| UniProt ID | SMUF2_HUMAN | |
|---|---|---|
| UniProt AC | Q9HAU4 | |
| Protein Name | E3 ubiquitin-protein ligase SMURF2 | |
| Gene Name | SMURF2 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 748 | |
| Subcellular Localization | Nucleus . Cytoplasm . Cell membrane . Membrane raft . Cytoplasmic in the presence of SMAD7. Colocalizes with CAV1, SMAD7 and TGF-beta receptor in membrane rafts. | |
| Protein Description | E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Interacts with SMAD1 and SMAD7 in order to trigger their ubiquitination and proteasome-dependent degradation. In addition, interaction with SMAD7 activates autocatalytic degradation, which is prevented by interaction with SCYE1. Forms a stable complex with the TGF-beta receptor-mediated phosphorylated SMAD2 and SMAD3. In this way, SMAD2 may recruit substrates, such as SNON, for ubiquitin-mediated degradation. Enhances the inhibitory activity of SMAD7 and reduces the transcriptional activity of SMAD2. Coexpression of SMURF2 with SMAD1 results in considerable decrease in steady-state level of SMAD1 protein and a smaller decrease of SMAD2 level.. | |
| Protein Sequence | MSNPGGRRNGPVKLRLTVLCAKNLVKKDFFRLPDPFAKVVVDGSGQCHSTDTVKNTLDPKWNQHYDLYIGKSDSVTISVWNHKKIHKKQGAGFLGCVRLLSNAINRLKDTGYQRLDLCKLGPNDNDTVRGQIVVSLQSRDRIGTGGQVVDCSRLFDNDLPDGWEERRTASGRIQYLNHITRTTQWERPTRPASEYSSPGRPLSCFVDENTPISGTNGATCGQSSDPRLAERRVRSQRHRNYMSRTHLHTPPDLPEGYEQRTTQQGQVYFLHTQTGVSTWHDPRVPRDLSNINCEELGPLPPGWEIRNTATGRVYFVDHNNRTTQFTDPRLSANLHLVLNRQNQLKDQQQQQVVSLCPDDTECLTVPRYKRDLVQKLKILRQELSQQQPQAGHCRIEVSREEIFEESYRQVMKMRPKDLWKRLMIKFRGEEGLDYGGVAREWLYLLSHEMLNPYYGLFQYSRDDIYTLQINPDSAVNPEHLSYFHFVGRIMGMAVFHGHYIDGGFTLPFYKQLLGKSITLDDMELVDPDLHNSLVWILENDITGVLDHTFCVEHNAYGEIIQHELKPNGKSIPVNEENKKEYVRLYVNWRFLRGIEAQFLALQKGFNEVIPQHLLKTFDEKELELIICGLGKIDVNDWKVNTRLKHCTPDSNIVKWFWKAVEFFDEERRARLLQFVTGSSRVPLQGFKALQGAAGPRLFTIHQIDACTNNLPKAHTCFNRIDIPPYESYEKLYEKLLTAIEETCGFAVE | |
| 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 |
|---|---|---|---|---|---|
| 26 | Sumoylation | LCAKNLVKKDFFRLP HHHHCCCCCCHHCCC | 50.20 | - | |
| 26 | Sumoylation | LCAKNLVKKDFFRLP HHHHCCCCCCHHCCC | 50.20 | - | |
| 38 | Ubiquitination | RLPDPFAKVVVDGSG CCCCCCCEEEECCCC | 35.62 | - | |
| 44 | Phosphorylation | AKVVVDGSGQCHSTD CEEEECCCCCCCCCC | 22.64 | 25849741 | |
| 49 | Phosphorylation | DGSGQCHSTDTVKNT CCCCCCCCCCCCCCC | 35.29 | 23312004 | |
| 50 | Phosphorylation | GSGQCHSTDTVKNTL CCCCCCCCCCCCCCC | 16.42 | 23312004 | |
| 144 | Phosphorylation | QSRDRIGTGGQVVDC ECCCCCCCCCEEEEH | 35.45 | 23312004 | |
| 168 | Phosphorylation | DGWEERRTASGRIQY CCHHHHHHHHHHEEE | 31.25 | 28152594 | |
