B3GL2_HUMAN - dbPTM
B3GL2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID B3GL2_HUMAN
UniProt AC Q8NCR0
Protein Name UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 2
Gene Name B3GALNT2
Organism Homo sapiens (Human).
Sequence Length 500
Subcellular Localization Golgi apparatus membrane
Single-pass type II membrane protein. Endoplasmic reticulum .
Protein Description Beta-1,3-N-acetylgalactosaminyltransferase that synthesizes a unique carbohydrate structure, GalNAc-beta-1-3GlcNAc, on N- and O-glycans. Has no galactose nor galactosaminyl transferase activity toward any acceptor substrate. Involved in alpha-dystroglycan (DAG1) glycosylation: acts coordinately with GTDC2/POMGnT2 to synthesize a GalNAc-beta3-GlcNAc-beta-terminus at the 4-position of protein O-mannose in the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan, which is required for binding laminin G-like domain-containing extracellular proteins with high affinity..
Protein Sequence MRNWLVLLCPCVLGAALHLWLRLRSPPPACASGAGPADQLALFPQWKSTHYDVVVGVLSARNNHELRNVIRSTWMRHLLQHPTLSQRVLVKFIIGAHGCEVPVEDREDPYSCKLLNITNPVLNQEIEAFSLSEDTSSGLPEDRVVSVSFRVLYPIVITSLGVFYDANDVGFQRNITVKLYQAEQEEALFIARFSPPSCGVQVNKLWYKPVEQFILPESFEGTIVWESQDLHGLVSRNLHKVTVNDGGGVLRVITAGEGALPHEFLEGVEGVAGGFIYTIQEGDALLHNLHSRPQRLIDHIRNLHEEDALLKEESSIYDDIVFVDVVDTYRNVPAKLLNFYRWTVETTSFNLLLKTDDDCYIDLEAVFNRIVQKNLDGPNFWWGNFRLNWAVDRTGKWQELEYPSPAYPAFACGSGYVISKDIVKWLASNSGRLKTYQGEDVSMGIWMAAIGPKRYQDSLWLCEKTCETGMLSSPQYSPWELTELWKLKERCGDPCRCQAR
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
116N-linked_GlycosylationPYSCKLLNITNPVLN
CCCCEEEECCCCCCC
49.85UniProtKB CARBOHYD
146PhosphorylationLPEDRVVSVSFRVLY
CCCCCEEEEEEEEHH
14.8026074081
148PhosphorylationEDRVVSVSFRVLYPI
CCCEEEEEEEEHHHH
10.3824719451
153PhosphorylationSVSFRVLYPIVITSL
EEEEEEHHHHEEEEE
6.5126074081
158PhosphorylationVLYPIVITSLGVFYD
EHHHHEEEEEEEEEC
13.6526074081
159PhosphorylationLYPIVITSLGVFYDA
HHHHEEEEEEEEECC
16.4126074081
164PhosphorylationITSLGVFYDANDVGF
EEEEEEEECCCCCCC
16.2526074081
174N-linked_GlycosylationNDVGFQRNITVKLYQ
CCCCCCCCEEEEEEE
24.41UniProtKB CARBOHYD
240UbiquitinationLVSRNLHKVTVNDGG
HHCCCCEEEEEECCC
42.6527667366
281UbiquitinationGFIYTIQEGDALLHN
EEEEEEECCCHHHHC
56.0127667366
335UbiquitinationTYRNVPAKLLNFYRW
HCCCCCHHHHHEEEE
47.6522817900
335 (in isoform 1)Ubiquitination-47.6521890473
376UbiquitinationRIVQKNLDGPNFWWG
HHHHHCCCCCCCCCC
78.7721890473
376 (in isoform 2)Ubiquitination-78.7721890473
428PhosphorylationDIVKWLASNSGRLKT
HHHHHHHHCCCCCCE
29.3826699800
430PhosphorylationVKWLASNSGRLKTYQ
HHHHHHCCCCCCEEC
23.8526699800

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 B3GL2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of B3GL2_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 B3GL2_HUMAN !!

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

Oops, there are no PPI records of B3GL2_HUMAN !!

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615181Muscular dystrophy-dystroglycanopathy congenital with brain and eye anomalies A11 (MDDGA11)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of B3GL2_HUMAN

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Related Literatures of Post-Translational Modification

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