ID   IFI2_MOUSE              Reviewed;         445 AA.
AC   Q9R002; E9QLD9; P15091; Q38JF1; Q7TMN6; Q8VEL7;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   24-JAN-2024, entry version 147.
DE   RecName: Full=Interferon-activable protein 202 {ECO:0000303|PubMed:10493828};
DE            Short=Ifi-202 {ECO:0000303|PubMed:10493828};
DE   AltName: Full=Interferon-inducible protein p202 {ECO:0000303|PubMed:2477366};
DE   AltName: Full=Lupus susceptibility protein p202 {ECO:0000303|PubMed:11567633};
GN   Name=Ifi202 {ECO:0000312|MGI:MGI:1347080};
GN   Synonyms=Ifi202a {ECO:0000303|PubMed:10493828}, Ifi202b
GN   {ECO:0000303|PubMed:10493828};
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 [MRNA], AND INDUCTION.
RC   STRAIN=AKR/J;
RX   PubMed=2477366; DOI=10.1016/s0021-9258(18)71476-2;
RA   Choubey D., Snoddy J., Chaturvedi V., Toniato E., Opdenakker G., Thakur A.,
RA   Samanta H., Engel D.A., Lengyel P.;
RT   "Interferons as gene activators. Indications for repeated gene duplication
RT   during the evolution of a cluster of interferon-activatable genes on murine
RT   chromosome 1.";
RL   J. Biol. Chem. 264:17182-17189(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/Sv;
RX   PubMed=10493828; DOI=10.1006/geno.1999.5923;
RA   Wang H., Chatterjee G., Meyer J.J., Liu C.J., Manjunath N.A., Bray-Ward P.,
RA   Lengyel P.;
RT   "Characteristics of three homologous 202 genes (Ifi202a, ifi202b, and
RT   ifi202c) from the murine interferon-activatable gene 200 cluster.";
RL   Genomics 60:281-294(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=NZB;
RA   Chen J., Choubey D.;
RT   "Coding cDNA sequence for p202 in New Zealand Black mice.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
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   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX   PubMed=8454910; DOI=10.1089/jir.1993.13.43;
RA   Choubey D., Lengyel P.;
RT   "Interferon action: cytoplasmic and nuclear localization of the interferon-
RT   inducible 52-kD protein that is encoded by the Ifi 200 gene from the gene
RT   200 cluster.";
RL   J. Interferon Res. 13:43-52(1993).
RN   [7]
RP   FUNCTION, INTERACTION WITH TP53BP1, AND MUTAGENESIS OF HIS-84 AND HIS-283.
RX   PubMed=8910340; DOI=10.1074/jbc.271.44.27544;
RA   Datta B., Li B., Choubey D., Nallur G., Lengyel P.;
RT   "p202, an interferon-inducible modulator of transcription, inhibits
RT   transcriptional activation by the p53 tumor suppressor protein, and a
RT   segment from the p53-binding protein 1 that binds to p202 overcomes this
RT   inhibition.";
RL   J. Biol. Chem. 271:27544-27555(1996).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH NFKB1 AND RELA.
RX   PubMed=8524315; DOI=10.1128/mcb.16.1.359;
RA   Min W., Ghosh S., Lengyel P.;
RT   "The interferon-inducible p202 protein as a modulator of transcription:
RT   inhibition of NF-kappa B, c-Fos, and c-Jun activities.";
RL   Mol. Cell. Biol. 16:359-368(1996).
RN   [9]
RP   SUBUNIT, AND MUTAGENESIS OF HIS-84 AND HIS-283.
RX   PubMed=9821952; DOI=10.1016/s0014-5793(98)01263-0;
RA   Koul D., Obeyesekere N.U., Gutterman J.U., Mills G.B., Choubey D.;
RT   "p202 self-associates through a sequence conserved among the members of the
RT   200-family proteins.";
RL   FEBS Lett. 438:21-24(1998).
RN   [10]
RP   POLYMORPHISM.
