GLYG2_HUMAN - dbPTM
GLYG2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GLYG2_HUMAN
UniProt AC O15488
Protein Name Glycogenin-2
Gene Name GYG2
Organism Homo sapiens (Human).
Sequence Length 501
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 MSETEFHHGAQAGLELLRSSNSPTSASQSAGMTVTDQAFVTLATNDIYCQGALVLGQSLRRHRLTRKLVVLITPQVSSLLRVILSKVFDEVIEVNLIDSADYIHLAFLKRPELGLTLTKLHCWTLTHYSKCVFLDADTLVLSNVDELFDRGEFSAAPDPGWPDCFNSGVFVFQPSLHTHKLLLQHAMEHGSFDGADQGLLNSFFRNWSTTDIHKHLPFIYNLSSNTMYTYSPAFKQFGSSAKVVHFLGSMKPWNYKYNPQSGSVLEQGSASSSQHQAAFLHLWWTVYQNNVLPLYKSVQAGEARASPGHTLCHSDVGGPCADSASGVGEPCENSTPSAGVPCANSPLGSNQPAQGLPEPTQIVDETLSLPEGRRSEDMIACPETETPAVITCDPLSQPSPQPADFTETETILQPANKVESVSSEETFEPSQELPAEALRDPSLQDALEVDLAVSVSQISIEEKVKELSPEEERRKWEEGRIDYMGKDAFARIQEKLDRFLQ
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------MSETEFHHG
------CCCCHHHHH		53.9127251275
2 (in isoform 3)Phosphorylation-53.9125072903
4 (in isoform 3)Phosphorylation-36.3225072903
8 (in isoform 3)Phosphorylation-38.3125072903
18 (in isoform 3)Phosphorylation-51.1425072903
78PhosphorylationLITPQVSSLLRVILS
ECCHHHHHHHHHHHH		32.3524719451
85PhosphorylationSLLRVILSKVFDEVI
HHHHHHHHHHHCCCC		18.69-
202PhosphorylationADQGLLNSFFRNWST
CCHHHHHHHHCCCCC		26.2324719451
208PhosphorylationNSFFRNWSTTDIHKH
HHHHCCCCCCCHHHH		25.6124275569
228O-linked_GlycosylationNLSSNTMYTYSPAFK
ECCCCCCEEECHHHH		10.659857012
230PhosphorylationSSNTMYTYSPAFKQF
CCCCCEEECHHHHHH		8.65-
240PhosphorylationAFKQFGSSAKVVHFL
HHHHHCCCCEEEHHH		32.27-
368PhosphorylationQIVDETLSLPEGRRS
CCEECCCCCCCCCCC		49.6624275569
375PhosphorylationSLPEGRRSEDMIACP
CCCCCCCCCCCEECC		36.2724275569
399PhosphorylationCDPLSQPSPQPADFT
ECCCCCCCCCCCCCC		28.6424275569
406PhosphorylationSPQPADFTETETILQ
CCCCCCCCCCCEEEE		42.4124275569
408 (in isoform 6)Phosphorylation-35.0624275569
410 (in isoform 6)Phosphorylation-34.1122468782
418 (in isoform 6)Phosphorylation-7.1322468782
420PhosphorylationQPANKVESVSSEETF
ECCCCCCCCCCCCCC		30.2222798277
422PhosphorylationANKVESVSSEETFEP
CCCCCCCCCCCCCCC		41.1122798277
423PhosphorylationNKVESVSSEETFEPS
CCCCCCCCCCCCCCC		36.9822798277
426PhosphorylationESVSSEETFEPSQEL
CCCCCCCCCCCCCCC		29.2822798277
456PhosphorylationVDLAVSVSQISIEEK
HCEEEEHHHCCHHHH		17.8124275569
459PhosphorylationAVSVSQISIEEKVKE
EEEHHHCCHHHHHHH		19.1321248752
468PhosphorylationEEKVKELSPEEERRK
HHHHHHCCHHHHHHH		31.2129255136
486UbiquitinationGRIDYMGKDAFARIQ
CCCCCCCHHHHHHHH		29.38-
491MethylationMGKDAFARIQEKLDR
CCHHHHHHHHHHHHH		25.35-
495MethylationAFARIQEKLDRFLQ-
HHHHHHHHHHHHHC-		39.03-
498MethylationRIQEKLDRFLQ----
HHHHHHHHHHC----		44.61-
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 GLYG2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GLYG2_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 GLYG2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GLYG_HUMANGYG1physical
9857012
A4_HUMANAPPphysical
21832049
GYS2_HUMANGYS2physical
21988832
OSCP1_HUMANOSCP1physical
28514442
GYS1_HUMANGYS1physical
28514442
GLYG_HUMANGYG1physical
28514442
SIR5_HUMANSIRT5physical
28514442
RAE1L_HUMANRAE1physical
28514442
MOT10_HUMANSLC16A10physical
28514442
WDR54_HUMANWDR54physical
28514442
OSTC_HUMANOSTCphysical
28514442
SCMC1_HUMANSLC25A24physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GLYG2_HUMAN

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Related Literatures of Post-Translational Modification
O-linked Glycosylation
ReferencePubMed
"Characterization of human glycogenin-2, a self-glucosylatinginitiator of liver glycogen metabolism.";
Mu J., Roach P.J.;
J. Biol. Chem. 273:34850-34856(1998).
Cited for: CHARACTERIZATION, AND GLYCOSYLATION AT TYR-228.

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