GDE_HUMAN - dbPTM
GDE_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GDE_HUMAN
UniProt AC P35573
Protein Name Glycogen debranching enzyme
Gene Name AGL
Organism Homo sapiens (Human).
Sequence Length 1532
Subcellular Localization Cytoplasm . Under glycogenolytic conditions localizes to the nucleus.
Protein Description Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6-glucosidase in glycogen degradation..
Protein Sequence MGHSKQIRILLLNEMEKLEKTLFRLEQGYELQFRLGPTLQGKAVTVYTNYPFPGETFNREKFRSLDWENPTEREDDSDKYCKLNLQQSGSFQYYFLQGNEKSGGGYIVVDPILRVGADNHVLPLDCVTLQTFLAKCLGPFDEWESRLRVAKESGYNMIHFTPLQTLGLSRSCYSLANQLELNPDFSRPNRKYTWNDVGQLVEKLKKEWNVICITDVVYNHTAANSKWIQEHPECAYNLVNSPHLKPAWVLDRALWRFSCDVAEGKYKEKGIPALIENDHHMNSIRKIIWEDIFPKLKLWEFFQVDVNKAVEQFRRLLTQENRRVTKSDPNQHLTIIQDPEYRRFGCTVDMNIALTTFIPHDKGPAAIEECCNWFHKRMEELNSEKHRLINYHQEQAVNCLLGNVFYERLAGHGPKLGPVTRKHPLVTRYFTFPFEEIDFSMEESMIHLPNKACFLMAHNGWVMGDDPLRNFAEPGSEVYLRRELICWGDSVKLRYGNKPEDCPYLWAHMKKYTEITATYFQGVRLDNCHSTPLHVAEYMLDAARNLQPNLYVVAELFTGSEDLDNVFVTRLGISSLIREAMSAYNSHEEGRLVYRYGGEPVGSFVQPCLRPLMPAIAHALFMDITHDNECPIVHRSAYDALPSTTIVSMACCASGSTRGYDELVPHQISVVSEERFYTKWNPEALPSNTGEVNFQSGIIAARCAISKLHQELGAKGFIQVYVDQVDEDIVAVTRHSPSIHQSVVAVSRTAFRNPKTSFYSKEVPQMCIPGKIEEVVLEARTIERNTKPYRKDENSINGTPDITVEIREHIQLNESKIVKQAGVATKGPNEYIQEIEFENLSPGSVIIFRVSLDPHAQVAVGILRNHLTQFSPHFKSGSLAVDNADPILKIPFASLASRLTLAELNQILYRCESEEKEDGGGCYDIPNWSALKYAGLQGLMSVLAEIRPKNDLGHPFCNNLRSGDWMIDYVSNRLISRSGTIAEVGKWLQAMFFYLKQIPRYLIPCYFDAILIGAYTTLLDTAWKQMSSFVQNGSTFVKHLSLGSVQLCGVGKFPSLPILSPALMDVPYRLNEITKEKEQCCVSLAAGLPHFSSGIFRCWGRDTFIALRGILLITGRYVEARNIILAFAGTLRHGLIPNLLGEGIYARYNCRDAVWWWLQCIQDYCKMVPNGLDILKCPVSRMYPTDDSAPLPAGTLDQPLFEVIQEAMQKHMQGIQFRERNAGPQIDRNMKDEGFNITAGVDEETGFVYGGNRFNCGTWMDKMGESDRARNRGIPATPRDGSAVEIVGLSKSAVRWLLELSKKNIFPYHEVTVKRHGKAIKVSYDEWNRKIQDNFEKLFHVSEDPSDLNEKHPNLVHKRGIYKDSYGASSPWCDYQLRPNFTIAMVVAPELFTTEKAWKALEIAEKKLLGPLGMKTLDPDDMVYCGIYDNALDNDNYNLAKGFNYHQGPEWLWPIGYFLRAKLYFSRLMGPETTAKTIVLVKNVLSRHYVHLERSPWKGLPELTNENAQYCPFSCETQAWSIATILETLYDL
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
17UbiquitinationLLLNEMEKLEKTLFR
HHHHHHHHHHHHHHH
61.71-
29PhosphorylationLFRLEQGYELQFRLG
HHHHHCCEEEEEEEC
17.11-
38PhosphorylationLQFRLGPTLQGKAVT
EEEEECCCCCCEEEE
29.8926437602
56PhosphorylationNYPFPGETFNREKFR
CCCCCCCCCCHHHHH
31.9326437602
