6.45	-
91	Ubiquitination	VPWNFHEPWPGQYQF CCCCCCCCCCCCCCC	33.71	-
91	Methylation	VPWNFHEPWPGQYQF CCCCCCCCCCCCCCC	33.71	-
93 (in isoform 2)	Phosphorylation	-	30.63	22210691
101 (in isoform 2)	Phosphorylation	-	41.93	22210691
105	Phosphorylation	FSEDHDVEYFLRLAH CCCCCCHHHHHHHHH	36.30	-
106	Phosphorylation	SEDHDVEYFLRLAHE CCCCCHHHHHHHHHH	14.04	-
154	Phosphorylation	LRSSDPDYLAAVDKW ECCCCHHHHHHHHHH	12.02	-
202	Phosphorylation	CDFDYLRFLQKRFRH ECHHHHHHHHHHHHH	8.60	-
225	Ubiquitination	FTTDGAHKTFLKCGA EECCCCCHHHHHHCC	40.20	-
225	Ubiquitination	FTTDGAHKTFLKCGA EECCCCCHHHHHHCC	40.20	21890473
225 (in isoform 1)	Ubiquitination	-	40.20	21890473
247	N-linked_Glycosylation	VDFGTGSNITDAFLS EECCCCCCHHHHHHH	42.39	24737316
283	O-linked_Glycosylation	HWGQPHSTIKTEAVA CCCCCCCCHHHHHHH	24.37	OGP
286	Phosphorylation	QPHSTIKTEAVASSL CCCCCHHHHHHHHHH	25.89	20068231
291	Phosphorylation	IKTEAVASSLYDILA HHHHHHHHHHHHHHH	17.80	20068231
292	Phosphorylation	KTEAVASSLYDILAR HHHHHHHHHHHHHHC	22.62	20068231
294	Phosphorylation	EAVASSLYDILARGA HHHHHHHHHHHHCCC	11.68	20068231
295	N-linked_Glycosylation	AVASSLYDILARGAS HHHHHHHHHHHCCCC	34.42	16399764
295	N-linked_Glycosylation	AVASSLYDILARGAS HHHHHHHHHHHCCCC	34.42	16399764
334	Phosphorylation	QPTSYDYDAPLSEAG CCCCCCCCCCHHHCC	38.52	20068231
342	Phosphorylation	APLSEAGDLTEKYFA CCHHHCCHHHHHHHH	58.42	20068231
368	Phosphorylation	PEGPIPPSTPKFAYG CCCCCCCCCCCCCCC	52.57	-
369	Phosphorylation	EGPIPPSTPKFAYGK CCCCCCCCCCCCCCE	35.95	-
381	2-Hydroxyisobutyrylation	YGKVTLEKLKTVGAA CCEEEHHHHHHHHHH	59.40	-
383	Ubiquitination	KVTLEKLKTVGAALD EEEHHHHHHHHHHHH	52.83	-
431	Ubiquitination	QDCSNPAPLSSPLNG CCCCCCCCCCCCCCC	33.75	-
464	N-linked_Glycosylation	RNNVITLNITGKAGA ECCEEEEEECCCCCC	22.56	16263699
485	Phosphorylation	ENMGRVNYGAYINDF HHCCCCCCEEEECCH	10.56	21406692
488	Phosphorylation	GRVNYGAYINDFKGL CCCCCEEEECCHHHH	8.90	21406692
493	Acetylation	GAYINDFKGLVSNLT EEEECCHHHHHCCCE	54.95	70347
498	N-linked_Glycosylation	DFKGLVSNLTLSSNI CHHHHHCCCEECCCC	29.57	24737316
512	N-linked_Glycosylation	ILTDWTIFPLDTEDA CCCCCEEEECCHHHH	3.73	16263699
512	N-linked_Glycosylation	ILTDWTIFPLDTEDA CCCCCEEEECCHHHH	3.73	16263699
533	Phosphorylation	GWGHRDSGHHDEAWA CCCCCCCCCCCCCCC	26.83	-
536	Phosphorylation	HRDSGHHDEAWAHNS CCCCCCCCCCCCCCC	41.45	-
542	N-linked_Glycosylation	HDEAWAHNSSNYTLP CCCCCCCCCCCCCCC	39.11	UniProtKB CARBOHYD
545	N-linked_Glycosylation	AWAHNSSNYTLPAFY CCCCCCCCCCCCEEE	33.36	UniProtKB CARBOHYD
546	N-linked_Glycosylation	WAHNSSNYTLPAFYM CCCCCCCCCCCEEEE	16.17	22128166
555	N-linked_Glycosylation	LPAFYMGNFSIPSGI CCEEEEECCCCCCCC	15.80	22128166
603	N-linked_Glycosylation	GPQLTLFVPQHILMT CCEEEEEECCEEECC	5.12	22128166
718	Ubiquitination	------------------------------------------------ ------------------------------------------------		-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of BGAL_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of BGAL_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of BGAL_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CG043_HUMAN	C7orf43	physical	28514442
TPC10_HUMAN	TRAPPC10	physical	28514442
TPPC9_HUMAN	TRAPPC9	physical	28514442
TPC6B_HUMAN	TRAPPC6B	physical	28514442
TPPC4_HUMAN	TRAPPC4	physical	28514442
TPPC3_HUMAN	TRAPPC3	physical	28514442
TPC2L_HUMAN	TRAPPC2L	physical	28514442
TPC2A_HUMAN	TRAPPC2	physical	28514442
TPC2B_HUMAN	TRAPPC2	physical	28514442
YPEL5_HUMAN	YPEL5	physical	27173435
VIME_HUMAN	VIM	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
230500	GM1-gangliosidosis 1 (GM1G1)
230600	GM1-gangliosidosis 2 (GM1G2)
230650	GM1-gangliosidosis 3 (GM1G3)
253010	Mucopolysaccharidosis 4B (MPS4B)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of BGAL_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple 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). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-464 AND ASN-555, AND MASSSPECTROMETRY.	19159218 [Abstract]
"Elucidation of N-glycosylation sites on human platelet proteins: aglycoproteomic approach."; Lewandrowski U., Moebius J., Walter U., Sickmann A.; Mol. Cell. Proteomics 5:226-233(2006). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-464, AND MASSSPECTROMETRY.	16263699 [Abstract]