| 170 | Phosphorylation | WEERRTASGRIQYLN HHHHHHHHHHEEEEH | 28.17 | 28152594 | |
| 203 | Phosphorylation | SSPGRPLSCFVDENT CCCCCCCEEEECCCC | 14.27 | - | |
| 232 | Methylation | DPRLAERRVRSQRHR CHHHHHHHHHHHHHH | 21.50 | 113708605 | |
| 234 | Dimethylation | RLAERRVRSQRHRNY HHHHHHHHHHHHHCC | 25.84 | - | |
| 234 | Methylation | RLAERRVRSQRHRNY HHHHHHHHHHHHHCC | 25.84 | 113708599 | |
| 237 | Methylation | ERRVRSQRHRNYMSR HHHHHHHHHHCCCCC | 31.79 | 113708619 | |
| 239 | Dimethylation | RVRSQRHRNYMSRTH HHHHHHHHCCCCCCC | 37.86 | - | |
| 239 | Methylation | RVRSQRHRNYMSRTH HHHHHHHHCCCCCCC | 37.86 | 113708611 | |
| 245 | Phosphorylation | HRNYMSRTHLHTPPD HHCCCCCCCCCCCCC | 22.83 | 22617229 | |
| 249 | Phosphorylation | MSRTHLHTPPDLPEG CCCCCCCCCCCCCCC | 42.76 | 29214152 | |
| 268 | Phosphorylation | TTQQGQVYFLHTQTG ECCCCEEEEEEECCC | 7.79 | 27642862 | |
| 323 | Phosphorylation | VDHNNRTTQFTDPRL EECCCCEEEECCCHH | 20.60 | - | |
| 364 | Phosphorylation | PDDTECLTVPRYKRD CCCCCCCCCCCHHHH | 39.87 | 24719451 | |
| 369 | Sumoylation | CLTVPRYKRDLVQKL CCCCCCHHHHHHHHH | 40.49 | - | |
| 369 | Sumoylation | CLTVPRYKRDLVQKL CCCCCCHHHHHHHHH | 40.49 | - | |
| 375 | Ubiquitination | YKRDLVQKLKILRQE HHHHHHHHHHHHHHH | 44.24 | - | |
| 377 | Ubiquitination | RDLVQKLKILRQELS HHHHHHHHHHHHHHH | 46.89 | - | |
| 406 | Phosphorylation | REEIFEESYRQVMKM HHHHHHHHHHHHHHC | 20.58 | - | |
| 407 | Phosphorylation | EEIFEESYRQVMKMR HHHHHHHHHHHHHCC | 14.35 | - | |
| 412 | Ubiquitination | ESYRQVMKMRPKDLW HHHHHHHHCCHHHHH | 32.66 | - | |
| 434 | Phosphorylation | RGEEGLDYGGVAREW CCCCCCCCCHHHHHH | 22.33 | - | |
| 499 | Phosphorylation | MAVFHGHYIDGGFTL HEEEECEEECCCCCH | 12.80 | - | |
| 570 | Phosphorylation | ELKPNGKSIPVNEEN ECCCCCCCCCCCCCC | 33.26 | 30108239 | |
| 578 | Ubiquitination | IPVNEENKKEYVRLY CCCCCCCHHHEEHHH | 50.70 | - | |
| 579 | Ubiquitination | PVNEENKKEYVRLYV CCCCCCHHHEEHHHH | 66.90 | - | |
| 638 | Ubiquitination | KIDVNDWKVNTRLKH CCCCCCCCCCCCCCC | 28.59 | - | |
| 730 | Ubiquitination | PPYESYEKLYEKLLT CCHHHHHHHHHHHHH | 48.40 | - | |
| 734 | Ubiquitination | SYEKLYEKLLTAIEE HHHHHHHHHHHHHHH | 34.93 | - |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| - | K | Ubiquitination | E3 ubiquitin ligase | TRAF4 | Q9BUZ4 | PMID:23973329 |
| - | K | Ubiquitination | E3 ubiquitin ligase | RNF11 | Q9Y3C5 | PMID:22199232 |
| - | K | Ubiquitination | E3 ubiquitin ligase | FBXL15 | Q9H469 | PMID:22199232 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SMUF2_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 SMUF2_HUMAN !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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