PNG1_YEAST - dbPTM
PNG1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PNG1_YEAST
UniProt AC Q02890
Protein Name Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase
Gene Name PNG1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 363
Subcellular Localization Cytoplasm. Nucleus.
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. Involved in the formation of free oligosaccharide in cytosol..
Protein Sequence MGEVYEKNNIDFDSIAKMLLIKYKDFILSKFKKAAPVENIRFQNLVHTNQFAQGVLGQSQHLCTVYDNPSWHSIVLETLDLDLIYKNVDKEFAKDGHAEGENIYTDYLVKELLRYFKQDFFKWCNKPDCNHCGQNTSENMTPLGSQGPNGEESKFNCGTVEIYKCNRCGNITRFPRYNDPIKLLETRKGRCGEWCNLFTLILKSFGLDVRYVWNREDHVWCEYFSNFLNRWVHVDSCEQSFDQPYIYSINWNKKMSYCIAFGKDGVVDVSKRYILQNELPRDQIKEEDLKFLCQFITKRLRYSLNDDEIYQLACRDEQEQIELIRGKTQETKSESVSAASKSSNRGRESGSADWKAQRGEDGK
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
7Ubiquitination-MGEVYEKNNIDFDS
-CCCCCCCCCCCHHH
37.2924961812
17UbiquitinationIDFDSIAKMLLIKYK
CCHHHHHHHHHHHHH
28.5417644757
22UbiquitinationIAKMLLIKYKDFILS
HHHHHHHHHHHHHHH
46.3317644757
24UbiquitinationKMLLIKYKDFILSKF
HHHHHHHHHHHHHHH
40.9517644757
30UbiquitinationYKDFILSKFKKAAPV
HHHHHHHHHHHCCCC
58.7317644757
32UbiquitinationDFILSKFKKAAPVEN
HHHHHHHHHCCCCCC
45.2817644757
33UbiquitinationFILSKFKKAAPVENI
HHHHHHHHCCCCCCE
53.5723749301
86UbiquitinationLDLDLIYKNVDKEFA
CCHHHEEECCCHHHH
43.4317644757
90UbiquitinationLIYKNVDKEFAKDGH
HEEECCCHHHHHCCC
50.9117644757
94UbiquitinationNVDKEFAKDGHAEGE
CCCHHHHHCCCCCCC
70.3517644757
94AcetylationNVDKEFAKDGHAEGE
CCCHHHHHCCCCCCC
70.3524489116
110UbiquitinationIYTDYLVKELLRYFK
HHHHHHHHHHHHHHH
39.8017644757
117AcetylationKELLRYFKQDFFKWC
HHHHHHHHHHHHHHC
39.7724489116
117UbiquitinationKELLRYFKQDFFKWC
HHHHHHHHHHHHHHC
39.7715699485
122UbiquitinationYFKQDFFKWCNKPDC
HHHHHHHHHCCCCCC
51.3215699485
154UbiquitinationGPNGEESKFNCGTVE
CCCCCCCCCCCCEEE
43.8223749301
164UbiquitinationCGTVEIYKCNRCGNI
CCEEEEEECCCCCCC
30.6023749301
182UbiquitinationPRYNDPIKLLETRKG
CCCCCHHHHHHHCCC
53.0224961812
188UbiquitinationIKLLETRKGRCGEWC
HHHHHHCCCCHHHHH
59.1217644757
203UbiquitinationNLFTLILKSFGLDVR
HHHHHHHHHCCCCEE
36.4217644757
253UbiquitinationIYSINWNKKMSYCIA
EEEEECCCCEEEEEE
41.2817644757
254UbiquitinationYSINWNKKMSYCIAF
EEEECCCCEEEEEEE
29.8417644757
271UbiquitinationDGVVDVSKRYILQNE
CCEEEHHHHHHHHCC
49.4117644757
285UbiquitinationELPRDQIKEEDLKFL
CCCHHHCCHHHHHHH
49.7923749301
290UbiquitinationQIKEEDLKFLCQFIT
HCCHHHHHHHHHHHH
48.9217644757
298UbiquitinationFLCQFITKRLRYSLN
HHHHHHHHHHHHCCC
44.6217644757
327UbiquitinationQIELIRGKTQETKSE
HHHHHCCCCCCCCHH
36.8722817900
332UbiquitinationRGKTQETKSESVSAA
CCCCCCCCHHCCCHH
52.0223749301
333PhosphorylationGKTQETKSESVSAAS
CCCCCCCHHCCCHHH
42.3923749301
335PhosphorylationTQETKSESVSAASKS
CCCCCHHCCCHHHHC
28.5928889911
337PhosphorylationETKSESVSAASKSSN
CCCHHCCCHHHHCCC
27.6528889911
340PhosphorylationSESVSAASKSSNRGR
HHCCCHHHHCCCCCC
32.5528889911
341UbiquitinationESVSAASKSSNRGRE
HCCCHHHHCCCCCCC
53.8523749301
351PhosphorylationNRGRESGSADWKAQR
CCCCCCCCCCHHHHC
32.1328889911
355UbiquitinationESGSADWKAQRGEDG
CCCCCCHHHHCCCCC
34.8823749301

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 PNG1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PNG1_YEAST !!

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 PNG1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAD23_YEASTRAD23physical
11259433
PRS7_YEASTRPT1physical
11259433
RAD23_YEASTRAD23physical
15964983
ATG19_YEASTATG19genetic
21228276
ATG8_YEASTATG8genetic
21228276
ATG1_YEASTATG1genetic
21228276
ATG3_YEASTATG3genetic
21228276
ATG7_YEASTATG7genetic
21228276
ATG10_YEASTATG10genetic
21228276
MRM2_YEASTMRM2genetic
27708008
C1TM_YEASTMIS1genetic
27708008
RV161_YEASTRVS161genetic
27708008
SLX5_YEASTSLX5genetic
27708008
SOK1_YEASTSOK1genetic
27708008
IRC4_YEASTIRC4genetic
27708008
ICE2_YEASTICE2genetic
27708008
SGN1_YEASTSGN1genetic
27708008
ELM1_YEASTELM1genetic
27708008
CTK1_YEASTCTK1genetic
27708008
TMN1_YEASTEMP70genetic
27708008
ACE2_YEASTACE2genetic
27708008
LIPB_YEASTLIP2genetic
27708008
MAM3_YEASTMAM3genetic
27708008
UBC11_YEASTUBC11genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PNG1_YEAST

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Related Literatures of Post-Translational Modification

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