| UniProt ID | EIPR1_HUMAN | |
|---|---|---|
| UniProt AC | Q53HC9 | |
| Protein Name | EARP-interacting protein {ECO:0000250|UniProtKB:Q5PPK9} | |
| Gene Name | EIPR1 {ECO:0000312|HGNC:HGNC:12383} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 387 | |
| Subcellular Localization | ||
| Protein Description | ||
| Protein Sequence | MEDDAPVIYGLEFQARALTPQTAETDAIRFLVGTQSLKYDNQIHIIDFDDENNIINKNVLLHQAGEIWHISASPADRGVLTTCYNRTSDSKVLTCAAVWRMPKELESGSHESPDDSSSTAQTLELLCHLDNTAHGNMACVVWEPMGDGKKIISLADNHILLWDLQESSSQAVLASSASLEGKGQLKFTSGRWSPHHNCTQVATANDTTLRGWDTRSMSQIYCIENAHGQLVRDLDFNPNKQYYLASCGDDCKVKFWDTRNVTEPVKTLEEHSHWVWNVRYNHSHDQLVLTGSSDSRVILSNMVSISSEPFGHLVDDDDISDQEDHRSEEKSKEPLQDNVIATYEEHEDSVYAVDWSSADPWLFASLSYDGRLVINRVPRALKYHILL | |
| 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 |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MEDDAPVI -------CCCCCCEE | 22814378 | ||
| 19 | Phosphorylation | EFQARALTPQTAETD EEEEEECCCCCCCCH | 25867546 | ||
| 22 | Phosphorylation | ARALTPQTAETDAIR EEECCCCCCCCHHHH | 25867546 | ||
| 25 | Phosphorylation | LTPQTAETDAIRFLV CCCCCCCCHHHHHHC | 25867546 | ||
| 34 | Phosphorylation | AIRFLVGTQSLKYDN HHHHHCCCCCCCCCC | - | ||
| 57 | Ubiquitination | DENNIINKNVLLHQA CCCCEECCCEEEEEC | - | ||
| 91 | Ubiquitination | YNRTSDSKVLTCAAV ECCCCCCCEEEHHEE | 21906983 | ||
| 94 | Phosphorylation | TSDSKVLTCAAVWRM CCCCCEEEHHEEEEC | - | ||
| 186 | Ubiquitination | LEGKGQLKFTSGRWS CCCCCEEEECCCCCC | - | ||
| 193 | Phosphorylation | KFTSGRWSPHHNCTQ EECCCCCCCCCCEEE | 20873877 | ||
| 199 | Phosphorylation | WSPHHNCTQVATAND CCCCCCEEEEEECCC | 20873877 | ||
| 216 | Phosphorylation | LRGWDTRSMSQIYCI ECCCCCCCCCEEEEE | 27251275 | ||
| 218 | Phosphorylation | GWDTRSMSQIYCIEN CCCCCCCCEEEEEEC | 27251275 | ||
| 240 | Ubiquitination | DLDFNPNKQYYLASC ECCCCCCCEEEEEEC | - | ||
| 242 | Phosphorylation | DFNPNKQYYLASCGD CCCCCCEEEEEECCC | - | ||
| 252 | Ubiquitination | ASCGDDCKVKFWDTR EECCCCCEEEEEECC | - | ||
| 254 | Ubiquitination | CGDDCKVKFWDTRNV CCCCCEEEEEECCCC | - | ||
| 266 | Ubiquitination | RNVTEPVKTLEEHSH CCCCCCCEEHHHHCC | - | ||
| 280 | Phosphorylation | HWVWNVRYNHSHDQL CEEEEEEECCCCCEE | - | ||
| 290 | Phosphorylation | SHDQLVLTGSSDSRV CCCEEEEEECCCCEE | - | ||
| 292 | Phosphorylation | DQLVLTGSSDSRVIL CEEEEEECCCCEEEE | - | ||
| 293 | Phosphorylation | QLVLTGSSDSRVILS EEEEEECCCCEEEEE | - | ||
| 300 | Phosphorylation | SDSRVILSNMVSISS CCCEEEEECCEEECC | 27080861 | ||
| 304 | Phosphorylation | VILSNMVSISSEPFG EEEECCEEECCCCCC | 30576142 | ||
| 306 | Phosphorylation | LSNMVSISSEPFGHL EECCEEECCCCCCCC | 30108239 | ||
| 307 | Phosphorylation | SNMVSISSEPFGHLV ECCEEECCCCCCCCC | 30108239 | ||
| 320 | Phosphorylation | LVDDDDISDQEDHRS CCCCCCCCCCCCCCC | 25159151 | ||
| 327 | Phosphorylation | SDQEDHRSEEKSKEP CCCCCCCCHHHCCCC | 30576142 | ||
| 331 | Phosphorylation | DHRSEEKSKEPLQDN CCCCHHHCCCCCCCC | 26074081 | ||
| 342 | Phosphorylation | LQDNVIATYEEHEDS CCCCEEEEEECCCCC | 26074081 | ||
| 343 | Phosphorylation | QDNVIATYEEHEDSV CCCEEEEEECCCCCE | 26074081 | ||
| 382 | Ubiquitination | NRVPRALKYHILL-- ECCCHHHHEEECC-- | - |
| 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 EIPR1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EIPR1_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 EIPR1_HUMAN !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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