TICRR_MOUSE
ID TICRR_MOUSE Reviewed; 1889 AA.
AC Q8BQ33; B2RY55; Q8C9N4; Q8CCI2;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 113.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1175 AND 1438-1889.
RC STRAIN=C57BL/6J; TISSUE=Spinal ganglion, Testis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599; SER-1002; SER-1027 AND
RP SER-1141, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TOPBP1 (via BRCT domains); interaction takes
CC place in a CDK2-dependent manner (By similarity). Component of the
CC replisome complex composed of at least DONSON, MCM2, MCM7, PCNA and
CC TICRR (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q7Z2Z1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Associates with
CC chromatin.
CC -!- SIMILARITY: Belongs to the treslin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH58634.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC28152.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC34701.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC114988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC158582; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC058634; AAH58634.1; ALT_INIT; mRNA.
DR EMBL; BC158103; AAI58104.1; -; mRNA.
DR EMBL; AK033104; BAC28152.1; ALT_INIT; mRNA.
DR EMBL; AK041726; BAC31045.1; -; mRNA.
DR EMBL; AK051639; BAC34701.1; ALT_FRAME; mRNA.
DR CCDS; CCDS21384.1; -.
DR RefSeq; NP_084111.1; NM_029835.1.
DR AlphaFoldDB; Q8BQ33; -.
DR STRING; 10090.ENSMUSP00000041377; -.
DR iPTMnet; Q8BQ33; -.
DR PhosphoSitePlus; Q8BQ33; -.
DR EPD; Q8BQ33; -.
DR jPOST; Q8BQ33; -.
DR MaxQB; Q8BQ33; -.
DR PaxDb; Q8BQ33; -.
DR PeptideAtlas; Q8BQ33; -.
DR PRIDE; Q8BQ33; -.
DR ProteomicsDB; 262921; -.
DR Antibodypedia; 64736; 44 antibodies from 18 providers.
DR DNASU; 77011; -.
DR Ensembl; ENSMUST00000035977; ENSMUSP00000041377; ENSMUSG00000046591.
DR GeneID; 77011; -.
DR KEGG; mmu:77011; -.
DR UCSC; uc009hyp.1; mouse.
DR CTD; 90381; -.
DR MGI; MGI:1924261; Ticrr.
DR VEuPathDB; HostDB:ENSMUSG00000046591; -.
DR eggNOG; ENOG502QW0J; Eukaryota.
DR GeneTree; ENSGT00390000005222; -.
DR HOGENOM; CLU_241727_0_0_1; -.
DR InParanoid; Q8BQ33; -.
DR OMA; DWKEPQM; -.
DR OrthoDB; 150355at2759; -.
DR PhylomeDB; Q8BQ33; -.
DR TreeFam; TF332114; -.
DR BioGRID-ORCS; 77011; 32 hits in 108 CRISPR screens.
DR ChiTaRS; Ticrr; mouse.
DR PRO; PR:Q8BQ33; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BQ33; protein.
DR Bgee; ENSMUSG00000046591; Expressed in animal zygote and 103 other tissues.
DR ExpressionAtlas; Q8BQ33; baseline and differential.
DR Genevisible; Q8BQ33; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; ISS:UniProtKB.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; ISS:UniProtKB.
DR GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
DR InterPro; IPR026153; Treslin.
DR InterPro; IPR032746; Treslin_N.
DR PANTHER; PTHR21556; PTHR21556; 1.
