TOB1B_XENLA
ID TOB1B_XENLA Reviewed; 1513 AA.
AC Q7ZZY3;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=DNA topoisomerase 2-binding protein 1-B;
DE AltName: Full=DNA topoisomerase II-binding protein 1-B;
DE Short=TopBP1-B;
DE AltName: Full=Xmus101 {ECO:0000312|EMBL:AAP03894.1};
GN Name=topbp1-B; Synonyms=mus101 {ECO:0000303|PubMed:12438414};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAP03894.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Ovary {ECO:0000269|PubMed:12438414};
RX PubMed=12438414; DOI=10.1083/jcb.200207090;
RA Van Hatten R.A., Tutter A.V., Holway A.H., Khederian A.M., Walter J.C.,
RA Michael W.M.;
RT "The Xenopus Xmus101 protein is required for the recruitment of Cdc45 to
RT origins of DNA replication.";
RL J. Cell Biol. 159:541-547(2002).
CC -!- FUNCTION: Has dual roles in initiation of DNA replication, and
CC regulation of checkpoint responses. Required for DNA replication
CC initiation but not for the formation of pre-replicative complexes or
CC the elongation stages. Necessary for the loading of replication factors
CC onto chromatin, including gemc1, cdc45, DNA polymerases and components
CC of the GINS complex such as ginsl/sld5. Binds chromatin in both S-phase
CC cyclin-dependent kinase (S-CDK)-independent and S-CDK-dependent modes.
CC Chromatin binding is required for the action of S-CDK, which in turn
CC triggers the formation of preinitiation complexes of DNA replication.
CC Its role in checkpoint activation is independent of the DNA replication
CC role. In response to DNA damage, triggers the recruitment of checkpoint
CC signaling proteins on chromatin, which activate the chek1 signaling
CC pathway and block S-phase progression. Increases the kinase activity of
CC atr to numerous substrates, and is required for the phosphorylation of
CC Rad1. {ECO:0000269|PubMed:12438414}.
CC -!- SUBUNIT: Interacts with cdc45. Interacts (via BRCT domains) with ticrr;
CC interaction is cdk2-dependent. Interacts with atr in the presence of
CC atrip. Interacts with recql4 (via N-terminus) (By similarity).
CC {ECO:0000250|UniProtKB:Q800K6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12438414}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Chromosome
CC {ECO:0000250}. Note=Associates with chromatin.
CC {ECO:0000269|PubMed:12438414}.
CC -!- DOMAIN: The N-terminal half is sufficient for DNA replication.
CC {ECO:0000250|UniProtKB:Q800K6}.
CC -!- PTM: Phosphorylation at 1131 is essential for phosphorylation of chek1,
CC and thus for checkpoint regulation. {ECO:0000250}.
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DR EMBL; AY253323; AAP03894.1; -; mRNA.
DR AlphaFoldDB; Q7ZZY3; -.
DR SMR; Q7ZZY3; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd17737; BRCT_TopBP1_rpt1; 1.
DR Gene3D; 3.40.50.10190; -; 9.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR035960; Secretoglobin_sf.
DR InterPro; IPR044737; TopBP1_BRCT_1.
DR Pfam; PF00533; BRCT; 5.
DR Pfam; PF12738; PTCB-BRCT; 1.
DR SMART; SM00292; BRCT; 9.
DR SUPFAM; SSF48201; SSF48201; 1.
DR SUPFAM; SSF52113; SSF52113; 6.
DR PROSITE; PS50172; BRCT; 7.
