ID M3YFT0_MUSPF Unreviewed; 1969 AA.
AC M3YFT0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=TP53-binding protein 1 isoform X1 {ECO:0000313|RefSeq:XP_004751297.1};
DE SubName: Full=Tumor protein p53 binding protein 1 {ECO:0000313|Ensembl:ENSMPUP00000010187.1};
GN Name=TP53BP1 {ECO:0000313|Ensembl:ENSMPUP00000010187.1,
GN ECO:0000313|RefSeq:XP_004751297.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000010187.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000010187.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004751297.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004751297.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AEYP01028374; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01028375; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01028376; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01028377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01028378; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01028379; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01028380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01028381; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01028382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01028383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004751297.1; XM_004751240.3.
DR STRING; 9669.ENSMPUP00000010187; -.
DR Ensembl; ENSMPUT00000010349.1; ENSMPUP00000010187.1; ENSMPUG00000010262.1.
DR GeneID; 101687215; -.
DR KEGG; mpuf:101687215; -.
DR CTD; 7158; -.
DR eggNOG; KOG3548; Eukaryota.
DR GeneTree; ENSGT00390000011891; -.
DR HOGENOM; CLU_002167_0_0_1; -.
DR OMA; EPCVENR; -.
DR OrthoDB; 5403076at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:1990391; C:DNA repair complex; IEA:Ensembl.
DR GO; GO:0000776; C:kinetochore; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0005657; C:replication fork; IEA:Ensembl.
DR GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
DR GO; GO:0003684; F:damaged DNA binding; IEA:Ensembl.
DR GO; GO:0140566; F:histone reader activity; IEA:Ensembl.
DR GO; GO:0035064; F:methylated histone binding; IEA:Ensembl.
DR GO; GO:0002039; F:p53 binding; IEA:Ensembl.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0042162; F:telomeric DNA binding; IEA:Ensembl.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:Ensembl.
DR GO; GO:0061649; F:ubiquitin modification-dependent histone binding; IEA:Ensembl.
DR GO; GO:0097680; P:double-strand break repair via classical nonhomologous end joining; IEA:Ensembl.
DR GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; IEA:Ensembl.
DR GO; GO:0045830; P:positive regulation of isotype switching; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
DR CDD; cd17745; BRCT_p53bp1_rpt1; 1.
DR CDD; cd17724; BRCT_p53bp1_rpt2; 1.
DR CDD; cd20383; Tudor_53BP1; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 2.
DR InterPro; IPR015125; 53-BP1_Tudor.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR047249; BRCT_p53bp1-like_rpt1.
DR InterPro; IPR047250; BRCT_p53bp1-like_rpt2.
DR InterPro; IPR014722; Rib_uL2_dom2.
DR InterPro; IPR047252; TP53BP1-like.
DR PANTHER; PTHR15321:SF3; TP53-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR15321; TUMOR SUPPRESSOR P53-BINDING PROTEIN 1; 1.
DR Pfam; PF09038; 53-BP1_Tudor; 1.
DR Pfam; PF18428; BRCT_3; 1.
DR SMART; SM00292; BRCT; 2.
DR SUPFAM; SSF52113; BRCT domain; 2.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR PROSITE; PS50172; BRCT; 2.
PE 4: Predicted;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715}.