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..1889
FT /note="Treslin"
FT /id="PRO_0000296624"
FT REGION 812..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 979..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1098..1421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1471..1508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1520..1543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1629..1714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1730..1751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1841..1875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..1014
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1063
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1254..1282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1352..1372
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1399..1421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1522..1543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1644..1662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1737..1751
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2Z1"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 820
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2Z1"
FT MOD_RES 861
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2Z1"
FT MOD_RES 919
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2Z1"
FT MOD_RES 934
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2Z1"
FT MOD_RES 1002
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1027
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1078
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2Z1"
FT MOD_RES 1134
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2Z1"
FT MOD_RES 1141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1406
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2Z1"
FT CONFLICT 7
FT /note="V -> G (in Ref. 3; BAC31045)"
FT /evidence="ECO:0000305"
FT CONFLICT 1513
FT /note="P -> A (in Ref. 3; BAC28152)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1889 AA; 208335 MW; EF97B85B7BFD3027 CRC64;
MACCHKVMLL VDTAGVSAPH SPARRAALRL LTYLSCRFGL ARVHWTFKFF DSQGARSRPS
RVSDFRELGS RSWEDFEEEL EARLGDRPPG AHLPGPTPRA THTHGALMET LLDYQWDRPE
ITSPTKPILR SSGRRLLDAD GEAREAQAAL GGFGNAVFLL APCPHSQREL LQFVSGCEAQ
AQRVPLTPKQ VMEKVLPKRV QEVMIARNIT LYWVDTTERS KLWASPDHVG YWTVCELLHH
GGGTILPAET WSLGFTKARE TVLPCGGELS HKPHPSPWIS ALPIDATVNC LLYNSEYEAS
FPRIEGTLFL PVQGKEIEET WAISLEPLAM HQRHFQKPVR IVLRGSVAQW SLPVSSALGT
DSWMLQSPEE HRSTQRLLFQ ELVSRLTAEE FHLVASVDPG EGWPPITGII SPFSANAMIL
TVFRAKEAEF QSHFLQTAAT EGSQDTASLF SDVVDSVLNQ SHNLFEDPAS SAPCVPEWVQ
QELSHTSSWS PALVEKWFPF SNASGATSDL MESFWLLHAA SPDNDESSKT ESELTRCLSE
LYQRSHEEST VVNQERSRKK RGIPRTPVRQ KMNTMSRSLK MLNVARLNVK AQKLHPDGSP
DTAVEKGLQK AVIGRTADKL EDRGRILRSS KLKEFKTEEE LLAYIHDNYQ KAVATEEITL
YSCAQNMVST IKMFLKSKDI KELEVACLSH VNSNLLKTSK TLRQNLAGKM DTEDKVGECQ
LQVFLRLEMC EQCPSVLDRP DEVERIVEEV TDLLRLVCLT KDSAYLSEFL EEILRLYIGS
IPGTIGQLYH SLGLKIPQKL AGVLPTGFFS DDSMSQESMS PPPSSSTHRS VSAITESEQL
EELRTRSAKK RRKNALIRHK SIAEISQTLR QIEVPKVSKR ATRNENSHSA SIQLPVPRKD
TIQEVTKVRR NLFNQEMLSP SKRGLKKGLP RSHSVSALEC LHHKQDKFKK TKSSTFQGYC
KLLTKSVAET PVHKQISRRL LHRQIKGRSS DPGPDIHVVE ESPEKEDEMT LRRSPRIKQL
SFSRTNSGSF YSVSQPKSRS VQRIHSSQQE SEQRENFPVQ SIQSPKTLLF GALSEIPSSS
KKGSAQIKRS LRSMLDSEIS TSYETPKKSN QKSPSFSKTT PRRFPRTAQT LLYTPERLQN
SPTEMTSAEG TISEATIKTP SSHGYNSPFA SKVTSQKTVS PAKEETSPPL TKLPSTPRES
DVQPPQCSSD CTWPHSVNSS PEGPYYPASP PPMAGQARSQ CLTPIRYSFR TPPRTALAGT
SKQQEHQELP LPRASQTQEP PQGLEKKALK IPKKPAHTST SPLSPEEHYS GCDVSPHQPR
NSLSASPPPG ELNWKEHQTS PSVTSSVSCP VPSTPPRTPQ RMTCPIPPSP PSKLRRSCRK
KSCPPQDFPE CHPGPSAAPV LSSATSPGAV TGSREEQSQF SEGQSYLGTG FRSDCHVSSP
VLTASDTKCL PLIDEAQLHG LKNQEVKSGI LPGEEGEEPE STIADELPSV SDPGILVPAP
SSVSSSSELL PYPLCCTADG KQRQDAAQQG SPRASEATSS PQTYEVELEM QASGLPKLRI
KKIDPGVLLE AEALGKEAPL GEEGALPALC MPKASKSSGR TEHPYLSPPC LRPSHSTPGK
NGGQTFICQS CTPSRCPPST PSPFQADAGV SWTPSPKQSG KTTPEIIKDW PRRKRAVDCS
AGPSAGRGEA SMDLPGSLSL LEPEPEGKER SLEQDLSKVL ISEEFELEGV CQLPDQSPPK
DSASVTEETS WGQFGLGRKR FLSAKEESEY KVKRVCDSLS EDPQASKQKE CSPRWSALPL
HSVGDDEVFV SGSTPPSGCM VRSCLSASGL QALTQSPLLF QGRTPSSHST DTRDEEVDVF
PSTAEESPFS HTLSRKRPFR TYTRKKLIS
