TP53B_MOUSE
ID TP53B_MOUSE Reviewed; 1969 AA.
AC P70399; A2AU89; A2AU91; Q68FD0; Q8CI97; Q91YC9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=TP53-binding protein 1 {ECO:0000305};
DE Short=53BP1 {ECO:0000303|PubMed:11801725};
DE Short=p53-binding protein 1 {ECO:0000303|PubMed:11801725};
DE Short=p53BP1;
GN Name=Tp53bp1 {ECO:0000250|UniProtKB:Q12888};
GN Synonyms=Trp53bp1 {ECO:0000312|MGI:MGI:1351320};
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Head, and 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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-1969 (ISOFORM 2), PHOSPHORYLATION, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=BALB/cJ;
RX PubMed=11801725; DOI=10.1242/jcs.115.1.71;
RA Jullien D., Vagnarelli P., Earnshaw W.C., Adachi Y.;
RT "Kinetochore localisation of the DNA damage response component 53BP1 during
RT mitosis.";
RL J. Cell Sci. 115:71-79(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1176-1273, AND INTERACTION WITH IFI202A.
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 [5]
RP SUBCELLULAR LOCATION.
RX PubMed=11673449; DOI=10.1074/jbc.c100569200;
RA Ward I.M., Chen J.;
RT "Histone H2AX is phosphorylated in an ATR-dependent manner in response to
RT replicational stress.";
RL J. Biol. Chem. 276:47759-47762(2001).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=12640136; DOI=10.1128/mcb.23.7.2556-2563.2003;
RA Ward I.M., Minn K., van Deursen J., Chen J.;
RT "p53 Binding protein 53BP1 is required for DNA damage responses and tumor
RT suppression in mice.";
RL Mol. Cell. Biol. 23:2556-2563(2003).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15159415; DOI=10.1083/jcb.200403021;
RA Ward I.M., Reina-San-Martin B., Olaru A., Minn K., Tamada K., Lau J.S.,
RA Cascalho M., Chen L., Nussenzweig A., Livak F., Nussenzweig M.C., Chen J.;
RT "53BP1 is required for class switch recombination.";
RL J. Cell Biol. 165:459-464(2004).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15077110; DOI=10.1038/ni1067;
RA Manis J.P., Morales J.C., Xia Z., Kutok J.L., Alt F.W., Carpenter P.B.;
RT "53BP1 links DNA damage-response pathways to immunoglobulin heavy chain
RT class-switch recombination.";
RL Nat. Immunol. 5:481-487(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1115, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [11]
RP FUNCTION.
RX PubMed=20362325; DOI=10.1016/j.cell.2010.03.012;
RA Bunting S.F., Callen E., Wong N., Chen H.T., Polato F., Gunn A.,
RA Bothmer A., Feldhahn N., Fernandez-Capetillo O., Cao L., Xu X., Deng C.X.,
RA Finkel T., Nussenzweig M., Stark J.M., Nussenzweig A.;
RT "53BP1 inhibits homologous recombination in Brca1-deficient cells by
RT blocking resection of DNA breaks.";
RL Cell 141:243-254(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; SER-267; SER-268;
RP SER-382; SER-429; SER-464; SER-552; SER-627; SER-631; SER-632; SER-716;
RP SER-719; SER-822; SER-1096; SER-1115; SER-1423; SER-1427; SER-1459;
RP SER-1470 AND SER-1628, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP FUNCTION.
RX PubMed=20453858; DOI=10.1038/nsmb.1831;
RA Bouwman P., Aly A., Escandell J.M., Pieterse M., Bartkova J.,
RA van der Gulden H., Hiddingh S., Thanasoula M., Kulkarni A., Yang Q.,
RA Haffty B.G., Tommiska J., Blomqvist C., Drapkin R., Adams D.J.,
RA Nevanlinna H., Bartek J., Tarsounas M., Ganesan S., Jonkers J.;
RT "53BP1 loss rescues BRCA1 deficiency and is associated with triple-negative
RT and BRCA-mutated breast cancers.";
RL Nat. Struct. Mol. Biol. 17:688-695(2010).
