PMGT1_HUMAN - dbPTM
PMGT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PMGT1_HUMAN
UniProt AC Q8WZA1
Protein Name Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1
Gene Name POMGNT1
Organism Homo sapiens (Human).
Sequence Length 660
Subcellular Localization Golgi apparatus membrane
Single-pass type II membrane protein .
Protein Description Participates in O-mannosyl glycosylation by catalyzing the addition of N-acetylglucosamine to O-linked mannose on glycoproteins. [PubMed: 11709191]
Protein Sequence MDDWKPSPLIKPFGARKKRSWYLTWKYKLTNQRALRRFCQTGAVLFLLVTVIVNIKLILDTRRAISEANEDPEPEQDYDEALGRLEPPRRRGSGPRRVLDVEVYSSRSKVYVAVDGTTVLEDEAREQGRGIHVIVLNQATGHVMAKRVFDTYSPHEDEAMVLFLNMVAPGRVLICTVKDEGSFHLKDTAKALLRSLGSQAGPALGWRDTWAFVGRKGGPVFGEKHSKSPALSSWGDPVLLKTDVPLSSAEEAECHWADTELNRRRRRFCSKVEGYGSVCSCKDPTPIEFSPDPLPDNKVLNVPVAVIAGNRPNYLYRMLRSLLSAQGVSPQMITVFIDGYYEEPMDVVALFGLRGIQHTPISIKNARVSQHYKASLTATFNLFPEAKFAVVLEEDLDIAVDFFSFLSQSIHLLEEDDSLYCISAWNDQGYEHTAEDPALLYRVETMPGLGWVLRRSLYKEELEPKWPTPEKLWDWDMWMRMPEQRRGRECIIPDVSRSYHFGIVGLNMNGYFHEAYFKKHKFNTVPGVQLRNVDSLKKEAYEVEVHRLLSEAEVLDHSKNPCEDSFLPDTEGHTYVAFIRMEKDDDFTTWTQLAKCLHIWDLDVRGNHRGLWRLFRKKNHFLMVGVPASPYSVKKPPSVTPIFLEPPPKEEGAPGAPEQT
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
7Phosphorylation-MDDWKPSPLIKPFG
-CCCCCCCCCCCCCC		28.7225159151
11UbiquitinationWKPSPLIKPFGARKK
CCCCCCCCCCCCCCC		41.81-
27PhosphorylationSWYLTWKYKLTNQRA
EEEEEEEEECCCHHH		11.6428152594
30PhosphorylationLTWKYKLTNQRALRR
EEEEEECCCHHHHHH		25.7528152594
41PhosphorylationALRRFCQTGAVLFLL
HHHHHHHHHHHHHHH		28.43-
66PhosphorylationLDTRRAISEANEDPE
HHHHHHHHHHCCCCC		29.6728355574
78PhosphorylationDPEPEQDYDEALGRL
CCCCCCCHHHHHHCC		18.5128985074
104PhosphorylationRVLDVEVYSSRSKVY
CEEEEEEEECCCCEE		6.3426074081
105PhosphorylationVLDVEVYSSRSKVYV
EEEEEEEECCCCEEE		25.1726074081
106PhosphorylationLDVEVYSSRSKVYVA
EEEEEEECCCCEEEE		23.9226074081
108PhosphorylationVEVYSSRSKVYVAVD
EEEEECCCCEEEEEC		28.5526074081
111PhosphorylationYSSRSKVYVAVDGTT
EECCCCEEEEECCCE		6.0926074081
117PhosphorylationVYVAVDGTTVLEDEA
EEEEECCCEEECHHH		14.8526074081
118PhosphorylationYVAVDGTTVLEDEAR
EEEECCCEEECHHHH		28.7326074081
182PhosphorylationCTVKDEGSFHLKDTA
EEECCCCCEEHHHHH		13.8824719451
188PhosphorylationGSFHLKDTAKALLRS
CCEEHHHHHHHHHHH		28.5924719451
242PhosphorylationGDPVLLKTDVPLSSA
CCCEEEECCCCCCCH		42.0525002506
247PhosphorylationLKTDVPLSSAEEAEC
EECCCCCCCHHHHHC		22.7926657352
248PhosphorylationKTDVPLSSAEEAECH
ECCCCCCCHHHHHCC		47.5924275569
285PhosphorylationVCSCKDPTPIEFSPD
CCCCCCCCCCCCCCC		47.2125690035
285O-linked_GlycosylationVCSCKDPTPIEFSPD
CCCCCCCCCCCCCCC		47.21OGP
521UbiquitinationEAYFKKHKFNTVPGV
HHHHHHCCCCCCCCE		49.54-
524O-linked_GlycosylationFKKHKFNTVPGVQLR
HHHCCCCCCCCEEEC		31.0755834227
535PhosphorylationVQLRNVDSLKKEAYE
EEECCHHHHHHHHHH		37.4928060719
537UbiquitinationLRNVDSLKKEAYEVE
ECCHHHHHHHHHHHH		53.1417370265
538UbiquitinationRNVDSLKKEAYEVEV
CCHHHHHHHHHHHHH		53.5217370265
550PhosphorylationVEVHRLLSEAEVLDH
HHHHHHHHHHHHHCC		39.08-
624 (in isoform 2)Phosphorylation-8.3222468782
628 (in isoform 2)Phosphorylation-22.2622468782
638PhosphorylationYSVKKPPSVTPIFLE
CCCCCCCCCCCCCCC		47.3426503514
638 (in isoform 2)Phosphorylation-47.3422468782
640PhosphorylationVKKPPSVTPIFLEPP
CCCCCCCCCCCCCCC		18.2726503514
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 PMGT1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PMGT1_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 PMGT1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZBT18_HUMANZBTB18physical
21988832
SOX6_HUMANSOX6physical
21988832
LNX1_HUMANLNX1physical
25416956
Drug and Disease Associations
Kegg Disease
OMIM Disease
253280Muscular dystrophy-dystroglycanopathy congenital with brain and eye anomalies A3 (MDDGA3)
613151Muscular dystrophy-dystroglycanopathy congenital with mental retardation B3 (MDDGB3)
613157Muscular dystrophy-dystroglycanopathy limb-girdle C3 (MDDGC3)
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PMGT1_HUMAN

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Related Literatures of Post-Translational Modification
Ubiquitylation
ReferencePubMed
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry.";
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
Proteomics 7:868-874(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-537 AND LYS-538, AND MASSSPECTROMETRY.

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