LARG1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LARG1_HUMAN
• UniProt AC: O95461
• Protein Name: LARGE xylosyl- and glucuronyltransferase 1 {ECO:0000312|HGNC:HGNC:6511}
• Gene Name: LARGE1 {ECO:0000312|HGNC:HGNC:6511}
• Organism: Homo sapiens (Human).
• Sequence Length: 756
• 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). [PubMed: 22223806 Phosphorylated O-mannosyl trisaccharid is required for binding laminin G-like domain-containing extracellular proteins with high affinity and plays a key role in skeletal muscle function and regeneration. LARGE elongates the glucuronyl-beta-1,4-xylose-beta disaccharide primer structure initiated by B3GNT1/B4GAT1 by adding repeating units [-3-Xylose-alpha-1,3-GlcA-beta-1-] to produce a heteropolysaccharide]
• Protein Sequence: MLGICRGRRKFLAASLSLLCIPAITWIYLFSGSFEDGKPVSLSPLESQAHSPRYTASSQRERESLEVRMREVEEENRALRRQLSLAQGRAPSHRRGNHSKTYSMEEGTGDSENLRAGIVAGNSSECGQQPVVEKCETIHVAIVCAGYNASRDVVTLVKSVLFHRRNPLHFHLIADSIAEQILATLFQTWMVPAVRVDFYNADELKSEVSWIPNKHYSGIYGLMKLVLTKTLPANLERVIVLDTDITFATDIAELWAVFHKFKGQQVLGLVENQSDWYLGNLWKNHRPWPALGRGYNTGVILLLLDKLRKMKWEQMWRLTAERELMGMLSTSLADQDIFNAVIKQNPFLVYQLPCFWNVQLSDHTRSEQCYRDVSDLKVIHWNSPKKLRVKNKHVEFFRNLYLTFLEYDGNLLRRELFGCPSEADVNSENLQKQLSELDEDDLCYEFRRERFTVHRTHLYFLHYEYEPAADSTDVTLVAQLSMDRLQMLEAICKHWEGPISLALYLSDAEAQQFLRYAQGSEVLMSRHNVGYHIVYKEGQFYPVNLLRNVAMKHISTPYMFLSDIDFLPMYGLYEYLRKSVIQLDLANTKKAMIVPAFETLRYRLSFPKSKAELLSMLDMGTLFTFRYHVWTKGHAPTNFAKWRTATTPYRVEWEADFEPYVVVRRDCPEYDRRFVGFGWNKVAHIMELDVQEYEFIVLPNAYMIHMPHAPSFDITKFRSNKQYRICLKTLKEEFQQDMSRRYGFAALKYLTAENNS

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
64	O-linked_Glycosylation	SSQRERESLEVRMRE CCHHHHHHHHHHHHH		OGP
97	N-linked_Glycosylation	APSHRRGNHSKTYSM CCCCCCCCCCCCEEC		UniProtKB CARBOHYD
122	N-linked_Glycosylation	RAGIVAGNSSECGQQ CEEEEECCCCCCCCC		UniProtKB CARBOHYD
148	N-linked_Glycosylation	AIVCAGYNASRDVVT EEEECCCCCCHHHHH		UniProtKB CARBOHYD
272	N-linked_Glycosylation	QVLGLVENQSDWYLG EEEEEEECCCCCEEH		UniProtKB CARBOHYD
295	Phosphorylation	WPALGRGYNTGVILL CCCCCCCCCHHHHHH		21403953
555	Phosphorylation	NVAMKHISTPYMFLS HHHHHHCCCCCCCHH		25072903
556	Phosphorylation	VAMKHISTPYMFLSD HHHHHCCCCCCCHHC		25072903
558	Phosphorylation	MKHISTPYMFLSDID HHHCCCCCCCHHCCC		25072903
562	Phosphorylation	STPYMFLSDIDFLPM CCCCCCHHCCCCHHH		25072903
570	Phosphorylation	DIDFLPMYGLYEYLR CCCCHHHCCHHHHHH		26074081
573	Phosphorylation	FLPMYGLYEYLRKSV CHHHCCHHHHHHHHC		26074081
575	Phosphorylation	PMYGLYEYLRKSVIQ HHCCHHHHHHHHCCC		26074081
579	Phosphorylation	LYEYLRKSVIQLDLA HHHHHHHHCCCCCCC		26074081
588	Phosphorylation	IQLDLANTKKAMIVP CCCCCCCCCCEEEEE		-
599	Phosphorylation	MIVPAFETLRYRLSF EEEECHHHHHHHHCC		-
602	Phosphorylation	PAFETLRYRLSFPKS ECHHHHHHHHCCCHH		-
728	Methylation	KQYRICLKTLKEEFQ CCEEEHHHHHHHHHH		23644510
728	Trimethylation	KQYRICLKTLKEEFQ CCEEEHHHHHHHHHH		-

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

Oops, there are no upstream regulatory protein records of LARG1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LARG1_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 LARG1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RBP10_HUMAN	RANBP10	physical	27173435

Drug and Disease Associations

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