RN [14]
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=23209566; DOI=10.1371/journal.pone.0049211;
RA Hartlerode A.J., Guan Y., Rajendran A., Ura K., Schotta G., Xie A.,
RA Shah J.V., Scully R.;
RT "Impact of histone H4 lysine 20 methylation on 53BP1 responses to
RT chromosomal double strand breaks.";
RL PLoS ONE 7:E49211-E49211(2012).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH RIF1.
RX PubMed=23333305; DOI=10.1016/j.molcel.2013.01.002;
RA Chapman J.R., Barral P., Vannier J.B., Borel V., Steger M., Tomas-Loba A.,
RA Sartori A.A., Adams I.R., Batista F.D., Boulton S.J.;
RT "RIF1 is essential for 53BP1-dependent nonhomologous end joining and
RT suppression of DNA double-strand break resection.";
RL Mol. Cell 49:858-871(2013).
RN [16]
RP SUBCELLULAR LOCATION, INTERACTION WITH RIF1, AND PHOSPHORYLATION.
RX PubMed=23306439; DOI=10.1126/science.1230624;
RA Di Virgilio M., Callen E., Yamane A., Zhang W., Jankovic M., Gitlin A.D.,
RA Feldhahn N., Resch W., Oliveira T.Y., Chait B.T., Nussenzweig A.,
RA Casellas R., Robbiani D.F., Nussenzweig M.C.;
RT "Rif1 prevents resection of DNA breaks and promotes immunoglobulin class
RT switching.";
RL Science 339:711-715(2013).
RN [17]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1329 AND ARG-1352, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [18]
RP FUNCTION.
RX PubMed=26308889; DOI=10.1038/nature14970;
RA Dong J., Panchakshari R.A., Zhang T., Zhang Y., Hu J., Volpi S.A.,
RA Meyers R.M., Ho Y.J., Du Z., Robbiani D.F., Meng F., Gostissa M.,
RA Nussenzweig M.C., Manis J.P., Alt F.W.;
RT "Orientation-specific joining of AID-initiated DNA breaks promotes antibody
RT class switching.";
RL Nature 525:134-139(2015).
RN [19]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=30297459; DOI=10.1128/mcb.00209-18;
RA Li M.L., Jiang Q., Bhanu N.V., Wu J., Li W., Garcia B.A., Greenberg R.A.;
RT "Phosphorylation of TIP60 Suppresses 53BP1 Localization at DNA Damage
RT Sites.";
RL Mol. Cell. Biol. 39:0-0(2019).
RN [20]
RP STRUCTURE BY NMR OF 1475-1629.
RX PubMed=15341721; DOI=10.1016/j.str.2004.06.014;
RA Charier G., Couprie J., Alpha-Bazin B., Meyer V., Quemeneur E., Guerois R.,
RA Callebaut I., Gilquin B., Zinn-Justin S.;
RT "The Tudor tandem of 53BP1: a new structural motif involved in DNA and RG-
RT rich peptide binding.";
RL Structure 12:1551-1562(2004).
CC -!- FUNCTION: Double-strand break (DSB) repair protein involved in response
CC to DNA damage, telomere dynamics and class-switch recombination (CSR)
CC during antibody genesis (PubMed:15159415, PubMed:15077110,
CC PubMed:20453858, PubMed:23333305, PubMed:26308889, PubMed:20362325).
CC Plays a key role in the repair of double-strand DNA breaks (DSBs) in
CC response to DNA damage by promoting non-homologous end joining (NHEJ)-
CC mediated repair of DSBs and specifically counteracting the function of
CC the homologous recombination (HR) repair protein BRCA1
CC (PubMed:23333305, PubMed:20362325, PubMed:30297459). In response to
CC DSBs, phosphorylation by ATM promotes interaction with RIF1 and
CC dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites.
CC Recruited to DSBs sites by recognizing and binding histone H2A
CC monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at
CC 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites.
