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Protein

E3 ubiquitin-protein ligase RNF146

Gene

RNF146

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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, leading to their degradation. Different ubiquitin linkage types have been observed: TNKS2 undergoes ubiquitination at 'Lys-48' and 'Lys-63', while AXIN1 is only ubiquitinated at 'Lys-48'. 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 (By similarity). 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.By similarity5 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.1 Publication
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 sitei108iso-ADP-ribose adenine ring group1 Publication1
Binding sitei111iso-ADP-ribose 5'-phosphate group1 Publication1
Binding sitei115iso-ADP-ribose 5'-phosphate group1 Publication1
Binding sitei145iso-ADP-ribose 1'-phosphate group1 Publication1
Binding sitei154iso-ADP-ribose adenine ring group1 Publication1
Binding sitei164iso-ADP-ribose 1'-phosphate group1 Publication1
Binding sitei176iso-ADP-ribose 5'-phosphate group1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri37 – 75RING-typePROSITE-ProRule annotationAdd BLAST39

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • poly-ADP-D-ribose binding Source: UniProtKB
  • ubiquitin protein ligase activity Source: Reactome
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • positive regulation of canonical Wnt signaling pathway Source: UniProtKB
  • protein autoubiquitination Source: UniProtKB
  • protein K48-linked ubiquitination Source: UniProtKB
  • protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
  • Wnt signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway, Wnt signaling pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000118518-MONOMER.
ReactomeiR-HSA-201681. TCF dependent signaling in response to WNT.
R-HSA-4641257. Degradation of AXIN.
R-HSA-5689880. Ub-specific processing proteases.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF146 (EC:6.3.2.-)
Alternative name(s):
Dactylidin
Iduna
RING finger protein 146
Gene namesi
Name:RNF146
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:21336. RNF146.

Subcellular locationi

  • Cytoplasmcytosol
  • Nucleus

  • Note: Translocates to the nucleus after DNA damage, such as laser-induced DNA breaks, and concentrates at DNA breaks. This translocation requires PARP1 activation and PAR-binding.

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Defects in RNF146 are a cause of susceptibility to breast cancer.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi54H → A: Partially suppression of WNT3A signaling and stabilization of AXIN1, TNKS and TNKS2 with or without WNT3A induction. No effect on TNKS1-binding. 1 Publication1
Mutagenesisi106W → A: No effect on Wnt signaling pathway. 1 Publication1
Mutagenesisi108Y → A: Loss of iso-ADP-ribose-binding. 1 Publication1
Mutagenesisi111R → A: Minor effect on iso-ADP-ribose-binding. 1 Publication1
Mutagenesisi115W → A: Strong decrease in iso-ADP-ribose-binding affinity. 1 Publication1
Mutagenesisi145Y → A: Loss of iso-ADP-ribose-binding. 1 Publication1
Mutagenesisi154Q → A: Loss of iso-ADP-ribose-binding affinity. 1 Publication1
Mutagenesisi163R → A: Abolishes the ability to recognize and bind PARsylated proteins. 1 Publication1
Mutagenesisi164R → A: Loss of iso-ADP-ribose-binding. 1 Publication1
Mutagenesisi176K → A: Minor effect on iso-ADP-ribose-binding. 1 Publication1

Organism-specific databases

DisGeNETi81847.
OpenTargetsiENSG00000118518.
PharmGKBiPA134910489.

Polymorphism and mutation databases

BioMutaiRNF146.
DMDMi60390653.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000561071 – 359E3 ubiquitin-protein ligase RNF146Add BLAST359

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki85Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki95Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki131Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki176Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei290PhosphoserineBy similarity1
Modified residuei294PhosphoserineBy similarity1

Post-translational modificationi

Ubiquitinated; autoubiquitinated. Polyubiquitinated in the presence of UBE2D1, UBE2D2 and UBE2D3. Multimonoubiquitinated in the presence of UBE2E1. Not ubiquitinated in the presence of UBE2H, CDC34, UBE2L3, UBE2L6, nor UBE2C. In the absence of PAR, autoubiquitination occurs on Lys-85, Lys-95 and Lys-176 via 'Lys-11' and 'Lys-48' ubiquitin linkages. In the presence of PAR, Lys-131 and Lys-176 are ubiquitinated via 'Lys-6', 'Lys-33' and 'Lys-48' ubiquitin linkages. Autoubiquitination is enhanced upon PAR-binding.3 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9NTX7.
PaxDbiQ9NTX7.
PeptideAtlasiQ9NTX7.
PRIDEiQ9NTX7.

PTM databases

iPTMnetiQ9NTX7.
PhosphoSitePlusiQ9NTX7.

