| UniProt ID | SYVN1_HUMAN | |
|---|---|---|
| UniProt AC | Q86TM6 | |
| Protein Name | E3 ubiquitin-protein ligase synoviolin | |
| Gene Name | SYVN1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 617 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . |
|
| Protein Description | Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC7 E2 ligase and transfers it to substrates, promoting their degradation. [PubMed: 12459480] | |
| Protein Sequence | MFRTAVMMAASLALTGAVVAHAYYLKHQFYPTVVYLTKSSPSMAVLYIQAFVLVFLLGKVMGKVFFGQLRAAEMEHLLERSWYAVTETCLAFTVFRDDFSPRFVALFTLLLFLKCFHWLAEDRVDFMERSPNISWLFHCRIVSLMFLLGILDFLFVSHAYHSILTRGASVQLVFGFEYAILMTMVLTIFIKYVLHSVDLQSENPWDNKAVYMLYTELFTGFIKVLLYMAFMTIMIKVHTFPLFAIRPMYLAMRQFKKAVTDAIMSRRAIRNMNTLYPDATPEELQAMDNVCIICREEMVTGAKRLPCNHIFHTSCLRSWFQRQQTCPTCRMDVLRASLPAQSPPPPEPADQGPPPAPHPPPLLPQPPNFPQGLLPPFPPGMFPLWPPMGPFPPVPPPPSSGEAVAPPSTSAAALSRPSGAATTTAAGTSATAASATASGPGSGSAPEAGPAPGFPFPPPWMGMPLPPPFAFPPMPVPPAGFAGLTPEELRALEGHERQHLEARLQSLRNIHTLLDAAMLQINQYLTVLASLGPPRPATSVNSTEETATTVVAAASSTSIPSSEATTPTPGASPPAPEMERPPAPESVGTEEMPEDGEPDAAELRRRRLQKLESPVAH | |
| 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 |
|---|---|---|---|---|---|
| 4 | Phosphorylation | ----MFRTAVMMAAS ----CHHHHHHHHHH | 16.61 | 24719451 | |
| 23 | Phosphorylation | GAVVAHAYYLKHQFY HHHHHHHHHHHHCCC | 10.24 | 24719451 | |
| 24 | Phosphorylation | AVVAHAYYLKHQFYP HHHHHHHHHHHCCCC | 15.28 | 24719451 | |
| 93 | Phosphorylation | TETCLAFTVFRDDFS HHHHHHHHCCCCCCC | 17.09 | - | |
| 162 | Phosphorylation | FVSHAYHSILTRGAS HHHHHHHHHHHCCCC | 13.45 | 24719451 | |
| 191 | Ubiquitination | MVLTIFIKYVLHSVD HHHHHHHHHHHHHCC | 20.68 | - | |
| 206 (in isoform 2) | Ubiquitination | - | 48.27 | 21906983 | |
| 252 (in isoform 2) | Ubiquitination | - | 2.98 | 21906983 | |
| 256 | Ubiquitination | YLAMRQFKKAVTDAI HHHHHHHHHHHHHHH | 31.33 | 22817900 | |
| 257 | Ubiquitination | LAMRQFKKAVTDAIM HHHHHHHHHHHHHHH | 49.75 | 21906983 | |
| 257 (in isoform 3) | Ubiquitination | - | 49.75 | 21906983 | |
| 257 (in isoform 1) | Ubiquitination | - | 49.75 | 21906983 | |
| 260 | Phosphorylation | RQFKKAVTDAIMSRR HHHHHHHHHHHHHHH | 25.27 | - | |
| 265 | Phosphorylation | AVTDAIMSRRAIRNM HHHHHHHHHHHHHHC | 16.70 | - | |
| 303 (in isoform 3) | Ubiquitination | - | 56.67 | 21906983 | |
| 303 (in isoform 1) | Ubiquitination | - | 56.67 | 21906983 | |
| 303 | 2-Hydroxyisobutyrylation | EEMVTGAKRLPCNHI HHHCCCCCCCCCCCE | 56.67 | - | |
| 303 | Ubiquitination | EEMVTGAKRLPCNHI HHHCCCCCCCCCCCE | 56.67 | 22817900 | |
| 506 | Phosphorylation | HLEARLQSLRNIHTL HHHHHHHHHHHHHHH | 33.61 | 29496963 | |
| 546 | Phosphorylation | SVNSTEETATTVVAA CCCCCHHHHHHHHHH | 24.07 | 24275569 | |
| 556 | Phosphorylation | TVVAAASSTSIPSSE HHHHHCCCCCCCCCC | 22.80 | 24275569 | |
| 557 | Phosphorylation | VVAAASSTSIPSSEA HHHHCCCCCCCCCCC | 28.34 | 24275569 | |
| 558 | Phosphorylation | VAAASSTSIPSSEAT HHHCCCCCCCCCCCC | 34.15 | 24275569 | |
| 561 | Phosphorylation | ASSTSIPSSEATTPT CCCCCCCCCCCCCCC | 38.86 | 24275569 | |
| 562 | Phosphorylation | SSTSIPSSEATTPTP CCCCCCCCCCCCCCC | 26.37 | 24275569 | |
| 565 | Phosphorylation | SIPSSEATTPTPGAS CCCCCCCCCCCCCCC | 29.29 | 24275569 | |
| 566 | Phosphorylation | IPSSEATTPTPGASP CCCCCCCCCCCCCCC | 32.01 | 24275569 | |
| 572 | Phosphorylation | TTPTPGASPPAPEME CCCCCCCCCCCCCCC | 37.01 | 24275569 | |
| 609 | Ubiquitination | ELRRRRLQKLESPVA HHHHHHHHHCCCCCC | 46.61 | 33845483 | |
| 610 | Ubiquitination | LRRRRLQKLESPVAH HHHHHHHHCCCCCCC | 59.83 | 33845483 | |
| 613 | Phosphorylation | RRLQKLESPVAH--- HHHHHCCCCCCC--- | 34.80 | 25159151 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SYVN1_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 SYVN1_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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| Phosphorylation | |
| Reference | PubMed |
| "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-613, 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-613, AND MASSSPECTROMETRY. | |
| "Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613, AND MASSSPECTROMETRY. | |
| "Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613, AND MASSSPECTROMETRY. | |
