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E3 ubiquitin-protein ligase RNF146 (EC 2.3.2.27) (Dactylidin) (Iduna) (RING finger protein 146) (RING-type E3 ubiquitin transferase RNF146)

 RN146_HUMAN             Reviewed;         359 AA.
Q9NTX7; E1P572; Q6FIB2; Q7L8H4; Q96K03; Q96T06; Q9NTX6;
01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
22-NOV-2017, entry version 144.
RecName: Full=E3 ubiquitin-protein ligase RNF146;
EC=2.3.2.27;
AltName: Full=Dactylidin;
AltName: Full=Iduna;
AltName: Full=RING finger protein 146;
AltName: Full=RING-type E3 ubiquitin transferase RNF146 {ECO:0000305};
Name=RNF146;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND SUBCELLULAR LOCATION.
TISSUE=Brain;
PubMed=15813938; DOI=10.1111/j.1460-9568.2005.03977.x;
von Rotz R.C., Kins S., Hipfel R., von der Kammer H., Nitsch R.M.;
"The novel cytosolic RING finger protein dactylidin is up-regulated in
brains of patients with Alzheimer's disease.";
Eur. J. Neurosci. 21:1289-1298(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
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., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Placenta, and Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
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.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
POSSIBLE INVOLVEMENT IN BREAST CANCER.
PubMed=18326623; DOI=10.1073/pnas.0800441105;
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.;
"Genome-wide association study provides evidence for a breast cancer
risk locus at 6q22.33.";
Proc. Natl. Acad. Sci. U.S.A. 105:4340-4345(2008).
[9]
POSSIBLE INVOLVEMENT IN BREAST CANCER.
PubMed=19690183; DOI=10.1158/1055-9965.EPI-09-0151;
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.;
"The 6q22.33 locus and breast cancer susceptibility.";
Cancer Epidemiol. Biomarkers Prev. 18:2468-2475(2009).
[10]
POSSIBLE INVOLVEMENT IN BREAST CANCER.
PubMed=19517271; DOI=10.1007/s10689-009-9255-7;
Menachem T.D., Laitman Y., Kaufman B., Friedman E.;
"The RNF146 and ECHDC1 genes as candidates for inherited breast and
ovarian cancer in Jewish Ashkenazi women.";
Fam. Cancer 8:399-402(2009).
[11]
POSSIBLE INVOLVEMENT IN BREAST CANCER.
PubMed=21445572; DOI=10.1007/s10549-011-1459-5;
Peng S., Lu B., Ruan W., Zhu Y., Sheng H., Lai M.;
"Genetic polymorphisms and breast cancer risk: evidence from meta-
analyses, pooled analyses, and genome-wide association studies.";
Breast Cancer Res. Treat. 127:309-324(2011).
[12]
FUNCTION, PATHWAY, DOMAIN WWE, UBIQUITINATION, INTERACTION WITH AXIN1;
AXIN2; CASC3 AND BLZF1, AND MUTAGENESIS OF ARG-163.
PubMed=21478859; DOI=10.1038/ncb2222;
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.;
"RNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin
degradation and Wnt signalling.";
Nat. Cell Biol. 13:623-629(2011).
[13]
FUNCTION IN NEUROPROTECTION.
PubMed=21602803; DOI=10.1038/nm.2387;
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.;
"Iduna protects the brain from glutamate excitotoxicity and stroke by
interfering with poly(ADP-ribose) polymer-induced cell death.";
Nat. Med. 17:692-699(2011).
[14]
FUNCTION IN WNT SIGNALING, INTERACTION WITH AXIN1; DDB1; DHX15;
IQGAP1; LRPPRC; PARP1; PARP2; PRKDC; RUVBL2; TNKS1 AND TNKS2,
UBIQUITINATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-54 AND
TRP-106.
PubMed=21799911; DOI=10.1371/journal.pone.0022595;
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.;
"Ubiquitin ligase RNF146 regulates tankyrase and Axin to promote Wnt
signaling.";
PLoS ONE 6:E22595-E22595(2011).