Expressioni

Tissue specificityi

Ubiquitously expressed. Up-regulated in brains from patients with Alzheimer disease.

Gene expression databases

BgeeiENSG00000118518.
CleanExiHS_RNF146.
ExpressionAtlasiQ9NTX7. baseline and differential.
GenevisibleiQ9NTX7. HS.

Organism-specific databases

HPAiHPA027158.
HPA027209.

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.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCDC155Q8N6L04EBI-11750630,EBI-749265
TRAF2Q129333EBI-722397,EBI-355744
TUBGCP4Q9UGJ13EBI-722397,EBI-1052544

Protein-protein interaction databases

BioGridi123598. 39 interactors.
DIPiDIP-52730N.
IntActiQ9NTX7. 8 interactors.
MINTiMINT-1370830.
STRINGi9606.ENSP00000357297.

Structurei

Secondary structure

1359
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi30 – 33Combined sources4
Beta strandi38 – 43Combined sources6
Beta strandi45 – 50Combined sources6
Turni51 – 53Combined sources3
Beta strandi54 – 57Combined sources4
Helixi58 – 63Combined sources6
Beta strandi68 – 70Combined sources3
Beta strandi72 – 74Combined sources3
Helixi80 – 83Combined sources4
Beta strandi104 – 109Combined sources6
Beta strandi111 – 116Combined sources6
Helixi119 – 130Combined sources12
Beta strandi134 – 140Combined sources7
Beta strandi143 – 148Combined sources6
Turni149 – 152Combined sources4
Beta strandi153 – 159Combined sources7
Beta strandi164 – 173Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2D8TNMR-A27-84[»]
3V3LX-ray1.65A/B100-184[»]
ProteinModelPortaliQ9NTX7.
SMRiQ9NTX7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NTX7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini92 – 168WWEPROSITE-ProRule annotationAdd BLAST77

Domaini

The WWE domain mediates non-covalent PAR-binding.1 Publication

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
Contains 1 WWE domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri37 – 75RING-typePROSITE-ProRule annotationAdd BLAST39

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0824. Eukaryota.
ENOG410ZTFC. LUCA.
GeneTreeiENSGT00390000000358.
HOVERGENiHBG057514.
InParanoidiQ9NTX7.
KOiK15700.
OMAiRMAGCGE.
OrthoDBiEOG091G0Y4Y.
PhylomeDBiQ9NTX7.
TreeFamiTF318925.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR033509. RNF146.
IPR004170. WWE-dom.
IPR018123. WWE-dom_subgr.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR13417. PTHR13417. 1 hit.
PfamiPF02825. WWE. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00678. WWE. 1 hit.
[Graphical view]
PROSITEiPS50918. WWE. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q9NTX7-1) [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
MMAGCGEIDH SINMLPTNRK ANESCSNTAP SLTVPECAIC LQTCVHPVSL
60 70 80 90 100
PCKHVFCYLC VKGASWLGKR CALCRQEIPE DFLDKPTLLS PEELKAASRG
110 120 130 140 150
NGEYAWYYEG RNGWWQYDER TSRELEDAFS KGKKNTEMLI AGFLYVADLE
160 170 180 190 200
NMVQYRRNEH GRRRKIKRDI IDIPKKGVAG LRLDCDANTV NLARESSADG
210 220 230 240 250
ADSVSAQSGA SVQPLVSSVR PLTSVDGQLT SPATPSPDAS TSLEDSFAHL
260 270 280 290 300
QLSGDNTAER SHRGEGEEDH ESPSSGRVPA PDTSIEETES DASSDSEDVS
310 320 330 340 350
AVVAQHSLTQ QRLLVSNANQ TVPDRSDRSG TDRSVAGGGT VSVSVRSRRP

DGQCTVTEV
Length:359
Mass (Da):38,950
Last modified:October 1, 2000 - v1
Checksum:i7337C410EDA30A7E
GO
Isoform 2 (identifier: Q9NTX7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: Missing.