RX   PubMed=11567633; DOI=10.1016/s1074-7613(01)00196-0;
RA   Rozzo S.J., Allard J.D., Choubey D., Vyse T.J., Izui S., Peltz G.,
RA   Kotzin B.L.;
RT   "Evidence for an interferon-inducible gene, Ifi202, in the susceptibility
RT   to systemic lupus.";
RL   Immunity 15:435-443(2001).
RN   [11]
RP   INDUCTION BY IL6.
RX   PubMed=14764608; DOI=10.1074/jbc.m313140200;
RA   Pramanik R., Jorgensen T.N., Xin H., Kotzin B.L., Choubey D.;
RT   "Interleukin-6 induces expression of Ifi202, an interferon-inducible
RT   candidate gene for lupus susceptibility.";
RL   J. Biol. Chem. 279:16121-16127(2004).
RN   [12]
RP   FUNCTION, AND INTERACTION WITH TP53.
RX   PubMed=16670293; DOI=10.4049/jimmunol.176.10.5863;
RA   Xin H., D'Souza S., Jorgensen T.N., Vaughan A.T., Lengyel P., Kotzin B.L.,
RA   Choubey D.;
RT   "Increased expression of Ifi202, an IFN-activatable gene, in B6.Nba2 lupus
RT   susceptible mice inhibits p53-mediated apoptosis.";
RL   J. Immunol. 176:5863-5870(2006).
RN   [13]
RP   FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=19131592; DOI=10.1126/science.1169841;
RA   Roberts T.L., Idris A., Dunn J.A., Kelly G.M., Burnton C.M., Hodgson S.,
RA   Hardy L.L., Garceau V., Sweet M.J., Ross I.L., Hume D.A., Stacey K.J.;
RT   "HIN-200 proteins regulate caspase activation in response to foreign
RT   cytoplasmic DNA.";
RL   Science 323:1057-1060(2009).
RN   [14] {ECO:0007744|PDB:4L5Q, ECO:0007744|PDB:4L5R, ECO:0007744|PDB:4L5S, ECO:0007744|PDB:4L5T}
RP   X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 46-243 IN COMPLEX WITH DNA,
RP   FUNCTION, SUBUNIT, DOMAIN, INTERACTION WITH AIM2, AND MUTAGENESIS OF
RP   LYS-48; LYS-53; ARG-224; ASN-236; TYR-321; ARG-376; 381-ASN-ASN-382;
RP   LYS-396; GLU-420; ASN-424; ARG-431 AND 434-ARG-TYR-435.
RX   PubMed=23850291; DOI=10.1016/j.celrep.2013.06.024;
RA   Yin Q., Sester D.P., Tian Y., Hsiao Y.S., Lu A., Cridland J.A.,
RA   Sagulenko V., Thygesen S.J., Choubey D., Hornung V., Walz T., Stacey K.J.,
RA   Wu H.;
RT   "Molecular mechanism for p202-mediated specific inhibition of AIM2
RT   inflammasome activation.";
RL   Cell Rep. 4:327-339(2013).
RN   [15] {ECO:0007744|PDB:4JBJ, ECO:0007744|PDB:4JBK}
RP   X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS) OF 46-242 IN COMPLEX WITH DNA,
RP   FUNCTION, DOMAIN, MUTAGENESIS OF LYS-48; LYS-53; GLY-54; LYS-76; LYS-79;
RP   SER-166; 182-ASN--SER-185; THR-187; LYS-189; LYS-198; 222-HIS--ARG-224;
RP   GLY-226; ASN-227; LYS-229 AND ASN-236, AND DNA BINDING.
RX   PubMed=23567559; DOI=10.1038/cr.2013.52;
RA   Ru H., Ni X., Zhao L., Crowley C., Ding W., Hung L.W., Shaw N., Cheng G.,
RA   Liu Z.J.;
RT   "Structural basis for termination of AIM2-mediated signaling by p202.";
RL   Cell Res. 23:855-858(2013).
RN   [16] {ECO:0007744|PDB:4LNQ}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 53-245 IN COMPLEX WITH DNA,
RP   FUNCTION, DOMAIN, AND MUTAGENESIS OF ARG-150; SER-166; LYS-180; ASN-182;
RP   LYS-184; SER-185; THR-187; LYS-198; HIS-222 AND ARG-224.
