RN146_MOUSE
ID RN146_MOUSE Reviewed; 359 AA.
AC Q9CZW6; E0CX97; Q3TF93; Q3U6Y7;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=E3 ubiquitin-protein ligase RNF146;
DE EC=2.3.2.27;
DE AltName: Full=Iduna;
DE AltName: Full=RING finger protein 146;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF146 {ECO:0000305};
GN Name=Rnf146;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryo, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=15813938; DOI=10.1111/j.1460-9568.2005.03977.x;
RA von Rotz R.C., Kins S., Hipfel R., von der Kammer H., Nitsch R.M.;
RT "The novel cytosolic RING finger protein dactylidin is up-regulated in
RT brains of patients with Alzheimer's disease.";
RL Eur. J. Neurosci. 21:1289-1298(2005).
RN [5]
RP FUNCTION IN NEUROPROTECTION, POLY(ADP-RIBOSE)-BINDING, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, INDUCTION, AND MUTAGENESIS OF TYR-156 AND
RP ARG-157.
RX PubMed=21602803; DOI=10.1038/nm.2387;
RA Andrabi S.A., Kang H.C., Haince J.F., Lee Y.I., Zhang J., Chi Z.,
RA West A.B., Koehler R.C., Poirier G.G., Dawson T.M., Dawson V.L.;
RT "Iduna protects the brain from glutamate excitotoxicity and stroke by
RT interfering with poly(ADP-ribose) polymer-induced cell death.";
RL Nat. Med. 17:692-699(2011).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF HIS-55; CYS-61; TYR-156 AND ARG-157.
RX PubMed=21825151; DOI=10.1073/pnas.1108799108;
RA Kang H.C., Lee Y.I., Shin J.H., Andrabi S.A., Chi Z., Gagne J.P., Lee Y.,
RA Ko H.S., Lee B.D., Poirier G.G., Dawson V.L., Dawson T.M.;
RT "Iduna is a poly(ADP-ribose) (PAR)-dependent E3 ubiquitin ligase that
RT regulates DNA damage.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:14103-14108(2011).
RN [7]
RP STRUCTURE BY NMR OF 83-179.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of WWE domain in BAB28015.";
RL Submitted (OCT-2004) to the PDB data bank.
CC -!- FUNCTION: E3 ubiquitin-protein ligase that specifically binds poly-ADP-
CC ribosylated (PARsylated) proteins and mediates their ubiquitination and
CC subsequent degradation. May regulate many important biological
CC processes, such as cell survival and DNA damage response. Acts as an
CC activator of the Wnt signaling pathway by mediating the ubiquitination
CC of PARsylated AXIN1 and AXIN2, 2 key components of the beta-catenin
CC destruction complex. Acts in cooperation with tankyrase proteins (TNKS
CC and TNKS2), which mediate PARsylation of target proteins AXIN1, AXIN2,
CC BLZF1, CASC3, TNKS and TNKS2. Recognizes and binds tankyrase-dependent
CC PARsylated proteins via its WWE domain and mediates their
CC ubiquitination (By similarity). May regulate TNKS and TNKS2 subcellular
CC location, preventing aggregation at a centrosomal location.
CC Neuroprotective protein. Protects the brain against N-methyl-D-
CC aspartate (NMDA) receptor-mediated glutamate excitotoxicity and
CC ischemia, by interfering with PAR-induced cell death, called
CC parthanatos. Prevents nuclear translocation of AIFM1 in a PAR-binding
CC dependent manner. Does not affect PARP1 activation (By similarity).
CC Protects against cell death induced by DNA damaging agents, such as N-
CC methyl-N-nitro-N-nitrosoguanidine (MNNG) and rescues cells from G1
CC arrest. Promotes cell survival after gamma-irradiation. Facilitates DNA
CC repair. Neuroprotective protein. Protects the brain against N-methyl-D-
CC aspartate (NMDA) receptor-mediated glutamate excitotoxicity and
CC ischemia, by interfering with PAR-induced cell death, called
CC parthanatos. Prevents nuclear translocation of AIFM1 in a PAR-binding
CC dependent manner. Does not affect PARP1 activation. {ECO:0000250,
CC ECO:0000269|PubMed:21602803, ECO:0000269|PubMed:21825151}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Can form homooligomers. Interacts with PARsylated AXIN1,
CC AXIN2, BLZF1, CASC3, H1-2, IPO7, LIG3, NCL, PARP1, XRCC1, XRCC5 and
CC XRCC6. Interacts with DDB1, DHX15, IQGAP1, LRPPRC, PARP2, PRKDC,
CC RUVBL2, TNKS1 and TNKS2. Binding often leads to interactor
CC ubiquitination, in the presence of the appropriate E1 and E2 enzymes,
CC and proteasomal degradation. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9CZW6; P51668: UBE2D1; Xeno; NbExp=2; IntAct=EBI-16124494, EBI-743540;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21602803}.