[15]
FUNCTION IN DNA DAMAGE RESPONSE, HOMOOLIGOMERIZATION, INTERACTION WITH
HIST1H1C; IPO7; LIG3; NCL; PARP1; XRCC1; XRCC5 AND XRCC6, SUBCELLULAR
LOCATION, AND AUTOUBIQUITINATION AT LYS-85; LYS-95; LYS-131 AND
LYS-176.
PubMed=21825151; DOI=10.1073/pnas.1108799108;
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.;
"Iduna is a poly(ADP-ribose) (PAR)-dependent E3 ubiquitin ligase that
regulates DNA damage.";
Proc. Natl. Acad. Sci. U.S.A. 108:14103-14108(2011).
[16]
STRUCTURE BY NMR OF 24-84.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the RING domain of the human RING finger
protein 146.";
Submitted (JUN-2006) to the PDB data bank.
[17]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 100-184 IN COMPLEX WITH
ISO-ADP-RIBOSE, FUNCTION, AND MUTAGENESIS OF TYR-108; ARG-111;
TRP-115; TYR-145; GLN-154; ARG-164 AND LYS-176.
PubMed=22267412; DOI=10.1101/gad.182618.111;
Wang Z., Michaud G.A., Cheng Z., Zhang Y., Hinds T.R., Fan E.,
Cong F., Xu W.;
"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.";
Genes Dev. 26:235-240(2012).
-!- 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. {ECO:0000250, ECO:0000269|PubMed:21478859,
ECO:0000269|PubMed:21602803, ECO:0000269|PubMed:21799911,
ECO:0000269|PubMed:21825151, ECO:0000269|PubMed:22267412}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000269|PubMed:21478859}.
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:21478859, ECO:0000269|PubMed:21799911,
ECO:0000269|PubMed:21825151, ECO:0000269|PubMed:22267412}.
-!- INTERACTION:
Q8N6L0:CCDC155; NbExp=4; IntAct=EBI-11750630, EBI-749265;
O95271:TNKS; NbExp=4; IntAct=EBI-722397, EBI-1105254;
Q12933:TRAF2; NbExp=3; IntAct=EBI-722397, EBI-355744;
Q9UGJ1:TUBGCP4; NbExp=3; IntAct=EBI-722397, EBI-1052544;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9NTX7-1; Sequence=Displayed;
Name=2;
IsoId=Q9NTX7-2; Sequence=VSP_012968;
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Up-regulated in brains
from patients with Alzheimer disease.
-!- DOMAIN: The WWE domain mediates non-covalent PAR-binding.
{ECO:0000269|PubMed:21478859}.
-!- PTM: 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. {ECO:0000269|PubMed:21478859,
ECO:0000269|PubMed:21799911, ECO:0000269|PubMed:21825151}.
-!- DISEASE: Note=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'
(PubMed:15813938). Was named Iduna after the Norse goddess of
protection and eternal youth (PubMed:21602803).
{ECO:0000305|PubMed:15813938, ECO:0000305|PubMed:21602803}.
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EMBL; AJ315122; CAC85986.1; -; mRNA.
EMBL; AL136829; CAB66763.1; -; mRNA.
EMBL; AK027558; BAB55196.1; -; mRNA.
EMBL; AK027436; BAB55108.1; -; mRNA.
EMBL; AK027776; BAB55359.1; -; mRNA.
EMBL; CR533514; CAG38545.1; -; mRNA.
EMBL; AL109939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471051; EAW48109.1; -; Genomic_DNA.
EMBL; CH471051; EAW48111.1; -; Genomic_DNA.
EMBL; BC008235; AAH08235.1; -; mRNA.