CC Required for immunoglobulin class-switch recombination (CSR) during
CC antibody genesis, a process that involves the generation of DNA DSBs
CC (PubMed:15159415, PubMed:15077110). Participates in the repair and the
CC orientation of the broken DNA ends during CSR (PubMed:26308889). In
CC contrast, it is not required for classic NHEJ and V(D)J recombination
CC (PubMed:15159415). Promotes NHEJ of dysfunctional telomeres (By
CC similarity). {ECO:0000250|UniProtKB:Q12888,
CC ECO:0000269|PubMed:15077110, ECO:0000269|PubMed:15159415,
CC ECO:0000269|PubMed:20362325, ECO:0000269|PubMed:20453858,
CC ECO:0000269|PubMed:23333305, ECO:0000269|PubMed:26308889,
CC ECO:0000269|PubMed:30297459}.
CC -!- SUBUNIT: Homoligomer (By similarity). Interacts with p53/TP53 (via the
CC central domain) (By similarity). Interacts with DCLRE1C (By
CC similarity). Interacts with histone H2AX and this requires
CC phosphorylation of H2AX on 'Ser-139' (By similarity). Interacts with
CC histone H4 that has been dimethylated at 'Lys-20' (H4K20me2)
CC (PubMed:23209566). Has low affinity for histone H4 containing
CC monomethylated 'Lys-20' (H4K20me1) (By similarity). Does not bind
CC histone H4 containing unmethylated or trimethylated 'Lys-20' (H4K20me3)
CC (By similarity). Has low affinity for histone H3 that has been
CC dimethylated on 'Lys-79' (By similarity). Has very low affinity for
CC histone H3 that has been monomethylated on 'Lys-79' (in vitro) (By
CC similarity). Does not bind unmethylated histone H3 (By similarity).
CC Interacts with histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) (By
CC similarity). Interacts with PWWP3A/EXPAND1 (By similarity). Interacts
CC with CHEK2; modulates CHEK2 phosphorylation at 'Thr-68' in response to
CC infrared (By similarity). Interacts with MSL1; this interaction may be
CC required for MSL1 DNA repair activity, but not for histone
CC acetyltransferase activity (By similarity). Interacts (when
CC phosphorylated by ATM) with RIF1 (PubMed:23333305, PubMed:23306439).
CC Interacts (via the Tudor-like domain) with NUDT16L1/TIRR; interaction
CC masks the Tudor-like domain and prevents recruitment to chromatin (By
CC similarity). Interacts with PAXIP1 (By similarity). Interacts with
CC IFI202A (PubMed:8910340). Interacts with SHLD2 (By similarity).
CC {ECO:0000250|UniProtKB:Q12888, ECO:0000269|PubMed:23209566,
CC ECO:0000269|PubMed:23306439, ECO:0000269|PubMed:23333305,
CC ECO:0000269|PubMed:8910340}.
CC -!- INTERACTION:
CC P70399-1; P53350: PLK1; Xeno; NbExp=2; IntAct=EBI-15790796, EBI-476768;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11801725}. Chromosome
CC {ECO:0000269|PubMed:11673449, ECO:0000269|PubMed:23209566,
CC ECO:0000269|PubMed:23306439, ECO:0000269|PubMed:23333305,
CC ECO:0000269|PubMed:30297459}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:11801725}. Note=Localizes to the nucleus in absence
CC of DNA damage (PubMed:11801725). Following DNA damage, recruited to
CC sites of DNA damage, such as double stand breaks (DSBs)
CC (PubMed:11673449, PubMed:23209566, PubMed:23333305, PubMed:23306439).
CC Recognizes and binds histone H2A monoubiquitinated at 'Lys-15'
CC (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two
CC histone marks that are present at DSBs sites (PubMed:23209566).
CC Associated with kinetochores during mitosis (PubMed:11801725).
CC {ECO:0000269|PubMed:11673449, ECO:0000269|PubMed:11801725,
CC ECO:0000269|PubMed:23209566, ECO:0000269|PubMed:23306439,
CC ECO:0000269|PubMed:23333305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P70399-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P70399-5; Sequence=VSP_058927;
CC Name=3;
CC IsoId=P70399-6; Sequence=VSP_058926, VSP_058927;
CC -!- DOMAIN: The Tudor-like region mediates binding to histone H4
CC dimethylated at 'Lys-20' (H4K20me2) (PubMed:23209566). Interaction with
CC NUDT16L1/TIRR masks the Tudor-like domain and prevents recruitment to
CC chromatin (By similarity). {ECO:0000250|UniProtKB:Q12888,
CC ECO:0000269|PubMed:23209566}.
