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Identification
HMDB Protein ID HMDBP09317
Secondary Accession Numbers
  • 15151
Name E3 ubiquitin-protein ligase synoviolin
Synonyms
  1. Synovial apoptosis inhibitor 1
Gene Name SYVN1
Protein Type Enzyme
Biological Properties
General Function Involved in protein binding
Specific Function 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. Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Also promotes the degradation of normal but naturally short-lived proteins such as SGK. Protects cells from ER stress-induced apoptosis. Protects neurons from apoptosis induced by polyglutamine-expanded huntingtin (HTT) or unfolded GPR37 by promoting their degradation. Sequesters TP53 in the cytoplasm and promotes its degradation, thereby negatively regulating its biological function in transcription, cell cycle regulation and apoptosis
Pathways Not Available
Reactions Not Available
GO Classification
Function
ion binding
cation binding
metal ion binding
binding
transition metal ion binding
zinc ion binding
protein binding
Cellular Location
  1. Endoplasmic reticulum membrane
  2. Multi-pass membrane protein
Gene Properties
Chromosome Location Chromosome:1
Locus 11q13
SNPs SYVN1
Gene Sequence
>1854 bp
ATGTTCCGCACGGCAGTGATGATGGCGGCCAGCCTGGCGCTGACCGGGGCTGTGGTGGCT
CACGCCTACTACCTCAAACACCAGTTCTACCCCACTGTGGTGTACCTGACCAAGTCCAGC
CCCAGCATGGCAGTCCTGTACATCCAGGCCTTTGTCCTTGTCTTCCTTCTGGGCAAGGTG
ATGGGCAAGGTGTTCTTTGGGCAACTGAGGGCAGCAGAGATGGAGCACCTTCTGGAACGT
TCCTGGTACGCCGTCACAGAGACTTGTCTGGCCTTCACCGTTTTTCGGGATGACTTCAGC
CCCCGCTTTGTTGCACTCTTCACTCTTCTTCTCTTCCTCAAATGTTTCCACTGGCTGGCT
GAGGACCGTGTGGACTTTATGGAACGCAGCCCCAACATCTCCTGGCTCTTTCACTGCCGC
ATTGTCTCTCTTATGTTCCTCCTGGGCATCCTGGACTTCCTCTTCGTCAGCCACGCCTAT
CACAGCATCCTGACCCGTGGGGCCTCTGTGCAGCTGGTGTTTGGCTTTGAGTATGCCATC
CTGATGACGATGGTGCTCACCATCTTCATCAAGTATGTGCTGCACTCCGTGGACCTCCAG
AGTGAGAACCCCTGGGACAACAAGGCTGTGTACATGCTCTACACAGAGCTGTTTACAGGC
TTCATCAAGGTTCTGCTGTACATGGCCTTCATGACCATCATGATCAAGGTGCACACCTTC
CCACTCTTTGCCATCCGGCCCATGTACCTGGCCATGAGACAGTTCAAGAAAGCTGTGACA
GATGCCATCATGTCTCGCCGAGCCATCCGCAACATGAACACCCTGTATCCAGATGCCACC
CCAGAGGAGCTCCAGGCAATGGACAATGTCTGCATCATCTGCCGAGAAGAGATGGTGACT
GGTGCCAAGAGACTGCCCTGCAACCACATTTTCCATACCAGCTGCCTGCGCTCCTGGTTC
CAGCGGCAGCAGACCTGCCCCACCTGCCGTATGGATGTCCTTCGTGCATCGCTGCCAGCG
CAGTCACCACCACCCCCGGAGCCTGCGGATCAGGGGCCACCCCCTGCCCCCCACCCCCCA
CCACTCTTGCCTCAGCCCCCCAACTTCCCCCAGGGCCTCCTGCCTCCTTTTCCTCCAGGC
ATGTTCCCACTGTGGCCCCCCATGGGCCCCTTTCCACCTGTCCCGCCTCCCCCCAGCTCA
GGAGAGGCTGTGGCTCCTCCATCCACCAGTGCAGCAGCCCTTTCTCGGCCCAGTGGAGCA
GCTACAACCACAGCTGCTGGCACCAGTGCTACTGCTGCTTCTGCCACAGCATCTGGCCCA