61UbiquitinationGETFNREKFRSLDWE
CCCCCHHHHHCCCCC
42.72-
64PhosphorylationFNREKFRSLDWENPT
CCHHHHHCCCCCCCC
33.5410571954
102PhosphorylationFLQGNEKSGGGYIVV
EEECCCCCCCCEEEE
36.1728152594
106PhosphorylationNEKSGGGYIVVDPIL
CCCCCCCEEEECCCE
8.2028152594
126GlutathionylationNHVLPLDCVTLQTFL
CCEEECHHHHHHHHH
3.1222555962
151UbiquitinationESRLRVAKESGYNMI
HHHHHHHHHHCCCEE
49.94-
155PhosphorylationRVAKESGYNMIHFTP
HHHHHHCCCEEECCC
15.7322468782
161PhosphorylationGYNMIHFTPLQTLGL
CCCEEECCCCHHHCC
14.6622468782
169PhosphorylationPLQTLGLSRSCYSLA
CCHHHCCCHHHHHHH
21.9824719451
171PhosphorylationQTLGLSRSCYSLANQ
HHHCCCHHHHHHHHH
17.6527251275
173PhosphorylationLGLSRSCYSLANQLE
HCCCHHHHHHHHHHC
14.1527251275
174PhosphorylationGLSRSCYSLANQLEL
CCCHHHHHHHHHHCC
25.9027251275
191UbiquitinationDFSRPNRKYTWNDVG
CCCCCCCCCCHHHHH
54.39-
192PhosphorylationFSRPNRKYTWNDVGQ
CCCCCCCCCHHHHHH
17.4722673903
193PhosphorylationSRPNRKYTWNDVGQL
CCCCCCCCHHHHHHH
22.3426437602
2652-HydroxyisobutyrylationSCDVAEGKYKEKGIP
CCCCCCCCCHHCCCC
44.66-
265AcetylationSCDVAEGKYKEKGIP
CCCCCCCCCHHCCCC
44.6626051181
265UbiquitinationSCDVAEGKYKEKGIP
CCCCCCCCCHHCCCC
44.66-
283PhosphorylationENDHHMNSIRKIIWE
CCCHHHHHHHHHHHH
19.05-
309 (in isoform 2)Ubiquitination-12.6021890473
310 (in isoform 3)Ubiquitination-6.7521890473
322MethylationRLLTQENRRVTKSDP
HHHHHHCCCCCCCCC
33.42-
326UbiquitinationQENRRVTKSDPNQHL
HHCCCCCCCCCCCCE
50.4321906983
326 (in isoform 1)Ubiquitination-50.4321890473
327PhosphorylationENRRVTKSDPNQHLT
HCCCCCCCCCCCCEE
49.2726437602
334PhosphorylationSDPNQHLTIIQDPEY
CCCCCCEEEECCHHH
17.5726437602
383PhosphorylationKRMEELNSEKHRLIN
HHHHHHCHHHHHHHH
61.7226437602
385AcetylationMEELNSEKHRLINYH
HHHHCHHHHHHHHHC
33.5727452117
415UbiquitinationRLAGHGPKLGPVTRK
HHCCCCCCCCCCCCC
71.34-
420PhosphorylationGPKLGPVTRKHPLVT
CCCCCCCCCCCCCEE
36.81-
475 (in isoform 2)Ubiquitination-28.1321890473
476 (in isoform 3)Ubiquitination-34.3121890473
479PhosphorylationAEPGSEVYLRRELIC
CCCCCEEEEEEEEEE
7.16-
492UbiquitinationICWGDSVKLRYGNKP
EECCCCEEECCCCCC
31.0621890473
492 (in isoform 1)Ubiquitination-31.0621890473
495PhosphorylationGDSVKLRYGNKPEDC
CCCEEECCCCCCCCC
35.1726437602
504PhosphorylationNKPEDCPYLWAHMKK
CCCCCCCCHHHHHHH
22.6226437602
510AcetylationPYLWAHMKKYTEITA
CCHHHHHHHCCCCCE
32.5324885255
519PhosphorylationYTEITATYFQGVRLD