RX   PubMed=24419611; DOI=10.1107/s2053230x1303135x;
RA   Li H., Wang J., Wang J., Cao L.S., Wang Z.X., Wu J.W.;
RT   "Structural mechanism of DNA recognition by the p202 HINa domain: insights
RT   into the inhibition of Aim2-mediated inflammatory signalling.";
RL   Acta Crystallogr. F Struct. Biol. Commun. 70:21-29(2014).
CC   -!- FUNCTION: DNA-binding protein involved in innate immune response and
CC       has anti-inflammatory activity (PubMed:19131592, PubMed:23850291,
CC       PubMed:23567559). Inhibits caspase activation in response to cytosolic
CC       DNA by preventing activation of the AIM2 inflammasome, probably by
CC       sequestering cytoplasmic DNA and preventing its being bound by AIM2
CC       (PubMed:19131592, PubMed:23850291, PubMed:23567559). Also inhibits
CC       activation of the AIM2 inflammasome via a direct interaction with AIM2,
CC       which prevents the interaction between AIM2 and PYCARD and formation of
CC       the AIM2 inflammasome (PubMed:23850291). Binds double-stranded DNA
CC       (dsDNA) in the cytosol (PubMed:19131592, PubMed:23850291,
CC       PubMed:23567559, PubMed:24419611). Has anti-apoptotic effects due to
CC       inhibition of the transcriptional activity of TP53/p53
CC       (PubMed:16670293). Inhibits the transcriptional activity of several
CC       transcription factors, including NF-kappa-B p50 and p65, FOS, JUN,
CC       E2F1, E2F4, MYOD1 and myogenin (PubMed:8524315).
CC       {ECO:0000269|PubMed:16670293, ECO:0000269|PubMed:19131592,
CC       ECO:0000269|PubMed:23567559, ECO:0000269|PubMed:23850291,
CC       ECO:0000269|PubMed:24419611, ECO:0000269|PubMed:8524315}.
CC   -!- SUBUNIT: Homomultimer; homotetramerizes (via HIN-200 domain 2),
CC       enhancing affinity for double-stranded DNA (dsDNA) (PubMed:9821952,
CC       PubMed:23850291). Interacts (via HIN-200 domain 2) with AIM2 (via HIN-
CC       200 domain); preventing activation of the AIM2 inflammasome
CC       (PubMed:23850291). Binds to several transcription factors, including
CC       NF-kappa-B p50 (NFKB1) and p65 (RELA), FOS, JUN, E2F1, E2F4, MYOD1 and
CC       myogenin (PubMed:8524315). Also binds TP53/p53, the hypophosphorylated,
CC       growth-inhibitory form of the retinoblastoma protein and the p53-
CC       binding protein 1 (TP53BP1) (PubMed:8910340, PubMed:16670293).
CC       {ECO:0000269|PubMed:16670293, ECO:0000269|PubMed:23850291,
CC       ECO:0000269|PubMed:8524315, ECO:0000269|PubMed:8910340,
CC       ECO:0000269|PubMed:9821952}.
CC   -!- INTERACTION:
CC       Q9R002; P13405: Rb1; NbExp=7; IntAct=EBI-3043899, EBI-971782;
CC       Q9R002; P06400: RB1; Xeno; NbExp=5; IntAct=EBI-3043899, EBI-491274;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19131592,
CC       ECO:0000269|PubMed:8454910}. Nucleus {ECO:0000269|PubMed:8454910}.
CC       Note=Accumulates first in the cytoplasm, and is translocated to the
CC       nucleus after a delay, where it is primarily chromatin-associated.
CC       {ECO:0000269|PubMed:8454910}.
CC   -!- INDUCTION: By beta interferon (PubMed:2477366, PubMed:14764608). By IL6
CC       in splenocytes (at protein level) (PubMed:14764608).
CC       {ECO:0000269|PubMed:14764608, ECO:0000269|PubMed:2477366}.
