UniProt ID | SMUF1_HUMAN | |
---|---|---|
UniProt AC | Q9HCE7 | |
Protein Name | E3 ubiquitin-protein ligase SMURF1 | |
Gene Name | SMURF1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 757 | |
Subcellular Localization |
Cytoplasm . Cell membrane Peripheral membrane protein Cytoplasmic side . |
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Protein Description | E3 ubiquitin-protein ligase that acts as a negative regulator of BMP signaling pathway. Mediates ubiquitination and degradation of SMAD1 and SMAD5, 2 receptor-regulated SMADs specific for the BMP pathway. Promotes ubiquitination and subsequent proteasomal degradation of TRAF family members and RHOA. Promotes ubiquitination and subsequent proteasomal degradation of MAVS. [PubMed: 23087404 Plays a role in dendrite formation by melanocytes] | |
Protein Sequence | MSNPGTRRNGSSIKIRLTVLCAKNLAKKDFFRLPDPFAKIVVDGSGQCHSTDTVKNTLDPKWNQHYDLYVGKTDSITISVWNHKKIHKKQGAGFLGCVRLLSNAISRLKDTGYQRLDLCKLNPSDTDAVRGQIVVSLQTRDRIGTGGSVVDCRGLLENEGTVYEDSGPGRPLSCFMEEPAPYTDSTGAAAGGGNCRFVESPSQDQRLQAQRLRNPDVRGSLQTPQNRPHGHQSPELPEGYEQRTTVQGQVYFLHTQTGVSTWHDPRIPSPSGTIPGGDAAFLYEFLLQGHTSEPRDLNSVNCDELGPLPPGWEVRSTVSGRIYFVDHNNRTTQFTDPRLHHIMNHQCQLKEPSQPLPLPSEGSLEDEELPAQRYERDLVQKLKVLRHELSLQQPQAGHCRIEVSREEIFEESYRQIMKMRPKDLKKRLMVKFRGEEGLDYGGVAREWLYLLCHEMLNPYYGLFQYSTDNIYMLQINPDSSINPDHLSYFHFVGRIMGLAVFHGHYINGGFTVPFYKQLLGKPIQLSDLESVDPELHKSLVWILENDITPVLDHTFCVEHNAFGRILQHELKPNGRNVPVTEENKKEYVRLYVNWRFMRGIEAQFLALQKGFNELIPQHLLKPFDQKELELIIGGLDKIDLNDWKSNTRLKHCVADSNIVRWFWQAVETFDEERRARLLQFVTGSTRVPLQGFKALQGSTGAAGPRLFTIHLIDANTDNLPKAHTCFNRIDIPPYESYEKLYEKLLTAVEETCGFAVE | |
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 |
---|---|---|---|---|---|
23 | Ubiquitination | RLTVLCAKNLAKKDF HHHHHHHHHHCCCCC | 52.04 | 33845483 | |
66 | Phosphorylation | DPKWNQHYDLYVGKT CCCHHHCEEEEEECC | 9.62 | - | |
69 | Phosphorylation | WNQHYDLYVGKTDSI HHHCEEEEEECCCEE | 12.31 | - | |
145 | Phosphorylation | QTRDRIGTGGSVVDC ECCCCCCCCCCEEEC | 35.68 | 24719451 | |
148 | Phosphorylation | DRIGTGGSVVDCRGL CCCCCCCCEEECCHH | 21.95 | 28857561 | |
163 | Phosphorylation | LENEGTVYEDSGPGR HCCCCCEEECCCCCC | 17.54 | 27642862 | |
200 | Phosphorylation | GNCRFVESPSQDQRL CCCEECCCCCHHHHH | 25.26 | 29255136 | |
202 | Phosphorylation | CRFVESPSQDQRLQA CEECCCCCHHHHHHH | 56.52 | 22210691 | |
223 | Phosphorylation | DVRGSLQTPQNRPHG CCCCCCCCCCCCCCC | 31.94 | 28555341 | |
233 | Phosphorylation | NRPHGHQSPELPEGY CCCCCCCCCCCCCCC | 18.05 | 28985074 | |
251 | Phosphorylation | TTVQGQVYFLHTQTG EEEEEEEEEEEECCC | 7.79 | - | |
260 | Phosphorylation | LHTQTGVSTWHDPRI EEECCCCCCCCCCCC | 27.42 | - | |
324 | Ubiquitination | TVSGRIYFVDHNNRT EEECEEEEEECCCCE | 4.91 | 21963094 | |