CCCCCEEEECCEECC
7.4626437602
567 (in isoform 2)Phosphorylation-6.11-
568 (in isoform 3)Phosphorylation-2.37-
575PhosphorylationVTRLGISSLIREAMS
HHHHHHHHHHHHHHH
26.3724719451
582PhosphorylationSLIREAMSAYNSHEE
HHHHHHHHHCCCCCC
34.3528796482
584PhosphorylationIREAMSAYNSHEEGR
HHHHHHHCCCCCCCC
15.1923401153
586PhosphorylationEAMSAYNSHEEGRLV
HHHHHCCCCCCCCEE
21.4327155012
638PhosphorylationPIVHRSAYDALPSTT
CCCCHHHHHCCCCCE
11.73-
662 (in isoform 2)Ubiquitination-43.0921890473
663 (in isoform 3)Ubiquitination-7.1121890473
672PhosphorylationPHQISVVSEERFYTK
CCCEEEEECHHHCCC
31.4226437602
679UbiquitinationSEERFYTKWNPEALP
ECHHHCCCCCCHHCC
33.3321906983
679 (in isoform 1)Ubiquitination-33.3321890473
706PhosphorylationIAARCAISKLHQELG
HHHHHHHHHHHHHHC
15.6130622161
707UbiquitinationAARCAISKLHQELGA
HHHHHHHHHHHHHCC
43.82-
738PhosphorylationAVTRHSPSIHQSVVA
EEECCCCCHHHHHHH
35.4026437602
747PhosphorylationHQSVVAVSRTAFRNP
HHHHHHEECCCCCCC
17.7424719451
771UbiquitinationPQMCIPGKIEEVVLE
CCCCCCCCHHHHHHH
41.40-
816AcetylationHIQLNESKIVKQAGV
HHCCCCCHHHHHCCC
45.3918530417
816UbiquitinationHIQLNESKIVKQAGV
HHCCCCCHHHHHCCC
45.39-
8192-HydroxyisobutyrylationLNESKIVKQAGVATK
CCCCHHHHHCCCCCC
37.59-
819AcetylationLNESKIVKQAGVATK
CCCCHHHHHCCCCCC
37.5925953088
819UbiquitinationLNESKIVKQAGVATK
CCCCHHHHHCCCCCC
37.59-
826AcetylationKQAGVATKGPNEYIQ
HHCCCCCCCCCHHEE
63.7318530425
858 (in isoform 2)Ubiquitination-4.9021890473
859 (in isoform 3)Ubiquitination-5.0321890473
871PhosphorylationRNHLTQFSPHFKSGS
HHHHHHCCCCCCCCC
13.9826437602
872 (in isoform 2)Ubiquitination-37.92-
875AcetylationTQFSPHFKSGSLAVD
HHCCCCCCCCCEECC
51.3725953088
875UbiquitinationTQFSPHFKSGSLAVD
HHCCCCCCCCCEECC
51.3721890473
875 (in isoform 1)Ubiquitination-51.3721890473
876PhosphorylationQFSPHFKSGSLAVDN
HCCCCCCCCCEECCC
32.4424275569
878PhosphorylationSPHFKSGSLAVDNAD
CCCCCCCCEECCCCC
21.90-
889UbiquitinationDNADPILKIPFASLA
CCCCCCHHCCHHHHH
49.40-
894PhosphorylationILKIPFASLASRLTL
CHHCCHHHHHHHCHH
25.5026437602
897PhosphorylationIPFASLASRLTLAEL
CCHHHHHHHCHHHHH
32.8724275569
978PhosphorylationSNRLISRSGTIAEVG
HHHHHCCCCCHHHHH
33.2326437602
980PhosphorylationRLISRSGTIAEVGKW
HHHCCCCCHHHHHHH
20.4726437602
1027PhosphorylationDTAWKQMSSFVQNGS
HHHHHHHHHHHHCCC
20.3822673903
1028PhosphorylationTAWKQMSSFVQNGST
HHHHHHHHHHHCCCH
