Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

E3 ubiquitin-protein ligase synoviolin

Gene

Syvn1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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:12975321, PubMed:15611074). 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 (PubMed:12975321, PubMed:15611074). Also promotes the degradation of normal but naturally short-lived proteins such as SGK. Protects cells from ER stress-induced apoptosis. Sequesters p53/TP53 in the cytoplasm and promotes its degradation, thereby negatively regulating its biological function in transcription, cell cycle regulation and apoptosis (PubMed:17170702). Required for embryogenesis (PubMed:15611074). Mediates the ubiquitination and subsequent degradation of cytoplasmic NFE2L1 (PubMed:21911472).4 Publications

Miscellaneous

Mice overexpressing Syvn1 develop severe spontaneous arthropathy. Mice lacking Syvn1 die in utero around E13.5 due to augmented apoptotic cell death.

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri291 – 330RING-type; atypicalPROSITE-ProRule annotationAdd BLAST40

GO - Molecular functioni

GO - Biological processi

  • endoplasmic reticulum unfolded protein response Source: GO_Central
  • ERAD pathway Source: ParkinsonsUK-UCL
  • in utero embryonic development Source: MGI
  • negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway Source: MGI
  • protein catabolic process Source: ParkinsonsUK-UCL
  • protein K48-linked ubiquitination Source: MGI
  • protein N-linked glycosylation via asparagine Source: UniProtKB
  • protein polyubiquitination Source: GO_Central
  • protein stabilization Source: ParkinsonsUK-UCL
  • protein ubiquitination Source: MGI
  • response to unfolded protein Source: MGI
  • retrograde protein transport, ER to cytosol Source: MGI
  • ubiquitin-dependent ERAD pathway Source: UniProtKB
  • ubiquitin-dependent protein catabolic process Source: UniProtKB

Keywordsi

Molecular functionDevelopmental protein, Transferase
Biological processUbl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase synoviolin (EC:2.3.2.27)
Alternative name(s):
RING-type E3 ubiquitin transferase synoviolinCurated
Synovial apoptosis inhibitor 1
Gene namesi
Name:Syvn1
Synonyms:Hrd1, Kiaa1810
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1921376 Syvn1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini23 – 41LumenalSequence analysisAdd BLAST19
Transmembranei42 – 62HelicalSequence analysisAdd BLAST21
Topological domaini63 – 98CytoplasmicSequence analysisAdd BLAST36
Transmembranei99 – 119HelicalSequence analysisAdd BLAST21
Topological domaini120 – 140LumenalSequence analysisAdd BLAST21
Transmembranei141 – 161HelicalSequence analysisAdd BLAST21
Topological domaini162 – 169CytoplasmicSequence analysis8
Transmembranei170 – 190HelicalSequence analysisAdd BLAST21
Topological domaini191 – 224LumenalSequence analysisAdd BLAST34
Transmembranei225 – 245HelicalSequence analysisAdd BLAST21
Topological domaini246 – 612CytoplasmicSequence analysisAdd BLAST367

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
ChainiPRO_000028054923 – 612E3 ubiquitin-protein ligase synoviolinAdd BLAST590

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei608PhosphoserineBy similarity1

Post-translational modificationi

Auto-ubiquitinated.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9DBY1
PeptideAtlasiQ9DBY1
PRIDEiQ9DBY1

PTM databases

iPTMnetiQ9DBY1
PhosphoSitePlusiQ9DBY1

Expressioni

Tissue specificityi

Ubiquitously expressed, with highest levels in bone, spleen, lung and testis. In the brain, present in neurons but not in glial cells. Up-regulated in synovial tissues from mice with collagen-induced arthritis (at protein level).2 Publications

Inductioni

By cerebral ischemia.1 Publication

Gene expression databases

CleanExiMM_SYVN1

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with p53/TP53 and HTT (PubMed:17170702). Interacts with VCP, HERPUD1 and DERL1. Part of a complex containing SYVN1, HERPUD1, SELENOS and DERL1; which probably transfer misfolded proteins from the ER to VCP (By similarity). Part of a complex containing SYVN1, SEL1L and DERL2 (By similarity). Interacts with UBXN6 (By similarity). Interacts (via N-terminal loop) with SEL1L; recruits ERLEC1 and OS9. May form a complex with ERLEC1; HSPA5; OS9 AND SEL1L (PubMed:27064360). Interacts with BAG6 (By similarity). Interacts with NFE2L1 (PubMed:21911472).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NcstnP577162EBI-644384,EBI-998934

GO - Molecular functioni

Protein-protein interaction databases

BioGridi216511, 4 interactors
IntActiQ9DBY1, 6 interactors
MINTiQ9DBY1
STRINGi10090.ENSMUSP00000114843

Structurei

3D structure databases

ProteinModelPortaliQ9DBY1
SMRiQ9DBY1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni21 – 42Interaction with SEL1L1 PublicationAdd BLAST22
Regioni236 – 270Interaction with p53/TP531 PublicationAdd BLAST35