CC -!- DOMAIN: The UDR (ubiquitin-dependent recruitment) motif specifically
CC recognizes and binds histone H2A monoubiquitinated at 'Lys-15'
CC (H2AK15ub). Phosphorylation of the UDR blocks interaction with
CC H2AK15ub. {ECO:0000250|UniProtKB:Q12888}.
CC -!- PTM: Phosphorylated at basal level in the absence of DNA damage (By
CC similarity). Phosphorylated by ATM in response to DNA damage:
CC phosphorylation at different sites promotes interaction with different
CC set of proteins: phosphorylation at the N-terminus by ATM (residues
CC from 11-181) promotes interaction with PAXIP1 and non-homologous end
CC joining (NHEJ) of dysfunctional telomeres (By similarity).
CC Phosphorylation by ATM at residues that are located more C-terminus
CC (residues 300-650) leads to promote interaction with RIF1
CC (PubMed:23333305, PubMed:23306439). Interaction with RIF1 leads to
CC disrupt interaction with NUDT16L1/TIRR (By similarity). Phosphorylation
CC at Thr-1606 and Ser-1615 in the UDR motif blocks interaction with
CC H2AK15ub (By similarity). Dephosphorylated by PPP4C (By similarity).
CC Hyperphosphorylation during mitosis correlates with its exclusion from
CC chromatin and DNA lesions (By similarity). Hyperphosphorylated in an
CC ATR-dependent manner in response to DNA damage induced by UV
CC irradiation (By similarity). Dephosphorylated by PPP5C (By similarity).
CC {ECO:0000250|UniProtKB:Q12888, ECO:0000269|PubMed:23306439,
CC ECO:0000269|PubMed:23333305}.
CC -!- PTM: Asymmetrically dimethylated on Arg residues by PRMT1. Methylation
CC is required for DNA binding. {ECO:0000250|UniProtKB:Q12888}.
CC -!- DISRUPTION PHENOTYPE: Mice display growth retardation and are immune
CC deficient, radiation-sensitive and cancer-prone (PubMed:12640136).
CC Cells show a slight S-phase checkpoint defect and prolonged G2/M arrest
CC after treatment with ionizing radiation (PubMed:12640136). Cells show
CC defects in the DNA damage response (PubMed:12640136). Mice display
CC defects in immunoglobulin class-switch recombination (CSR) during
CC antibody genesis (PubMed:15159415, PubMed:15077110). In contrast, no
CC defects are observed in classic NHEJ and V(D)J recombination
CC (PubMed:15159415). {ECO:0000269|PubMed:12640136,
CC ECO:0000269|PubMed:15077110, ECO:0000269|PubMed:15159415}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH79906.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL929059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC035206; AAH35206.1; -; mRNA.
DR EMBL; BC079906; AAH79906.1; ALT_INIT; mRNA.
DR EMBL; AJ414734; CAC94013.1; -; mRNA.
DR EMBL; U67885; AAC52876.1; -; mRNA.
DR CCDS; CCDS50684.1; -. [P70399-1]
DR RefSeq; NP_001277759.1; NM_001290830.1.
DR RefSeq; NP_038763.3; NM_013735.4. [P70399-1]
DR RefSeq; XP_011237883.1; XM_011239581.2. [P70399-1]
DR PDB; 1SSF; NMR; -; A=1475-1629.
DR PDBsum; 1SSF; -.
DR AlphaFoldDB; P70399; -.
DR BMRB; P70399; -.
DR SMR; P70399; -.
DR BioGRID; 205144; 43.
DR DIP; DIP-31595N; -.
DR IntAct; P70399; 30.
DR MINT; P70399; -.
DR STRING; 10090.ENSMUSP00000106278; -.
DR ChEMBL; CHEMBL4295790; -.
DR iPTMnet; P70399; -.
DR PhosphoSitePlus; P70399; -.
DR SwissPalm; P70399; -.
DR EPD; P70399; -.
DR jPOST; P70399; -.
DR MaxQB; P70399; -.
DR PaxDb; P70399; -.