GGCTCTGGCTCTGCCCCAGAGGCTGGCCCTGCCCCTGGTTTCCCCTTCCCTCCTCCCTGG
ATGGGTATGCCCCTGCCTCCACCCTTTGCCTTCCCCCCAATGCCTGTGCCCCCTGCGGGC
TTTGCTGGGCTGACCCCAGAGGAGCTACGAGCTCTGGAGGGCCATGAGCGGCAGCACCTG
GAGGCCCGGCTGCAGAGCCTGCGTAACATCCACACACTGCTGGACGCCGCCATGCTGCAG
ATCAACCAGTACCTCACCGTGCTGGCCTCCTTGGGGCCCCCCCGGCCTGCCACTTCAGTC
AACTCCACTGAGGGGACTGCCACTACAGTTGTTGCTGCTGCCTCCTCCACCAGCATCCCT
AGCTCAGAGGCCACGACCCCAACCCCAGGAGCCTCCCCACCAGCCCCTGAAATGGAAAGG
CCTCCAGCTCCTGAGTCAGTGGGCACAGAGGAGATGCCTGAGGATGGAGAGCCCGATGCA
GCAGAGCTCCGCCGGCGCCGCCTGCAGAAGCTGGAGTCTCCTGTTGCCCACTGA
Protein Properties
Number of Residues 617
Molecular Weight 67684.1
Theoretical pI 6.95
Pfam Domain Function
Signals
  • 1-22
Transmembrane Regions
  • 42-62
  • 99-119
  • 141-161
  • 170-190
  • 225-245
Protein Sequence
>E3 ubiquitin-protein ligase synoviolin
MFRTAVMMAASLALTGAVVAHAYYLKHQFYPTVVYLTKSSPSMAVLYIQAFVLVFLLGKV
MGKVFFGQLRAAEMEHLLERSWYAVTETCLAFTVFRDDFSPRFVALFTLLLFLKCFHWLA
EDRVDFMERSPNISWLFHCRIVSLMFLLGILDFLFVSHAYHSILTRGASVQLVFGFEYAI
LMTMVLTIFIKYVLHSVDLQSENPWDNKAVYMLYTELFTGFIKVLLYMAFMTIMIKVHTF
PLFAIRPMYLAMRQFKKAVTDAIMSRRAIRNMNTLYPDATPEELQAMDNVCIICREEMVT
GAKRLPCNHIFHTSCLRSWFQRQQTCPTCRMDVLRASLPAQSPPPPEPADQGPPPAPHPP
PLLPQPPNFPQGLLPPFPPGMFPLWPPMGPFPPVPPPPSSGEAVAPPSTSAAALSRPSGA
ATTTAAGTSATAASATASGPGSGSAPEAGPAPGFPFPPPWMGMPLPPPFAFPPMPVPPAG
FAGLTPEELRALEGHERQHLEARLQSLRNIHTLLDAAMLQINQYLTVLASLGPPRPATSV
NSTEETATTVVAAASSTSIPSSEATTPTPGASPPAPEMERPPAPESVGTEEMPEDGEPDA
AELRRRRLQKLESPVAH
GenBank ID Protein 28460644
UniProtKB/Swiss-Prot ID Q86TM6
UniProtKB/Swiss-Prot Entry Name SYVN1_HUMAN
PDB IDs Not Available
GenBank Gene ID AB024690
GeneCard ID SYVN1
GenAtlas ID SYVN1
HGNC ID HGNC:20738
References
General References
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  9. Christianson JC, Shaler TA, Tyler RE, Kopito RR: OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD. Nat Cell Biol. 2008 Mar;10(3):272-82. doi: 10.1038/ncb1689. Epub 2008 Feb 10. [PubMed:18264092 ]
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  11. Ye Y, Shibata Y, Kikkert M, van Voorden S, Wiertz E, Rapoport TA: Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane. Proc Natl Acad Sci U S A. 2005 Oct 4;102(40):14132-8. Epub 2005 Sep 26. [PubMed:16186510 ]
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  19. Arteaga MF, Wang L, Ravid T, Hochstrasser M, Canessa CM: An amphipathic helix targets serum and glucocorticoid-induced kinase 1 to the endoplasmic reticulum-associated ubiquitin-conjugation machinery. Proc Natl Acad Sci U S A. 2006 Jul 25;103(30):11178-83. Epub 2006 Jul 17. [PubMed:16847254 ]
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