| UniProt ID | HMDH2_YEAST | |
|---|---|---|
| UniProt AC | P12684 | |
| Protein Name | 3-hydroxy-3-methylglutaryl-coenzyme A reductase 2 | |
| Gene Name | HMG2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1045 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein. Nucleus envelope. |
|
| Protein Description | One of 2 isozymes that catalyze the conversion of HMG-CoA to mevalonate. It is the rate-limiting enzyme of the sterol biosynthesis pathway. Involved in ergosterol biosynthesis.. | |
| Protein Sequence | MSLPLKTIVHLVKPFACTARFSARYPIHVIVVAVLLSAAAYLSVTQSYLNEWKLDSNQYSTYLSIKPDELFEKCTHYYRSPVSDTWKLLSSKEAADIYTPFHYYLSTISFQSKDNSTTLPSLDDVIYSVDHTRYLLSEEPKIPTELVSENGTKWRLRNNSNFILDLHNIYRNMVKQFSNKTSEFDQFDLFIILAAYLTLFYTLCCLFNDMRKIGSKFWLSFSALSNSACALYLSLYTTHSLLKKPASLLSLVIGLPFIVVIIGFKHKVRLAAFSLQKFHRISIDKKITVSNIIYEAMFQEGAYLIRDYLFYISSFIGCAIYARHLPGLVNFCILSTFMLVFDLLLSATFYSAILSMKLEINIIHRSTVIRQTLEEDGVVPTTADIIYKDETASEPHFLRSNVAIILGKASVIGLLLLINLYVFTDKLNATILNTVYFDSTIYSLPNFINYKDIGNLSNQVIISVLPKQYYTPLKKYHQIEDSVLLIIDSVSNAIRDQFISKLLFFAFAVSISINVYLLNAAKIHTGYMNFQPQSNKIDDLVVQQKSATIEFSETRSMPASSGLETPVTAKDIIISEEIQNNECVYALSSQDEPIRPLSNLVELMEKEQLKNMNNTEVSNLVVNGKLPLYSLEKKLEDTTRAVLVRRKALSTLAESPILVSEKLPFRNYDYDRVFGACCENVIGYMPIPVGVIGPLIIDGTSYHIPMATTEGCLVASAMRGCKAINAGGGATTVLTKDGMTRGPVVRFPTLIRSGACKIWLDSEEGQNSIKKAFNSTSRFARLQHIQTCLAGDLLFMRFRTTTGDAMGMNMISKGVEYSLKQMVEEYGWEDMEVVSVSGNYCTDKKPAAINWIEGRGKSVVAEATIPGDVVKSVLKSDVSALVELNISKNLVGSAMAGSVGGFNAHAANLVTALFLALGQDPAQNVESSNCITLMKEVDGDLRISVSMPSIEVGTIGGGTVLEPQGAMLDLLGVRGPHPTEPGANARQLARIIACAVLAGELSLCSALAAGHLVQSHMTHNRKTNKANELPQPSNKGPPCKTSALL | |
| 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 |
|---|---|---|---|---|---|
| 13 | Acetylation | KTIVHLVKPFACTAR HHHHHHHHCCCCCHH | 40.55 | 24489116 | |
| 98 | Phosphorylation | SKEAADIYTPFHYYL CHHHHHCCCCCHHHH | 14.65 | 23749301 | |
| 99 | Phosphorylation | KEAADIYTPFHYYLS HHHHHCCCCCHHHHE | 21.58 | 23749301 | |
| 103 | Phosphorylation | DIYTPFHYYLSTISF HCCCCCHHHHEEEEE | 13.38 | 23749301 | |
| 112 | Phosphorylation | LSTISFQSKDNSTTL HEEEEEECCCCCCCC | 39.71 | 23749301 | |
| 115 | N-linked_Glycosylation | ISFQSKDNSTTLPSL EEEECCCCCCCCCCH | 45.02 | - | |
| 150 | N-linked_Glycosylation | PTELVSENGTKWRLR CHHHCCCCCCEEEEC | 56.80 | - | |
| 158 | N-linked_Glycosylation | GTKWRLRNNSNFILD CCEEEECCCCCCEEE | 61.96 | - | |
| 179 | N-linked_Glycosylation | NMVKQFSNKTSEFDQ HHHHHHCCCCCCCCH | 53.57 | - | |
| 277 | Acetylation | LAAFSLQKFHRISID HHHHHHCCHHCCCCC | 48.72 | 24489116 | |
| 428 | N-linked_Glycosylation | YVFTDKLNATILNTV HHHHHCCCCEECCCC | 40.55 | - | |
| 455 | N-linked_Glycosylation | INYKDIGNLSNQVII CCHHHHHCCCCCCCE | 40.40 | - | |
| 546 | Phosphorylation | DLVVQQKSATIEFSE CEEEECCCCEEEEEC | 26.72 | 27214570 | |
| 548 | Phosphorylation | VVQQKSATIEFSETR EEECCCCEEEEECCC | 28.29 | 20377248 | |
| 556 | Phosphorylation | IEFSETRSMPASSGL EEEECCCCCCCCCCC | 36.22 | 23749301 | |
| 560 | Phosphorylation | ETRSMPASSGLETPV CCCCCCCCCCCCCCC | 21.04 | 27214570 | |
| 561 | Phosphorylation | TRSMPASSGLETPVT CCCCCCCCCCCCCCC | 49.88 | 29688323 | |
| 565 | Phosphorylation | PASSGLETPVTAKDI CCCCCCCCCCCHHHE | 28.27 | 17330950 | |
| 568 | Phosphorylation | SGLETPVTAKDIIIS CCCCCCCCHHHEEEE | 29.23 | 27214570 | |
| 633 | Acetylation | LPLYSLEKKLEDTTR CCCEECHHHHCCCCH | 68.87 | 22865919 | |
| 647 | Acetylation | RAVLVRRKALSTLAE HHHHHHHHHHHHHHC | 43.02 | 24489116 | |
| 650 | Phosphorylation | LVRRKALSTLAESPI HHHHHHHHHHHCCCE | 26.66 | 21126336 | |
| 655 | Phosphorylation | ALSTLAESPILVSEK HHHHHHCCCEEECCC | 16.19 | 21440633 | |
| 662 | Acetylation | SPILVSEKLPFRNYD CCEEECCCCCCCCCC | 54.69 | 24489116 | |
| 662 | Ubiquitination | SPILVSEKLPFRNYD CCEEECCCCCCCCCC | 54.69 | 24961812 | |
| 722 | Ubiquitination | ASAMRGCKAINAGGG HHHHHCCCEEECCCC | 55.94 | 23749301 | |
| 736 | Ubiquitination | GATTVLTKDGMTRGP CCEEEECCCCCCCCC | 48.39 | 24961812 | |
| 749 | Phosphorylation | GPVVRFPTLIRSGAC CCEEECCCHHCCCCC | 31.91 | 27017623 | |
| 844 | Ubiquitination | SGNYCTDKKPAAINW ECCCCCCCCCCCEEE | 42.37 | 17644757 | |
| 845 | Ubiquitination | GNYCTDKKPAAINWI CCCCCCCCCCCEEEE | 42.57 | 17644757 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HMDH2_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 HMDH2_YEAST !! | ||||||
| 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 THR-548; THR-565; THR-568AND SER-655, AND MASS SPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-565, AND MASSSPECTROMETRY. | |