ID A0A096N6U5_PAPAN Unreviewed; 1975 AA.
AC A0A096N6U5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Tumor protein p53 binding protein 1 {ECO:0000313|Ensembl:ENSPANP00000008222.3};
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000008222.3, ECO:0000313|Proteomes:UP000028761};
RN [1] {ECO:0000313|Ensembl:ENSPANP00000008222.3, ECO:0000313|Proteomes:UP000028761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT "Whole Genome Assembly of Papio anubis.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPANP00000008222.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR Ensembl; ENSPANT00000017850.3; ENSPANP00000008222.3; ENSPANG00000018477.3.
DR eggNOG; KOG3548; Eukaryota.
DR GeneTree; ENSGT00390000011891; -.
DR HOGENOM; CLU_002167_0_0_1; -.
DR OMA; EPCVENR; -.
DR Proteomes; UP000028761; Chromosome 7.
DR Bgee; ENSPANG00000018477; Expressed in mammillary body and 66 other cell types or tissues.
DR ExpressionAtlas; A0A096N6U5; baseline.
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:UP000028761}.
FT DOMAIN 1727..1851
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 1867..1967
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1000..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1049..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1186..1235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1271..1481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1625..1722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1748..1771
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..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..816
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..906
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1085
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1186..1207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1219..1235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1287..1332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1635..1658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1672..1686
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1975 AA; 214016 MW; A90BA84135CE0101 CRC64;
MPGEQMDPTG SQLDSDFSQQ DTPCLIIEDS QPESQVLEDD SGSHFSMLSR HLPNLQTHKE
NPVLDVVSNP EQTAGEERGD SSSGFNEHLK ENKIADPVDS SNLDTCGSIS QVIEQLPQPN
RTSSVLGMSV ESAPAVEEEK GEELKQKEKE KEEDTSGNTT HSLGAEDTAS SQLGFGVLEL
SQSQDVEENT VPYEADKEHL QSVTTNSGYT RPSDVDANDA IKHEEQSNED IPIAERSSKD
IPVTAQPSKD VHVVKEQNPP PARSEDMRFS PKVAAMEAKE QFSAQELTEC GLQIQKSPEP
EVLSTQEDLF DQSNKTVSSD GCSTPSREEG GCSLASTPAT TLHLLQLSGQ RSLVQESLST
NSSDLVAPSP DAFRSTPFIV PSSPTEQEGR QDKPMDMSML SEGGGEPFQK KLQSDEPVEL
ENHPLPPEPT VSPQASTPIS QSTPVFTSGS LPIPSQPQFS HDIFIPSPSL EEQSNNGKKD
GDLHSSSLTV ECSKTSEIEP KNSPEDLGLS LTGDSCKLML STSEYSQSPK MESLSSHRID
EDGENTQIED TEPMSPVLNS KFIPAENDSI LMNPAQDGEV QLSQNDDKTK GDDTDTRDDI
SILATGCKGR EETVAEDVCI DLTCDSGSQA VPSPATRSEA LSSVLDQEEA MEIKEHHPEE
GSSGSEVEEI PETPCESQGE ELKEENMESV PLHLSLTETQ SQGLCLQKES PKKECSEAME
VETSVISIDS PQKLAILDQE LEHKDQEAWE EATSEDSSVV IVDVKEPSPR VDVSCEPLEG
VEKCSDSQSW EDVAPEIEPC AENRLDTKEE KSVEYEGVLK SGTAEAEPVE EDSSQPPLPL
VRADDPLRLD QELRQPQTQE KTNNLLTEDL KMANAKQLSS GAEAQKLGKP SAHASQSFCE
SSSETPFHFT LPKEGDIIPP LTGATPPLIG HLKLEPKRHS TPIGISNYPE STIAASDVMS
ESMVETHDPI LGSDKGDSGA APDMDDKLCL RMKLVSPETE ASEESLQFNL EKPATGERKN
GSTAVAESVA SPQKTMSVFS CICEVRQENE AGSEDPPTAP IRGNLLHFPS SQGEEEKEKL
EGDHTIRQSQ QPMKPISPVK DPVSPASQKM VIQGPSSPQG EAMVTDVLED QKEGRNTNQE
NPSKALIERP SQNNIGIQTM ECSLRVPETV SAATQTIKNV CEQGTSTVDQ NCGKQDATVQ
TERGSGEKPV SASGDDTESL HSQGEEEFDM PQPPHGHVLH RHMRTIREVR TLVTRVITDV
YYVDGTEVER KVTEETEEPI VECQECETEV SPSQTGGSSG DLGDISSFSS KASSLHRTSS
GTSLSAMHSS GSSGKGAGPL KGKTSGTEPA DFALPSSRGG PGKLSPRKGV SQTGTPVCEE
DGDAGLGIRQ GGKAPVTPRG RGRRGRPPSR TTGTRETAVP GPLGIEDISP NLSPDDKSFS
RVVPRVPDST RRTDVGAGAL RRSDSPEIPF QAAAGPSDGL DASSPGNSFV GLRVVAKWSS
NGYFYSGKIT RDVGAGKYKL LFDDGYECDV LGKDILLCDP IPLDTEVTAL SEDEYFSAGV
VKGHRKESGE LYYSIEKEGQ RKWYKRMAVI LSLEQGNRLR EQYGLGPYEA VTPLTKAADI
SLDNLVEGKR KRRSNVSSPA TPTASSSSST TPTRKITESP RASMGVLSGK RKLITSEEER
SPAKRGRKSA TVKPGAVGAG EFVSPCESGD NTGEPSALEE QRGPLPLNKT LFLGYAFLLT
MATTSDKLAS RSKLSDGPTG SSEEEEEFLE IPPFNKQYTE SQLRAGAGYI LEDFNEAQCN
TAYQCLLIAD QHCRTRKYFL CLASGIPCVS HVWVHDSCHA NQLQNYRNYL LPAGYSLEEQ
RILDWQPREN PFQNLKVLLV SDQQQNFLEL WSEILMTGGA ASVKQHHSSA HNKDIALGVF
DVVVTDPSCP ASVLKCAEAL QLPVVSQEWV IQCLIVGERI GFKQHPKYKH DYVSH
//