CCDS; CCDS5136.1; -. [Q9NTX7-2]
CCDS; CCDS56449.1; -. [Q9NTX7-1]
RefSeq; NP_001229773.1; NM_001242844.1. [Q9NTX7-2]
RefSeq; NP_001229774.1; NM_001242845.1. [Q9NTX7-2]
RefSeq; NP_001229775.1; NM_001242846.1. [Q9NTX7-2]
RefSeq; NP_001229776.1; NM_001242847.1. [Q9NTX7-2]
RefSeq; NP_001229777.1; NM_001242848.1. [Q9NTX7-2]
RefSeq; NP_001229778.1; NM_001242849.1. [Q9NTX7-1]
RefSeq; NP_001229779.1; NM_001242850.1. [Q9NTX7-1]
RefSeq; NP_001229780.1; NM_001242851.1. [Q9NTX7-1]
RefSeq; NP_001229781.1; NM_001242852.1. [Q9NTX7-2]
RefSeq; NP_112225.2; NM_030963.3. [Q9NTX7-2]
RefSeq; XP_006715634.1; XM_006715571.3. [Q9NTX7-2]
RefSeq; XP_011534463.1; XM_011536161.2. [Q9NTX7-2]
RefSeq; XP_011534464.1; XM_011536162.2. [Q9NTX7-2]
RefSeq; XP_011534465.1; XM_011536163.2. [Q9NTX7-2]
RefSeq; XP_011534466.1; XM_011536164.2. [Q9NTX7-2]
RefSeq; XP_016866825.1; XM_017011336.1. [Q9NTX7-1]
RefSeq; XP_016866826.1; XM_017011337.1. [Q9NTX7-2]
RefSeq; XP_016866827.1; XM_017011338.1. [Q9NTX7-2]
RefSeq; XP_016866828.1; XM_017011339.1. [Q9NTX7-2]
RefSeq; XP_016866829.1; XM_017011340.1. [Q9NTX7-2]
RefSeq; XP_016866830.1; XM_017011341.1. [Q9NTX7-2]
RefSeq; XP_016866831.1; XM_017011342.1. [Q9NTX7-2]
RefSeq; XP_016866832.1; XM_017011343.1. [Q9NTX7-2]
UniGene; Hs.267120; -.
PDB; 2D8T; NMR; -; A=27-84.
PDB; 3V3L; X-ray; 1.65 A; A/B=100-184.
PDBsum; 2D8T; -.
PDBsum; 3V3L; -.
ProteinModelPortal; Q9NTX7; -.
SMR; Q9NTX7; -.
BioGrid; 123598; 39.
DIP; DIP-52730N; -.
IntAct; Q9NTX7; 11.
MINT; MINT-1370830; -.
STRING; 9606.ENSP00000357297; -.
iPTMnet; Q9NTX7; -.
PhosphoSitePlus; Q9NTX7; -.
BioMuta; RNF146; -.
DMDM; 60390653; -.
MaxQB; Q9NTX7; -.
PaxDb; Q9NTX7; -.
PeptideAtlas; Q9NTX7; -.
PRIDE; Q9NTX7; -.
DNASU; 81847; -.
Ensembl; ENST00000309649; ENSP00000309365; ENSG00000118518. [Q9NTX7-2]
Ensembl; ENST00000368314; ENSP00000357297; ENSG00000118518. [Q9NTX7-1]
Ensembl; ENST00000608991; ENSP00000477168; ENSG00000118518. [Q9NTX7-2]
Ensembl; ENST00000610153; ENSP00000476814; ENSG00000118518. [Q9NTX7-1]
Ensembl; ENST00000616343; ENSP00000479890; ENSG00000118518. [Q9NTX7-1]
GeneID; 81847; -.
KEGG; hsa:81847; -.
UCSC; uc003qav.4; human. [Q9NTX7-1]
CTD; 81847; -.
DisGeNET; 81847; -.
EuPathDB; HostDB:ENSG00000118518.15; -.
GeneCards; RNF146; -.
HGNC; HGNC:21336; RNF146.
HPA; HPA027158; -.
HPA; HPA027209; -.
MIM; 612137; gene.
neXtProt; NX_Q9NTX7; -.
OpenTargets; ENSG00000118518; -.
PharmGKB; PA134910489; -.
eggNOG; KOG0824; Eukaryota.
eggNOG; ENOG410ZTFC; LUCA.
