| UniProt ID | HXKG_YEAST | |
|---|---|---|
| UniProt AC | P17709 | |
| Protein Name | Glucokinase-1 | |
| Gene Name | GLK1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 500 | |
| Subcellular Localization | ||
| Protein Description | Two isoenzymes, hexokinase-1 and hexokinase-2, can phosphorylate keto- and aldohexoses in yeast, whereas a third isoenzyme, GLK, is specific for aldohexoses. All glucose phosphorylating enzymes are involved in glucose uptake.. | |
| Protein Sequence | MSFDDLHKATERAVIQAVDQICDDFEVTPEKLDELTAYFIEQMEKGLAPPKEGHTLASDKGLPMIPAFVTGSPNGTERGVLLAADLGGTNFRICSVNLHGDHTFSMEQMKSKIPDDLLDDENVTSDDLFGFLARRTLAFMKKYHPDELAKGKDAKPMKLGFTFSYPVDQTSLNSGTLIRWTKGFRIADTVGKDVVQLYQEQLSAQGMPMIKVVALTNDTVGTYLSHCYTSDNTDSMTSGEISEPVIGCIFGTGTNGCYMEEINKITKLPQELRDKLIKEGKTHMIINVEWGSFDNELKHLPTTKYDVVIDQKLSTNPGFHLFEKRVSGMFLGEVLRNILVDLHSQGLLLQQYRSKEQLPRHLTTPFQLSSEVLSHIEIDDSTGLRETELSLLQSLRLPTTPTERVQIQKLVRAISRRSAYLAAVPLAAILIKTNALNKRYHGEVEIGCDGSVVEYYPGFRSMLRHALALSPLGAEGERKVHLKIAKDGSGVGAALCALVA | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MSFDDLHKA ------CCHHHHHHH | 37.07 | 22814378 | |
| 2 | Phosphorylation | ------MSFDDLHKA ------CCHHHHHHH | 37.07 | 22369663 | |
| 8 | Acetylation | MSFDDLHKATERAVI CCHHHHHHHHHHHHH | 65.39 | 24489116 | |
| 60 | Acetylation | GHTLASDKGLPMIPA CCCCCCCCCCCCCCE | 60.91 | 24489116 | |
| 72 | Phosphorylation | IPAFVTGSPNGTERG CCEEEECCCCCCCEE | 13.06 | 30377154 | |
| 76 | Phosphorylation | VTGSPNGTERGVLLA EECCCCCCCEEEEEE | 29.20 | 30377154 | |
| 110 | Acetylation | TFSMEQMKSKIPDDL CCCHHHHHHCCCHHH | 48.57 | 24489116 | |
| 142 | Acetylation | RTLAFMKKYHPDELA HHHHHHHHHCHHHHH | 36.68 | 25381059 | |
| 150 | Acetylation | YHPDELAKGKDAKPM HCHHHHHCCCCCCCC | 78.20 | 22865919 | |
| 174 | Phosphorylation | VDQTSLNSGTLIRWT CCCCCCCCCCEEEEC | 38.15 | 28889911 | |
| 182 | 2-Hydroxyisobutyrylation | GTLIRWTKGFRIADT CCEEEECCCEEEECC | 49.44 | - | |
| 266 | Phosphorylation | MEEINKITKLPQELR HHHHHHHHCCCHHHH | 28.30 | 22369663 | |
| 267 | Acetylation | EEINKITKLPQELRD HHHHHHHCCCHHHHH | 62.74 | 22865919 | |
| 267 | Succinylation | EEINKITKLPQELRD HHHHHHHCCCHHHHH | 62.74 | 23954790 | |
| 278 | 2-Hydroxyisobutyrylation | ELRDKLIKEGKTHMI HHHHHHHHCCCCEEE | 71.50 | - | |
| 304 | Acetylation | LKHLPTTKYDVVIDQ HCCCCCCCEEEEECC | 41.76 | 22865919 | |
| 304 | 2-Hydroxyisobutyrylation | LKHLPTTKYDVVIDQ HCCCCCCCEEEEECC | 41.76 | - | |
| 312 | Acetylation | YDVVIDQKLSTNPGF EEEEECCCCCCCCCC | 40.43 | 24489116 | |
