GALT1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GALT1_MOUSE
• UniProt AC: O08912
• Protein Name: Polypeptide N-acetylgalactosaminyltransferase 1
• Gene Name: Galnt1
• Organism: Mus musculus (Mouse).
• Sequence Length: 559
• Subcellular Localization: Polypeptide N-acetylgalactosaminyltransferase 1: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein.; Polypeptide N-acetylgalactosaminyltransferase 1 soluble form: Secreted.
• Protein Description: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7..
• Protein Sequence: MRKFAYCKVVLATSLVWVLLDMFLLLYFSECNKCEEKQERGLPAGDVLELVQKPHEGPGEMGKPVVIPKEDQEKMKEMFKINQFNLMASEMIALNRSLPDVRLEGCKTKVYPDNLPTTSVVIVFHNEAWSTLLRTVHSVINRSPRHMIEEIVLVDDASERDFLKRPLESYVKKLKVPVHVIRMEQRSGLIRARLKGAAVSRGQVITFLDAHCECTAGWLEPLLARIKHDRRTVVCPIIDVISDDTFEYMAGSDMTYGGFNWKLNFRWYPVPQREMDRRKGDRTLPVRTPTMAGGLFSIDRDYFQEIGTYDAGMDIWGGENLEISFRIWQCGGTLEIVTCSHVGHVFRKATPYTFPGGTGQIINKNNRRLAEVWMDEFKNFFYIISPGVTKVDYGDISSRLGLRRKLQCKPFSWYLENIYPDSQIPRHYFSLGEIRNVETNQCLDNMARKENEKVGIFNCHGMGGNQVFSYTANKEIRTDDLCLDVSKLNGPVTMLKCHHLKGNQLWEYDPVKLTLQHVNSNQCLDKATEEDSQVPSIRDCTGSRSQQWLLRNVTLPEIF

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
95	N-linked_Glycosylation	ASEMIALNRSLPDVR HHHHHHHCCCCCCCE	23.60	-
143	Phosphorylation	VHSVINRSPRHMIEE HHHHHHCCCCCCEEE	23.07	-
195	Acetylation	GLIRARLKGAAVSRG CHHHHHHHCCCCCCC	40.73	2389441
290	Phosphorylation	TLPVRTPTMAGGLFS CCCCCCCCCCCCCEE	21.02	21454597
552	N-linked_Glycosylation	SQQWLLRNVTLPEIF HHHHHHHCCCCCCCC	30.97	15486088

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

Oops, there are no upstream regulatory protein records of GALT1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of GALT1_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of GALT1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of GALT1_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"The beginnings of mucin biosynthesis: the crystal structure of UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-T1.";
Fritz T.A., Hurley J.H., Trinh L.B., Shiloach J., Tabak L.A.;
Proc. Natl. Acad. Sci. U.S.A. 101:15307-15312(2004).
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 88-559, GLYCOSYLATION ATASN-552, AND DISULFIDE BONDS.
PubMed: 15486088