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Q9NTX7

- RN146_HUMAN

UniProt

Q9NTX7 - RN146_HUMAN

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Protein

E3 ubiquitin-protein ligase RNF146

Gene
RNF146
Organism
Homo sapiens (Human)
Status
Reviewed - 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.5 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei108 – 1081iso-ADP-ribose adenine ring group
Binding sitei111 – 1111iso-ADP-ribose 5'-phosphate group
Binding sitei115 – 1151iso-ADP-ribose 5'-phosphate group
Binding sitei145 – 1451iso-ADP-ribose 1'-phosphate group
Binding sitei154 – 1541iso-ADP-ribose adenine ring group
Binding sitei164 – 1641iso-ADP-ribose 1'-phosphate group
Binding sitei176 – 1761iso-ADP-ribose 5'-phosphate group

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri37 – 7539RING-typeAdd
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. poly-ADP-D-ribose binding Source: UniProtKB
  3. protein binding Source: UniProtKB
  4. ubiquitin-protein transferase activity Source: UniProtKB
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. positive regulation of canonical Wnt signaling pathway Source: UniProtKB
  2. protein autoubiquitination Source: UniProtKB
  3. protein K48-linked ubiquitination Source: UniProtKB
  4. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
  5. Wnt signaling pathway Source: UniProtKB-KW
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

ReactomeiREACT_200766. degradation of AXIN.
REACT_200777. TCF dependent signaling in response to WNT.
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
ProteomesiUP000005640: 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.3 Publications

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi54 – 541H → A: Partially suppression of WNT3A signaling and stabilization of AXIN1, TNKS and TNKS2 with or without WNT3A induction. No effect on TNKS1-binding. 1 Publication
Mutagenesisi106 – 1061W → A: No effect on Wnt signaling pathway. 1 Publication
Mutagenesisi108 – 1081Y → A: Loss of iso-ADP-ribose-binding. 1 Publication
Mutagenesisi111 – 1111R → A: Minor effect on iso-ADP-ribose-binding. 1 Publication
Mutagenesisi115 – 1151W → A: Strong decrease in iso-ADP-ribose-binding affinity. 1 Publication
Mutagenesisi145 – 1451Y → A: Loss of iso-ADP-ribose-binding. 1 Publication
Mutagenesisi154 – 1541Q → A: Loss of iso-ADP-ribose-binding affinity. 1 Publication
Mutagenesisi163 – 1631R → A: Abolishes the ability to recognize and bind PARsylated proteins. 1 Publication
Mutagenesisi164 – 1641R → A: Loss of iso-ADP-ribose-binding. 1 Publication
Mutagenesisi176 – 1761K → A: Minor effect on iso-ADP-ribose-binding. 1 Publication

Organism-specific databases

PharmGKBiPA134910489.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 359359E3 ubiquitin-protein ligase RNF146PRO_0000056107Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki85 – 85Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki95 – 95Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki131 – 131Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki176 – 176Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

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, Ubl conjugation

Proteomic databases

MaxQBiQ9NTX7.
PaxDbiQ9NTX7.
PRIDEiQ9NTX7.

PTM databases

PhosphoSiteiQ9NTX7.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9NTX7.
CleanExiHS_RNF146.
GenevestigatoriQ9NTX7.

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.3 Publications

Protein-protein interaction databases

BioGridi123598. 25 interactions.
IntActiQ9NTX7. 4 interactions.
MINTiMINT-1370830.
STRINGi9606.ENSP00000309365.

Structurei

Secondary structure

1
359
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 334
Beta strandi38 – 436
Beta strandi45 – 506
Turni51 – 533
Beta strandi54 – 574
Helixi58 – 636
Beta strandi68 – 703
Beta strandi72 – 743
Helixi80 – 834
Beta strandi104 – 1096
Beta strandi111 – 1166
Helixi119 – 13012
Beta strandi134 – 1407
Beta strandi143 – 1486
Turni149 – 1524
Beta strandi153 – 1597
Beta strandi164 – 17310

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D8TNMR-A27-84[»]
3V3LX-ray1.65A/B100-184[»]
ProteinModelPortaliQ9NTX7.
SMRiQ9NTX7. Positions 24-84, 100-184.

Miscellaneous databases

EvolutionaryTraceiQ9NTX7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini92 – 16877WWEAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 WWE domain.

