| UniProt ID | RER1_HUMAN | |
|---|---|---|
| UniProt AC | O15258 | |
| Protein Name | Protein RER1 | |
| Gene Name | RER1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 196 | |
| Subcellular Localization |
Golgi apparatus membrane Multi-pass membrane protein. |
|
| Protein Description | Involved in the retrieval of endoplasmic reticulum membrane proteins from the early Golgi compartment.. | |
| Protein Sequence | MSEGDSVGESVHGKPSVVYRFFTRLGQIYQSWLDKSTPYTAVRWVVTLGLSFVYMIRVYLLQGWYIVTYALGIYHLNLFIAFLSPKVDPSLMEDSDDGPSLPTKQNEEFRPFIRRLPEFKFWHAATKGILVAMVCTFFDAFNVPVFWPILVMYFIMLFCITMKRQIKHMIKYRYIPFTHGKRRYRGKEDAGKAFAS | |
| 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 | Phosphorylation | ------MSEGDSVGE ------CCCCCCCCC | 50.73 | 29255136 | |
| 2 | Acetylation | ------MSEGDSVGE ------CCCCCCCCC | 50.73 | 20068231 | |
| 6 | Phosphorylation | --MSEGDSVGESVHG --CCCCCCCCCCCCC | 42.76 | 22167270 | |
| 10 | Phosphorylation | EGDSVGESVHGKPSV CCCCCCCCCCCCHHH | 17.31 | 22167270 | |
| 14 | Malonylation | VGESVHGKPSVVYRF CCCCCCCCHHHHHHH | 21.17 | 26320211 | |
| 14 | Ubiquitination | VGESVHGKPSVVYRF CCCCCCCCHHHHHHH | 21.17 | 21890473 | |
| 16 | Phosphorylation | ESVHGKPSVVYRFFT CCCCCCHHHHHHHHH | 27.92 | 29396449 | |
| 19 | Phosphorylation | HGKPSVVYRFFTRLG CCCHHHHHHHHHHHH | 10.27 | 29396449 | |
| 35 | Ubiquitination | IYQSWLDKSTPYTAV HHHHHHCCCCCCHHH | 54.80 | 21906983 | |
| 54 | Phosphorylation | TLGLSFVYMIRVYLL HHHHHHHHHHHHHHH | 5.70 | - | |
| 59 | Phosphorylation | FVYMIRVYLLQGWYI HHHHHHHHHHCHHHH | 7.58 | - | |
| 84 | Phosphorylation | NLFIAFLSPKVDPSL HHHHHHHCCCCCHHH | 19.07 | - | |
| 90 | Phosphorylation | LSPKVDPSLMEDSDD HCCCCCHHHCCCCCC | 35.57 | 30266825 | |
| 92 | Sulfoxidation | PKVDPSLMEDSDDGP CCCCHHHCCCCCCCC | 6.71 | 21406390 | |
| 95 | Phosphorylation | DPSLMEDSDDGPSLP CHHHCCCCCCCCCCC | 25.05 | 29255136 | |
| 100 | Phosphorylation | EDSDDGPSLPTKQNE CCCCCCCCCCCCCCH | 53.13 | 30266825 | |
| 103 | Phosphorylation | DDGPSLPTKQNEEFR CCCCCCCCCCCHHCH | 51.02 | 23927012 | |
| 171 | Ubiquitination | RQIKHMIKYRYIPFT HHHHHHHHHCCCCCC | 18.99 | - | |
| 174 | Phosphorylation | KHMIKYRYIPFTHGK HHHHHHCCCCCCCCC | 15.17 | 28152594 | |
| 181 | Ubiquitination | YIPFTHGKRRYRGKE CCCCCCCCCCCCCCC | 26.54 | 21890473 | |
| 192 | Ubiquitination | RGKEDAGKAFAS--- CCCCCCHHHCCC--- | 41.89 | - |
| 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 RER1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RER1_HUMAN !! | ||||||
* 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 RER1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| MIC60_HUMAN | IMMT | physical | 16169070 | |
| HAP1_HUMAN | HAP1 | physical | 16169070 | |
| SH3G3_HUMAN | SH3GL3 | physical | 16169070 | |
| PMP22_HUMAN | PMP22 | physical | 25385046 | |
| STX12_HUMAN | STX12 | physical | 26344197 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND MASSSPECTROMETRY. | |
| "Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND MASSSPECTROMETRY. | |
| "A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND MASSSPECTROMETRY. | |
| "Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-95, AND MASSSPECTROMETRY. | |