NGLY1_HUMAN - dbPTM
NGLY1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NGLY1_HUMAN
UniProt AC Q96IV0
Protein Name Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase
Gene Name NGLY1
Organism Homo sapiens (Human).
Sequence Length 654
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..
Protein Sequence MAAAALGSSSGSASPAVAELCQNTPETFLEASKLLLTYADNILRNPNDEKYRSIRIGNTAFSTRLLPVRGAVECLFEMGFEEGETHLIFPKKASVEQLQKIRDLIAIERSSRLDGSNKSHKVKSSQQPAASTQLPTTPSSNPSGLNQHTRNRQGQSSDPPSASTVAADSAILEVLQSNIQHVLVYENPALQEKALACIPVQELKRKSQEKLSRARKLDKGINISDEDFLLLELLHWFKEEFFHWVNNVLCSKCGGQTRSRDRSLLPSDDELKWGAKEVEDHYCDACQFSNRFPRYNNPEKLLETRCGRCGEWANCFTLCCRAVGFEARYVWDYTDHVWTEVYSPSQQRWLHCDACEDVCDKPLLYEIGWGKKLSYVIAFSKDEVVDVTWRYSCKHEEVIARRTKVKEALLRDTINGLNKQRQLFLSENRRKELLQRIIVELVEFISPKTPKPGELGGRISGSVAWRVARGEMGLQRKETLFIPCENEKISKQLHLCYNIVKDRYVRVSNNNQTISGWENGVWKMESIFRKVETDWHMVYLARKEGSSFAYISWKFECGSVGLKVDSISIRTSSQTFQTGTVEWKLRSDTAQVELTGDNSLHSYADFSGATEVILEAELSRGDGDVAWQHTQLFRQSLNDHEENCLEIIIKFSDL
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
2Acetylation------MAAAALGSS
------CCCCHHCCC		13.0519413330
8UbiquitinationMAAAALGSSSGSASP
CCCCHHCCCCCCCCH		23.3729967540
41UbiquitinationLLLTYADNILRNPND
HHHHHHHHHHHCCCC		27.3322817900
44UbiquitinationTYADNILRNPNDEKY
HHHHHHHHCCCCHHC		53.4122817900
46UbiquitinationADNILRNPNDEKYRS
HHHHHHCCCCHHCCC		43.1222817900
50UbiquitinationLRNPNDEKYRSIRIG
HHCCCCHHCCCCEEC		49.1529967540
58UbiquitinationYRSIRIGNTAFSTRL
CCCCEECCCCCCCCC		26.3433845483
76UbiquitinationRGAVECLFEMGFEEG
CCHHHHHHHCCCCCC		10.3222817900
79UbiquitinationVECLFEMGFEEGETH
HHHHHHCCCCCCCEE		21.4422817900
81UbiquitinationCLFEMGFEEGETHLI
HHHHCCCCCCCEEEE		60.4027667366
92UbiquitinationTHLIFPKKASVEQLQ
EEEEECCCCCHHHHH		46.2429967540
100UbiquitinationASVEQLQKIRDLIAI
CCHHHHHHHHHHHHH		48.5833845483
110PhosphorylationDLIAIERSSRLDGSN
HHHHHHHHCCCCCCC		13.66-
111PhosphorylationLIAIERSSRLDGSNK
HHHHHHHCCCCCCCC		42.98-
116PhosphorylationRSSRLDGSNKSHKVK
HHCCCCCCCCCCCCC		40.5326699800
118UbiquitinationSRLDGSNKSHKVKSS
CCCCCCCCCCCCCCC		56.4822817900
119PhosphorylationRLDGSNKSHKVKSSQ
CCCCCCCCCCCCCCC		32.5626699800
121UbiquitinationDGSNKSHKVKSSQQP
CCCCCCCCCCCCCCC		59.4522817900
123 (in isoform 2)Ubiquitination-49.5521890473
123 (in isoform 1)Ubiquitination-49.5521890473
123 (in isoform 3)Ubiquitination-49.5521890473
123UbiquitinationSNKSHKVKSSQQPAA
CCCCCCCCCCCCCCC		49.5521906983
125PhosphorylationKSHKVKSSQQPAAST
CCCCCCCCCCCCCCC		27.4128857561
127UbiquitinationHKVKSSQQPAASTQL
CCCCCCCCCCCCCCC		31.3923000965
129UbiquitinationVKSSQQPAASTQLPT
CCCCCCCCCCCCCCC		15.0923000965
131PhosphorylationSSQQPAASTQLPTTP
CCCCCCCCCCCCCCC		20.8428450419
132PhosphorylationSQQPAASTQLPTTPS