PE 2: Evidence at transcript level;
KW Cell cycle; Chromosome; Cytoplasm; Cytoskeleton; DNA damage; DNA repair;
KW DNA replication; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..1513
FT /note="DNA topoisomerase 2-binding protein 1-B"
FT /id="PRO_0000397211"
FT DOMAIN 101..189
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 194..283
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 354..444
FT /note="BRCT 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 538..611
FT /note="BRCT 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 629..726
FT /note="BRCT 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 892..984
FT /note="BRCT 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 1253..1344
FT /note="BRCT 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 1383..1480
FT /note="BRCT 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 289..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 844..850
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 1508..1511
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 786..803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q800K6"
SQ SEQUENCE 1513 AA; 169121 MW; D6B5A3D201D067C3 CRC64;
MASSENAPFC VKFMKCGENS EYFLKGYEAM KQIQSDESLQ LTEEREALVL KEKDKCVYIC
DPFSGAAFSH LKKLGCRIVG PQVVIFCMES QRRVPRAEYP VYNMAMADVT ISCTSLDKET
REDVHHYVQI MGGCVYRDLN VSVTHLIAGE VGSNKYLVAA SLEKPILLPS WVKELWEKSN
QRIIRYSDVN MTEYLCPIFR GCTICVTGLS SLDRKEVQRL TALHGGEYTG QLKMNESTHL
IVQEAKGQKY ECARKWIVHC ISVQWFFDSI EKGFCQDETM YKIEPASTIK SVPDTSTPTG
GNSKPNSRTL YDVSQISNIS TSCVNESAFN SAMASRLDPP ADTLENLDIS SLQAPDDLLD
GCRIYLCGFG GRKLDKLRKL INNGGGVRFN QLTGDVTHII VGETDEELKQ FLNKTQHRPY
VLTVKWLLDS FAKGHLQPEE IYFHSSYQQT EMPSPFEPAI NLTANKMSST RDPLNHTRNH
QADEDLLSQY TENNSTLIED EHPKTSNTNS ISQITCSEDL TTCTSQSGLA DPSTIIEGGL
FSRKQFMVLG FLEEDEACII DIRKKSAGKV LSSQKRAIAD YAVVPLLGCE VESTVGEVVT
NAWLGMCIEQ EKLLDPHSNA LFTPVPFLEG STPLRECVLS VSQFMGAERD SLVYLAGLLG
AKVQEFFVRK ANPKKGMFAR SHLDLKDAEG SKYEAAKKWN LPAVTMNWLL QCARTGKKAD
EDSYLVDNVP EEDKDESFIN QTYKPQAIRL SMHAPCHLEN HPEALTKAAV TPLDMNRFKS
KACQSVISQH NKNPQTSGGE SKVLQREPSL HLDTPSKFLS KDKLFKPSFD VKDALAALET
PGGPNQKNRT QSTPLSEVIG RNLQLAIANS TRQTAAVTAS PQLKAAEKKE FDNSKLLINV
VICVSKKLIK KQGELNGIAA SLGAEYRWCF DESVTHFIYH GRQNDMSREY KSVKERSGIY
IVSEHWLFAC SEQQKRVPEA LYPHTYNPKM SLDISAVKMG SYTASKFSAD TSLQQDENSE
LQLQQNNKFG ETSDDQVKKA AGDGNPQNPS KDVKGALTQT LEMRENFQRQ LQEFMSATSV
VKPRGSVGRA GFDNSPCTPE GARSTRNGRS RVLEALRQSR QAMTDLNTEP SQNEQIIWDD
PTAREERAKL VSNLQWPDSP SQYSEQLQHN MNDAGGNYTP AKESLTDTEI AELEACEFEP
KSAMRTPVIE NNLQSPTKPD HLTPTPQAPS IAFPLANPPV APQPREKPVQ PFSKEETLKE
RRFQLSSLDP QERIDYSQLI EELGGVVIEK QCFDPSCTHI VVGHPLRNEK YLASMAAGKW
VLHRSYLEAC RAAKRFIQEE DYEWGSMSIL SAVTNINPQQ RMLAEAAMRW RKKLQGIKQN
MGIAEGAFSG WKVILNVDQT KEPGFKRLLQ SGGAKVFAGH SSPLFKEASH LFADFSKLKP
DEPRVNVAEA AAQGVNCLKP EYIADYLMKE LPPPMNNYCL PDAIPYVRVT GTGLSRKRKT
SGDVSDVKRS RHY
