LARG2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LARG2_HUMAN
• UniProt AC: Q8N3Y3
• Protein Name: LARGE xylosyl- and glucuronyltransferase 2 {ECO:0000312|HGNC:HGNC:16522}
• Gene Name: LARGE2 {ECO:0000312|HGNC:HGNC:16522}
• Organism: Homo sapiens (Human).
• Sequence Length: 721
• Subcellular Localization: Golgi apparatus membrane ; Single-pass type II membrane protein .
• Protein Description: Bifunctional glycosyltransferase with both xylosyltransferase and beta-1,3-glucuronyltransferase activities involved 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 (DAG1). Phosphorylated O-mannosyl trisaccharid is required for binding laminin G-like domain-containing extracellular proteins with high affinity. Elongates the glucuronyl-beta-1,4-xylose-beta disaccharide primer structure by adding repeating units [-3-Xylose-alpha-1,3-GlcA-beta-1-] to produce a heteropolysaccharide. Has a higher activity toward alpha-dystroglycan than LARGE..
• Protein Sequence: MLPRGRPRALGAAALLLLLLLLGFLLFGGDLGCERREPGGRAGAPGCFPGPLMPRVPPDGRLRRAAALDGDPGAGPGDHNRSDCGPQPPPPPKCELLHVAIVCAGHNSSRDVITLVKSMLFYRKNPLHLHLVTDAVARNILETLFHTWMVPAVRVSFYHADQLKPQVSWIPNKHYSGLYGLMKLVLPSALPAELARVIVLDTDVTFASDISELWALFAHFSDTQAIGLVENQSDWYLGNLWKNHRPWPALGRGFNTGVILLRLDRLRQAGWEQMWRLTARRELLSLPATSLADQDIFNAVIKEHPGLVQRLPCVWNVQLSDHTLAERCYSEASDLKVIHWNSPKKLRVKNKHVEFFRNFYLTFLEYDGNLLRRELFVCPSQPPPGAEQLQQALAQLDEEDPCFEFRQQQLTVHRVHVTFLPHEPPPPRPHDVTLVAQLSMDRLQMLEALCRHWPGPMSLALYLTDAEAQQFLHFVEASPVLAARQDVAYHVVYREGPLYPVNQLRNVALAQALTPYVFLSDIDFLPAYSLYDYLRASIEQLGLGSRRKAALVVPAFETLRYRFSFPHSKVELLALLDAGTLYTFRYHEWPRGHAPTDYARWREAQAPYRVQWAANYEPYVVVPRDCPRYDPRFVGFGWNKVAHIVELDAQEYELLVLPEAFTIHLPHAPSLDISRFRSSPTYRDCLQALKDEFHQDLSRHHGAAALKYLPALQQPQSPARG

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
80	N-linked_Glycosylation	GAGPGDHNRSDCGPQ CCCCCCCCCCCCCCC	50.30	UniProtKB CARBOHYD
107	N-linked_Glycosylation	AIVCAGHNSSRDVIT EEEECCCCCHHHHHH	40.54	UniProtKB CARBOHYD
168	Phosphorylation	DQLKPQVSWIPNKHY HHHCCCCCCCCCCCC	17.65	23898821
231	N-linked_Glycosylation	QAIGLVENQSDWYLG CEEEEEECCCCCEEH	38.89	UniProtKB CARBOHYD
679	Phosphorylation	DISRFRSSPTYRDCL CHHHCCCCCCHHHHH	19.60	20166139
681	Phosphorylation	SRFRSSPTYRDCLQA HHCCCCCCHHHHHHH	32.89	20166139
682	Phosphorylation	RFRSSPTYRDCLQAL HCCCCCCHHHHHHHH	14.08	20166139

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

Oops, there are no upstream regulatory protein records of LARG2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LARG2_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of LARG2_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of LARG2_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.