CC   -!- DOMAIN: The HIN-200 domain 1 mediates non-specific double-stranded DNA
CC       (dsDNA)-binding via electrostatic interactions: it recognizes both
CC       strands of DNA (PubMed:23567559, PubMed:24419611). The HIN-200 domain 2
CC       mediates homotetramerization and interaction with AIM2
CC       (PubMed:23850291). {ECO:0000269|PubMed:23567559,
CC       ECO:0000269|PubMed:23850291, ECO:0000269|PubMed:24419611}.
CC   -!- PTM: Phosphorylated. {ECO:0000269|PubMed:8454910}.
CC   -!- POLYMORPHISM: NZB mice express 10 to 100 fold more Ifi202 in spleen
CC       than B6 or NZW mice (PubMed:11567633). This could account for the high
CC       susceptibility of NZB mice to systemic lupus (PubMed:11567633).
CC       {ECO:0000269|PubMed:11567633}.
CC   -!- SIMILARITY: Belongs to the HIN-200 family. {ECO:0000305}.
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DR   EMBL; M31418; AAA39312.1; -; mRNA.
DR   EMBL; AF140672; AAF04260.1; -; mRNA.
DR   EMBL; DQ222946; ABB00055.1; -; mRNA.
DR   EMBL; AC170584; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC018233; AAH18233.1; -; mRNA.
DR   EMBL; BC055888; AAH55888.1; -; mRNA.
DR   CCDS; CCDS35794.1; -.
DR   PIR; A34457; A34457.
DR   RefSeq; NP_032353.2; NM_008327.2.
DR   RefSeq; NP_036070.2; NM_011940.2.
DR   RefSeq; XP_006536966.1; XM_006536903.2.
DR   PDB; 4JBJ; X-ray; 2.69 A; A/B=46-242.
DR   PDB; 4JBK; X-ray; 2.96 A; A/B/C/D=46-242.
DR   PDB; 4L5Q; X-ray; 2.23 A; A=46-243.
DR   PDB; 4L5R; X-ray; 1.87 A; C=46-243.
DR   PDB; 4L5S; X-ray; 2.94 A; A/B=46-243.
DR   PDB; 4L5T; X-ray; 3.40 A; A/B/C/D=244-445.
DR   PDB; 4LNQ; X-ray; 2.00 A; A/B=53-245.
DR   PDBsum; 4JBJ; -.
DR   PDBsum; 4JBK; -.
DR   PDBsum; 4L5Q; -.
DR   PDBsum; 4L5R; -.
DR   PDBsum; 4L5S; -.
DR   PDBsum; 4L5T; -.
DR   PDBsum; 4LNQ; -.
DR   AlphaFoldDB; Q9R002; -.
DR   SMR; Q9R002; -.
DR   BioGRID; 204945; 4.
DR   ELM; Q9R002; -.
DR   IntAct; Q9R002; 3.
DR   STRING; 10090.ENSMUSP00000000266; -.
DR   iPTMnet; Q9R002; -.
DR   PhosphoSitePlus; Q9R002; -.
DR   MaxQB; Q9R002; -.
DR   PaxDb; 10090-ENSMUSP00000000266; -.
DR   ProteomicsDB; 267198; -.
DR   Pumba; Q9R002; -.
DR   DNASU; 26388; -.
DR   Ensembl; ENSMUST00000000266.9; ENSMUSP00000000266.8; ENSMUSG00000026535.10.
DR   GeneID; 26388; -.
DR   KEGG; mmu:26388; -.
DR   UCSC; uc007dsk.2; mouse.
DR   AGR; MGI:1347080; -.
DR   AGR; MGI:1347083; -.
DR   CTD; 26388; -.
DR   MGI; MGI:1347080; Ifi202a.
DR   MGI; MGI:1347083; Ifi202b.
DR   VEuPathDB; HostDB:ENSMUSG00000026535; -.
DR   eggNOG; ENOG502QTQS; Eukaryota.
DR   GeneTree; ENSGT00390000013296; -.
DR   HOGENOM; CLU_615313_0_0_1; -.
DR   InParanoid; Q9R002; -.
DR   OMA; CEIGNTI; -.
DR   OrthoDB; 4893941at2759; -.
DR   PhylomeDB; Q9R002; -.
DR   TreeFam; TF337385; -.
