GLYG_HUMAN - dbPTM
GLYG_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GLYG_HUMAN
UniProt AC P46976
Protein Name Glycogenin-1
Gene Name GYG1
Organism Homo sapiens (Human).
Sequence Length 350
Subcellular Localization
Protein Description Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase..
Protein Sequence MTDQAFVTLTTNDAYAKGALVLGSSLKQHRTTRRLVVLATPQVSDSMRKVLETVFDEVIMVDVLDSGDSAHLTLMKRPELGVTLTKLHCWSLTQYSKCVFMDADTLVLANIDDLFDREELSAAPDPGWPDCFNSGVFVYQPSVETYNQLLHLASEQGSFDGGDQGILNTFFSSWATTDIRKHLPFIYNLSSISIYSYLPAFKVFGASAKVVHFLGRVKPWNYTYDPKTKSVKSEAHDPNMTHPEFLILWWNIFTTNVLPLLQQFGLVKDTCSYVNVLSDLVYTLAFSCGFCRKEDVSGAISHLSLGEIPAMAQPFVSSEERKERWEQGQADYMGADSFDNIKRKLDTYLQ
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
2Phosphorylation------MTDQAFVTL
------CCCCEEEEE
36.5022673903
2Acetylation------MTDQAFVTL
------CCCCEEEEE
36.5022223895
8PhosphorylationMTDQAFVTLTTNDAY
CCCCEEEEEECCCHH
16.3722673903
10PhosphorylationDQAFVTLTTNDAYAK
CCEEEEEECCCHHHC
17.7522673903
11PhosphorylationQAFVTLTTNDAYAKG
CEEEEEECCCHHHCC
33.9322673903
15PhosphorylationTLTTNDAYAKGALVL
EEECCCHHHCCCEEE
16.2322673903
24PhosphorylationKGALVLGSSLKQHRT
CCCEEECHHHHHCCC
28.4721406692
25PhosphorylationGALVLGSSLKQHRTT
CCEEECHHHHHCCCC
37.4724719451
27UbiquitinationLVLGSSLKQHRTTRR
EEECHHHHHCCCCCE
46.1130230243
44PhosphorylationVLATPQVSDSMRKVL
EEECHHCCHHHHHHH
20.7920068231
46PhosphorylationATPQVSDSMRKVLET
ECHHCCHHHHHHHHH
17.0026437602
55UbiquitinationRKVLETVFDEVIMVD
HHHHHHHCCEEEEEE
9.6521890473
150UbiquitinationVETYNQLLHLASEQG
HHHHHHHHHHHHHCC
1.9321890473
173UbiquitinationILNTFFSSWATTDIR
HHHHHHHHHCCCHHH
18.6424816145
195O-linked_GlycosylationNLSSISIYSYLPAFK
ECCCCCHHHHCHHHH
5.6222160680
196PhosphorylationLSSISIYSYLPAFKV
CCCCCHHHHCHHHHH
20.65-
197PhosphorylationSSISIYSYLPAFKVF
CCCCHHHHCHHHHHH
10.34-
209 (in isoform 1)Ubiquitination-42.1521890473
209 (in isoform 2)Ubiquitination-42.1521890473
209UbiquitinationKVFGASAKVVHFLGR
HHHCCEEEEEHHHCC
42.1522817900
218UbiquitinationVHFLGRVKPWNYTYD
EHHHCCCCCCCCCCC
42.8530230243
222PhosphorylationGRVKPWNYTYDPKTK
CCCCCCCCCCCCCCC
11.6525278378
223PhosphorylationRVKPWNYTYDPKTKS
CCCCCCCCCCCCCCC
20.4525278378
224PhosphorylationVKPWNYTYDPKTKSV
CCCCCCCCCCCCCCC
21.6425278378
226 (in isoform 3)Phosphorylation-35.48-
228PhosphorylationNYTYDPKTKSVKSEA
CCCCCCCCCCCCCCC
33.6625278378
230PhosphorylationTYDPKTKSVKSEAHD
CCCCCCCCCCCCCCC
39.7525278378
233PhosphorylationPKTKSVKSEAHDPNM
CCCCCCCCCCCCCCC
37.55-
254PhosphorylationILWWNIFTTNVLPLL
HHHHHHHHHCHHHHH
17.42-
255PhosphorylationLWWNIFTTNVLPLLQ
HHHHHHHHCHHHHHH
16.75-
268UbiquitinationLQQFGLVKDTCSYVN
HHHHCCCHHHHHHHH
52.9824816145
273 (in isoform 2)Phosphorylation-9.74-
287 (in isoform 2)Phosphorylation-14.0227251275
297PhosphorylationFCRKEDVSGAISHLS
CCCCCCCCHHHHHCC
34.52-
300 (in isoform 2)Phosphorylation-2.8028348404
301 (in isoform 2)Phosphorylation-20.1728348404
304PhosphorylationSGAISHLSLGEIPAM
CHHHHHCCCCCCCHH
28.98-
317PhosphorylationAMAQPFVSSEERKER
HHHCCCCCHHHHHHH
32.2025627689
318PhosphorylationMAQPFVSSEERKERW
HHCCCCCHHHHHHHH
37.8725627689
327UbiquitinationERKERWEQGQADYMG
HHHHHHHHHCCCCCC
42.1924816145
332PhosphorylationWEQGQADYMGADSFD
HHHHCCCCCCCCCHH
10.6428796482
333SulfoxidationEQGQADYMGADSFDN
HHHCCCCCCCCCHHH
3.5230846556
337PhosphorylationADYMGADSFDNIKRK
CCCCCCCCHHHHHHH
33.6828857561
3422-HydroxyisobutyrylationADSFDNIKRKLDTYL
CCCHHHHHHHHHHHC
50.13-
344UbiquitinationSFDNIKRKLDTYLQ-
CHHHHHHHHHHHCC-
45.7924816145
347PhosphorylationNIKRKLDTYLQ----
HHHHHHHHHCC----
36.2523532336

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 GLYG_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GLYG_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 GLYG_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GYS1_HUMANGYS1physical
16189514
P121A_HUMANPOM121physical
16189514
TRIM7_HUMANTRIM7physical
11916970
GLYG2_HUMANGYG2physical
9857012
TRIM7_HUMANTRIM7physical
14984203
GYS1_HUMANGYS1physical
25416956
ESTD_HUMANESDphysical
26344197
GGT1_HUMANGGT1physical
26344197

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613507Glycogen storage disease 15 (GSD15)
616199Polyglucosan body myopathy 2 (PGBM2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GLYG_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP