| UniProt ID | EMC2_HUMAN | |
|---|---|---|
| UniProt AC | Q15006 | |
| Protein Name | ER membrane protein complex subunit 2 | |
| Gene Name | EMC2 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 297 | |
| Subcellular Localization | Nucleus. Cytoplasm . | |
| Protein Description | ||
| Protein Sequence | MAKVSELYDVTWEEMRDKMRKWREENSRNSEQIVEVGEELINEYASKLGDDIWIIYEQVMIAALDYGRDDLALFCLQELRRQFPGSHRVKRLTGMRFEAMERYDDAIQLYDRILQEDPTNTAARKRKIAIRKAQGKNVEAIRELNEYLEQFVGDQEAWHELAELYINEHDYAKAAFCLEELMMTNPHNHLYCQQYAEVKYTQGGLENLELSRKYFAQALKLNNRNMRALFGLYMSASHIASNPKASAKTKKDNMKYASWAASQINRAYQFAGRSKKETKYSLKAVEDMLETLQITQS | |
| 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 | ------MAKVSELYD ------CCCHHHHCC | 22.43 | 22814378 | |
| 5 | Phosphorylation | ---MAKVSELYDVTW ---CCCHHHHCCCCH | 22.60 | 26074081 | |
| 8 | Phosphorylation | MAKVSELYDVTWEEM CCCHHHHCCCCHHHH | 12.33 | 26074081 | |
| 11 | Phosphorylation | VSELYDVTWEEMRDK HHHHCCCCHHHHHHH | 25.02 | 26074081 | |
| 103 | Phosphorylation | RFEAMERYDDAIQLY CHHHHHHHHHHHHHH | 12.60 | 20068231 | |
| 110 | Phosphorylation | YDDAIQLYDRILQED HHHHHHHHHHHHHHC | 6.18 | 29978859 | |
| 112 | Methylation | DAIQLYDRILQEDPT HHHHHHHHHHHHCCC | 20.26 | 115919093 | |
| 119 | Phosphorylation | RILQEDPTNTAARKR HHHHHCCCCHHHHHH | 58.48 | 29255136 | |
| 121 | Phosphorylation | LQEDPTNTAARKRKI HHHCCCCHHHHHHHH | 24.95 | 25849741 | |
| 132 | Ubiquitination | KRKIAIRKAQGKNVE HHHHHHHHHCCCCHH | 38.66 | 24816145 | |
| 133 | Ubiquitination | RKIAIRKAQGKNVEA HHHHHHHHCCCCHHH | 17.32 | 24816145 | |
| 136 | Acetylation | AIRKAQGKNVEAIRE HHHHHCCCCHHHHHH | 45.82 | 26051181 | |
| 136 | Ubiquitination | AIRKAQGKNVEAIRE HHHHHCCCCHHHHHH | 45.82 | 29967540 | |
| 137 | Ubiquitination | IRKAQGKNVEAIREL HHHHCCCCHHHHHHH | 43.62 | 29967540 | |
| 141 | Ubiquitination | QGKNVEAIRELNEYL CCCCHHHHHHHHHHH | 1.91 | 24816145 | |
| 145 | Ubiquitination | VEAIRELNEYLEQFV HHHHHHHHHHHHHHH | 30.98 | 29967540 | |
| 201 | Phosphorylation | QYAEVKYTQGGLENL HCCEEEECCCCHHHH | 18.28 | 30387612 | |
| 211 | Phosphorylation | GLENLELSRKYFAQA CHHHHHHHHHHHHHH | 19.83 | 30387612 | |
| 213 | Acetylation | ENLELSRKYFAQALK HHHHHHHHHHHHHHH | 41.15 | 27452117 | |
| 220 | Ubiquitination | KYFAQALKLNNRNMR HHHHHHHHHCCHHHH | 52.78 | 21890473 | |
| 221 | Ubiquitination | YFAQALKLNNRNMRA HHHHHHHHCCHHHHH | 7.75 | 21890473 | |
| 229 | Ubiquitination | NNRNMRALFGLYMSA CCHHHHHHHHHHHCH | 2.17 | 21890473 | |
| 235 | Phosphorylation | ALFGLYMSASHIASN HHHHHHHCHHHHHHC | 17.05 | 24719451 | |
| 241 | Phosphorylation | MSASHIASNPKASAK HCHHHHHHCCCCCCC | 53.73 | 24719451 | |
| 250 | Ubiquitination | PKASAKTKKDNMKYA CCCCCCCCHHHHHHH | 58.38 | 22817900 | |
| 251 | Ubiquitination | KASAKTKKDNMKYAS CCCCCCCHHHHHHHH | 60.61 | 22817900 | |
| 252 | Ubiquitination | ASAKTKKDNMKYASW CCCCCCHHHHHHHHH | 63.11 | 22817900 | |
| 255 | Acetylation | KTKKDNMKYASWAAS CCCHHHHHHHHHHHH | 43.87 | 19608861 | |
| 255 | Ubiquitination | KTKKDNMKYASWAAS CCCHHHHHHHHHHHH | 43.87 | 22817900 | |
| 256 | Phosphorylation | TKKDNMKYASWAASQ CCHHHHHHHHHHHHH | 8.63 | 30257219 | |
| 256 | Ubiquitination | TKKDNMKYASWAASQ CCHHHHHHHHHHHHH | 8.63 | 21890473 | |
| 258 | Phosphorylation | KDNMKYASWAASQIN HHHHHHHHHHHHHHH | 17.73 | 20639409 | |
| 259 | Ubiquitination | DNMKYASWAASQINR HHHHHHHHHHHHHHH | 6.41 | 22817900 | |
| 260 | Ubiquitination | NMKYASWAASQINRA HHHHHHHHHHHHHHH | 8.50 | 22817900 | |
| 264 | Ubiquitination | ASWAASQINRAYQFA HHHHHHHHHHHHHHC | 3.31 | 21890473 | |
| 276 | Acetylation | QFAGRSKKETKYSLK HHCCCCCCCCHHHHH | 72.38 | 7298959 | |
| 279 | Acetylation | GRSKKETKYSLKAVE CCCCCCCHHHHHHHH | 33.65 | 7298969 | |
| 281 | Phosphorylation | SKKETKYSLKAVEDM CCCCCHHHHHHHHHH | 25.58 | 24719451 | |
| 283 | Acetylation | KETKYSLKAVEDMLE CCCHHHHHHHHHHHH | 44.43 | 7298979 | |
| 297 | Phosphorylation | ETLQITQS------- HHHHHHCC------- | 33.27 | 27251275 |
| 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 EMC2_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EMC2_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 EMC2_HUMAN !! | ||||||
| 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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| Acetylation | |
| Reference | PubMed |
| "Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-255, AND MASS SPECTROMETRY. | |