DR   BioGRID-ORCS; 26388; 3 hits in 76 CRISPR screens.
DR   ChiTaRS; Ifi202b; mouse.
DR   PRO; PR:Q9R002; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q9R002; Protein.
DR   Bgee; ENSMUSG00000026535; Expressed in conjunctival fornix and 122 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR   GO; GO:0060090; F:molecular adaptor activity; IDA:UniProt.
DR   GO; GO:0002218; P:activation of innate immune response; IBA:GO_Central.
DR   GO; GO:0035458; P:cellular response to interferon-beta; IDA:MGI.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0140972; P:negative regulation of AIM2 inflammasome complex assembly; IDA:UniProtKB.
DR   GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR   GO; GO:0045824; P:negative regulation of innate immune response; IDA:UniProtKB.
DR   GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR   GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 4.
DR   InterPro; IPR040205; HIN-200.
DR   InterPro; IPR004021; HIN200/IF120x.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR12200; INTERFERON-INDUCIBLE PROTEIN AIM2 FAMILY MEMBER; 1.
DR   PANTHER; PTHR12200:SF25; PYRIN AND HIN DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF02760; HIN; 2.
DR   SUPFAM; SSF159141; HIN-2000 domain-like; 4.
DR   PROSITE; PS50834; HIN_200; 2.
DR   Genevisible; Q9R002; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; DNA-binding; Immunity; Inflammatory response;
KW   Innate immunity; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..445
FT                   /note="Interferon-activable protein 202"
FT                   /id="PRO_0000153719"
FT   DOMAIN          46..243
FT                   /note="HIN-200 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00106"
FT   DOMAIN          244..441
FT                   /note="HIN-200 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00106"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          82..89
FT                   /note="Required for homomultimerization"
FT                   /evidence="ECO:0000269|PubMed:9821952"
FT   REGION          281..288
FT                   /note="Required for homomultimerization"
FT                   /evidence="ECO:0000269|PubMed:9821952"
FT   COMPBIAS        1..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            84
FT                   /note="Mediates interaction with TP53BP1"
FT                   /evidence="ECO:0000269|PubMed:8910340"
FT   SITE            283
FT                   /note="Mediates interaction with TP53BP1"
FT                   /evidence="ECO:0000269|PubMed:8910340"
FT   MUTAGEN         48
FT                   /note="K->A: Reduced DNA-binding. Strongly reduces affinity
FT                   for DNA; when associated with A-53 and W-54."
FT                   /evidence="ECO:0000269|PubMed:23567559,
FT                   ECO:0000269|PubMed:23850291"
FT   MUTAGEN         53
FT                   /note="K->A: Reduced DNA-binding. Strongly reduces affinity
FT                   for DNA; when associated with A-48 and W-54."
FT                   /evidence="ECO:0000269|PubMed:23567559,
FT                   ECO:0000269|PubMed:23850291"
FT   MUTAGEN         54
FT                   /note="G->W: Strongly reduces affinity for DNA; when
FT                   associated with A-48 and A-53."
FT                   /evidence="ECO:0000269|PubMed:23567559"
FT   MUTAGEN         76
FT                   /note="K->A: Strongly reduces affinity for DNA; when
FT                   associated with A-79 and A-236."
FT                   /evidence="ECO:0000269|PubMed:23567559"
FT   MUTAGEN         79
FT                   /note="K->A: Strongly reduces affinity for DNA; when
FT                   associated with A-76 and A-236."
FT                   /evidence="ECO:0000269|PubMed:23567559"
FT   MUTAGEN         84
FT                   /note="H->F: Loss of interaction with TP53BP1; when
FT                   associated with F-283."
FT                   /evidence="ECO:0000269|PubMed:8910340"
FT   MUTAGEN         84
FT                   /note="H->G: Abolished homomultimerization."
FT                   /evidence="ECO:0000269|PubMed:9821952"
FT   MUTAGEN         150
FT                   /note="R->E: Does not affect DNA-binding."
FT                   /evidence="ECO:0000269|PubMed:24419611"
FT   MUTAGEN         166
FT                   /note="S->A: Strongly reduces affinity for DNA; when
FT                   associated with."
