dbPTM

AGAL_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AGAL_HUMAN
UniProt AC	P06280
Protein Name	Alpha-galactosidase A
Gene Name	GLA
Organism	Homo sapiens (Human).
Sequence Length	429
Subcellular Localization	Lysosome.
Protein Description
Protein Sequence	MQLRNPELHLGCALALRFLALVSWDIPGARALDNGLARTPTMGWLHWERFMCNLDCQEEPDSCISEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQRDSEGRLQADPQRFPHGIRQLANYVHSKGLKLGIYADVGNKTCAGFPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSLENLADGYKHMSLALNRTGRSIVYSCEWPLYMWPFQKPNYTEIRQYCNHWRNFADIDDSWKSIKSILDWTSFNQERIVDVAGPGGWNDPDMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAINQDPLGKQGYQLRQGDNFEVWERPLSGLAWAVAMINRQEIGGPRSYTIAVASLGKGVACNPACFITQLLPVKRKLGFYEWTSRLRSHINPTGTVLLQLENTMQMSLKDLL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
23	Phosphorylation	LRFLALVSWDIPGAR HHHHHHHCCCCCCHH	21.63	21406692
86	Phosphorylation	EGWKDAGYEYLCIDD CCHHHCCCEEEEEEC	11.79	25072903
88	Phosphorylation	WKDAGYEYLCIDDCW HHHCCCEEEEEECCE	9.82	25072903
127	Ubiquitination	LANYVHSKGLKLGIY HHHHHHHCCCEEEEE	54.08	-
139	N-linked_Glycosylation	GIYADVGNKTCAGFP EEEEECCCCCCCCCC	35.99	15003450
139	N-linked_Glycosylation	GIYADVGNKTCAGFP EEEEECCCCCCCCCC	35.99	15003450
185	Ubiquitination	ENLADGYKHMSLALN HHHCHHHHHHHHHCC	38.06	-
192	N-linked_Glycosylation	KHMSLALNRTGRSIV HHHHHHCCCCCCEEE	33.58	15003450
192	N-linked_Glycosylation	KHMSLALNRTGRSIV HHHHHHCCCCCCEEE	33.58	15003450
215	N-linked_Glycosylation	MWPFQKPNYTEIRQY ECCCCCCCHHHHHHH	64.49	15003450
215	N-linked_Glycosylation	MWPFQKPNYTEIRQY ECCCCCCCHHHHHHH	64.49	15003450
237	Ubiquitination	ADIDDSWKSIKSILD CCCCCHHHHHHHHHH	46.37	-
240	Ubiquitination	DDSWKSIKSILDWTS CCHHHHHHHHHHHCC	38.24	21890473
240	Ubiquitination	DDSWKSIKSILDWTS CCHHHHHHHHHHHCC	38.24	21890473
308	Ubiquitination	RHISPQAKALLQDKD HHCCHHHHHHHCCCC	34.03	21890473
314	Ubiquitination	AKALLQDKDVIAINQ HHHHHCCCCEEEECC	40.72	21906983
326	Ubiquitination	INQDPLGKQGYQLRQ ECCCCCCCCCEEECC	48.51	21890473
326	Ubiquitination	INQDPLGKQGYQLRQ ECCCCCCCCCEEECC	48.51	21890473
371	Phosphorylation	SYTIAVASLGKGVAC CEEEEEEECCCCCCC	30.93	-
391	Ubiquitination	ITQLLPVKRKLGFYE HHHHHCCHHHHCCHH	41.71	-
393	Ubiquitination	QLLPVKRKLGFYEWT HHHCCHHHHCCHHHH	47.44	21890473
393	Ubiquitination	QLLPVKRKLGFYEWT HHHCCHHHHCCHHHH	47.44	21890473
401	Phosphorylation	LGFYEWTSRLRSHIN HCCHHHHHHHHHHCC	30.32	30631047
402	Methylation	GFYEWTSRLRSHINP CCHHHHHHHHHHCCC	27.09	-
408	N-linked_Glycosylation	SRLRSHINPTGTVLL HHHHHHCCCCCCEEE	23.74	UniProtKB CARBOHYD
424	Phosphorylation	LENTMQMSLKDLL-- ECCHHHHCHHHHC--	18.51	-

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 AGAL_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IF4H_HUMAN	EIF4H	physical	22863883
CNOT2_HUMAN	CNOT2	physical	27173435
CNO11_HUMAN	CNOT11	physical	27173435
CNOT6_HUMAN	CNOT6	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
301500	Fabry disease (FD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of AGAL_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"The molecular defect leading to Fabry disease: structure of humanalpha-galactosidase."; Garman S.C., Garboczi D.N.; J. Mol. Biol. 337:319-335(2004). Cited for: X-RAY CRYSTALLOGRAPHY (3.45 ANGSTROMS) OF 32-422 IN COMPLEX WITHPRODUCT, HOMODIMERIZATION, AND GLYCOSYLATION AT ASN-139; ASN-192 ANDASN-215.	15003450 [Abstract]
"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-215, AND MASSSPECTROMETRY.	19159218 [Abstract]