| UniProt ID | GET2_YEAST | |
|---|---|---|
| UniProt AC | P40056 | |
| Protein Name | Golgi to ER traffic protein 2 {ECO:0000255|HAMAP-Rule:MF_03114} | |
| Gene Name | GET2 {ECO:0000255|HAMAP-Rule:MF_03114} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 285 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein. Golgi apparatus membrane Multi-pass membrane protein. |
|
| Protein Description | Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Together with GET1, acts as a membrane receptor for soluble GET3, which recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. The GET complex cooperates with the HDEL receptor ERD2 to mediate the ATP-dependent retrieval of resident ER proteins that contain a C-terminal H-D-E-L retention signal from the Golgi to the ER. Involved in DNA replication and DNA damage response and also in cell wall function.. | |
| Protein Sequence | MSELTEAEKRRLLRERRQKKFSNGGASSRLNKITGQASSHLNAESPLDAPSAAKTTPPASVHSATPDIKEDSNVAPQLDLLKQLAAMQGQGTGKSTPQDSSTPDLLSLLSSMNTGMPSAEGTPSFGQAAPAAPINQAALDYHDYLLNRLKAWTILVKWVFFLLPYLYLITRPNSSVWPAYAFTQSAWFAPLRNPSNFTRIFATFEFLSISIYYQLLKNVEHKSKIKNLQDTNKLVKLVSLVPEGVIPVANLKGKLITLLQYWDLLSMLITDISFVLIVLGLLTYL | |
| 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 | ------MSELTEAEK ------CCHHCHHHH | 41.11 | 22814378 | |
| 20 | Acetylation | LRERRQKKFSNGGAS HHHHHHHHHCCCCHH | 45.76 | 25381059 | |
| 22 | Phosphorylation | ERRQKKFSNGGASSR HHHHHHHCCCCHHHH | 43.37 | 21440633 | |
| 27 | Phosphorylation | KFSNGGASSRLNKIT HHCCCCHHHHHHHHH | 21.18 | 21551504 | |
| 28 | Phosphorylation | FSNGGASSRLNKITG HCCCCHHHHHHHHHC | 40.01 | 19823750 | |
| 34 | Phosphorylation | SSRLNKITGQASSHL HHHHHHHHCCCCHHC | 25.50 | 19823750 | |
| 38 | Phosphorylation | NKITGQASSHLNAES HHHHCCCCHHCCCCC | 15.48 | 19823750 | |
| 39 | Phosphorylation | KITGQASSHLNAESP HHHCCCCHHCCCCCC | 34.70 | 21551504 | |
| 45 | Phosphorylation | SSHLNAESPLDAPSA CHHCCCCCCCCCCCH | 28.49 | 17330950 | |
| 51 | Phosphorylation | ESPLDAPSAAKTTPP CCCCCCCCHHCCCCC | 42.45 | 21440633 | |
| 55 | Phosphorylation | DAPSAAKTTPPASVH CCCCHHCCCCCCCCC | 39.55 | 22369663 | |
| 56 | Phosphorylation | APSAAKTTPPASVHS CCCHHCCCCCCCCCC | 26.94 | 22369663 | |
| 60 | Phosphorylation | AKTTPPASVHSATPD HCCCCCCCCCCCCCC | 26.57 | 22369663 | |
| 63 | Phosphorylation | TPPASVHSATPDIKE CCCCCCCCCCCCCCC | 31.51 | 22369663 | |
| 65 | Phosphorylation | PASVHSATPDIKEDS CCCCCCCCCCCCCCC | 25.22 | 20377248 | |
| 69 | Acetylation | HSATPDIKEDSNVAP CCCCCCCCCCCCCHH | 63.95 | 24489116 | |
| 72 | Phosphorylation | TPDIKEDSNVAPQLD CCCCCCCCCCHHHHH | 34.00 | 22369663 | |
| 82 | Acetylation | APQLDLLKQLAAMQG HHHHHHHHHHHHHCC | 51.03 | 24489116 | |
| 92 | Phosphorylation | AAMQGQGTGKSTPQD HHHCCCCCCCCCCCC | 33.28 | 28889911 | |
| 173 | N-linked_Glycosylation | LYLITRPNSSVWPAY HHHHHCCCCCCCCCE | 43.56 | - | |
| 196 | N-linked_Glycosylation | APLRNPSNFTRIFAT CCCCCCCCCHHHHHH | 43.49 | - | |
| 226 | Ubiquitination | VEHKSKIKNLQDTNK CCCHHHCCCHHHHHH | 56.17 | 23749301 |
| 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 GET2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GET2_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 GET2_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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 SER-45, AND MASSSPECTROMETRY. | |
| "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-56, AND MASSSPECTROMETRY. | |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-56, AND MASSSPECTROMETRY. | |
