TICRR_XENLA
ID TICRR_XENLA Reviewed; 1985 AA.
AC D3IUT5; Q6GPQ1;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Treslin;
DE AltName: Full=TopBP1-interacting checkpoint and replication regulator;
DE AltName: Full=TopBP1-interacting, replication-stimulating protein;
GN Name=ticrr;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP WITH TOPBP1, AND PHOSPHORYLATION.
RX PubMed=20116089; DOI=10.1016/j.cell.2009.12.049;
RA Kumagai A., Shevchenko A., Shevchenko A., Dunphy W.G.;
RT "Treslin collaborates with TopBP1 in triggering the initiation of DNA
RT replication.";
RL Cell 140:349-359(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1367.
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulator of DNA replication and S/M and G2/M checkpoints.
CC Regulates the triggering of DNA replication initiation via its
CC interaction with topbp1 by participating in cdk2-mediated loading of
CC cdc45l onto replication origins. Required for the transition from pre-
CC replication complex (pre-RC) to pre-initiation complex (pre-IC).
CC Required to prevent mitotic entry after treatment with ionizing
CC radiation. {ECO:0000269|PubMed:20116089}.
CC -!- SUBUNIT: Interacts with topbp1 (via BRCT domains); interaction is cdk2-
CC dependent (PubMed:20116089). Component of the replisome complex (By
CC similarity). {ECO:0000250|UniProtKB:Q7Z2Z1,
CC ECO:0000269|PubMed:20116089}.
CC -!- INTERACTION:
CC D3IUT5; Q800K6: topbp1-A; NbExp=4; IntAct=EBI-2607396, EBI-2607374;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20116089}.
CC Note=Associates with chromatin.
CC -!- PTM: Phosphorylated during interphase. Cdk2 promotes both
CC phosphorylation and formation of a ticrr-topbp1 complex.
CC {ECO:0000269|PubMed:20116089}.
CC -!- SIMILARITY: Belongs to the treslin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH73061.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH73061.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; GQ227788; ADC30134.1; -; mRNA.
DR EMBL; BC073061; AAH73061.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001165777.1; NM_001172306.1.
DR AlphaFoldDB; D3IUT5; -.
DR BioGRID; 101781; 1.
DR IntAct; D3IUT5; 1.
DR PRIDE; D3IUT5; -.
DR GeneID; 443616; -.
DR KEGG; xla:443616; -.
DR CTD; 443616; -.
DR Xenbase; XB-GENE-963896; ticrr.L.
DR OrthoDB; 150355at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 443616; Expressed in egg cell and 20 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IEA:InterPro.
DR GO; GO:0010212; P:response to ionizing radiation; IEA:InterPro.
DR InterPro; IPR026153; Treslin.
DR InterPro; IPR032746; Treslin_N.
DR PANTHER; PTHR21556; PTHR21556; 2.
DR Pfam; PF15292; Treslin_N; 1.
PE 1: Evidence at protein level;
KW Cell cycle; DNA damage; DNA repair; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1985
FT /note="Treslin"
FT /id="PRO_0000394240"
FT REGION 574..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1072..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1184..1243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1849..1875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1938..1966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..609