DR PeptideAtlas; P70399; -.
DR PRIDE; P70399; -.
DR ProteomicsDB; 260722; -. [P70399-1]
DR ProteomicsDB; 260723; -. [P70399-5]
DR ProteomicsDB; 260724; -. [P70399-6]
DR Antibodypedia; 1749; 996 antibodies from 41 providers.
DR DNASU; 27223; -.
DR Ensembl; ENSMUST00000110648; ENSMUSP00000106278; ENSMUSG00000043909. [P70399-1]
DR GeneID; 27223; -.
DR KEGG; mmu:27223; -.
DR UCSC; uc008lye.4; mouse.
DR CTD; 27223; -.
DR MGI; MGI:1351320; Trp53bp1.
DR VEuPathDB; HostDB:ENSMUSG00000043909; -.
DR eggNOG; KOG3548; Eukaryota.
DR GeneTree; ENSGT00390000011891; -.
DR InParanoid; P70399; -.
DR OMA; PIVDDTC; -.
DR TreeFam; TF350227; -.
DR Reactome; R-MMU-3232118; SUMOylation of transcription factors.
DR Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-MMU-5693571; Nonhomologous End-Joining (NHEJ).
DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
DR BioGRID-ORCS; 27223; 4 hits in 110 CRISPR screens.
DR ChiTaRS; Trp53bp1; mouse.
DR EvolutionaryTrace; P70399; -.
DR PRO; PR:P70399; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P70399; protein.
DR Bgee; ENSMUSG00000043909; Expressed in respiratory primordium and 263 other tissues.
DR ExpressionAtlas; P70399; baseline and differential.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:1990391; C:DNA repair complex; IDA:MGI.
DR GO; GO:0000776; C:kinetochore; IDA:MGI.
DR GO; GO:0016604; C:nuclear body; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005657; C:replication fork; IDA:MGI.
DR GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
DR GO; GO:0003684; F:damaged DNA binding; IDA:MGI.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0002039; F:p53 binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:MGI.
DR GO; GO:0003712; F:transcription coregulator activity; ISO:MGI.
DR GO; GO:0061649; F:ubiquitin modification-dependent histone binding; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0071481; P:cellular response to X-ray; IEA:Ensembl.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IDA:MGI.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IDA:UniProtKB.
DR GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; IDA:UniProtKB.
DR GO; GO:0045830; P:positive regulation of isotype switching; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:MGI.
DR CDD; cd04508; TUDOR; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 3.40.50.10190; -; 2.
DR InterPro; IPR015125; 53-BP1_Tudor.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF09038; 53-BP1_Tudor; 1.
DR SMART; SM00292; BRCT; 2.
DR SUPFAM; SSF52113; SSF52113; 2.
DR PROSITE; PS50172; BRCT; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Centromere; Chromosome;
KW DNA damage; DNA repair; DNA-binding; Isopeptide bond; Kinetochore;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1969
FT /note="TP53-binding protein 1"
FT /id="PRO_0000072644"
FT DOMAIN 1749..1845
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 1861..1961
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1034..1144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1178..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1267..1478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1481..1600
FT /note="Tudor-like"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT REGION 1492..1520
FT /note="Interaction with dimethylated histone H4"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT REGION 1624..1715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1393..1400
FT /note="GAR"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOTIF 1601..1628
FT /note="UDR"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT COMPBIAS 8..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..653
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..775
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..950