FT                   /evidence="ECO:0000269|PubMed:23567559"
FT   MUTAGEN         166
FT                   /note="S->E: Reduced DNA-binding."
FT                   /evidence="ECO:0000269|PubMed:24419611"
FT   MUTAGEN         180
FT                   /note="K->E: Abolished DNA-binding."
FT                   /evidence="ECO:0000269|PubMed:24419611"
FT   MUTAGEN         182..185
FT                   /note="NDKS->ADAA: Strongly reduces affinity for DNA."
FT                   /evidence="ECO:0000269|PubMed:23567559"
FT   MUTAGEN         182
FT                   /note="N->E: Abolished DNA-binding."
FT                   /evidence="ECO:0000269|PubMed:24419611"
FT   MUTAGEN         184
FT                   /note="K->E: Does not affect DNA-binding."
FT                   /evidence="ECO:0000269|PubMed:24419611"
FT   MUTAGEN         185
FT                   /note="S->E: Abolished DNA-binding."
FT                   /evidence="ECO:0000269|PubMed:24419611"
FT   MUTAGEN         187
FT                   /note="T->A: Strongly reduces affinity for DNA; when
FT                   associated with A-189 and A-198."
FT                   /evidence="ECO:0000269|PubMed:23567559"
FT   MUTAGEN         187
FT                   /note="T->E: Abolished DNA-binding."
FT                   /evidence="ECO:0000269|PubMed:24419611"
FT   MUTAGEN         189
FT                   /note="K->A: Strongly reduces affinity for DNA; when
FT                   associated with A-187 and A-198."
FT                   /evidence="ECO:0000269|PubMed:23567559"
FT   MUTAGEN         198
FT                   /note="K->A: Strongly reduces affinity for DNA; when
FT                   associated with A-187 and A-189."
FT                   /evidence="ECO:0000269|PubMed:23567559"
FT   MUTAGEN         198
FT                   /note="K->E: Abolished DNA-binding."
FT                   /evidence="ECO:0000269|PubMed:24419611"
FT   MUTAGEN         222..224
FT                   /note="HLR->ALA: Strongly reduces affinity for DNA."
FT                   /evidence="ECO:0000269|PubMed:23567559"
FT   MUTAGEN         222
FT                   /note="H->E: Abolished DNA-binding."
FT                   /evidence="ECO:0000269|PubMed:24419611"
FT   MUTAGEN         224
FT                   /note="R->E: Abolished DNA-binding."
FT                   /evidence="ECO:0000269|PubMed:23850291,
FT                   ECO:0000269|PubMed:24419611"
FT   MUTAGEN         226
FT                   /note="G->W: Strongly reduces affinity for DNA; when
FT                   associated with A-166; A-227 and A-229."
FT                   /evidence="ECO:0000269|PubMed:23567559"
FT   MUTAGEN         227
FT                   /note="N->A: Strongly reduces affinity for DNA; when
FT                   associated with A-166; W-226 and A-229."
FT                   /evidence="ECO:0000269|PubMed:23567559"
FT   MUTAGEN         229
FT                   /note="K->A: Strongly reduces affinity for DNA; when
FT                   associated with A-166; W-226 and A-227."
FT                   /evidence="ECO:0000269|PubMed:23567559"
FT   MUTAGEN         236
FT                   /note="N->A: Does not affect DNA-binding. Strongly reduces
FT                   affinity for DNA; when associated with A-76 and A-79."
FT                   /evidence="ECO:0000269|PubMed:23567559,
FT                   ECO:0000269|PubMed:23850291"
FT   MUTAGEN         283
FT                   /note="H->F: Loss of interaction with TP53BP1; when
FT                   associated with F-84."
FT                   /evidence="ECO:0000269|PubMed:8910340"
FT   MUTAGEN         283
FT                   /note="H->G: Abolished homomultimerization."
FT                   /evidence="ECO:0000269|PubMed:9821952"
FT   MUTAGEN         321
FT                   /note="Y->R: Impaired homotetramerization."
FT                   /evidence="ECO:0000269|PubMed:23850291"
FT   MUTAGEN         376
FT                   /note="R->E: Promotes formation of a homodimer."