Show »
Length:358
Mass (Da):38,819
Checksum:iE46AA6522DA8D48B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti69K → R in BAB55359 (PubMed:14702039).Curated1
Sequence conflicti74C → R in BAB55108 (PubMed:14702039).Curated1
Sequence conflicti100G → E in CAG38545 (Ref. 4) Curated1
Sequence conflicti166I → V in CAG38545 (Ref. 4) Curated1
Sequence conflicti229L → S in BAB55108 (PubMed:14702039).Curated1
Sequence conflicti329S → L in BAB55108 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06524925C → R.Corresponds to variant rs10081141dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0129681Missing in isoform 2. 5 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ315122 mRNA. Translation: CAC85986.1.
AL136829 mRNA. Translation: CAB66763.1.
AK027558 mRNA. Translation: BAB55196.1.
AK027436 mRNA. Translation: BAB55108.1.
AK027776 mRNA. Translation: BAB55359.1.
CR533514 mRNA. Translation: CAG38545.1.
AL109939 Genomic DNA. Translation: CAB76254.1.
AL109939 Genomic DNA. Translation: CAB76255.1.
CH471051 Genomic DNA. Translation: EAW48109.1.
CH471051 Genomic DNA. Translation: EAW48111.1.
BC008235 mRNA. Translation: AAH08235.1.
CCDSiCCDS5136.1. [Q9NTX7-2]
CCDS56449.1. [Q9NTX7-1]
RefSeqiNP_001229773.1. NM_001242844.1. [Q9NTX7-2]
NP_001229774.1. NM_001242845.1. [Q9NTX7-2]
NP_001229775.1. NM_001242846.1. [Q9NTX7-2]
NP_001229776.1. NM_001242847.1. [Q9NTX7-2]
NP_001229777.1. NM_001242848.1. [Q9NTX7-2]
NP_001229778.1. NM_001242849.1. [Q9NTX7-1]
NP_001229779.1. NM_001242850.1. [Q9NTX7-1]
NP_001229780.1. NM_001242851.1. [Q9NTX7-1]
NP_001229781.1. NM_001242852.1. [Q9NTX7-2]
NP_112225.2. NM_030963.3. [Q9NTX7-2]
XP_006715634.1. XM_006715571.3. [Q9NTX7-2]
XP_011534463.1. XM_011536161.2. [Q9NTX7-2]
XP_011534464.1. XM_011536162.2. [Q9NTX7-2]
XP_011534465.1. XM_011536163.2. [Q9NTX7-2]
XP_011534466.1. XM_011536164.2. [Q9NTX7-2]
XP_016866825.1. XM_017011336.1. [Q9NTX7-1]
XP_016866826.1. XM_017011337.1. [Q9NTX7-2]
XP_016866827.1. XM_017011338.1. [Q9NTX7-2]
XP_016866828.1. XM_017011339.1. [Q9NTX7-2]
XP_016866829.1. XM_017011340.1. [Q9NTX7-2]
XP_016866830.1. XM_017011341.1. [Q9NTX7-2]
XP_016866831.1. XM_017011342.1. [Q9NTX7-2]
XP_016866832.1. XM_017011343.1. [Q9NTX7-2]
UniGeneiHs.267120.

Genome annotation databases

EnsembliENST00000309649; ENSP00000309365; ENSG00000118518. [Q9NTX7-2]
ENST00000368314; ENSP00000357297; ENSG00000118518. [Q9NTX7-1]
ENST00000608991; ENSP00000477168; ENSG00000118518. [Q9NTX7-2]
ENST00000610153; ENSP00000476814; ENSG00000118518. [Q9NTX7-1]
ENST00000616343; ENSP00000479890; ENSG00000118518. [Q9NTX7-1]
GeneIDi81847.
KEGGihsa:81847.
UCSCiuc003qav.4. human. [Q9NTX7-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ315122 mRNA. Translation: CAC85986.1.
AL136829 mRNA. Translation: CAB66763.1.
AK027558 mRNA. Translation: BAB55196.1.
AK027436 mRNA. Translation: BAB55108.1.
AK027776 mRNA. Translation: BAB55359.1.
CR533514 mRNA. Translation: CAG38545.1.
AL109939 Genomic DNA. Translation: CAB76254.1.
AL109939 Genomic DNA. Translation: CAB76255.1.
CH471051 Genomic DNA. Translation: EAW48109.1.
CH471051 Genomic DNA. Translation: EAW48111.1.
BC008235 mRNA. Translation: AAH08235.1.
CCDSiCCDS5136.1. [Q9NTX7-2]
CCDS56449.1. [Q9NTX7-1]
RefSeqiNP_001229773.1. NM_001242844.1. [Q9NTX7-2]
NP_001229774.1. NM_001242845.1. [Q9NTX7-2]
NP_001229775.1. NM_001242846.1. [Q9NTX7-2]
NP_001229776.1. NM_001242847.1. [Q9NTX7-2]
NP_001229777.1. NM_001242848.1. [Q9NTX7-2]
NP_001229778.1. NM_001242849.1. [Q9NTX7-1]
NP_001229779.1. NM_001242850.1. [Q9NTX7-1]
NP_001229780.1. NM_001242851.1. [Q9NTX7-1]
NP_001229781.1. NM_001242852.1. [Q9NTX7-2]
NP_112225.2. NM_030963.3. [Q9NTX7-2]
XP_006715634.1. XM_006715571.3. [Q9NTX7-2]
XP_011534463.1. XM_011536161.2. [Q9NTX7-2]
XP_011534464.1. XM_011536162.2. [Q9NTX7-2]
XP_011534465.1. XM_011536163.2. [Q9NTX7-2]
XP_011534466.1. XM_011536164.2. [Q9NTX7-2]
XP_016866825.1. XM_017011336.1. [Q9NTX7-1]
XP_016866826.1. XM_017011337.1. [Q9NTX7-2]
XP_016866827.1. XM_017011338.1. [Q9NTX7-2]
XP_016866828.1. XM_017011339.1. [Q9NTX7-2]
XP_016866829.1. XM_017011340.1. [Q9NTX7-2]
XP_016866830.1. XM_017011341.1. [Q9NTX7-2]
XP_016866831.1. XM_017011342.1. [Q9NTX7-2]
XP_016866832.1. XM_017011343.1. [Q9NTX7-2]
UniGeneiHs.267120.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2D8TNMR-A27-84[»]
3V3LX-ray1.65A/B100-184[»]
ProteinModelPortaliQ9NTX7.
SMRiQ9NTX7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123598. 39 interactors.
DIPiDIP-52730N.
IntActiQ9NTX7. 8 interactors.
MINTiMINT-1370830.
STRINGi9606.ENSP00000357297.

