| UniProt ID | GYS2_HUMAN | |
|---|---|---|
| UniProt AC | P54840 | |
| Protein Name | Glycogen [starch] synthase, liver | |
| Gene Name | GYS2 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 703 | |
| Subcellular Localization | ||
| Protein Description | Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.. | |
| Protein Sequence | MLRGRSLSVTSLGGLPQWEVEELPVEELLLFEVAWEVTNKVGGIYTVIQTKAKTTADEWGENYFLIGPYFEHNMKTQVEQCEPVNDAVRRAVDAMNKHGCQVHFGRWLIEGSPYVVLFDIGYSAWNLDRWKGDLWEACSVGIPYHDREANDMLIFGSLTAWFLKEVTDHADGKYVVAQFHEWQAGIGLILSRARKLPIATIFTTHATLLGRYLCAANIDFYNHLDKFNIDKEAGERQIYHRYCMERASVHCAHVFTTVSEITAIEAEHMLKRKPDVVTPNGLNVKKFSAVHEFQNLHAMYKARIQDFVRGHFYGHLDFDLEKTLFLFIAGRYEFSNKGADIFLESLSRLNFLLRMHKSDITVMVFFIMPAKTNNFNVETLKGQAVRKQLWDVAHSVKEKFGKKLYDALLRGEIPDLNDILDRDDLTIMKRAIFSTQRQSLPPVTTHNMIDDSTDPILSTIRRIGLFNNRTDRVKVILHPEFLSSTSPLLPMDYEEFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSVTTNLSGFGCFMQEHVADPTAYGIYIVDRRFRSPDDSCNQLTKFLYGFCKQSRRQRIIQRNRTERLSDLLDWRYLGRYYQHARHLTLSRAFPDKFHVELTSPPTTEGFKYPRPSSVPPSPSGSQASSPQSSDVEDEVEDERYDEEEEAERDRLNIKSPFSLSHVPHGKKKLHGEYKN | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 6 | Phosphorylation | --MLRGRSLSVTSLG --CCCCCCCEEECCC | 28.02 | - | |
| 8 | Phosphorylation | MLRGRSLSVTSLGGL CCCCCCCEEECCCCC | 25.29 | 24275569 | |
| 10 | Phosphorylation | RGRSLSVTSLGGLPQ CCCCCEEECCCCCCC | 18.17 | 24275569 | |
| 11 | Phosphorylation | GRSLSVTSLGGLPQW CCCCEEECCCCCCCC | 23.90 | 24275569 | |
| 45 | Phosphorylation | TNKVGGIYTVIQTKA HHHCCCEEEEEEECC | 9.76 | 20090780 | |
| 46 | Phosphorylation | NKVGGIYTVIQTKAK HHCCCEEEEEEECCC | 14.82 | 20068231 | |
| 50 | Phosphorylation | GIYTVIQTKAKTTAD CEEEEEEECCCCCHH | 23.11 | 20068231 | |
| 203 | Phosphorylation | LPIATIFTTHATLLG CCCEEEECCHHHHHH | 17.52 | - | |
| 304 | Ubiquitination | HAMYKARIQDFVRGH HHHHHHHHHHHHHHH | 5.72 | 23000965 | |
| 310 | Ubiquitination | RIQDFVRGHFYGHLD HHHHHHHHHCCCCCC | 15.23 | 23000965 | |
| 371 | Acetylation | VFFIMPAKTNNFNVE EEEEEECCCCCCCHH | 46.01 | 10563019 | |
| 379 | Phosphorylation | TNNFNVETLKGQAVR CCCCCHHHHCCHHHH | 29.50 | 28857561 | |
| 381 | Ubiquitination | NFNVETLKGQAVRKQ CCCHHHHCCHHHHHH | 57.29 | 23000965 | |
| 387 | Acetylation | LKGQAVRKQLWDVAH HCCHHHHHHHHHHHH | 43.05 | 20167786 | |
| 387 | Ubiquitination | LKGQAVRKQLWDVAH HCCHHHHHHHHHHHH | 43.05 | 23000965 | |
| 397 | Acetylation | WDVAHSVKEKFGKKL HHHHHHHHHHHHHHH | 59.19 | 20167786 | |
| 405 | Phosphorylation | EKFGKKLYDALLRGE HHHHHHHHHHHHCCC | 14.19 | - | |
| 426 | Phosphorylation | ILDRDDLTIMKRAIF CCCHHHCHHHHHHHH | 26.48 | - | |
| 459 | Phosphorylation | STDPILSTIRRIGLF CCCHHHHHHHHHCCC | 18.30 | 20363803 | |
