ID A0A0D9R9T7_CHLSB Unreviewed; 1977 AA.
AC A0A0D9R9T7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Tumor protein p53 binding protein 1 {ECO:0000313|Ensembl:ENSCSAP00000005376.1};
GN Name=TP53BP1 {ECO:0000313|Ensembl:ENSCSAP00000005376.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000005376.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000005376.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000005376.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AQIB01116194; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01116195; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_008015041.1; XM_008016850.1.
DR STRING; 60711.ENSCSAP00000005376; -.
DR Ensembl; ENSCSAT00000007189.1; ENSCSAP00000005376.1; ENSCSAG00000009121.1.
DR GeneID; 103245740; -.
DR CTD; 7158; -.
DR eggNOG; KOG3548; Eukaryota.
DR GeneTree; ENSGT00390000011891; -.
DR OMA; EPCVENR; -.
DR OrthoDB; 5403076at2759; -.
DR BioGRID-ORCS; 103245740; 0 hits in 9 CRISPR screens.
DR Proteomes; UP000029965; Chromosome 26.
DR Bgee; ENSCSAG00000009121; Expressed in caudate nucleus and 7 other cell types or tissues.
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:UP000029965}.
FT DOMAIN 1729..1853
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 1869..1969
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1133..1153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1188..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1273..1483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1627..1724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1750..1773
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..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..908
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1087
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1289..1334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1637..1660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1674..1688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1977 AA; 214269 MW; 091AF59C3F1A6BDE CRC64;
MPGEQMDPTG SQLDSDFSQQ DTPCLIIEDS QPESQVLEDD SGSHFSMLSR HLPNLQTHKE
NPVLDVVSNP EQTAGEERGD SNSGFNEHLK ENKVADPVDS SNLDTCGSVS QVIEQLPQPN
RTSSVLGMSV ESAPAVEEEK GEELKQKEKE KEEDTSGNTT HSLGAEDTAS SQLGFGVLEL
SQSQDVEENT VPYEVDKEHL QSVTTNSGYT RLSDVDANAA IKHEEQSNED IPIAERSSKD
IPVTAQPSKD VHVVKEQNLP PARSEDMRFS PKVCLAAVEA KEQLSAQELT ECGLQIQKSP
EPEVLSTQED LFDQSNKTVS SDGCSTPSRE EGGCSLASTP ATTLHLLQLS GQRSLVQESL
STNSSDLVAP SPDAFRSTPF IVPSSPTEQE GRQDKPMDMS VLSEEGGEPF QKKLQSDEPV
ELENRPLPPE PAVSPQASTP ISQSTPVFTS GSLPIPSQPQ FSHDIFIPSP SLEEQSNDGK
KDGDLHSSSL TVECSKTSEI EPKNSPEDLG LSLTGDSCKL MLSTSEYSQS PKMESLSSHR
IDEDGENTQI EDTEPMSPVL NSKFIPAEND SILMNPAQDG EVQLSQNDDK TKGDDTDTRD
DISILATGCK GREETVAEDV CIDLTCDSGS QAVPSPATRS EALSSVLDQE EAMEIKEHHP
EEGSSGSEVE EIPETPCESQ GEELKEENME SVPLHLSLTE TQSQGLCLQK EIPKKECSEA
MEVETSVITI DSPQKLAILD QELEHKDQEA WEEATSEDSS VVIVDVKEPS PRVDVSCEPL
EGVEKCSDSQ SWEDVAPEIE PCAENRLDTK EEKSVEYEGV LKSGTAEAEP VEEDSSQPPL
PLVRADDPLR LDQELQQPQT QEKTNNLLTE DSKMANAKQL SSGAEAQKLG KPSAHASQSF
CESSSETPFH FTLPKEGDII PPLTGATPPL IGHLKLEPKR HSTPIGISNY PESTIAASDV
MSESMVETHD PILGSDKGDS GAAPDMDDKL CLRMKLVSPE TEASEESLQF NLEKPATGER
KNGSTAVAES VASPQKTMSV FSCICEARQE NEAGSEDPPT APIRGNLLHF PSSQGEEEKE
KLEGDHTIRQ SQQPMKPISP VKDPVSPASQ KMVIQGPSSP QGETMVTHVL EDQKEGRNTN
QENPSKALIE RPSQNNIGIQ TMEYSLRVPE TVSAATQTIK NVCEQGTSTV DQNCGKQDAT
VQTERGSGEK PVSASGDDTE SLHSQGEEEF DMPQPPHGHV LHRHMRTIRE VRTLVTRVIT
DVYYVDGTEV ERKVTEETEE PIVECQECET EVSPSQTGGS SGDLGDISSF SSKASSLHRT
SSGTSLSAMH SSGSSGKGAG PLKGKTSGTE PADFALPSSR GGPGKLSPRK GVSQTGTPVC
EEDGDAGLGI RQGGKAPVTP RGRGRRGRPP SRTTGTRETA VPGPLGIEDI SPNLSPDDKS
FSRVVPRVPD STRRTDVGAG ALRRSDSPEI PFQAAAGPSD GLDASSPGNS FVGLRVVAKW
SSNGYFYSGK ITRDVGAGKY KLLFDDGYEC DVLGKDILLC DPIPLDTEVT ALSEDEYFSA
GVVKGHRKES GELYYSIEKE GQRKWYKRMA VILSLEQGNR LREQYGLGPY EAVTPLTKAA
DISLDNLVEG KRKRRSNVSS PATPTASSSS STTPTRKITE SPRASMGVLS GKRKLTTSEE
ERSPAKRGRK SATVKPGAVG AGEFVSPCES GDNTGEPSAL EEQRGPLPLN KTLFLGYAFL
LTMATTSDKL ASRSKLSDGP TGSSEEEEEF LEIPPFNKQY TESQLRAGAG YILEDFNEAQ
CNTAYQCLLI ADQHCRTRKY FLCLASGIPC VSHVWVHDSC HANQLQNYRN YLLPAGYSLE
EQRILDWQPR ENPFQNLKVL LVSDQQQNFL ELWSEILMTG GAASVKQHHS SAHNKDIALG
VFDVVVTDPS CPASVLKCAE ALQLPVVSQE WVIQCLIVGE RIGFKQHPKY KHDYVSH
//