FT DOMAIN 1721..1845
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 1861..1961
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 996..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1178..1229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1266..1432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1451..1475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1619..1716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1742..1763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..154
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..825
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1068
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1086
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1149
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..1229
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 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"
SQ SEQUENCE 1969 AA; 212464 MW; 7FBED34D11349F5F CRC64;
MPGEQMDPTG SQLDSDFSQQ DTPCLIIEDS QPESQVLEDD SGSHFSMLSR HLPNLQTHKE
NPVLDVVSNP EQTAGEEQGD SNSGFNEHLK ENKAAEPMDS SHLDTCSSIS QVIEQLPQPN
RTSSVLGISV ESAPPVGEEK EEDMEEEEEE KEEDTRDGTI THSLGAEDSA SSQLGFGVLE
LSQSQDVEEH TVPYEVAKEP PLSVTTNSTY TRLSDVDANT GSKHEEQSIE DTPTAEQPSK
GVPVAAQPSK DVHVVEEQNS PPGRSEESPK VSLAAVETNE RVTAQELLQG GLKIQKSPEP
EVLSTQEDLF DQSNKTASDG CSTPSREEGG CSLASTPATT LHVLQLSGQR SLAQESLSTN
SSDLVAPSPD AFRSTPFIVP SSPTEQEGRK DEPMDMSVLS EGKGESFEKK LENDEPVETE
NPPLPPESTV SPQASTPVSQ STPVFTPGSL PIPSQPEFSH DIFIPSPSLE ERSSDGKKGG
DLHSSSLTVE CSKTSETEPK NATEDLGLSL TGDSCKLMLS TSEYSQSPKM ESLSSHRIDE
DGENTQIEDT EPMSPVLNSK LAPAENDNIL MNPAQDGQVE LNQNDKTRGD DTETRDDIGI
LASGCKGREE TVAEDVCIDL TCDSGSQAVP SPATRSEALS SVLDQEEAME IKEHHPEEGS
SGSEVEEIPE TPCESQGEEP KGENTESVPL HLSLTETQSQ AFCLPKEIPK QECQEAMEVE
TSVISIDSPQ KIPVPDQELE HKDQEAWEEV TSEDSSVVIV DVKEPSPRVD VSSEPLEGVE
KCSDSQSWED DAPEIEPCAE NRADAQEGKS AEYEGDLKSV TAEKEPVEVH SSQPPLTLER
AGDALGPDLE MQQAEPPEKT DNSLTKDSKI ANAKQLGSSV EAPELEKGSA HASQSFCESS
SETPFHFTLP KEGEIIPPLT GATPPLIGHL KLEPKRHSTP IGISNYPEST IATSDVMSES
MVESNDPILG NVKGDLGAAP EMDDKLCLKM KLVSPVTETS EESLQFSLEK PTTGERKNGS
TAVAEAVASS PKTVSVFSCV CEAQQDDEAR SQNPPSVPMR GNSLSFPSTQ DEEEKEKLEG
EQRTRKSQQP MKPSCPVKDP PSPVSQQVAT QGPSSPQGEA METDVLEGQN TNQEKPSNAL
TERPSQNNIG IQTIERSLWV PETVSAATQT VKNVCEQGTS TVDQNSGKQD ATVQTERGTG
EKPVSAPGDD TESLHSQGEE EFDMPQPPHG HVLHRHMRTI REVRTLVTRV ITDVYYVDGT
EVERKVTEET EEPIVECQEC ETEVSPSQTG GSSGDLGDIS SFSSKASSLH RTSSGTSLSA
MHSSGSSGRG AGPLKGKTSG TEPADFALPS SRGGPGKLSP RKGVSQTGAP VCEEDGDAGL
GIRQGGKAPV TPRGRGRRGR PPSRTTGTRE AAVPGPLGIE DISPSMSPED KSFTRIVPRV
PDSTRRADVG AGALRRSDSP EIPFQAAAGP SDGLDASSPG NSFVGLRVVA KWSSNGYFYS
GKITRDVGAG KYKLLFDDGY ECDVLGKDIL LCDPIPLDTE VTALSEDEYF SAGVVKGHRK
ESGELYYSIE KEGQRKWYKR MAVILSLEQG NRLREQYGLG PYEAVTPLTK AADISLDNLV
EGKRKRRSNI SSPATPAASS SSSTTPTRKT TESPRASSGV PSGKRKLITS EEERSPAKRG
RKSATVKPGA VGAGEFVSPC ESGDNMGEPS ALEEQRGPLP LNKTLFLGYA FLLTMATTSD
KLASRSKLPD GPTGSSEEEE EFLEIPPFNK QYTESQLRAG AGYILEDFNE AQCNTAYQCL
LIADQHCRTR KYFLCLASGI PCVSHVWVHD SCHANQLQNY RNYLLPAGYS LEEQRILDWQ
PRENPFHNLK VLLVSDQQQN FLELWSEILM TGGAASVKQH HSSAHNKDIA LGVFDVVVTD
PSCPASVLKC AEALQLPVVS QEWVIQCLIV GERIGFKQHP KYKHDYVSH
//