| 612 | Phosphorylation | YQHARHLTLSRAFPD HHHHHHHHHCCCCCC | 19.30 | 24719451 | |
| 626 | Phosphorylation | DKFHVELTSPPTTEG CCEEEEECCCCCCCC | 26.19 | 25072903 | |
| 627 | Phosphorylation | KFHVELTSPPTTEGF CEEEEECCCCCCCCC | 41.32 | 25072903 | |
| 630 | Phosphorylation | VELTSPPTTEGFKYP EEECCCCCCCCCCCC | 40.64 | 25072903 | |
| 631 | Phosphorylation | ELTSPPTTEGFKYPR EECCCCCCCCCCCCC | 39.63 | 25072903 | |
| 641 | Phosphorylation | FKYPRPSSVPPSPSG CCCCCCCCCCCCCCC | 41.13 | - | |
| 645 | Phosphorylation | RPSSVPPSPSGSQAS CCCCCCCCCCCCCCC | 26.15 | - | |
| 649 | Phosphorylation | VPPSPSGSQASSPQS CCCCCCCCCCCCCCC | 27.23 | - | |
| 653 | Phosphorylation | PSGSQASSPQSSDVE CCCCCCCCCCCCCCC | 29.94 | - | |
| 657 | Phosphorylation | QASSPQSSDVEDEVE CCCCCCCCCCCHHHH | 40.19 | - | |
| 683 | Phosphorylation | RDRLNIKSPFSLSHV HHHCCCCCCCCHHCC | 27.64 | 8203908 | |
| 686 | Phosphorylation | LNIKSPFSLSHVPHG CCCCCCCCHHCCCCC | 32.14 | 25072903 | |
| 688 | Phosphorylation | IKSPFSLSHVPHGKK CCCCCCHHCCCCCCC | 22.65 | 25072903 | |
| 694 | Acetylation | LSHVPHGKKKLHGEY HHCCCCCCCCCCCCC | 43.64 | - | |
| 695 | Acetylation | SHVPHGKKKLHGEYK HCCCCCCCCCCCCCC | 66.22 | - | |
| 696 | Acetylation | HVPHGKKKLHGEYKN CCCCCCCCCCCCCCC | 49.56 | - |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 8 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
| 641 | S | Phosphorylation | Kinase | GSK3-ALPHA | P49840 | Uniprot |
| 641 | S | Phosphorylation | Kinase | GSK3-BETA | P49841 | Uniprot |
| 645 | S | Phosphorylation | Kinase | GSK3-ALPHA | P49840 | Uniprot |
| 645 | S | Phosphorylation | Kinase | GSK3-BETA | P49841 | Uniprot |
| 649 | S | Phosphorylation | Kinase | GSK3-ALPHA | P49840 | Uniprot |
| 649 | S | Phosphorylation | Kinase | GSK3-BETA | P49841 | Uniprot |
| 653 | S | Phosphorylation | Kinase | GSK3-ALPHA | P49840 | Uniprot |
| 653 | S | Phosphorylation | Kinase | GSK3-BETA | P49841 | Uniprot |
| 657 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 8 | S | Phosphorylation |
| - |
| 8 | S | Phosphorylation |
| - |
| 641 | S | Phosphorylation |
| - |
| 641 | S | Phosphorylation |
| - |
| 641 | S | Phosphorylation |
| - |
| 645 | S | Phosphorylation |
| - |
| 645 | S | Phosphorylation |
| - |
| 649 | S | Phosphorylation |
| - |
| 653 | S | Phosphorylation |
| - |
| 657 | S | Phosphorylation |
| - |
* 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 GYS2_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| TNR1A_HUMAN | TNFRSF1A | physical | 21988832 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 240600 | Glycogen storage disease 0 (GSD0) | |||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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