UniProt ID | GLG1_YEAST | |
---|---|---|
UniProt AC | P36143 | |
Protein Name | Glycogenin-1 | |
Gene Name | GLG1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 616 | |
Subcellular Localization | ||
Protein Description | Self-glucosylating initiator of glycogen synthesis. Catalyzes the formation of a short alpha (1,4)-glucosyl chain covalently attached via a glucose 1-O-tyrosyl linkage to internal tyrosine residues. These chains act as primers for the elongation reaction catalyzed by glycogen synthase. Capable of transferring glucosyl residues to unbound acceptors such as free oligoglucans or oligoglucan derivatives.. | |
Protein Sequence | MYKKLAIATLLYSADYLPGVFALGHQVNKLLEEAGKKGDIETCLIVTTSLFNGTLSELAKNILQSIYTKIVLVEPLNCQEESIQKNSENLALLERPELSFALIKARLWELTQFEQVLYLDSDTLPLNKEFLKLFDIMSKQTTSQVGAIADIGWPDMFNSGVMMLIPDADTASVLQNYIFENTSIDGSDQGILNQFFNQNCCTDELVKDSFSREWVQLSFTYNVTIPNLGYQSSPAMNYFKPSIKLIHFIGKHKPWSLWSQKNFIKNEYHDQWNEVYEEFKEEHQLNNEVSKPKISDSDKTETPETITPVDAPPSNEPTTNQEIDTISTVEENVDNQNAEPVPNSDHSPAPNPVPLDFTKWLTTFINKDHLTNQPVNESREYSKENDNNIINSSSNRDQESPPNSTQELNSSYSVVSTQADSDEHQNAEEEDSTTDNASNSGEESHLDDISTAASSNNNVSNQPDGKNFSNSKENNISVESSPSNPEQKRSTDNIQKPSVSTNDLPDDVEPHTSVDDNIQYLEKDKEGYEEFLPDVYESNAIDNEEEFFDDDARDATEGETKTSAVADKQEDMKLTAEETNQPQQEMPNFKFDWEDSDYLSKVERCFPDDIFEYAVE | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
230 | O-linked_Glycosylation | VTIPNLGYQSSPAMN EECCCCCCCCCCHHH | 14.37 | - | |
477 | Phosphorylation | NSKENNISVESSPSN CCCCCCEECCCCCCC | 23.19 | 22369663 | |
480 | Phosphorylation | ENNISVESSPSNPEQ CCCEECCCCCCCHHH | 45.45 | 22369663 | |
481 | Phosphorylation | NNISVESSPSNPEQK CCEECCCCCCCHHHH | 20.88 | 22369663 | |
483 | Phosphorylation | ISVESSPSNPEQKRS EECCCCCCCHHHHCC | 67.95 | 22369663 | |
512 | Phosphorylation | PDDVEPHTSVDDNIQ CCCCCCCCCHHHHHH | 40.95 | 28889911 | |
513 | Phosphorylation | DDVEPHTSVDDNIQY CCCCCCCCHHHHHHH | 22.10 | 21440633 | |
596 | Phosphorylation | FKFDWEDSDYLSKVE CCCCCCCCHHHHHHH | 19.35 | 28889911 | |
598 | O-linked_Glycosylation | FDWEDSDYLSKVERC CCCCCCHHHHHHHHH | 19.48 | - |
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 GLG1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GLG1_YEAST !! |
* 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 GLG1_YEAST !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
GLG2_YEAST | GLG2 | genetic | 8524228 | |
GYS2_YEAST | GSY2 | physical | 18467557 | |
GDE1_YEAST | GDE1 | genetic | 21623372 | |
QCR7_YEAST | QCR7 | genetic | 21623372 | |
QCR10_YEAST | QCR10 | genetic | 21623372 | |
PHSG_YEAST | GPH1 | genetic | 21623372 | |
DDP1_YEAST | DDP1 | genetic | 21623372 | |
VRP1_YEAST | VRP1 | genetic | 27708008 | |
RL19A_YEAST | RPL19B | genetic | 27708008 | |
RL19B_YEAST | RPL19B | genetic | 27708008 | |
RS8A_YEAST | RPS8A | genetic | 27708008 | |
RS8B_YEAST | RPS8A | genetic | 27708008 | |
ADPP_YEAST | YSA1 | genetic | 27708008 | |
YCZ2_YEAST | YCR102C | genetic | 27708008 | |
BDF2_YEAST | BDF2 | genetic | 27708008 | |
GNTK_YEAST | YDR248C | genetic | 27708008 | |
GGA1_YEAST | GGA1 | genetic | 27708008 | |
DOT1_YEAST | DOT1 | genetic | 27708008 | |
VPS53_YEAST | VPS53 | genetic | 27708008 | |
YJQ3_YEAST | YJL163C | genetic | 27708008 | |
TLG2_YEAST | TLG2 | genetic | 27708008 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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