CCCCCCCCCCCCCCC		29.4228450419
133UbiquitinationQQPAASTQLPTTPSS
CCCCCCCCCCCCCCC		42.8423000965
136PhosphorylationAASTQLPTTPSSNPS
CCCCCCCCCCCCCCC		60.9925627689
137PhosphorylationASTQLPTTPSSNPSG
CCCCCCCCCCCCCCC		21.1625159151
139PhosphorylationTQLPTTPSSNPSGLN
CCCCCCCCCCCCCCC		40.4328450419
140PhosphorylationQLPTTPSSNPSGLNQ
CCCCCCCCCCCCCCH		54.7028450419
143PhosphorylationTTPSSNPSGLNQHTR
CCCCCCCCCCCHHCC		61.2328450419
149PhosphorylationPSGLNQHTRNRQGQS
CCCCCHHCCCCCCCC		21.6328450419
162UbiquitinationQSSDPPSASTVAADS
CCCCCCCHHHHHHHH		18.2623000965
164UbiquitinationSDPPSASTVAADSAI
CCCCCHHHHHHHHHH		17.5523000965
168UbiquitinationSASTVAADSAILEVL
CHHHHHHHHHHHHHH		28.9423000965
177PhosphorylationAILEVLQSNIQHVLV
HHHHHHHHCCCEEEE		31.5728857561
204UbiquitinationCIPVQELKRKSQEKL
CCCHHHHHHHHHHHH		57.9623000965
204 (in isoform 1)Ubiquitination-57.9621890473
204 (in isoform 2)Ubiquitination-57.9621890473
204MethylationCIPVQELKRKSQEKL
CCCHHHHHHHHHHHH		57.9621675315
204 (in isoform 3)Ubiquitination-57.9621890473
206UbiquitinationPVQELKRKSQEKLSR
CHHHHHHHHHHHHHH		55.7023000965
210TrimethylationLKRKSQEKLSRARKL
HHHHHHHHHHHHHHC		44.09-
210MethylationLKRKSQEKLSRARKL
HHHHHHHHHHHHHHC		44.09-
210UbiquitinationLKRKSQEKLSRARKL
HHHHHHHHHHHHHHC		44.0923000965
223UbiquitinationKLDKGINISDEDFLL
HCCCCCCCCHHHHHH		5.3322817900
230UbiquitinationISDEDFLLLELLHWF
CCHHHHHHHHHHHHH		3.3632015554
234UbiquitinationDFLLLELLHWFKEEF
HHHHHHHHHHHHHHH		2.1633845483
258UbiquitinationSKCGGQTRSRDRSLL
HHCCCCCCCCCCCCC		23.0822817900
263PhosphorylationQTRSRDRSLLPSDDE
CCCCCCCCCCCCCCC		38.2530622161
267PhosphorylationRDRSLLPSDDELKWG
CCCCCCCCCCCCCCC		58.6330622161
272UbiquitinationLPSDDELKWGAKEVE
CCCCCCCCCCCCCCH		41.3532015554
276UbiquitinationDELKWGAKEVEDHYC
CCCCCCCCCCHHHHC		59.3533845483
295PhosphorylationFSNRFPRYNNPEKLL
CCCCCCCCCCHHHHH		21.38-
300 (in isoform 3)Ubiquitination-60.6821890473
300UbiquitinationPRYNNPEKLLETRCG
CCCCCHHHHHHCCCC		60.6821906983
300 (in isoform 2)Ubiquitination-60.6821890473
300 (in isoform 1)Ubiquitination-60.6821890473
327UbiquitinationCRAVGFEARYVWDYT
HHHHCCEEEEEEECC		13.0723000965
329UbiquitinationAVGFEARYVWDYTDH
HHCCEEEEEEECCCC		16.9723000965
342UbiquitinationDHVWTEVYSPSQQRW
CCEEEECCCCCCCEE		14.5023000965
352UbiquitinationSQQRWLHCDACEDVC
CCCEEEECCCCHHHC		3.1233845483
362UbiquitinationCEDVCDKPLLYEIGW
CHHHCCCCCEEECCC		17.8523000965
364UbiquitinationDVCDKPLLYEIGWGK
HHCCCCCEEECCCCC		4.9723000965
374UbiquitinationIGWGKKLSYVIAFSK
CCCCCCEEEEEEEEC		26.6627667366
377UbiquitinationGKKLSYVIAFSKDEV
CCCEEEEEEEECCCE		2.1423000965
377UbiquitinationGKKLSYVIAFSKDEV
CCCEEEEEEEECCCE		2.1421890473
386UbiquitinationFSKDEVVDVTWRYSC
EECCCEEEEEEEEEC		36.9923000965