GeneTree; ENSGT00390000000358; -.
HOVERGEN; HBG057514; -.
InParanoid; Q9NTX7; -.
KO; K15700; -.
OMA; RMAGCGE; -.
OrthoDB; EOG091G0Y4Y; -.
PhylomeDB; Q9NTX7; -.
TreeFam; TF318925; -.
Reactome; R-HSA-201681; TCF dependent signaling in response to WNT.
Reactome; R-HSA-4641257; Degradation of AXIN.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
UniPathway; UPA00143; -.
EvolutionaryTrace; Q9NTX7; -.
GeneWiki; RNF146; -.
GenomeRNAi; 81847; -.
PRO; PR:Q9NTX7; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000118518; -.
CleanEx; HS_RNF146; -.
ExpressionAtlas; Q9NTX7; baseline and differential.
Genevisible; Q9NTX7; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0072572; F:poly-ADP-D-ribose binding; IDA:UniProtKB.
GO; GO:0061630; F:ubiquitin protein ligase activity; TAS:Reactome.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0070936; P:protein K48-linked ubiquitination; IMP:UniProtKB.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0016055; P:Wnt signaling pathway; TAS:Reactome.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR033509; RNF146.
InterPro; IPR004170; WWE-dom.
InterPro; IPR018123; WWE-dom_subgr.
InterPro; IPR037197; WWE_dom_sf.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
PANTHER; PTHR13417:SF2; PTHR13417:SF2; 1.
Pfam; PF02825; WWE; 1.
SMART; SM00184; RING; 1.
SMART; SM00678; WWE; 1.
SUPFAM; SSF117839; SSF117839; 1.
PROSITE; PS50918; WWE; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Transferase; Ubl conjugation;
Ubl conjugation pathway; Wnt signaling pathway; Zinc; Zinc-finger.
CHAIN 1 359 E3 ubiquitin-protein ligase RNF146.
/FTId=PRO_0000056107.
DOMAIN 92 168 WWE. {ECO:0000255|PROSITE-
ProRule:PRU00248}.
ZN_FING 37 75 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
BINDING 108 108 iso-ADP-ribose adenine ring group.
{ECO:0000269|PubMed:22267412}.
BINDING 111 111 iso-ADP-ribose 5'-phosphate group.
{ECO:0000269|PubMed:22267412}.
BINDING 115 115 iso-ADP-ribose 5'-phosphate group.
{ECO:0000269|PubMed:22267412}.
BINDING 145 145 iso-ADP-ribose 1'-phosphate group.
{ECO:0000269|PubMed:22267412}.
BINDING 154 154 iso-ADP-ribose adenine ring group.
{ECO:0000269|PubMed:22267412}.
BINDING 164 164 iso-ADP-ribose 1'-phosphate group.
{ECO:0000269|PubMed:22267412}.
BINDING 176 176 iso-ADP-ribose 5'-phosphate group.
{ECO:0000269|PubMed:22267412}.
MOD_RES 290 290 Phosphoserine.
{ECO:0000250|UniProtKB:Q5XIK5}.
MOD_RES 294 294 Phosphoserine.
{ECO:0000250|UniProtKB:Q5XIK5}.
CROSSLNK 85 85 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:21825151}.
CROSSLNK 95 95 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:21825151}.
CROSSLNK 131 131 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:21825151}.
CROSSLNK 176 176 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:21825151}.
VAR_SEQ 1 1 Missing (in isoform 2).
{ECO:0000303|PubMed:11230166,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:15813938,
ECO:0000303|Ref.4}.
/FTId=VSP_012968.
VARIANT 25 25 C -> R (in dbSNP:rs10081141).
/FTId=VAR_065249.
MUTAGEN 54 54 H->A: Partially suppression of WNT3A
signaling and stabilization of AXIN1,
TNKS and TNKS2 with or without WNT3A
induction. No effect on TNKS1-binding.
{ECO:0000269|PubMed:21799911}.
MUTAGEN 106 106 W->A: No effect on Wnt signaling pathway.
{ECO:0000269|PubMed:21799911}.
