GLGB_HUMAN - dbPTM
GLGB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GLGB_HUMAN
UniProt AC Q04446
Protein Name 1,4-alpha-glucan-branching enzyme
Gene Name GBE1
Organism Homo sapiens (Human).
Sequence Length 702
Subcellular Localization
Protein Description Required for normal glycogen accumulation. [PubMed: 8463281]
Protein Sequence MAAPMTPAARPEDYEAALNAALADVPELARLLEIDPYLKPYAVDFQRRYKQFSQILKNIGENEGGIDKFSRGYESFGVHRCADGGLYCKEWAPGAEGVFLTGDFNGWNPFSYPYKKLDYGKWELYIPPKQNKSVLVPHGSKLKVVITSKSGEILYRISPWAKYVVREGDNVNYDWIHWDPEHSYEFKHSRPKKPRSLRIYESHVGISSHEGKVASYKHFTCNVLPRIKGLGYNCIQLMAIMEHAYYASFGYQITSFFAASSRYGTPEELQELVDTAHSMGIIVLLDVVHSHASKNSADGLNMFDGTDSCYFHSGPRGTHDLWDSRLFAYSSWEILRFLLSNIRWWLEEYRFDGFRFDGVTSMLYHHHGVGQGFSGDYSEYFGLQVDEDALTYLMLANHLVHTLCPDSITIAEDVSGMPALCSPISQGGGGFDYRLAMAIPDKWIQLLKEFKDEDWNMGDIVYTLTNRRYLEKCIAYAESHDQALVGDKSLAFWLMDAEMYTNMSVLTPFTPVIDRGIQLHKMIRLITHGLGGEGYLNFMGNEFGHPEWLDFPRKGNNESYHYARRQFHLTDDDLLRYKFLNNFDRDMNRLEERYGWLAAPQAYVSEKHEGNKIIAFERAGLLFIFNFHPSKSYTDYRVGTALPGKFKIVLDSDAAEYGGHQRLDHSTDFFSEAFEHNGRPYSLLVYIPSRVALILQNVDLPN
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------MAAPMTPAA
------CCCCCCCCC		21.9222223895
6Phosphorylation--MAAPMTPAARPED
--CCCCCCCCCCHHH		14.5528450419
14PhosphorylationPAARPEDYEAALNAA
CCCCHHHHHHHHHHH		13.0528450419
37PhosphorylationRLLEIDPYLKPYAVD
HHHCCCCCCCHHHHH		24.49-
39UbiquitinationLEIDPYLKPYAVDFQ
HCCCCCCCHHHHHHH		30.0921890473
41PhosphorylationIDPYLKPYAVDFQRR
CCCCCCHHHHHHHHH		20.0519690332
50UbiquitinationVDFQRRYKQFSQILK
HHHHHHHHHHHHHHH		42.95-
53PhosphorylationQRRYKQFSQILKNIG
HHHHHHHHHHHHHHC		17.51-
57UbiquitinationKQFSQILKNIGENEG
HHHHHHHHHHCCCCC		48.42-
68UbiquitinationENEGGIDKFSRGYES
CCCCCHHHCCCCHHH		43.2321890473
68MalonylationENEGGIDKFSRGYES
CCCCCHHHCCCCHHH		43.2326320211
68UbiquitinationENEGGIDKFSRGYES
CCCCCHHHCCCCHHH		43.2321890473
68AcetylationENEGGIDKFSRGYES
CCCCCHHHCCCCHHH		43.2323236377
682-HydroxyisobutyrylationENEGGIDKFSRGYES
CCCCCHHHCCCCHHH		43.23-
70PhosphorylationEGGIDKFSRGYESFG
CCCHHHCCCCHHHCC		30.4520873877
73PhosphorylationIDKFSRGYESFGVHR
HHHCCCCHHHCCCEE		13.8030576142
75PhosphorylationKFSRGYESFGVHRCA
HCCCCHHHCCCEEEC		20.8628857561
81S-nitrosylationESFGVHRCADGGLYC
HHCCCEEECCCCEEC		2.152212679
87PhosphorylationRCADGGLYCKEWAPG
EECCCCEECCCCCCC		12.54-
88S-nitrosylationCADGGLYCKEWAPGA
ECCCCEECCCCCCCC		3.762212679
121UbiquitinationYKKLDYGKWELYIPP
CCCCCCCCEEEECCC		31.13-
132UbiquitinationYIPPKQNKSVLVPHG
ECCCCCCCEEEEECC		39.17-
133PhosphorylationIPPKQNKSVLVPHGS