CC Nucleus {ECO:0000250}. Note=Translocates to the nucleus after DNA
CC damage, such as laser-induced DNA breaks, and concentrates at DNA
CC breaks. This translocation requires PARP1 activation and PAR-binding
CC (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed at relatively high levels in the brain.
CC Also present in spleen, heart, kidney, testis and liver. In the brain,
CC expressed in the cerebellum, hippocampus, striatum, cortex, frontal
CC cortex and, at lowest levels, in olfactory bulb (at protein level).
CC Predominantly expressed in neurons. {ECO:0000269|PubMed:15813938,
CC ECO:0000269|PubMed:21602803}.
CC -!- INDUCTION: Up-regulated in cortical neurons by treatment with N-methyl-
CC D-aspartate (NMDA). Toxic doses of NMDA fail to induce Iduna
CC expression. Sublethal exposure to oxygen-glucose deprivation also
CC induces Iduna protein expression. Also induced by treatments that
CC result in resistance to subsequent ischemic injury, such as 5 minute
CC bilateral common carotid artery occlusion (at protein level).
CC {ECO:0000269|PubMed:21602803}.
CC -!- DOMAIN: The WWE domain mediates non-covalent PAR-binding.
CC -!- PTM: Ubiquitinated; autoubiquitinated. Autoubiquitination is enhanced
CC upon PAR-binding (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Was named Iduna after the Norse goddess of protection
CC and eternal youth. {ECO:0000305|PubMed:21602803}.
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DR EMBL; AK012080; BAB28015.2; -; mRNA.
DR EMBL; AK169237; BAE41005.1; -; mRNA.
DR EMBL; AK152856; BAE31549.1; -; mRNA.
DR EMBL; AK152907; BAE31587.1; -; mRNA.
DR EMBL; AC153912; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050795; AAH50795.1; -; mRNA.
DR CCDS; CCDS48529.1; -.
DR RefSeq; NP_001103666.1; NM_001110196.1.
DR RefSeq; NP_001103667.1; NM_001110197.1.
DR RefSeq; NP_001103668.1; NM_001110198.1.
DR RefSeq; NP_001271208.1; NM_001284279.1.
DR RefSeq; NP_080794.2; NM_026518.4.
DR PDB; 1UJR; NMR; -; A=83-179.
DR PDB; 2RSF; NMR; -; A=83-179.
DR PDB; 4QPL; X-ray; 1.90 A; A/C=32-185.
DR PDBsum; 1UJR; -.
DR PDBsum; 2RSF; -.
DR PDBsum; 4QPL; -.
DR AlphaFoldDB; Q9CZW6; -.
DR SMR; Q9CZW6; -.
DR BioGRID; 212611; 1.
DR DIP; DIP-61462N; -.
DR IntAct; Q9CZW6; 1.
DR STRING; 10090.ENSMUSP00000124215; -.
DR iPTMnet; Q9CZW6; -.
DR PhosphoSitePlus; Q9CZW6; -.
DR MaxQB; Q9CZW6; -.
DR PaxDb; Q9CZW6; -.
DR PRIDE; Q9CZW6; -.
DR ProteomicsDB; 300414; -.
DR ABCD; Q9CZW6; 1 sequenced antibody.
DR Antibodypedia; 19579; 68 antibodies from 18 providers.
DR DNASU; 68031; -.
DR Ensembl; ENSMUST00000037548; ENSMUSP00000037224; ENSMUSG00000038876.
DR Ensembl; ENSMUST00000160144; ENSMUSP00000124288; ENSMUSG00000038876.
DR Ensembl; ENSMUST00000160372; ENSMUSP00000124215; ENSMUSG00000038876.
DR Ensembl; ENSMUST00000162335; ENSMUSP00000124772; ENSMUSG00000038876.
DR GeneID; 68031; -.
DR KEGG; mmu:68031; -.
DR UCSC; uc007esy.2; mouse.
DR CTD; 81847; -.
DR MGI; MGI:1915281; Rnf146.
DR VEuPathDB; HostDB:ENSMUSG00000038876; -.
DR eggNOG; KOG0824; Eukaryota.
DR GeneTree; ENSGT00390000000358; -.
DR HOGENOM; CLU_067425_0_0_1; -.
DR InParanoid; Q9CZW6; -.
DR OMA; KTNESCA; -.
DR OrthoDB; 1469576at2759; -.
DR PhylomeDB; Q9CZW6; -.
DR TreeFam; TF318925; -.
DR Reactome; R-MMU-201681; TCF dependent signaling in response to WNT.
DR Reactome; R-MMU-4641257; Degradation of AXIN.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 68031; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Rnf146; mouse.