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi339 – 472Pro-richAdd BLAST134
Compositional biasi599 – 602Poly-Arg4

Domaini

The RING-type zinc finger is required for E3 ligase activity.By similarity

Sequence similaritiesi

Belongs to the HRD1 family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri291 – 330RING-type; atypicalPROSITE-ProRule annotationAdd BLAST40

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiKOG0802 Eukaryota
COG5243 LUCA
HOGENOMiHOG000294196
HOVERGENiHBG094015
InParanoidiQ9DBY1
KOiK10601
PhylomeDBiQ9DBY1
TreeFamiTF318635

Family and domain databases

Gene3Di3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR032832 E3_lig_synoviolin/Hrd1
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
PANTHERiPTHR44251 PTHR44251, 1 hit
PfamiView protein in Pfam
PF13639 zf-RING_2, 1 hit
SMARTiView protein in SMART
SM00184 RING, 1 hit
PROSITEiView protein in PROSITE
PS50089 ZF_RING_2, 1 hit

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9DBY1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MFRTAVMMAA SLALTGAVVA HAYYLKHQFY PTVVYLTKSS PSMAVLYIQA
60 70 80 90 100
FVLVFLLGKV MGKVFFGQLR AAEMEHLLER SWYAVTETCL AFTVFRDDFS
110 120 130 140 150
PRFVALFTLL LFLKCFHWLA EDRVDFMERS PNISWLFHCR IVSLMFLLGI
160 170 180 190 200
LDFLFVSHAY HSILTRGASV QLVFGFEYAI LMTMVLTIFI KYVLHSVDLQ
210 220 230 240 250
SENPWDNKAV YMLYTELFTG FIKVLLYMAF MTIMIKVHTF PLFAIRPMYL
260 270 280 290 300
AMRQFKKAVT DAIMSRRAIR NMNTLYPDAT PEELQAVDNV CIICREEMVT
310 320 330 340 350
GAKRLPCNHI FHTSCLRSWF QRQQTCPTCR MDVLRASLPA QSPPPPEPAD
360 370 380 390 400
QGPPPAPHPQ PLLPQPPNFP QGLLPPFPPG MFPLWPPMGP FPPVPPPPSS
410 420 430 440 450
GEAAAPPPTS TAVSRPSGAA TTTAAGTSTS APAPGSVPGP EAGPAPGFPF
460 470 480 490 500
PPPWMGMPLP PPFAFPPMPV PPAGFAGLTP EELRALEGHE RQHLEARLQS
510 520 530 540 550
LRNIHTLLDA AMLQINQYLT VLASLGPPRP ATSVNPTEET ASTVVSAAPS
560 570 580 590 600
TSAPSSEAPT PSPGASPPIP EAEKPPAPES VGIVEELPED GEPDAAELRR
610
RRLQKLESPV AH
Length:612
Mass (Da):67,296
Last modified:March 20, 2007 - v3
Checksum:i8F7620E5016DF1F2
GO
Isoform 2 (identifier: Q9DBY1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     75-75: E → EVICWWPQRTGFRGGYPNDWFSYHPLLTPQ
     127-177: Missing.
     369-375: FPQGLLP → CKWPFIC
     577-578: AP → GK
     579-612: Missing.

Note: No experimental confirmation available.
Show »
Length:556
Mass (Da):61,254
Checksum:i1566257B166A4A97
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti287V → M in BAB23474 (PubMed:16141072).Curated1
Sequence conflicti287V → M in AAH46829 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_02377975E → EVICWWPQRTGFRGGYPNDW FSYHPLLTPQ in isoform 2. 1 Publication1
Alternative sequenceiVSP_023780127 – 177Missing in isoform 2. 1 PublicationAdd BLAST51
Alternative sequenceiVSP_023781369 – 375FPQGLLP → CKWPFIC in isoform 2. 1 Publication7
Alternative sequenceiVSP_023782577 – 578AP → GK in isoform 2. 1 Publication2
Alternative sequenceiVSP_023783579 – 612Missing in isoform 2. 1 PublicationAdd BLAST34

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK122558 Transcribed RNA Translation: BAC65840.3 Sequence problems.
AK004688 mRNA Translation: BAB23474.2
BC042199 mRNA Translation: AAH42199.1
BC046829 mRNA Translation: AAH46829.1
BC057917 mRNA Translation: AAH57917.1
BC080722 mRNA Translation: AAH80722.1
CCDSiCCDS29487.1 [Q9DBY1-1]
RefSeqiNP_001158181.1, NM_001164709.1
NP_083045.4, NM_028769.5
XP_006531913.1, XM_006531850.3
UniGeneiMm.149870

Genome annotation databases

GeneIDi74126
KEGGimmu:74126
UCSCiuc008ggm.2 mouse [Q9DBY1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiSYVN1_MOUSE
AccessioniPrimary (citable) accession number: Q9DBY1
Secondary accession number(s): Q80T88, Q8CGB5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: March 20, 2007
Last modified: May 23, 2018
This is version 146 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health