CCCCCCCEEEEECCC		28.3828857561
140PhosphorylationSVLVPHGSKLKVVIT
EEEEECCCEEEEEEE		31.6127251275
141UbiquitinationVLVPHGSKLKVVITS
EEEECCCEEEEEEEC		57.85-
143UbiquitinationVPHGSKLKVVITSKS
EECCCEEEEEEECCC		37.89-
149AcetylationLKVVITSKSGEILYR
EEEEEECCCCCEEEE		54.5526822725
149UbiquitinationLKVVITSKSGEILYR
EEEEEECCCCCEEEE		54.5521906983
149MalonylationLKVVITSKSGEILYR
EEEEEECCCCCEEEE		54.5526320211
150PhosphorylationKVVITSKSGEILYRI
EEEEECCCCCEEEEE		41.2327762562
162UbiquitinationYRISPWAKYVVREGD
EEECHHHCEEEECCC		34.4121890473
162UbiquitinationYRISPWAKYVVREGD
EEECHHHCEEEECCC		34.4121890473
162AcetylationYRISPWAKYVVREGD
EEECHHHCEEEECCC		34.4125953088
173PhosphorylationREGDNVNYDWIHWDP
ECCCCCCEEECCCCC		14.3615452297
183PhosphorylationIHWDPEHSYEFKHSR
CCCCCCCCCCCCCCC		25.3728450419
184PhosphorylationHWDPEHSYEFKHSRP
CCCCCCCCCCCCCCC		27.5628450419
187UbiquitinationPEHSYEFKHSRPKKP
CCCCCCCCCCCCCCC		28.82-
196PhosphorylationSRPKKPRSLRIYESH
CCCCCCCCEEEEECC		30.44-
200PhosphorylationKPRSLRIYESHVGIS
CCCCEEEEECCCCCC		12.6327155012
202PhosphorylationRSLRIYESHVGISSH
CCEEEEECCCCCCCC		13.3928857561
208PhosphorylationESHVGISSHEGKVAS
ECCCCCCCCCCCEEE		24.5228857561
212UbiquitinationGISSHEGKVASYKHF
CCCCCCCCEEECCCE		31.4821890473
212UbiquitinationGISSHEGKVASYKHF
CCCCCCCCEEECCCE		31.4821890473
212MalonylationGISSHEGKVASYKHF
CCCCCCCCEEECCCE		31.4826320211
215PhosphorylationSHEGKVASYKHFTCN
CCCCCEEECCCEECC		37.3928857561
217MalonylationEGKVASYKHFTCNVL
CCCEEECCCEECCCH		29.7326320211
217UbiquitinationEGKVASYKHFTCNVL
CCCEEECCCEECCCH		29.73-
217AcetylationEGKVASYKHFTCNVL
CCCEEECCCEECCCH		29.7325953088
232PhosphorylationPRIKGLGYNCIQLMA
HHCCCCCCCHHHHHH		16.3528961369
245PhosphorylationMAIMEHAYYASFGYQ
HHHHHHHHHHHHCHH		11.0628961369
251PhosphorylationAYYASFGYQITSFFA
HHHHHHCHHHHHHHH		8.5028961369
254PhosphorylationASFGYQITSFFAASS
HHHCHHHHHHHHHHH		12.1728961369
255PhosphorylationSFGYQITSFFAASSR
HHCHHHHHHHHHHHC		21.7228961369
260PhosphorylationITSFFAASSRYGTPE
HHHHHHHHHCCCCHH		16.3628961369
296PhosphorylationHSHASKNSADGLNMF
HHCCCCCCCCCCCCC		31.3220873877
302SulfoxidationNSADGLNMFDGTDSC
CCCCCCCCCCCCCCC		3.7830846556
306PhosphorylationGLNMFDGTDSCYFHS
CCCCCCCCCCCEECC		26.9528857561
308PhosphorylationNMFDGTDSCYFHSGP
CCCCCCCCCEECCCC		15.5628857561
310PhosphorylationFDGTDSCYFHSGPRG
CCCCCCCEECCCCCC		14.3127251275
313PhosphorylationTDSCYFHSGPRGTHD
CCCCEECCCCCCCCC		40.3628857561
442UbiquitinationLAMAIPDKWIQLLKE
HEEECCHHHHHHHHH		40.6221890473
442UbiquitinationLAMAIPDKWIQLLKE