332 | Phosphorylation | VDHNNRTTQFTDPRL EECCCCEEEECCHHH | 20.60 | - | |
350 | Ubiquitination | MNHQCQLKEPSQPLP HCCCCCCCCCCCCCC | 41.52 | PubMed | |
355 | Ubiquitination | QLKEPSQPLPLPSEG CCCCCCCCCCCCCCC | 40.04 | 29967540 | |
360 | Phosphorylation | SQPLPLPSEGSLEDE CCCCCCCCCCCCCCC | 63.37 | 28348404 | |
363 | Phosphorylation | LPLPSEGSLEDEELP CCCCCCCCCCCCCCC | 25.24 | 28348404 | |
381 | Ubiquitination | YERDLVQKLKVLRHE HHHHHHHHHHHHHHH | 42.68 | 21572392 | |
383 | Ubiquitination | RDLVQKLKVLRHELS HHHHHHHHHHHHHHC | 46.38 | 21572392 | |
390 | Phosphorylation | KVLRHELSLQQPQAG HHHHHHHCCCCCCCC | 22.58 | 22210691 | |
392 | Ubiquitination | LRHELSLQQPQAGHC HHHHHCCCCCCCCCC | 49.92 | 25015289 | |
404 | Phosphorylation | GHCRIEVSREEIFEE CCCEEEECHHHHHHH | 22.60 | 22210691 | |
412 | Phosphorylation | REEIFEESYRQIMKM HHHHHHHHHHHHHHC | 20.58 | 22210691 | |
413 | Phosphorylation | EEIFEESYRQIMKMR HHHHHHHHHHHHHCC | 15.15 | 22210691 | |
418 | Ubiquitination | ESYRQIMKMRPKDLK HHHHHHHHCCHHHHH | 33.13 | 25015289 | |
440 | Phosphorylation | RGEEGLDYGGVAREW CCCCCCCCCHHHHHH | 22.33 | - | |
495 | Ubiquitination | YFHFVGRIMGLAVFH HHHHHHHHHHHEEEE | 1.80 | 29967540 | |
521 | Ubiquitination | FYKQLLGKPIQLSDL HHHHHHCCCEEHHHH | 38.63 | 29967540 | |
526 | Phosphorylation | LGKPIQLSDLESVDP HCCCEEHHHHHHCCH | 24.63 | 18452278 | |
656 | Phosphorylation | LKHCVADSNIVRWFW HHHHHCCHHHHHHHH | 20.79 | 23312004 | |
667 | Ubiquitination | RWFWQAVETFDEERR HHHHHHHHHCCHHHH | 46.93 | 27667366 | |
693 | Ubiquitination | RVPLQGFKALQGSTG CCCCCCHHHHCCCCC | 55.82 | 27667366 | |
739 | Ubiquitination | PPYESYEKLYEKLLT CCHHHHHHHHHHHHH | 48.40 | - |
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 | FBXL15 | Q9H469 | PMID:21572392 |
- | K | Ubiquitination | E3 ubiquitin ligase | FBXO3 | Q9UK99 | PMID:25721664 |
- | K | Ubiquitination | E3 ubiquitin ligase | SMURF2 | Q9HAU4 | PMID:16373342 |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
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Oops, there are no SNP-PTM records of SMUF1_HUMAN !! |
Kegg Disease | ||||||
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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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Ubiquitylation | |
Reference | PubMed |
"SCF(FBXL15) regulates BMP signalling by directing the degradation ofHECT-type ubiquitin ligase Smurf1."; Cui Y., He S., Xing C., Lu K., Wang J., Xing G., Meng A., Jia S.,He F., Zhang L.; EMBO J. 30:2675-2689(2011). Cited for: SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-381 AND LYS-383,INTERACTION WITH FBXL15, AND MUTAGENESIS OF LYS-350; LYS-381; LYS-383AND CYS-725. |