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..915
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..942
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1032
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1849..1869
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 1246
FT /note="W -> R (in Ref. 2; AAH73061)"
FT /evidence="ECO:0000305"
FT CONFLICT 1270
FT /note="S -> L (in Ref. 2; AAH73061)"
FT /evidence="ECO:0000305"
FT CONFLICT 1279
FT /note="C -> Y (in Ref. 2; AAH73061)"
FT /evidence="ECO:0000305"
FT CONFLICT 1305
FT /note="T -> A (in Ref. 2; AAH73061)"
FT /evidence="ECO:0000305"
FT CONFLICT 1314
FT /note="Q -> R (in Ref. 2; AAH73061)"
FT /evidence="ECO:0000305"
FT CONFLICT 1330
FT /note="Y -> C (in Ref. 2; AAH73061)"
FT /evidence="ECO:0000305"
FT CONFLICT 1343
FT /note="T -> S (in Ref. 2; AAH73061)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1985 AA; 221396 MW; FE3B4C817FD867C5 CRC64;
MAPSHNVVLL VDTAESSDKS RLRRVSLRLL NFLACRAGLG QVRWSYRFLN SSGGRCRPPR
RSDLRELGPR GWEEFEDELE ACWERARNCR PSSTQSSRAQ LLQTALMETL ADFQWDRPDI
TSPTKPTLLR SRRGRIVAAD EPLKDDSPDN FINPHSRNSI FLLSSCPHSG TELGQFAATS
GDFSTQKVMD KLLPKSLQKI VSSKRVRVYW LDTSDWTQFG SSSDHSGYWT MVELMHQVEG
RILPSESILG SSCQKAKTLP SFSVPPINIP FESVLNYLIF SEPDYQLWFP RRDGILFLTG
KDGTKQLDCA VSLEPVSMIQ KLSTSLMTIE LKGTMQNCNL PLAGLRVETW LLHNSDCVQL
QKLTKELMLK ELHMIATVTL EDDVLPRTGI LSPLSETAAV LNVICSERTL GLDNLHVQGS
VHETDKETFS DLPDIVMSVL NHVYSSEDNT LAPDFPVPEW IKQELSQSSR WTSSVTARWY
PLSGVSGASC NLMESFRLIN AASSNCDEHL KFDQELTNYL SEFYQKKSVD DAGLGVHREN
QKKSGLPRTP VRQKMKTLPR ALQMLNAARL NVKAQKADST LPVPNEKNSQ MKRRSSGKQD
NKPKQLKPTE FQSEDGLISY IKENYEEAVS LVDHSTMTWA RDTLTTIKSY LKSIGSEQIE
TEAIDKVKLL FKTSKVIRQN YRNNQDKEVK LKECQLQVFL RLEMFVQCPV IQMDSDELEL
IIEEITDILR IVSLTEDPLF LTKFLEVDVL TQYIASVPKI LADIYFSLGT QIPEVLVLVL
PSDGDDSIMH EEKSVKSQPS TSRVPSVAPI GAETDQLEDL RTRSAKKRRS TALARHRSVA
ESSQSFRQIE VPKRQPNKEN VQSNAVVVLE KLKLPLPAQP QKDAEAKVRR NLFIQETRSP
SKRCSKMPRS QSVSAVESLK RKRSKSHDGS KDHHKLLTKK VSETPVHKQT ANRLLLRQIK
GRPSESNSNI SIVEESPEKE IRDIDLRRSP RIKQLSLTRR NSSSFYASQP KSRNLERVNS
ATQLQQSRER PGSCLISEVK TPKRLLFGEV LGMISPPTTK RSRRILDMVN PVYKTPGKTP
RKTPSKNIPN FEDQSGNMLV KSPCTPYTPR TPSRTPKRLK TPSKGSTERK KAAKNLGKLF
SPSKPEEKSP LKLWGRRSER LAQMTPGKDG SPYKQSVCQT LMEVKTPQKL QRLESKDFRT
PSRTPTRSNN TTPAKQSMQI SNTPRKSDLK HPQEHESRGP SGYILWTPQK RILASVPHTP
ILQTPQKPIS ASVPRTPVCR TPQKAILSSV PSTPVCQTPN KAILTSVSRT PVYQTPQKAI
LASVMSTPVY QTPQKPVLAS VPTTPILKTP QRSALASVSH TPSPKKYIMK ELTVAITRMR
ECTPEKVLGS NLSSSATPSS ALKSFCSEKT TSVCQTPKKS SIALLKPCDS LEFSGAPERL
MDSLCSNKDS TKAETACTVP SQISTQMQNV INAGECTDSL SQTSVSSPSI PFTDKSLSPD
LKDALSDVTS SKAEGVTIVS EKLDSSSMDS QEATDSFINS SQTEESIDIS EARVVSTEAS
ELKMKVLITR KPSGSGVSYL PTTPKCLGNV CSTSTYGLRC TPDRRQREAA ARLGTPEIPA
KFSTPKSHCK MIPQSIYEVE LEMQESGLPK LRFKRTDSNS TIDMDVNKTP KISRKRKGDE
SPFNEKWCSK HAVRTEPACV SPSCVRTSHY TPGKSGIQTF ICQSYTPNRC LSAAASPSQS
DAGVPWTPSP KEKLSTDVIN SWPRKKKASA LCTNLLKCDK IPEYAEEDGG DFELEGVSKL
LEKSPVIEQQ SKVDGGTFGL RSRKRVFSLV SPTKETENPV KRVCTFNRHE DSSTATHRHQ
TKEEMEIFSS DQSRSSYLSS SQQSICDDVF NMSDFTPPSK VPKNPLSACG LLTLTQSPLL
YKGKTPSSKR KEKIQDVFSD GDSDHGTPTL KRPTNPAAVS DDSPFRKVNP LRSISKTYSR
KKLIT