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1008
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1071
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1281..1326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1444..1478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1629..1658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1666..1680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 305
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 543
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 548
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 622
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 716
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 719
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 763
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 822
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 912
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 965
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 1018
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 1075
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 1096
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1211
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 1213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 1216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 1314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 1329
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 1352
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1359
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 1365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 1423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1427
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1457
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 1459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1470
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1471
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 1606
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 1615
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 1628
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1632
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 1635
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 1645
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 1653
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 1670
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 1675
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 1698
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT MOD_RES 1756
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT CROSSLNK 220
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT CROSSLNK 220
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT CROSSLNK 920
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT CROSSLNK 974
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT CROSSLNK 1362
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT CROSSLNK 1431
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT CROSSLNK 1431
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT CROSSLNK 1560
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT CROSSLNK 1560
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q12888"
FT VAR_SEQ 1..949
FT /note="Missing (in isoform 3)"
FT /id="VSP_058926"
FT VAR_SEQ 1101..1106
FT /note="Missing (in isoform 2 and isoform 3)"
FT /id="VSP_058927"
FT CONFLICT 145
FT /note="Missing (in Ref. 3; CAC94013)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="V -> A (in Ref. 3; CAC94013)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="A -> T (in Ref. 3; CAC94013)"
FT /evidence="ECO:0000305"
FT CONFLICT 675
FT /note="P -> A (in Ref. 3; CAC94013)"
FT /evidence="ECO:0000305"
FT CONFLICT 1070
FT /note="P -> L (in Ref. 2; AAH79906)"