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG298024.
HOVERGENiHBG057514.
InParanoidiQ9NTX7.
KOiK15700.
OMAiRMAGCGE.
OrthoDBiEOG7DVDC1.
PhylomeDBiQ9NTX7.
TreeFamiTF318925.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR004170. WWE-dom.
IPR018123. WWE-dom_subgr.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF02825. WWE. 1 hit.
PF00097. zf-C3HC4. 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. Align

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

MMAGCGEIDH SINMLPTNRK ANESCSNTAP SLTVPECAIC LQTCVHPVSL    50
PCKHVFCYLC VKGASWLGKR CALCRQEIPE DFLDKPTLLS PEELKAASRG 100
NGEYAWYYEG RNGWWQYDER TSRELEDAFS KGKKNTEMLI AGFLYVADLE 150
NMVQYRRNEH GRRRKIKRDI IDIPKKGVAG LRLDCDANTV NLARESSADG 200
ADSVSAQSGA SVQPLVSSVR PLTSVDGQLT SPATPSPDAS TSLEDSFAHL 250
QLSGDNTAER SHRGEGEEDH ESPSSGRVPA PDTSIEETES DASSDSEDVS 300
AVVAQHSLTQ QRLLVSNANQ TVPDRSDRSG TDRSVAGGGT VSVSVRSRRP 350
DGQCTVTEV 359
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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti25 – 251C → R.
Corresponds to variant rs10081141 [ dbSNP | Ensembl ].
VAR_065249

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11Missing in isoform 2. VSP_012968

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 691K → R in BAB55359. 1 Publication
Sequence conflicti74 – 741C → R in BAB55108. 1 Publication
Sequence conflicti100 – 1001G → E in CAG38545. 1 Publication
Sequence conflicti166 – 1661I → V in CAG38545. 1 Publication
Sequence conflicti229 – 2291L → S in BAB55108. 1 Publication
Sequence conflicti329 – 3291S → L in BAB55108. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_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_006715571.1. [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]
GeneIDi81847.
KEGGihsa:81847.
UCSCiuc003qat.3. human. [Q9NTX7-1]

Polymorphism databases

DMDMi60390653.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS5136.1. [Q9NTX7-2 ]
CCDS56449.1. [Q9NTX7-1 ]
RefSeqi NP_001229773.1. NM_001242844.1. [Q9NTX7-2 ]
NP_001229774.1. NM_001242845.1. [Q9NTX7-2 ]
NP_001229775.1. NM_001242846.1. [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_006715571.1. [Q9NTX7-2 ]
UniGenei Hs.267120.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2D8T NMR - A 27-84 [» ]
3V3L X-ray 1.65 A/B 100-184 [» ]
ProteinModelPortali Q9NTX7.
SMRi Q9NTX7. Positions 24-84, 100-184.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123598. 25 interactions.
IntActi Q9NTX7. 4 interactions.
MINTi MINT-1370830.
STRINGi 9606.ENSP00000309365.

PTM databases

PhosphoSitei Q9NTX7.

Polymorphism databases

DMDMi 60390653.

Proteomic databases

MaxQBi Q9NTX7.
PaxDbi Q9NTX7.
PRIDEi Q9NTX7.

Protocols and materials databases

DNASUi 81847.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000309649 ; ENSP00000309365 ; ENSG00000118518 . [Q9NTX7-2 ]
ENST00000368314 ; ENSP00000357297 ; ENSG00000118518 . [Q9NTX7-1 ]
ENST00000608991 ; ENSP00000477168 ; ENSG00000118518 . [Q9NTX7-2 ]
ENST00000610153 ; ENSP00000476814 ; ENSG00000118518 . [Q9NTX7-1 ]
GeneIDi 81847.
KEGGi hsa:81847.
UCSCi uc003qat.3. human. [Q9NTX7-1 ]

Organism-specific databases

CTDi 81847.
GeneCardsi GC06P127587.
HGNCi HGNC:21336. RNF146.
HPAi HPA027158.
HPA027209.
MIMi 612137. gene.
neXtProti NX_Q9NTX7.
PharmGKBi PA134910489.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG298024.
HOVERGENi HBG057514.
InParanoidi Q9NTX7.
KOi K15700.
OMAi RMAGCGE.
OrthoDBi EOG7DVDC1.
PhylomeDBi Q9NTX7.
TreeFami TF318925.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_200766. degradation of AXIN.
REACT_200777. TCF dependent signaling in response to WNT.

Miscellaneous databases

EvolutionaryTracei Q9NTX7.
GeneWikii RNF146.
GenomeRNAii 81847.
NextBioi 72150.
PROi Q9NTX7.
SOURCEi Search...