DR EvolutionaryTrace; Q9CZW6; -.
DR PRO; PR:Q9CZW6; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9CZW6; protein.
DR Bgee; ENSMUSG00000038876; Expressed in dorsal pancreas and 253 other tissues.
DR ExpressionAtlas; Q9CZW6; baseline and differential.
DR Genevisible; Q9CZW6; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0072572; F:poly-ADP-D-ribose binding; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; ISO:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd16546; RING-HC_RNF146; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.30.720.50; -; 1.
DR InterPro; IPR044110; RING-HC_RNF146.
DR InterPro; IPR033509; RNF146.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR018123; WWE-dom_subgr.
DR InterPro; IPR037197; WWE_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR13417:SF2; PTHR13417:SF2; 1.
DR Pfam; PF02825; WWE; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00678; WWE; 1.
DR SUPFAM; SSF117839; SSF117839; 1.
DR PROSITE; PS50918; WWE; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Wnt signaling pathway; Zinc; Zinc-finger.
FT CHAIN 1..359
FT /note="E3 ubiquitin-protein ligase RNF146"
FT /id="PRO_0000056108"
FT DOMAIN 93..169
FT /note="WWE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00248"
FT ZN_FING 38..76
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 197..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 109
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group"
FT /ligand_part_id="ChEBI:CHEBI:157741"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group"
FT /ligand_part_id="ChEBI:CHEBI:157741"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group"
FT /ligand_part_id="ChEBI:CHEBI:157741"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group"
FT /ligand_part_id="ChEBI:CHEBI:157741"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group"
FT /ligand_part_id="ChEBI:CHEBI:157741"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group"
FT /ligand_part_id="ChEBI:CHEBI:157741"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group"
FT /ligand_part_id="ChEBI:CHEBI:157741"
FT /evidence="ECO:0000250"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XIK5"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XIK5"
FT CROSSLNK 86
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9NTX7"
FT CROSSLNK 96
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9NTX7"
FT CROSSLNK 132
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9NTX7"
FT CROSSLNK 177
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9NTX7"
FT MUTAGEN 55
FT /note="H->A: Loss of ubiquitination activity."
FT /evidence="ECO:0000269|PubMed:21825151"
FT MUTAGEN 61
FT /note="C->A: Loss of ubiquitination activity. Loss of
FT protection against DNA damage. No effect on PAR-binding."
FT /evidence="ECO:0000269|PubMed:21825151"
FT MUTAGEN 156
FT /note="Y->A: Loss of PAR-binding and of protection against
FT DNA damage; when associated with A-157."
FT /evidence="ECO:0000269|PubMed:21602803,
FT ECO:0000269|PubMed:21825151"
FT MUTAGEN 157
FT /note="R->A: Loss of PAR-binding and of protection against
FT DNA damage; when associated with A-156."
FT /evidence="ECO:0000269|PubMed:21602803,
FT ECO:0000269|PubMed:21825151"
FT CONFLICT 339
FT /note="G -> R (in Ref. 1; BAE31587/BAE31549)"
FT /evidence="ECO:0000305"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:4QPL"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:4QPL"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:4QPL"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:4QPL"
FT HELIX 59..66
FT /evidence="ECO:0007829|PDB:4QPL"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:4QPL"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:4QPL"
FT TURN 81..85
FT /evidence="ECO:0007829|PDB:4QPL"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:4QPL"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:4QPL"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:4QPL"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:4QPL"
FT HELIX 120..131
FT /evidence="ECO:0007829|PDB:4QPL"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:4QPL"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:4QPL"
FT TURN 150..153
FT /evidence="ECO:0007829|PDB:4QPL"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:4QPL"
FT STRAND 163..174
FT /evidence="ECO:0007829|PDB:4QPL"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:4QPL"
SQ SEQUENCE 359 AA; 38934 MW; B4449DB4897A41E0 CRC64;
MEMAGCGEID HSINMLPTNK KANESCSNTA PSLTVPECAI CLQTCVHPVS LPCKHVFCYL
CVKGASWLGK RCALCRQEIP EDFLDKPTLL SPEELKAASR GNGEYAWYYE GRNGWWQYDE
RTSRELEDAF SKGKKNTEML IAGFLYVADL ENMVQYRRNE HGRRRKIKRD IIDIPKKGVA
GLRLDCDTNT VNLARESSAD GADSGSAQTG ASVQLAVPSS TRPLTSVDGQ LTSPVTPSPD
AGISLEDSFA HLQLSGDSIA ERSHRGEGEE DHESPSSGRV PDTSVEETES DASSDSEDAP
VVVAQHSLTQ QRPLVPNGNQ TVADQSDRSG TDRSVAGGGT MSVNVRSRRP DGQCTVTEV