FT /evidence="ECO:0000305"
FT CONFLICT 1071
FT /note="K -> N (in Ref. 2; AAH35206)"
FT /evidence="ECO:0000305"
FT CONFLICT 1183..1184
FT /note="EQ -> DE (in Ref. 4; AAC52876)"
FT /evidence="ECO:0000305"
FT CONFLICT 1187
FT /note="G -> R (in Ref. 3; CAC94013)"
FT /evidence="ECO:0000305"
FT CONFLICT 1206
FT /note="A -> T (in Ref. 4; AAC52876)"
FT /evidence="ECO:0000305"
FT CONFLICT 1271
FT /note="E -> G (in Ref. 4; AAC52876)"
FT /evidence="ECO:0000305"
FT CONFLICT 1359..1408
FT /note="Missing (in Ref. 2; AAH79906)"
FT /evidence="ECO:0000305"
FT CONFLICT 1771
FT /note="Q -> H (in Ref. 2; AAH79906)"
FT /evidence="ECO:0000305"
FT STRAND 1487..1490
FT /evidence="ECO:0007829|PDB:1SSF"
FT STRAND 1495..1505
FT /evidence="ECO:0007829|PDB:1SSF"
FT TURN 1508..1510
FT /evidence="ECO:0007829|PDB:1SSF"
FT STRAND 1511..1515
FT /evidence="ECO:0007829|PDB:1SSF"
FT STRAND 1521..1525
FT /evidence="ECO:0007829|PDB:1SSF"
FT TURN 1526..1528
FT /evidence="ECO:0007829|PDB:1SSF"
FT STRAND 1529..1532
FT /evidence="ECO:0007829|PDB:1SSF"
FT STRAND 1537..1545
FT /evidence="ECO:0007829|PDB:1SSF"
FT TURN 1547..1549
FT /evidence="ECO:0007829|PDB:1SSF"
FT STRAND 1551..1561
FT /evidence="ECO:0007829|PDB:1SSF"
FT STRAND 1564..1571
FT /evidence="ECO:0007829|PDB:1SSF"
FT STRAND 1574..1578
FT /evidence="ECO:0007829|PDB:1SSF"
FT HELIX 1580..1582
FT /evidence="ECO:0007829|PDB:1SSF"
FT STRAND 1583..1586
FT /evidence="ECO:0007829|PDB:1SSF"
FT HELIX 1587..1591
FT /evidence="ECO:0007829|PDB:1SSF"
FT TURN 1592..1596
FT /evidence="ECO:0007829|PDB:1SSF"
FT STRAND 1597..1599
FT /evidence="ECO:0007829|PDB:1SSF"
SQ SEQUENCE 1969 AA; 212735 MW; F673EA87B3BA1FDE CRC64;
MPGEQMDPTG SQLDSDFSQQ DTPCLIIEDS QPESQVLEED AGSHFSVLSR HLPNLQMHKE
NPVLDIVSNP EQSAVEQGDS NSSFNEHLKE KKASDPVESS HLGTSGSISQ VIERLPQPNR
TSSALAVTVE AASLPEEEKE EEELEEEKEG VGANAPGADS LAAEDSASSQ LGFGVLELSQ
SQDVEEHTVP YDVNQEHLQL VTTNSGSSPL SDVDASTAIK CEEQPTEDIA MIEQPSKDIP
VTVQPGKGIH VVEEQNLPLV RSEDRPSSPQ VSVAAVETKE QVPARELLEE GPQVQPSSEP
EVSSTQEDLF DQSSKTASDG CSTPSREEGG CSPVSTPATT LQLLQLSGQK PLVQESLSTN
SSDLVAPSPD AFRSTPFIVP SSPTEQGGRK DEPMDMSVIP VGGEPFQKLH DDEAMETEKP
LLPSQPAVSP QASTPVSRST PVFTPGSLPI PSQPEFSHDI FIPSPSLEEP SDDVKKGGGL
HSSSLTVECS KTSESEPKNF TDDLGLSMTG DSCKLMLSTS EYSQSSKMES LGSPRTEEDR
ENTQIDDTEP LSPVSNSKLP ADSENVLVTP SQDDQVEMSQ NVDKAKEDET EDRGDCKGRE
DAVAEDVCID LTCDSGSQAV PSPATRSEAL SSVLDQEEAM DTKEHHPEEG FSGSEVEEVP
ETPCGSHREE PKEEPMESIP LHLSLTETQS EALCLQKEAP KEECPEAMEV ETSVISIDSP
QKLQVLDQEL EHKDPDTWEE ATSEDSSVVI VDVKEPSPRA DVSCEPLEEV EKCSDSQSWE
GVAPEEEPCA ENRLDTPEEK RIECDGDSKA ETTEKDAVTE DSPQPPLPSV RDEPVRPDQE
TQQPQVQEKE SPVTVDAEVA DDKQLGPEGA CQQLEKAPAC ASQSFCESSS ETPFHFTLPK
EGDIIPPLTG ATPPLIGHLK LEPKRHSTPI GISNYPESTI ATSDVTSESM VEINDPLLGN
EKGDSESAPE MDGKLSLKMK LVSPETEASE ESLQFSLEKP TTAERKNGST AIAEPVASLQ
KPVPVFGCIY EAQQEKEAQS EAPPSAPDRA NLLHFPSAQE EDKERPDVTP KLRQSEQPVK
PVGPVMDDAA PEDSASPVSQ QRASQEQRAS QEPFSPAEDV METDLLEGLA ANQDRPSKML
MDRPTQSNIG IQTVDHSLCA PETVSAATQT VKSVCEQGTS TAEQNSGKQD ATVQTERGSG
EKPASAPVDD TESLHSQGEE EFEMPQPPHG HVLHRHMRTI REVRTLVTRV ITDVYYVDGT
EVERKVTEET EEPIVECQEC ETEVSPSQTG GSSGDLGDIS SFSSKASSSH HTSSGTSLSA
IHSSGSSGRG AGPLKGKASG TEAADFALPS SRGGPGKLSP RKGISQTGAP VCEEDGDAGL
GIRQGGKAPV TPRGRGRRGR PPSRTTGTRE TVVSGPLGVE DISPSMSPDD KSFTRIMPRV
PDSTKRTDAS SSTLRRSDSP EIPFQAATGS SDGLDSSSSG NSFVGLRVVA KWSSNGYFYS
GKITRDVGAG KYKLLFDDGY ECDVLGKDIL LCDPIPLDTE VTALSEDEYF SAGVVKGHRK
ESGELYYSIE KEGQRKWYKR MAVILSLEQG NRLREQYGLG PYEAVTPLTK AADISLDNLV
EGKRKRRSNI SSPVTPTAAS SSSTTPTRKA TESPRASTGV PSGKRKLPTS EEERSPAKRG
RKSATVKPGT VGAAEFVSPC ETGDNIGEPS VLEEPRGPLP LNKTLFLGYA FLLTMATTSD
KLASRSKLLD GPTGSSEEEE EFLEIPPFNK QYTECQLRAG AGYILEDFNE AQCNTAYQCL
LIADQHCRTR KYFLCLASGI PCVSHVWVHD SCHANQLQNY RNYLLPAGYS LEEQRILDWQ
PRENPFQNLK VLLVSDQQQN FLELWSEILM TGGAASVKQH HSSAHNKDIA LGVFDVVVTD
PSCPASVLKC AEALQLPVVS QEWVIQCLIV GERIGFKQHP KYKHDYVSH
