AGM1_HUMAN - dbPTM
AGM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AGM1_HUMAN
UniProt AC O95394
Protein Name Phosphoacetylglucosamine mutase {ECO:0000305}
Gene Name PGM3 {ECO:0000312|HGNC:HGNC:8907}
Organism Homo sapiens (Human).
Sequence Length 542
Subcellular Localization
Protein Description Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, a sugar nucleotide critical to multiple glycosylation pathways including protein N- and O-glycosylation..
Protein Sequence MDLGAITKYSALHAKPNGLILQYGTAGFRTKAEHLDHVMFRMGLLAVLRSKQTKSTIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEHATCLANAEEQDMQRVLIDISEKEAVNLQQDAFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMVYCRNTGGRYGKATIEGYYQKLSKAFVELTKQASCSGDEYRSLKVDCANGIGALKLREMEHYFSQGLSVQLFNDGSKGKLNHLCGADFVKSHQKPPQGMEIKSNERCCSFDGDADRIVYYYHDADGHFHLIDGDKIATLISSFLKELLVEIGESLNIGVVQTAYANGSSTRYLEEVMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALFSTAVEMKIKQSAEQLEDKKRKAAKMLENIIDLFNQAAGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQLKVQVADRRVISTTDAERQAVTPPGLQEAINDLVKKYKLSRAFVRPSGTEDVVRVYAEADSQESADHLAHEVSLAVFQLAGGIGERPQPGF
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
1Acetylation-------MDLGAITK
-------CCCCHHCC		9.6522223895
8UbiquitinationMDLGAITKYSALHAK
CCCCHHCCHHHHHCC		30.9721890473
42SulfoxidationLDHVMFRMGLLAVLR
HHHHHHHHHHHHHHH		2.7928465586
50PhosphorylationGLLAVLRSKQTKSTI
HHHHHHHCCCCCCEE		25.5928985074
55PhosphorylationLRSKQTKSTIGVMVT
HHCCCCCCEEEEEEE		28.7523927012
56PhosphorylationRSKQTKSTIGVMVTA
HCCCCCCEEEEEEEC		24.2523927012
60OxidationTKSTIGVMVTASHNP
CCCEEEEEEECCCCC		1.5417322306
62PhosphorylationSTIGVMVTASHNPEE
CEEEEEEECCCCCCC		12.3522167270
64PhosphorylationIGVMVTASHNPEEDN
EEEEEECCCCCCCCC		17.9029255136
86PhosphorylationLGEMLAPSWEEHATC
CHHCCCCCHHHHHHH		41.3230206219
92PhosphorylationPSWEEHATCLANAEE
CCHHHHHHHHHCCCH		15.2330206219
110PhosphorylationQRVLIDISEKEAVNL
HHEEEECCHHHHCCC		38.5829759185
177UbiquitinationNTGGRYGKATIEGYY
CCCCCCCEEEHHHHH		33.16-
177MalonylationNTGGRYGKATIEGYY
CCCCCCCEEEHHHHH		33.1626320211
186UbiquitinationTIEGYYQKLSKAFVE
EHHHHHHHHHHHHHH		38.31-
189UbiquitinationGYYQKLSKAFVELTK
HHHHHHHHHHHHHHH		57.171890473
196UbiquitinationKAFVELTKQASCSGD
HHHHHHHHHCCCCCC		57.39-
199PhosphorylationVELTKQASCSGDEYR
HHHHHHCCCCCCCCC		13.3030624053
205 (in isoform 1)Ubiquitination-15.3921906983
209AcetylationGDEYRSLKVDCANGI
CCCCCCCEEECCCCC		36.9626051181
209UbiquitinationGDEYRSLKVDCANGI
CCCCCCCEEECCCCC		36.96-
217 (in isoform 1)Ubiquitination-26.6721906983
220UbiquitinationANGIGALKLREMEHY
CCCCCHHHHHHHHHH		44.99-
244AcetylationFNDGSKGKLNHLCGA
ECCCCCCCHHHHCCC		50.2625953088
244UbiquitinationFNDGSKGKLNHLCGA
ECCCCCCCHHHHCCC		50.26-
255UbiquitinationLCGADFVKSHQKPPQ
HCCCCHHHHCCCCCC		42.06-
259UbiquitinationDFVKSHQKPPQGMEI
CHHHHCCCCCCCCEE		53.92-
264SulfoxidationHQKPPQGMEIKSNER
CCCCCCCCEECCCCC		3.9730846556
267UbiquitinationPPQGMEIKSNERCCS
CCCCCEECCCCCEEC		33.64-
307PhosphorylationKIATLISSFLKELLV
HHHHHHHHHHHHHHH		27.8324719451
319PhosphorylationLLVEIGESLNIGVVQ
HHHHHHHHCCEEEEE		22.8524719451
327PhosphorylationLNIGVVQTAYANGSS
CCEEEEEEEECCCCC		15.2723828894
343UbiquitinationRYLEEVMKVPVYCTK
HHHHHHHCCCEEECC		48.87-
347PhosphorylationEVMKVPVYCTKTGVK
HHHCCCEEECCCCCC		6.5824719451
349PhosphorylationMKVPVYCTKTGVKHL
HCCCEEECCCCCCCC		17.60-
350UbiquitinationKVPVYCTKTGVKHLH
CCCEEECCCCCCCCC		39.46-
350MalonylationKVPVYCTKTGVKHLH
CCCEEECCCCCCCCC		39.4626320211
350AcetylationKVPVYCTKTGVKHLH
CCCEEECCCCCCCCC		39.4625953088
354UbiquitinationYCTKTGVKHLHHKAQ
EECCCCCCCCCCCCC		41.62-
376PhosphorylationFEANGHGTALFSTAV
EEECCCCEEEHHHHH		17.95-
388UbiquitinationTAVEMKIKQSAEQLE
HHHHHHHHHHHHHHH		32.4521906983
397UbiquitinationSAEQLEDKKRKAAKM
HHHHHHHHHHHHHHH		45.142190698
398AcetylationAEQLEDKKRKAAKML
HHHHHHHHHHHHHHH		72.037481271
416 (in isoform 1)Ubiquitination-13.4621906983
425 (in isoform 1)Ubiquitination-2.7421906983
453UbiquitinationDLPNRQLKVQVADRR
CCCCCEEEEEEECCE		23.45-
453AcetylationDLPNRQLKVQVADRR
CCCCCEEEEEEECCE		23.4525953088
453MalonylationDLPNRQLKVQVADRR
CCCCCEEEEEEECCE		23.4526320211
463PhosphorylationVADRRVISTTDAERQ
EECCEEECCCHHHHH		23.5420068231
464PhosphorylationADRRVISTTDAERQA
ECCEEECCCHHHHHC		19.9920068231
465PhosphorylationDRRVISTTDAERQAV
CCEEECCCHHHHHCC		26.8220068231
498PhosphorylationSRAFVRPSGTEDVVR
CCEECCCCCCCCEEE		48.0227050516
500PhosphorylationAFVRPSGTEDVVRVY
EECCCCCCCCEEEEE		33.0923186163
526PhosphorylationLAHEVSLAVFQLAGG
HHHHHHHHHHHHCCC		7.8024719451
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 AGM1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AGM1_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 AGM1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
ENOPH_HUMANENOPH1physical
26344197
HDHD1_HUMANHDHD1physical
26344197
LACB2_HUMANLACTB2physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615816Immunodeficiency 23 (IMD23)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AGM1_HUMAN

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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 MET-1, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND MASSSPECTROMETRY.

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