PTM databases

iPTMnetiQ9NTX7.
PhosphoSitePlusiQ9NTX7.

Polymorphism and mutation databases

BioMutaiRNF146.
DMDMi60390653.

Proteomic databases

MaxQBiQ9NTX7.
PaxDbiQ9NTX7.
PeptideAtlasiQ9NTX7.
PRIDEiQ9NTX7.

Protocols and materials databases

DNASUi81847.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000309649; ENSP00000309365; ENSG00000118518. [Q9NTX7-2]
ENST00000368314; ENSP00000357297; ENSG00000118518. [Q9NTX7-1]
ENST00000608991; ENSP00000477168; ENSG00000118518. [Q9NTX7-2]
ENST00000610153; ENSP00000476814; ENSG00000118518. [Q9NTX7-1]
ENST00000616343; ENSP00000479890; ENSG00000118518. [Q9NTX7-1]
GeneIDi81847.
KEGGihsa:81847.
UCSCiuc003qav.4. human. [Q9NTX7-1]

Organism-specific databases

CTDi81847.
DisGeNETi81847.
GeneCardsiRNF146.
HGNCiHGNC:21336. RNF146.
HPAiHPA027158.
HPA027209.
MIMi612137. gene.
neXtProtiNX_Q9NTX7.
OpenTargetsiENSG00000118518.
PharmGKBiPA134910489.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0824. Eukaryota.
ENOG410ZTFC. LUCA.
GeneTreeiENSGT00390000000358.
HOVERGENiHBG057514.
InParanoidiQ9NTX7.
KOiK15700.
OMAiRMAGCGE.
OrthoDBiEOG091G0Y4Y.
PhylomeDBiQ9NTX7.
TreeFamiTF318925.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciZFISH:ENSG00000118518-MONOMER.
ReactomeiR-HSA-201681. TCF dependent signaling in response to WNT.
R-HSA-4641257. Degradation of AXIN.
R-HSA-5689880. Ub-specific processing proteases.

Miscellaneous databases

EvolutionaryTraceiQ9NTX7.
GeneWikiiRNF146.
GenomeRNAii81847.
PROiQ9NTX7.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000118518.
CleanExiHS_RNF146.
ExpressionAtlasiQ9NTX7. baseline and differential.
GenevisibleiQ9NTX7. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR033509. RNF146.
IPR004170. WWE-dom.
IPR018123. WWE-dom_subgr.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR13417. PTHR13417. 1 hit.
PfamiPF02825. WWE. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00678. WWE. 1 hit.
[Graphical view]
PROSITEiPS50918. WWE. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRN146_HUMAN
AccessioniPrimary (citable) accession number: Q9NTX7
Secondary accession number(s): E1P572
, Q6FIB2, Q7L8H4, Q96K03, Q96T06, Q9NTX6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: October 1, 2000
Last modified: November 30, 2016
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Was named dactylidin after the Greek term 'daktylidi' for ring, 'the thing around the finger' (PubMed:15813938). Was named Iduna after the Norse goddess of protection and eternal youth (PubMed:21602803).2 Publications

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.