388UbiquitinationKDEVVDVTWRYSCKH
CCCEEEEEEEEECCH		10.3623000965
391PhosphorylationVVDVTWRYSCKHEEV
EEEEEEEEECCHHHH		15.2425278378
392PhosphorylationVDVTWRYSCKHEEVI
EEEEEEEECCHHHHH		14.2325278378
394UbiquitinationVTWRYSCKHEEVIAR
EEEEEECCHHHHHHH		48.3833845483
401UbiquitinationKHEEVIARRTKVKEA
CHHHHHHHHHHHHHH		35.3623000965
401 (in isoform 2)Ubiquitination-35.3621890473
404UbiquitinationEVIARRTKVKEALLR
HHHHHHHHHHHHHHH		49.8823000965
406UbiquitinationIARRTKVKEALLRDT
HHHHHHHHHHHHHHH		38.5323000965
409UbiquitinationRTKVKEALLRDTING
HHHHHHHHHHHHHHH		4.1733845483
411UbiquitinationKVKEALLRDTINGLN
HHHHHHHHHHHHHHH		39.6227667366
413PhosphorylationKEALLRDTINGLNKQ
HHHHHHHHHHHHHHH		15.20-
419 (in isoform 1)Ubiquitination-52.4821890473
419 (in isoform 3)Ubiquitination-52.4821890473
419UbiquitinationDTINGLNKQRQLFLS
HHHHHHHHHHHHHCC		52.4823000965
426PhosphorylationKQRQLFLSENRRKEL
HHHHHHCCHHHHHHH		26.0320873877
433UbiquitinationSENRRKELLQRIIVE
CHHHHHHHHHHHHHH		5.7633845483
435UbiquitinationNRRKELLQRIIVELV
HHHHHHHHHHHHHHH		47.3429967540
446UbiquitinationVELVEFISPKTPKPG
HHHHHHHCCCCCCCC		26.1827667366
448UbiquitinationLVEFISPKTPKPGEL
HHHHHCCCCCCCCCC		71.34-
449PhosphorylationVEFISPKTPKPGELG
HHHHCCCCCCCCCCC		39.6721406692
451UbiquitinationFISPKTPKPGELGGR
HHCCCCCCCCCCCCC		71.5333845483
459UbiquitinationPGELGGRISGSVAWR
CCCCCCCCCCCHHHH		6.5529967540
462PhosphorylationLGGRISGSVAWRVAR
CCCCCCCCHHHHHHC		11.2428857561
470UbiquitinationVAWRVARGEMGLQRK
HHHHHHCCCCCCCCE		21.3627667366
477UbiquitinationGEMGLQRKETLFIPC
CCCCCCCEEEEEEEC		41.9329967540
488UbiquitinationFIPCENEKISKQLHL
EEECCCHHHHHHHHH		64.9527667366
501UbiquitinationHLCYNIVKDRYVRVS
HHHHHHHHCCEEEEC		32.46-
584UbiquitinationQTGTVEWKLRSDTAQ
CCEEEEEEEECCEEE		22.10-
619PhosphorylationVILEAELSRGDGDVA
EEEEEEHHCCCCCHH		26.2324702127
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 NGLY1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NGLY1_HUMAN !!
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 NGLY1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RD23A_HUMANRAD23Aphysical
22575648
RD23B_HUMANRAD23Bphysical
22575648
TERA_HUMANVCPphysical
16807242
FAF1_HUMANFAF1physical
16807242
NSF1C_HUMANNSFL1Cphysical
16807242
DERL1_HUMANDERL1physical
16055502
A4_HUMANAPPphysical
21832049
TRI54_HUMANTRIM54physical
25416956
GUCD1_HUMANGUCD1physical
25416956
UBX2B_HUMANUBXN2Bphysical
25416956
RD23B_HUMANRAD23Bphysical
22119785
TERA_HUMANVCPphysical
22119785
RD23B_HUMANRAD23Bphysical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615273Congenital disorder of glycosylation 1V (CDG1V)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NGLY1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory