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Protein

E3 ubiquitin-protein ligase RNF146

Gene

Rnf146

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

E3 ubiquitin-protein ligase that specifically binds poly-ADP-ribosylated (PARsylated) proteins and mediates their ubiquitination and subsequent degradation. May regulate many important biological processes, such as cell survival and DNA damage response. Acts as an activator of the Wnt signaling pathway by mediating the ubiquitination of PARsylated AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex. Acts in cooperation with tankyrase proteins (TNKS and TNKS2), which mediate PARsylation of target proteins AXIN1, AXIN2, BLZF1, CASC3, TNKS and TNKS2. Recognizes and binds tankyrase-dependent PARsylated proteins via its WWE domain and mediates their ubiquitination. May regulate TNKS and TNKS2 subcellular location, preventing aggregation at a centrosomal location. Neuroprotective protein. Protects the brain against N-methyl-D-aspartate (NMDA) receptor-mediated glutamate excitotoxicity and ischemia, by interfering with PAR-induced cell death, called parthanatos. Prevents nuclear translocation of AIFM1 in a PAR-binding dependent manner. Does not affect PARP1 activation. Protects against cell death induced by DNA damaging agents, such as N-methyl-N-nitro-N-nitrosoguanidine (MNNG) and rescues cells from G1 arrest. Promotes cell survival after gamma-irradiation. Facilitates DNA repair. Neuroprotective protein. Protects the brain against N-methyl-D-aspartate (NMDA) receptor-mediated glutamate excitotoxicity and ischemia, by interfering with PAR-induced cell death, called parthanatos. Prevents nuclear translocation of AIFM1 in a PAR-binding dependent manner. Does not affect PARP1 activation (By similarity).By similarity

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei107iso-ADP-ribose adenine ring groupBy similarity1
Binding sitei110iso-ADP-ribose 5'-phosphate groupBy similarity1
Binding sitei114iso-ADP-ribose 5'-phosphate groupBy similarity1
Binding sitei144iso-ADP-ribose 1'-phosphate groupBy similarity1
Binding sitei153iso-ADP-ribose adenine ring groupBy similarity1
Binding sitei163iso-ADP-ribose 1'-phosphate groupBy similarity1
Binding sitei175iso-ADP-ribose 5'-phosphate groupBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri36 – 74RING-typePROSITE-ProRule annotationAdd BLAST39

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processUbl conjugation pathway, Wnt signaling pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF146 (EC:2.3.2.27)
Alternative name(s):
Iduna
RING finger protein 146
RING-type E3 ubiquitin transferase RNF146Curated
Gene namesi
Name:Rnf146
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1306482 Rnf146

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000561101 – 352E3 ubiquitin-protein ligase RNF146Add BLAST352

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki84Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki94Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki130Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki175Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei288PhosphoserineCombined sources1
Modified residuei292PhosphoserineCombined sources1

Post-translational modificationi

Ubiquitinated; autoubiquitinated. Autoubiquitination is enhanced upon poly(ADP-ribose)-binding (By similarity).By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ5XIK5
PRIDEiQ5XIK5

PTM databases

iPTMnetiQ5XIK5
PhosphoSitePlusiQ5XIK5

Expressioni

Gene expression databases

GenevisibleiQ5XIK5 RN

Interactioni

Subunit structurei

Can form homooligomers. Interacts with PARsylated AXIN1, AXIN2, BLZF1, CASC3, HIST1H1C, IPO7, LIG3, NCL, PARP1, XRCC1, XRCC5 and XRCC6. Interacts with DDB1, DHX15, IQGAP1, LRPPRC, PARP2, PRKDC, RUVBL2, TNKS1 and TNKS2. Binding often leads to interactor ubiquitination, in the presence of the appropriate E1 and E2 enzymes, and proteasomal degradation (By similarity).By similarity

Protein-protein interaction databases

BioGridi258888, 1 interactor
STRINGi10116.ENSRNOP00000015421

Structurei

3D structure databases

ProteinModelPortaliQ5XIK5
SMRiQ5XIK5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini91 – 167WWEPROSITE-ProRule annotationAdd BLAST77

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni142 – 165PAR-bindingBy similarityAdd BLAST24

Domaini

The WWE domain mediates non-covalent poly(ADP-ribose)-binding.By similarity

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri36 – 74RING-typePROSITE-ProRule annotationAdd BLAST39

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0824 Eukaryota
ENOG410ZTFC LUCA
HOGENOMiHOG000128547
HOVERGENiHBG057514
InParanoidiQ5XIK5
KOiK15700
OrthoDBiEOG091G0Y4Y
PhylomeDBiQ5XIK5

Family and domain databases

Gene3Di3.30.40.10, 1 hit
3.30.720.50, 1 hit
InterProiView protein in InterPro
IPR033509 RNF146
IPR004170 WWE-dom
IPR018123 WWE-dom_subgr
IPR037197 WWE_dom_sf
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS
PANTHERiPTHR13417:SF2 PTHR13417:SF2, 2 hits
PfamiView protein in Pfam
PF02825 WWE, 1 hit
SMARTiView protein in SMART
SM00184 RING, 1 hit
SM00678 WWE, 1 hit
SUPFAMiSSF117839 SSF117839, 1 hit
PROSITEiView protein in PROSITE
PS50918 WWE, 1 hit
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 1 hit

Sequencei

Sequence statusi: Complete.

Q5XIK5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGCGEIDHS LNMLPTNKKA SETCSNTAPS LTVPECAICL QTCVHPVSLP
60 70 80 90 100
CKHVFCYLCV KGASWLGKRC ALCRQEIPED FLDKPTLLSP EELKAASRGN
110 120 130 140 150
GEYVWYYEGR NGWWQYDERT SRELEDAFSK GKKNTEMLIA GFLYVADLEN
160 170 180 190 200
MVQYRRNEHG RRRKIKRDII DIPKKGVAGL RLDCDSNTVN LARESSADGA
210 220 230 240 250
DSGSAHTGAS VQLPVPSSTR PLTSVDGQLT SPVTPSPDAG ASLEDSFAHL
260 270 280 290 300
QLSGDSIAER SHRGEGEEDH ESPSSGRVPD TSTEETESDA SSDIEDAPVV
310 320 330 340 350
VAQHSLTQQR LLVSSANQTV AERSDRPVAG GGTMSVNVRS RRPDGQCTVT

EV
Length:352
Mass (Da):38,224
Last modified:November 23, 2004 - v1
Checksum:iA0AE19B1F23560C1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083675 mRNA Translation: AAH83675.1
RefSeqiNP_001012060.2, NM_001012060.2
UniGeneiRn.167060
Rn.16849

Genome annotation databases

GeneIDi308051
KEGGirno:308051
UCSCiRGD:1306482 rat

Similar proteinsi

Entry informationi

Entry nameiRN146_RAT
AccessioniPrimary (citable) accession number: Q5XIK5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: November 23, 2004
Last modified: April 25, 2018
This is version 97 of the entry and version 1 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways

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