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Q9NTX7

- RN146_HUMAN

UniProt

Q9NTX7 - RN146_HUMAN

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
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei108 – 1081iso-ADP-ribose adenine ring group1 Publication
    Binding sitei111 – 1111iso-ADP-ribose 5'-phosphate group1 Publication
    Binding sitei115 – 1151iso-ADP-ribose 5'-phosphate group1 Publication
    Binding sitei145 – 1451iso-ADP-ribose 1'-phosphate group1 Publication
    Binding sitei154 – 1541iso-ADP-ribose adenine ring group1 Publication
    Binding sitei164 – 1641iso-ADP-ribose 1'-phosphate group1 Publication
    Binding sitei176 – 1761iso-ADP-ribose 5'-phosphate group1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri37 – 7539RING-typePROSITE-ProRule annotationAdd
    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

    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.

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. nucleus Source: UniProtKB-SubCell

    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.4 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NTX7.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini92 – 16877WWEPROSITE-ProRule annotationAdd
    BLAST

    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)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri37 – 7539RING-typePROSITE-ProRule annotationAdd
    BLAST

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti69 – 691K → R in BAB55359. (PubMed:14702039)Curated
    Sequence conflicti74 – 741C → R in BAB55108. (PubMed:14702039)Curated
    Sequence conflicti100 – 1001G → E in CAG38545. 1 PublicationCurated
    Sequence conflicti166 – 1661I → V in CAG38545. 1 PublicationCurated
    Sequence conflicti229 – 2291L → S in BAB55108. (PubMed:14702039)Curated
    Sequence conflicti329 – 3291S → L in BAB55108. (PubMed:14702039)Curated

    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. 5 PublicationsVSP_012968

    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

    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: October 1, 2014
    This is version 115 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

    External Data

    Dasty 3