FT                   /evidence="ECO:0000269|PubMed:23850291"
FT   MUTAGEN         381..382
FT                   /note="NN->AA: Impaired homotetramerization."
FT                   /evidence="ECO:0000269|PubMed:23850291"
FT   MUTAGEN         396
FT                   /note="K->A: Impaired homotetramerization."
FT                   /evidence="ECO:0000269|PubMed:23850291"
FT   MUTAGEN         420
FT                   /note="E->A: Impaired homotetramerization."
FT                   /evidence="ECO:0000269|PubMed:23850291"
FT   MUTAGEN         424
FT                   /note="N->A: Impaired homotetramerization."
FT                   /evidence="ECO:0000269|PubMed:23850291"
FT   MUTAGEN         431
FT                   /note="R->A: Impaired homotetramerization."
FT                   /evidence="ECO:0000269|PubMed:23850291"
FT   MUTAGEN         434..435
FT                   /note="RY->AA: Impaired homotetramerization."
FT                   /evidence="ECO:0000269|PubMed:23850291"
FT   CONFLICT        13..15
FT                   /note="EFS -> DLA (in Ref. 2; AAF04260 and 5; AAH55888)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        79
FT                   /note="K -> N (in Ref. 3; ABB00055)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        92
FT                   /note="Q -> K (in Ref. 2; AAF04260 and 5; AAH18233)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        109
FT                   /note="E -> G (in Ref. 3; ABB00055)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        111
FT                   /note="K -> Q (in Ref. 5; AAH18233)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        127
FT                   /note="I -> F (in Ref. 3; ABB00055)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        141..142
FT                   /note="II -> MF (in Ref. 1; AAA39312, 2; AAF04260, 3;
FT                   ABB00055 and 5; AAH18233/AAH55888)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        187
FT                   /note="T -> I (in Ref. 3; ABB00055)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        190
FT                   /note="I -> V (in Ref. 3; ABB00055)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        204
FT                   /note="K -> E (in Ref. 1; AAA39312, 2; AAF04260, 3;
FT                   ABB00055 and 5; AAH18233/AAH55888)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        240
FT                   /note="I -> V (in Ref. 2; AAF04260)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        350
FT                   /note="L -> P (in Ref. 1; AAA39312, 2; AAF04260, 3;
FT                   ABB00055 and 5; AAH18233/AAH55888)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        364
FT                   /note="K -> E (in Ref. 1; AAA39312, 2; AAF04260, 3;
FT                   ABB00055 and 5; AAH18233/AAH55888)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        368
FT                   /note="V -> F (in Ref. 1; AAA39312)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        379
FT                   /note="T -> S (in Ref. 1; AAA39312, 2; AAF04260, 3;
FT                   ABB00055 and 5; AAH18233/AAH55888)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        432
FT                   /note="S -> A (in Ref. 1; AAA39312, 2; AAF04260, 3;
FT                   ABB00055 and 5; AAH18233/AAH55888)"
FT                   /evidence="ECO:0000305"
FT   TURN            47..50
FT                   /evidence="ECO:0007829|PDB:4L5R"
FT   STRAND          56..58
FT                   /evidence="ECO:0007829|PDB:4L5R"
FT   STRAND          62..69
FT                   /evidence="ECO:0007829|PDB:4L5R"
FT   STRAND          73..75
FT                   /evidence="ECO:0007829|PDB:4L5R"