HEEECCHHHHHHHHH		40.6221890473
457SulfoxidationFKDEDWNMGDIVYTL
HCCCCCCHHHHHHHH		4.4430846556
469PhosphorylationYTLTNRRYLEKCIAY
HHHHCHHHHHHHHHH		18.90-
472UbiquitinationTNRRYLEKCIAYAES
HCHHHHHHHHHHHHH		28.48-
476PhosphorylationYLEKCIAYAESHDQA
HHHHHHHHHHHCCCC		7.32-
500PhosphorylationWLMDAEMYTNMSVLT
HHHCHHHHCCCCCCC		6.1026074081
501PhosphorylationLMDAEMYTNMSVLTP
HHCHHHHCCCCCCCC		24.1226074081
504PhosphorylationAEMYTNMSVLTPFTP
HHHHCCCCCCCCCCC		18.9526074081
507PhosphorylationYTNMSVLTPFTPVID
HCCCCCCCCCCCCCC		17.7526074081
510PhosphorylationMSVLTPFTPVIDRGI
CCCCCCCCCCCCHHH		20.1826074081
539SulfoxidationGEGYLNFMGNEFGHP
CCCHHHCCCCCCCCC		5.6930846556
554UbiquitinationEWLDFPRKGNNESYH
HHHCCCCCCCCCCHH		67.2521890473
559PhosphorylationPRKGNNESYHYARRQ
CCCCCCCCHHHHHHE		21.2320873877
560PhosphorylationRKGNNESYHYARRQF
CCCCCCCHHHHHHEE		7.8320873877
562PhosphorylationGNNESYHYARRQFHL
CCCCCHHHHHHEECC		8.12-
578UbiquitinationDDDLLRYKFLNNFDR
HHHHHHHHHHHCCHH		36.6221890473
578UbiquitinationDDDLLRYKFLNNFDR
HHHHHHHHHHHCCHH		36.6221890473
605PhosphorylationAAPQAYVSEKHEGNK
HCCHHEECCCCCCCE		28.4028857561
640PhosphorylationYTDYRVGTALPGKFK
CCCCCCCCCCCCCEE		23.3628857561
645UbiquitinationVGTALPGKFKIVLDS
CCCCCCCCEEEEECC		41.36-
647UbiquitinationTALPGKFKIVLDSDA
CCCCCCEEEEECCCH		35.08-
652PhosphorylationKFKIVLDSDAAEYGG
CEEEEECCCHHHHCC		25.62-
657PhosphorylationLDSDAAEYGGHQRLD
ECCCHHHHCCCCCCC		24.5518083107
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 GLGB_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GLGB_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 GLGB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRDMT_HUMANTRDMT1physical
21988832
ANM6_HUMANPRMT6physical
23455924
ACOC_HUMANACO1physical
26344197
MIF_HUMANMIFphysical
26344197
GYS1_HUMANGYS1physical
28514442
GLYG_HUMANGYG1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
232500Glycogen storage disease 4 (GSD4)
Note=Neuromuscular perinatal glycogen storage disease type 4 is associated with non-immune hydrops fetalis, a generalized edema of the fetus with fluid accumulation in the body cavities due to non-immune causes. Non-immune hydrops fetalis is not a diagnosis in itself but a symptom, a feature of many genetic disorders, and the end-stage of a wide variety of disorders.
263570
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GLGB_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-173, AND MASSSPECTROMETRY.

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