24.8826437602
1060PhosphorylationFPSLPILSPALMDVP
CCCCCCCCHHHHCCC
14.62-
1060 (in isoform 2)Ubiquitination-14.6221890473
1075UbiquitinationYRLNEITKEKEQCCV
CHHHHHHHCHHHHHH
72.89-
1077UbiquitinationLNEITKEKEQCCVSL
HHHHHHCHHHHHHHH
55.4222053931
1130O-linked_GlycosylationIILAFAGTLRHGLIP
HHHHHHHHHHCCCCH
19.7230379171
1130PhosphorylationIILAFAGTLRHGLIP
HHHHHHHHHHCCCCH
19.7221406692
1245PhosphorylationTAGVDEETGFVYGGN
CEEECCCCCCEECCC
33.59-
1262UbiquitinationNCGTWMDKMGESDRA
CCCCHHHHCCHHHHH
32.47-
1277PhosphorylationRNRGIPATPRDGSAV
HHCCCCCCCCCCCCE
17.3221406692
1290PhosphorylationAVEIVGLSKSAVRWL
CEEEEECCHHHHHHH
20.73-
1291UbiquitinationVEIVGLSKSAVRWLL
EEEEECCHHHHHHHH
47.69-
1314AcetylationPYHEVTVKRHGKAIK
CCCEEEEEECCEEEE
29.3425953088
1314MalonylationPYHEVTVKRHGKAIK
CCCEEEEEECCEEEE
29.3426320211
1330UbiquitinationSYDEWNRKIQDNFEK
CHHHHHHHHHHHHHH
41.32-
1337UbiquitinationKIQDNFEKLFHVSED
HHHHHHHHHHCCCCC
52.92-
1351UbiquitinationDPSDLNEKHPNLVHK
CHHHCCCCCCCHHHH
64.39-
1358UbiquitinationKHPNLVHKRGIYKDS
CCCCHHHHCCCCCCC
44.85-
1365PhosphorylationKRGIYKDSYGASSPW
HCCCCCCCCCCCCCC
22.7028258704
1399UbiquitinationFTTEKAWKALEIAEK
CCCHHHHHHHHHHHH
48.21-
1406AcetylationKALEIAEKKLLGPLG
HHHHHHHHHCCCCCC
39.432402129
1425GlutathionylationDPDDMVYCGIYDNAL
CCCCCEEEEECCCCC
1.4922555962
1464PhosphorylationYFLRAKLYFSRLMGP
HHHHHHHHHHHHHCC
9.98-
1466PhosphorylationLRAKLYFSRLMGPET
HHHHHHHHHHHCCCC
15.79-
1474O-linked_GlycosylationRLMGPETTAKTIVLV
HHHCCCCCHHHHHHH
25.2130379171

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
-KUbiquitinationE3 ubiquitin ligaseNHLRC1Q6VVB1
PMID:17908927

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GDE_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 GDE_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LGUL_HUMANGLO1physical
22939629
NNRD_HUMANCARKDphysical
26344197
CATA_HUMANCATphysical
26344197
FKB1A_HUMANFKBP1Aphysical
26344197
FKB1B_HUMANFKBP1Bphysical
26344197
GSH1_HUMANGCLCphysical
26344197
GRHPR_HUMANGRHPRphysical
26344197

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
232400Glycogen storage disease 3 (GSD3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GDE_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-584, AND MASSSPECTROMETRY.

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