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Q9NTX7 (RN146_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase RNF146

EC=6.3.2.-
Alternative name(s):
Dactylidin
Iduna
RING finger protein 146
Gene names
Name:RNF146
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.12 Ref.13 Ref.14 Ref.15 Ref.17

Pathway

Protein modification; protein ubiquitination. Ref.12

Subunit structure

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. Ref.12 Ref.14 Ref.15

Subcellular location

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. Ref.1 Ref.14 Ref.15

Tissue specificity

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

Domain

The WWE domain mediates non-covalent PAR-binding. Ref.12

Post-translational modification

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. Ref.12 Ref.14 Ref.15

Involvement in disease

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

Miscellaneous

Was named dactylidin after the Greek term 'daktylidi' for ring, 'the thing around the finger' (Ref.1). Was named Iduna after the Norse goddess of protection and eternal youth (Ref.13).

Sequence similarities

Contains 1 RING-type zinc finger.

Contains 1 WWE domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NTX7-1)

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.
Isoform 2 (identifier: Q9NTX7-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 359359E3 ubiquitin-protein ligase RNF146
PRO_0000056107

Regions

Domain92 – 16877WWE
Zinc finger37 – 7539RING-type

Sites

Binding site1081iso-ADP-ribose adenine ring group
Binding site1111iso-ADP-ribose 5'-phosphate group
Binding site1151iso-ADP-ribose 5'-phosphate group
Binding site1451iso-ADP-ribose 1'-phosphate group
Binding site1541iso-ADP-ribose adenine ring group
Binding site1641iso-ADP-ribose 1'-phosphate group
Binding site1761iso-ADP-ribose 5'-phosphate group

Amino acid modifications

Cross-link85Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.15
Cross-link95Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.15
Cross-link131Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.15
Cross-link176Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.15

Natural variations

Alternative sequence11Missing in isoform 2.
VSP_012968
Natural variant251C → R.
Corresponds to variant rs10081141 [ dbSNP | Ensembl ].
VAR_065249

Experimental info

Mutagenesis541H → A: Partially suppression of WNT3A signaling and stabilization of AXIN1, TNKS and TNKS2 with or without WNT3A induction. No effect on TNKS1-binding. Ref.14
Mutagenesis1061W → A: No effect on Wnt signaling pathway. Ref.14
Mutagenesis1081Y → A: Loss of iso-ADP-ribose-binding. Ref.17
Mutagenesis1111R → A: Minor effect on iso-ADP-ribose-binding. Ref.17
Mutagenesis1151W → A: Strong decrease in iso-ADP-ribose-binding affinity. Ref.17
Mutagenesis1451Y → A: Loss of iso-ADP-ribose-binding. Ref.17
Mutagenesis1541Q → A: Loss of iso-ADP-ribose-binding affinity. Ref.17
Mutagenesis1631R → A: Abolishes the ability to recognize and bind PARsylated proteins. Ref.12
Mutagenesis1641R → A: Loss of iso-ADP-ribose-binding. Ref.17
Mutagenesis1761K → A: Minor effect on iso-ADP-ribose-binding. Ref.17
Sequence conflict691K → R in BAB55359. Ref.3
Sequence conflict741C → R in BAB55108. Ref.3
Sequence conflict1001G → E in CAG38545. Ref.4
Sequence conflict1661I → V in CAG38545. Ref.4
Sequence conflict2291L → S in BAB55108. Ref.3
Sequence conflict3291S → L in BAB55108. Ref.3

Secondary structure

.............................. 359
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 7337C410EDA30A7E

FASTA35938,950
        10         20         30         40         50         60 
MMAGCGEIDH SINMLPTNRK ANESCSNTAP SLTVPECAIC LQTCVHPVSL PCKHVFCYLC 

        70         80         90        100        110        120 
VKGASWLGKR CALCRQEIPE DFLDKPTLLS PEELKAASRG NGEYAWYYEG RNGWWQYDER 

       130        140        150        160        170        180 
TSRELEDAFS KGKKNTEMLI AGFLYVADLE NMVQYRRNEH GRRRKIKRDI IDIPKKGVAG 

       190        200        210        220        230        240 
LRLDCDANTV NLARESSADG ADSVSAQSGA SVQPLVSSVR PLTSVDGQLT SPATPSPDAS 

       250        260        270        280        290        300 
TSLEDSFAHL QLSGDNTAER SHRGEGEEDH ESPSSGRVPA PDTSIEETES DASSDSEDVS 

       310        320        330        340        350 
AVVAQHSLTQ QRLLVSNANQ TVPDRSDRSG TDRSVAGGGT VSVSVRSRRP DGQCTVTEV 

« Hide

Isoform 2 [UniParc].

