ID A0A2R8ZMW5_PANPA Unreviewed; 1473 AA.
AC A0A2R8ZMW5;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=DNA topoisomerase II binding protein 1 {ECO:0000313|Ensembl:ENSPPAP00000006289.1};
GN Name=TOPBP1 {ECO:0000313|Ensembl:ENSPPAP00000006289.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000006289.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000006289.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000006289.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AJFE02078328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02078329; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02078330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02078331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; A0A2R8ZMW5; -.
DR STRING; 9597.ENSPPAP00000006289; -.
DR Ensembl; ENSPPAT00000027356.1; ENSPPAP00000006289.1; ENSPPAG00000024667.1.
DR GeneTree; ENSGT00940000157001; -.
DR OMA; NVHCLKT; -.
DR Proteomes; UP000240080; Chromosome 3.
DR Bgee; ENSPPAG00000024667; Expressed in testis and 6 other cell types or tissues.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0070532; C:BRCA1-B complex; IEA:Ensembl.
DR GO; GO:0000794; C:condensed nuclear chromosome; IEA:Ensembl.
DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0016605; C:PML body; IEA:Ensembl.
DR GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
DR GO; GO:0140463; F:chromatin-protein adaptor activity; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0140031; F:phosphorylation-dependent protein binding; IEA:Ensembl.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IEA:Ensembl.
DR GO; GO:0051276; P:chromosome organization; IEA:Ensembl.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:Ensembl.
DR GO; GO:0000076; P:DNA replication checkpoint signaling; IEA:Ensembl.
DR GO; GO:0097681; P:double-strand break repair via alternative nonhomologous end joining; IEA:Ensembl.
DR GO; GO:0097680; P:double-strand break repair via classical nonhomologous end joining; IEA:Ensembl.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:Ensembl.
DR GO; GO:1990166; P:protein localization to site of double-strand break; IEA:Ensembl.
DR GO; GO:0010212; P:response to ionizing radiation; IEA:Ensembl.
DR CDD; cd17737; BRCT_TopBP1_rpt1; 1.
DR CDD; cd17731; BRCT_TopBP1_rpt2_like; 1.
DR CDD; cd17718; BRCT_TopBP1_rpt3; 1.
DR CDD; cd17749; BRCT_TopBP1_rpt4; 1.
DR CDD; cd18434; BRCT_TopBP1_rpt5; 1.
DR CDD; cd17727; BRCT_TopBP1_rpt6; 1.
DR CDD; cd17738; BRCT_TopBP1_rpt7; 1.
DR CDD; cd17728; BRCT_TopBP1_rpt8; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 10.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR035960; Secretoglobin_sf.
DR InterPro; IPR049542; TopBP1-like_BRCT0.
DR InterPro; IPR044737; TopBP1_BRCT_1.
DR PANTHER; PTHR13561; DNA REPLICATION REGULATOR DPB11-RELATED; 1.
DR PANTHER; PTHR13561:SF20; DNA TOPOISOMERASE 2-BINDING PROTEIN 1; 1.
DR Pfam; PF00533; BRCT; 7.
DR Pfam; PF21298; TopBP1_BRCT0; 1.
DR SMART; SM00292; BRCT; 7.
DR SUPFAM; SSF52113; BRCT domain; 6.
DR SUPFAM; SSF48201; Uteroglobin-like; 1.
DR PROSITE; PS50172; BRCT; 7.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000240080}.
FT DOMAIN 115..164
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 187..276
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 331..421
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 525..610
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 618..715
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 877..968
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 1236..1328
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 471..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 998..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1454..1473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1035
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1473 AA; 165454 MW; 725AB31B80D7672F CRC64;
MSRNDKEPFF VKFLKSSDNS KCFFKALESI KEFQSEEYLQ IITEEEALKI KENDRSLYIC
DPFSGVVFDH LKKLGCRIVG PQVVIFCMHH QRCVPRAEHP VYNMVMSDVT ISCTKVHKYV
QMMGGRVYRD LNVSVTHLIA GEVGSKKYLV AANLKKPILL PSWIKTLWEK SQEKKITRYT
DINMEDFKCP IFLGCIICVT GLCGLDRKEV QQLTVKHGGQ YMGQLKMNEC THLIVQEPKG
QKYECAKRWN VHCVTTQWFF DSIEKGFCQD ESIYKTEPRP EAKTMPNSST PTSQINTIDS
RTLSDVSNIS NINASCISES ICNSLNSKLE PTLENLENLD IYLCGFSGRK LDKLRRLINS
GGGVRFNQLN EDVTHVIVGD YDDELKQFWN KSAHRPHVVG AKWLLECFSK GYMLSEEPYI
HANYQQVEIP VSHQPESKAA LLKKKNSSFS KKDFAPSEKH EQADEDLLSQ YENDSSTVVE
AKTSEARPFN DSTHAEPLND STHISLQEEN QSSVSHCVPD VSTITEEGLF SQKSFLVLGF
SNENESNIAN IIKENAGKIM SLLSRTVVDY AVVPLLGCEV EATVGEVVTN TWLVTCIDYQ
TLFDPKSNPL FTPVPVMTGM TPLEDCVISF SQCAGAEKES LTFLANLLGA SVQEYFVRKS
NAKKGMFAST HLILKERGGS KYEAAKKWNL PAVTIAWLLE TARTGKRADE SHFLIENSSK
EERSLETEIT NGINLNSDTA EHPGTRLQTH RKTVVTPLDM NRFQSKAFRA VVSQHARQVA
ASPAVGQPLQ KEPSLHLDTP SKFLSKDKLF KPSFDVKDAL AALETPGRPS QQKRKLSTPL
SEVIVKNLQL ALANSSRNAV ALSASPQLKE AQSEKEEAPK PLHKVVVCVS KKLGKKQSEL
NGIAASLGAD YRWSFDETVT HFIYQGRPND TNREYKSVKE RGVHIVSEHW LLDCAQECKH
LPESLYPHTY NPKMSLDISA VQDGRLCNSR LLSAVSATKD DEPDPLILEE NDVDNMATNN
KESAPSNGSG KNDSKGVLTQ TLEMRENFQK QLQEIMSATS IVKPQGQRTS LSRSGCNSAS
STPDSTRSAR SGRSRVLEAL RQSRQTVPDV NTEPSQNEQI IWDDPTAREE RARLASNLQW
PSCPTQYSEL QVDIQNLEDS PFQKPLHDSE IAKQAVCDPG NIRVTEAPKH PISEELETPI
KDSHLIPTPQ APSIAFPLAN PPVAPHPREK IIMIEETHEE LKKQYIFQLS SLNPQERIDY
CHLIEKLGGL VIEKQCFDPT CTHIVVGHPL RNEKYLASVA AGKWVLHRSY LEACRTAGHF
VQEEDYEWGS SSILDVLTGI NVQQRRLALA AMRWRKKIQQ RQESGIVEGA FSGWKVILHV
DQSREAGFKR LLQSGGAKVL PGHSVPLFKE NVYCLRTEYI ADYLMQESPP HVENYCLPEA
ISFIQNNKEL GTGLSQKRKA PAEKNKIKRP RVH
//