Gene expression databases

Bgeei Q9NTX7.
CleanExi HS_RNF146.
Genevestigatori Q9NTX7.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR004170. WWE-dom.
IPR018123. WWE-dom_subgr.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view ]
Pfami PF02825. WWE. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view ]
SMARTi SM00184. RING. 1 hit.
SM00678. WWE. 1 hit.
[Graphical view ]
PROSITEi PS50918. WWE. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The novel cytosolic RING finger protein dactylidin is up-regulated in brains of patients with Alzheimer's disease."
    von Rotz R.C., Kins S., Hipfel R., von der Kammer H., Nitsch R.M.
    Eur. J. Neurosci. 21:1289-1298(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION.
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Testis.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Placenta and Teratocarcinoma.
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  5. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Eye.
  8. Cited for: POSSIBLE INVOLVEMENT IN BREAST CANCER.
  9. Cited for: POSSIBLE INVOLVEMENT IN BREAST CANCER.
  10. "The RNF146 and ECHDC1 genes as candidates for inherited breast and ovarian cancer in Jewish Ashkenazi women."
    Menachem T.D., Laitman Y., Kaufman B., Friedman E.
    Fam. Cancer 8:399-402(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE INVOLVEMENT IN BREAST CANCER.
  11. "Genetic polymorphisms and breast cancer risk: evidence from meta-analyses, pooled analyses, and genome-wide association studies."
    Peng S., Lu B., Ruan W., Zhu Y., Sheng H., Lai M.
    Breast Cancer Res. Treat. 127:309-324(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE INVOLVEMENT IN BREAST CANCER.
  12. "RNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin degradation and Wnt signalling."
    Zhang Y., Liu S., Mickanin C., Feng Y., Charlat O., Michaud G.A., Schirle M., Shi X., Hild M., Bauer A., Myer V.E., Finan P.M., Porter J.A., Huang S.M., Cong F.
    Nat. Cell Biol. 13:623-629(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PATHWAY, DOMAIN WWE, UBIQUITINATION, INTERACTION WITH AXIN1; AXIN2; CASC3 AND BLZF1, MUTAGENESIS OF ARG-163.
  13. "Iduna protects the brain from glutamate excitotoxicity and stroke by interfering with poly(ADP-ribose) polymer-induced cell death."
    Andrabi S.A., Kang H.C., Haince J.F., Lee Y.I., Zhang J., Chi Z., West A.B., Koehler R.C., Poirier G.G., Dawson T.M., Dawson V.L.
    Nat. Med. 17:692-699(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NEUROPROTECTION.
  14. Cited for: FUNCTION IN WNT SIGNALING, INTERACTION WITH AXIN1; DDB1; DHX15; IQGAP1; LRPPRC; PARP1; PARP2; PRKDC; RUVBL2; TNKS1 AND TNKS2, UBIQUITINATION, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-54 AND TRP-106.
  15. "Iduna is a poly(ADP-ribose) (PAR)-dependent E3 ubiquitin ligase that regulates DNA damage."
    Kang H.C., Lee Y.I., Shin J.H., Andrabi S.A., Chi Z., Gagne J.P., Lee Y., Ko H.S., Lee B.D., Poirier G.G., Dawson V.L., Dawson T.M.
    Proc. Natl. Acad. Sci. U.S.A. 108:14103-14108(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DNA DAMAGE RESPONSE, HOMOOLIGOMERIZATION, INTERACTION WITH HIST1H1C; IPO7; LIG3; NCL; PARP1; XRCC1; XRCC5 AND XRCC6, SUBCELLULAR LOCATION, AUTOUBIQUITINATION AT LYS-85; LYS-95; LYS-131 AND LYS-176.
  16. "Solution structure of the RING domain of the human RING finger protein 146."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUN-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 24-84.
  17. "Recognition of the iso-ADP-ribose moiety in poly(ADP-ribose) by WWE domains suggests a general mechanism for poly(ADP-ribosyl)ation-dependent ubiquitination."
    Wang Z., Michaud G.A., Cheng Z., Zhang Y., Hinds T.R., Fan E., Cong F., Xu W.
    Genes Dev. 26:235-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 100-184 IN COMPLEX WITH ISO-ADP-RIBOSE, FUNCTION, MUTAGENESIS OF TYR-108; ARG-111; TRP-115; TYR-145; GLN-154; ARG-164 AND LYS-176.

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: September 3, 2014
This is version 114 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' (1 Publication). Was named Iduna after the Norse goddess of protection and eternal youth (1 Publication).

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

External Data

Dasty 3

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