Checksum: E46AA6522DA8D48B
Show »

FASTA35838,819

References

« Hide 'large scale' references
[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]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Genome-wide association study provides evidence for a breast cancer risk locus at 6q22.33."
Gold B., Kirchhoff T., Stefanov S., Lautenberger J., Viale A., Garber J., Friedman E., Narod S., Olshen A.B., Gregersen P., Kosarin K., Olsh A., Bergeron J., Ellis N.A., Klein R.J., Clark A.G., Norton L., Dean M., Boyd J., Offit K.
Proc. Natl. Acad. Sci. U.S.A. 105:4340-4345(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE INVOLVEMENT IN BREAST CANCER.
[9]"The 6q22.33 locus and breast cancer susceptibility."
Kirchhoff T., Chen Z.Q., Gold B., Pal P., Gaudet M.M., Kosarin K., Levine D.A., Gregersen P., Spencer S., Harlan M., Robson M., Klein R.J., Hudis C.A., Norton L., Dean M., Offit K.
Cancer Epidemiol. Biomarkers Prev. 18:2468-2475(2009) [PubMed] [Europe PMC] [Abstract]
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]"Ubiquitin ligase RNF146 regulates tankyrase and Axin to promote Wnt signaling."
Callow M.G., Tran H., Phu L., Lau T., Lee J., Sandoval W.N., Liu P.S., Bheddah S., Tao J., Lill J.R., Hongo J.A., Davis D., Kirkpatrick D.S., Polakis P., Costa M.
PLoS ONE 6:E22595-E22595(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS5136.1. [Q9NTX7-2]
CCDS56449.1. [Q9NTX7-1]
RefSeqNP_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]
UniGeneHs.267120.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2D8TNMR-A27-84[»]
3V3LX-ray1.65A/B100-184[»]
ProteinModelPortalQ9NTX7.
SMRQ9NTX7. Positions 24-84, 100-184.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123598. 25 interactions.
IntActQ9NTX7. 4 interactions.
MINTMINT-1370830.
STRING9606.ENSP00000309365.

PTM databases

PhosphoSiteQ9NTX7.

Polymorphism databases

DMDM60390653.

Proteomic databases

MaxQBQ9NTX7.
PaxDbQ9NTX7.
PRIDEQ9NTX7.

Protocols and materials databases

DNASU81847.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309649; ENSP00000309365; ENSG00000118518. [Q9NTX7-2]
ENST00000368314; ENSP00000357297; ENSG00000118518. [Q9NTX7-1]
ENST00000608991; ENSP00000477168; ENSG00000118518. [Q9NTX7-2]
ENST00000610153; ENSP00000476814; ENSG00000118518. [Q9NTX7-1]
GeneID81847.
KEGGhsa:81847.
UCSCuc003qat.3. human. [Q9NTX7-1]

Organism-specific databases

CTD81847.
GeneCardsGC06P127587.
HGNCHGNC:21336. RNF146.
HPAHPA027158.
HPA027209.
MIM612137. gene.
neXtProtNX_Q9NTX7.
PharmGKBPA134910489.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG298024.
HOVERGENHBG057514.
InParanoidQ9NTX7.
KOK15700.
OMARMAGCGE.
OrthoDBEOG7DVDC1.
PhylomeDBQ9NTX7.
TreeFamTF318925.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
UniPathwayUPA00143.

Gene expression databases

BgeeQ9NTX7.
CleanExHS_RNF146.
GenevestigatorQ9NTX7.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR004170. 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]
PfamPF02825. WWE. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
SM00678. WWE. 1 hit.
[Graphical view]
PROSITEPS50918. WWE. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9NTX7.
GeneWikiRNF146.
GenomeRNAi81847.
NextBio72150.
PROQ9NTX7.
SOURCESearch...

Entry information

Entry nameRN146_HUMAN
AccessionPrimary (citable) accession number: Q9NTX7
Secondary accession number(s): E1P572 expand/collapse secondary AC list , Q6FIB2, Q7L8H4, Q96K03, Q96T06, Q9NTX6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM