NGLY1_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NGLY1_RAT
• UniProt AC: Q5XI55
• Protein Name: Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase
• Gene Name: Ngly1
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 651
• Subcellular Localization: Cytoplasm.
• Protein Description: Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins (By similarity)..
• Protein Sequence: MASATLGSSSSSASPAVAELCQNTPETFLEASKLLLTYADNILRNPSDEKYRSIRIGNTAFSTRLLPVRGAVECLFEMGFEEGETHLIFPKKASVEQLQKIRDLIAVERRSRLDGSSQKVEFSQHPAAVRLPAEQPEDPTGLMQHSGNQPGQPLSLPSAPLVVGDSTIFKVLQSNIQHVQLYENPVLQEKALACIPVNELKRKSQEKLFRARKLDKGTKVSDEDFLLLELLHWFKEEFFHWVNNVVCSRCGRETRSRDEALPPNDDELKWGAKNVEDHYCDACQLSNRFPRYNNPEKLLETRCGRCGEWANCFTLCCRALGFEARYVWDYTDHVWTEVYSPSQQRWLHCDACEDVCDKPLLYEIGWGKKLSYIIAFSKDEVVDVTWRYSCKHEEVMSRRTKVKEELLRETINGLNKQRQLLLSESRRKELLQRIIVELVEFISPKTPRPGELGGRVSGSLAWRVARGETCLERKEILFIPSENEKISKQFHLRYDIVRDRYIRVSDNNANISGWENGVWKMESIFRKVEKDWNMVYLARKEGSSFAYISWKFECGSAGLKVDNVSIRTSSQSFETGSVRWKLRSEMAQVNLLGDRNLRSYDDFCGATEVTLEAELSRGDGDVAWQHTQLFRQSLNDHAENGLEIIITFSDL

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
2	Acetylation	------MASATLGSS ------CCCCCCCCC	14.10	-
111	Phosphorylation	LIAVERRSRLDGSSQ HHHHHHHHCCCCCCC	43.34	25575281
116	Phosphorylation	RRSRLDGSSQKVEFS HHHCCCCCCCCEEEC	29.30	25575281
117	Phosphorylation	RSRLDGSSQKVEFSQ HHCCCCCCCCEEECC	39.28	25575281
123	Phosphorylation	SSQKVEFSQHPAAVR CCCCEEECCCCCCEE	17.67	25575281
216	Ubiquitination	FRARKLDKGTKVSDE HHHHCCCCCCCCCHH	78.05	-
416	Ubiquitination	ETINGLNKQRQLLLS HHHHHHHHHHHHHCC	52.48	-
423	Phosphorylation	KQRQLLLSESRRKEL HHHHHHCCHHHHHHH	33.23	30181290
425	Phosphorylation	RQLLLSESRRKELLQ HHHHCCHHHHHHHHH	33.73	30181290

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

Oops, there are no upstream regulatory protein records of NGLY1_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NGLY1_RAT !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of NGLY1_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of NGLY1_RAT !!

Drug and Disease Associations

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