GALC_HUMAN - dbPTM
GALC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GALC_HUMAN
UniProt AC P54803
Protein Name Galactocerebrosidase
Gene Name GALC
Organism Homo sapiens (Human).
Sequence Length 685
Subcellular Localization Lysosome.
Protein Description Hydrolyzes the galactose ester bonds of galactosylceramide, galactosylsphingosine, lactosylceramide, and monogalactosyldiglyceride. Enzyme with very low activity responsible for the lysosomal catabolism of galactosylceramide, a major lipid in myelin, kidney and epithelial cells of small intestine and colon..
Protein Sequence MAEWLLSASWQRRAKAMTAAAGSAGRAAVPLLLCALLAPGGAYVLDDSDGLGREFDGIGAVSGGGATSRLLVNYPEPYRSQILDYLFKPNFGASLHILKVEIGGDGQTTDGTEPSHMHYALDENYFRGYEWWLMKEAKKRNPNITLIGLPWSFPGWLGKGFDWPYVNLQLTAYYVVTWIVGAKRYHDLDIDYIGIWNERSYNANYIKILRKMLNYQGLQRVKIIASDNLWESISASMLLDAELFKVVDVIGAHYPGTHSAKDAKLTGKKLWSSEDFSTLNSDMGAGCWGRILNQNYINGYMTSTIAWNLVASYYEQLPYGRCGLMTAQEPWSGHYVVESPVWVSAHTTQFTQPGWYYLKTVGHLEKGGSYVALTDGLGNLTIIIETMSHKHSKCIRPFLPYFNVSQQFATFVLKGSFSEIPELQVWYTKLGKTSERFLFKQLDSLWLLDSDGSFTLSLHEDELFTLTTLTTGRKGSYPLPPKSQPFPSTYKDDFNVDYPFFSEAPNFADQTGVFEYFTNIEDPGEHHFTLRQVLNQRPITWAADASNTISIIGDYNWTNLTIKCDVYIETPDTGGVFIAGRVNKGGILIRSARGIFFWIFANGSYRVTGDLAGWIIYALGRVEVTAKKWYTLTLTIKGHFTSGMLNDKSLWTDIPVNFPKNGWAAIGTHSFEFAQFDNFLVEATR
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
11 (in isoform 5)Phosphorylation-23.6124043423
12 (in isoform 5)Phosphorylation-33.9824043423
15AcetylationASWQRRAKAMTAAAG
HHHHHHHHHHHHHHH
36.5610723477
18PhosphorylationQRRAKAMTAAAGSAG
HHHHHHHHHHHHHHH
20.2922985185
68PhosphorylationVSGGGATSRLLVNYP
CCCCCHHCEEECCCC
22.01-
143N-linked_GlycosylationEAKKRNPNITLIGLP
HHHHHCCCEEEEECC
43.35UniProtKB CARBOHYD
261AcetylationYPGTHSAKDAKLTGK
CCCCCCHHHCCCCCC
62.327964635
379N-linked_GlycosylationALTDGLGNLTIIIET
EEECCCCCEEEEEEE
38.77UniProtKB CARBOHYD
381PhosphorylationTDGLGNLTIIIETMS
ECCCCCEEEEEEECC
17.71-
403N-linked_GlycosylationRPFLPYFNVSQQFAT
CCCCCCCCHHHHHHE
27.04UniProtKB CARBOHYD
529PhosphorylationDPGEHHFTLRQVLNQ
CCCCCCEEHHHHHHC
19.3724719451
556N-linked_GlycosylationISIIGDYNWTNLTIK
EEEEECCCCCCEEEE
43.78UniProtKB CARBOHYD
559N-linked_GlycosylationIGDYNWTNLTIKCDV
EECCCCCCEEEEEEE
27.14UniProtKB CARBOHYD
602N-linked_GlycosylationIFFWIFANGSYRVTG
EEEEEECCCCEEECH
29.24UniProtKB CARBOHYD
608PhosphorylationANGSYRVTGDLAGWI
CCCCEEECHHHHHHH
18.91-
625PhosphorylationALGRVEVTAKKWYTL
HCCCEEEEECCEEEE
21.18-

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 GALC_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GALC_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 GALC_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NEUL4_HUMANNEURL4physical
27173435

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GALC_HUMAN

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Related Literatures of Post-Translational Modification

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