FT   TURN            76..79
FT                   /evidence="ECO:0007829|PDB:4L5R"
FT   STRAND          80..88
FT                   /evidence="ECO:0007829|PDB:4L5R"
FT   STRAND          93..98
FT                   /evidence="ECO:0007829|PDB:4L5R"
FT   HELIX           101..106
FT                   /evidence="ECO:0007829|PDB:4L5R"
FT   STRAND          112..121
FT                   /evidence="ECO:0007829|PDB:4L5R"
FT   STRAND          124..127
FT                   /evidence="ECO:0007829|PDB:4L5R"
FT   STRAND          132..135
FT                   /evidence="ECO:0007829|PDB:4L5R"
FT   HELIX           138..140
FT                   /evidence="ECO:0007829|PDB:4L5R"
FT   HELIX           146..153
FT                   /evidence="ECO:0007829|PDB:4L5R"
FT   HELIX           158..161
FT                   /evidence="ECO:0007829|PDB:4L5R"
FT   STRAND          169..181
FT                   /evidence="ECO:0007829|PDB:4L5R"
FT   STRAND          186..191
FT                   /evidence="ECO:0007829|PDB:4L5R"
FT   STRAND          196..201
FT                   /evidence="ECO:0007829|PDB:4L5R"
FT   TURN            211..213
FT                   /evidence="ECO:0007829|PDB:4L5S"
FT   STRAND          216..224
FT                   /evidence="ECO:0007829|PDB:4L5R"
FT   STRAND          226..228
FT                   /evidence="ECO:0007829|PDB:4L5R"
FT   STRAND          231..233
FT                   /evidence="ECO:0007829|PDB:4L5R"
FT   STRAND          239..242
FT                   /evidence="ECO:0007829|PDB:4L5R"
FT   STRAND          253..256
FT                   /evidence="ECO:0007829|PDB:4L5T"
FT   STRAND          260..267
FT                   /evidence="ECO:0007829|PDB:4L5T"
FT   STRAND          271..274
FT                   /evidence="ECO:0007829|PDB:4L5T"
FT   TURN            275..278
FT                   /evidence="ECO:0007829|PDB:4L5T"
FT   STRAND          279..287
FT                   /evidence="ECO:0007829|PDB:4L5T"
FT   STRAND          289..297
FT                   /evidence="ECO:0007829|PDB:4L5T"
FT   HELIX           300..306
FT                   /evidence="ECO:0007829|PDB:4L5T"
FT   STRAND          311..314
FT                   /evidence="ECO:0007829|PDB:4L5T"
FT   STRAND          316..320
FT                   /evidence="ECO:0007829|PDB:4L5T"
FT   STRAND          323..326
FT                   /evidence="ECO:0007829|PDB:4L5T"
FT   HELIX           329..331
FT                   /evidence="ECO:0007829|PDB:4L5T"
FT   STRAND          332..334
FT                   /evidence="ECO:0007829|PDB:4L5T"
FT   HELIX           356..361
FT                   /evidence="ECO:0007829|PDB:4L5T"
FT   STRAND          368..379
FT                   /evidence="ECO:0007829|PDB:4L5T"
FT   STRAND          381..389
FT                   /evidence="ECO:0007829|PDB:4L5T"
FT   STRAND          395..399
FT                   /evidence="ECO:0007829|PDB:4L5T"
FT   HELIX           401..405
FT                   /evidence="ECO:0007829|PDB:4L5T"
FT   STRAND          413..422
FT                   /evidence="ECO:0007829|PDB:4L5T"
FT   STRAND          429..441
FT                   /evidence="ECO:0007829|PDB:4L5T"
SQ   SEQUENCE   445 AA;  50466 MW;  5EA0E93E143C58EA CRC64;
     MSNRNLRSST NSEFSEGQHQ TPSSDSSGHG EDQPQASPGP NKKSHTPKKN ISKGAVLHEK
     PMTVMVLTAT EPFNYKEGKE NMFHATVATE SQYYRVKVFN MDLKEKFTEN KFITISKYFN
     SSGILEINET ATVSEAAPNQ IIEVPKNIIR SAKETLKISK IKELDSGTLI YGVFAVEKKK
     VNDKSITFKI KDNEDNIKVV WDKKQHNINY EKGDKLQLFS FHLRKGNGKP ILHSGNHSFI
     KGEKLLKESF EGDGYHKGPK QVVALKATKL FTYDSIKSKK MFHATVATDT EFFRVMVFEE
     NLEKKFIPGN TIALSDYFGM YGSLAIHEYS SVSEVKSQNK EDSSSSDERL IEHLKICDLH
     LQTKERLVDG EFKVYRKSTG NNCICYGIWD DTGAMKVVVS GQLTSVNCEI GNTIRLVCFE
     LTSNADEWFL RSTRYSYMEV IMPEK
//