| 315 | Phosphorylation | VIDQKLSTNPGFHLF EECCCCCCCCCCCCE | 56.73 | 27017623 | |
| 324 | 2-Hydroxyisobutyrylation | PGFHLFEKRVSGMFL CCCCCEEHHHHCHHH | 51.25 | - | |
| 324 | Acetylation | PGFHLFEKRVSGMFL CCCCCEEHHHHCHHH | 51.25 | 24489116 | |
| 327 | Phosphorylation | HLFEKRVSGMFLGEV CCEEHHHHCHHHHHH | 28.68 | 22369663 | |
| 355 | 2-Hydroxyisobutyrylation | LLQQYRSKEQLPRHL HHHHHCCHHHCCHHC | 40.24 | - | |
| 355 | Ubiquitination | LLQQYRSKEQLPRHL HHHHHCCHHHCCHHC | 40.24 | 23749301 | |
| 409 | Acetylation | TERVQIQKLVRAISR CHHHHHHHHHHHHHH | 51.05 | 25381059 | |
| 418 | Phosphorylation | VRAISRRSAYLAAVP HHHHHHHHHHHHHHH | 21.83 | 30377154 | |
| 438 | 2-Hydroxyisobutyrylation | IKTNALNKRYHGEVE HHHCCCCCCCCCEEE | 56.00 | - | |
| 470 | Phosphorylation | LRHALALSPLGAEGE HHHHHHHCCCCCCCC | 16.69 | 25752575 | |
| 483 | 2-Hydroxyisobutyrylation | GERKVHLKIAKDGSG CCEEEEEEECCCCCC | 26.24 | - | |
| 489 | Phosphorylation | LKIAKDGSGVGAALC EEECCCCCCHHHHHH | 40.20 | 30377154 |
| 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 HXKG_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HXKG_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 HXKG_YEAST !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| ARGR2_YEAST | ARG81 | physical | 10688190 | |
| FIG1_YEAST | FIG1 | physical | 10688190 | |
| HXKA_YEAST | HXK1 | genetic | 10217505 | |
| HXKB_YEAST | HXK2 | genetic | 10217505 | |
| HXKG_YEAST | GLK1 | physical | 11283351 | |
| HXKA_YEAST | HXK1 | genetic | 16941010 | |
| HXKB_YEAST | HXK2 | genetic | 16941010 | |
| GGPPS_YEAST | BTS1 | genetic | 21623372 | |
| ELO3_YEAST | ELO3 | genetic | 21623372 | |
| CALM_YEAST | CMD1 | genetic | 27708008 | |
| MPS1_YEAST | MPS1 | genetic | 27708008 | |
| PRP9_YEAST | PRP9 | genetic | 27708008 | |
| SNU23_YEAST | SNU23 | genetic | 27708008 | |
| CDC48_YEAST | CDC48 | genetic | 27708008 | |
| DAD1_YEAST | DAD1 | genetic | 27708008 | |
| RRP1_YEAST | RRP1 | genetic | 27708008 | |
| NBP35_YEAST | NBP35 | genetic | 27708008 | |
| PRP43_YEAST | PRP43 | genetic | 27708008 | |
| BRL1_YEAST | BRL1 | genetic | 27708008 | |
| KRE9_YEAST | KRE9 | genetic | 27708008 | |
| YJ9I_YEAST | YJR141W | genetic | 27708008 | |
| NMT_YEAST | NMT1 | genetic | 27708008 | |
| NAB3_YEAST | NAB3 | genetic | 27708008 | |
| IF6_YEAST | TIF6 | genetic | 27708008 | |
| KEAP1_HUMAN | KEAP1 | physical | 27107014 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-174 AND SER-470,AND MASS SPECTROMETRY. | |