MUTAGEN 108 108 Y->A: Loss of iso-ADP-ribose-binding.
{ECO:0000269|PubMed:22267412}.
MUTAGEN 111 111 R->A: Minor effect on iso-ADP-ribose-
binding. {ECO:0000269|PubMed:22267412}.
MUTAGEN 115 115 W->A: Strong decrease in iso-ADP-ribose-
binding affinity.
{ECO:0000269|PubMed:22267412}.
MUTAGEN 145 145 Y->A: Loss of iso-ADP-ribose-binding.
{ECO:0000269|PubMed:22267412}.
MUTAGEN 154 154 Q->A: Loss of iso-ADP-ribose-binding
affinity. {ECO:0000269|PubMed:22267412}.
MUTAGEN 163 163 R->A: Abolishes the ability to recognize
and bind PARsylated proteins.
{ECO:0000269|PubMed:21478859}.
MUTAGEN 164 164 R->A: Loss of iso-ADP-ribose-binding.
{ECO:0000269|PubMed:22267412}.
MUTAGEN 176 176 K->A: Minor effect on iso-ADP-ribose-
binding. {ECO:0000269|PubMed:22267412}.
CONFLICT 69 69 K -> R (in Ref. 3; BAB55359).
{ECO:0000305}.
CONFLICT 74 74 C -> R (in Ref. 3; BAB55108).
{ECO:0000305}.
CONFLICT 100 100 G -> E (in Ref. 4; CAG38545).
{ECO:0000305}.
CONFLICT 166 166 I -> V (in Ref. 4; CAG38545).
{ECO:0000305}.
CONFLICT 229 229 L -> S (in Ref. 3; BAB55108).
{ECO:0000305}.
CONFLICT 329 329 S -> L (in Ref. 3; BAB55108).
{ECO:0000305}.
STRAND 30 33 {ECO:0000244|PDB:2D8T}.
STRAND 38 43 {ECO:0000244|PDB:2D8T}.
STRAND 45 50 {ECO:0000244|PDB:2D8T}.
TURN 51 53 {ECO:0000244|PDB:2D8T}.
STRAND 54 57 {ECO:0000244|PDB:2D8T}.
HELIX 58 63 {ECO:0000244|PDB:2D8T}.
STRAND 68 70 {ECO:0000244|PDB:2D8T}.
STRAND 72 74 {ECO:0000244|PDB:2D8T}.
HELIX 80 83 {ECO:0000244|PDB:2D8T}.
STRAND 104 109 {ECO:0000244|PDB:3V3L}.
STRAND 111 116 {ECO:0000244|PDB:3V3L}.
HELIX 119 130 {ECO:0000244|PDB:3V3L}.
STRAND 134 140 {ECO:0000244|PDB:3V3L}.
STRAND 143 148 {ECO:0000244|PDB:3V3L}.
TURN 149 152 {ECO:0000244|PDB:3V3L}.
STRAND 153 159 {ECO:0000244|PDB:3V3L}.
STRAND 164 173 {ECO:0000244|PDB:3V3L}.
SEQUENCE 359 AA; 38950 MW; 7337C410EDA30A7E CRC64;
MMAGCGEIDH SINMLPTNRK ANESCSNTAP SLTVPECAIC LQTCVHPVSL PCKHVFCYLC
VKGASWLGKR CALCRQEIPE DFLDKPTLLS PEELKAASRG NGEYAWYYEG RNGWWQYDER
TSRELEDAFS KGKKNTEMLI AGFLYVADLE NMVQYRRNEH GRRRKIKRDI IDIPKKGVAG
LRLDCDANTV NLARESSADG ADSVSAQSGA SVQPLVSSVR PLTSVDGQLT SPATPSPDAS
TSLEDSFAHL QLSGDNTAER SHRGEGEEDH ESPSSGRVPA PDTSIEETES DASSDSEDVS
AVVAQHSLTQ QRLLVSNANQ TVPDRSDRSG TDRSVAGGGT VSVSVRSRRP DGQCTVTEV


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