ID TIPIN_MOUSE Reviewed; 278 AA. AC Q91WA1; Q9CQM3; Q9D1J4; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 02-OCT-2007, sequence version 2. DT 25-MAY-2022, entry version 115. DE RecName: Full=TIMELESS-interacting protein; GN Name=Tipin; 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 MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo, 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Salivary gland; 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 IDENTIFICATION, INTERACTION WITH TIMELESS, TISSUE SPECIFICITY, RP DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION. RX PubMed=12875843; DOI=10.1016/s0022-2836(03)00633-8; RA Gotter A.L.; RT "Tipin, a novel timeless-interacting protein, is developmentally co- RT expressed with timeless and disrupts its self-association."; RL J. Mol. Biol. 331:167-176(2003). RN [4] RP INTERACTION WITH RPA2 AND PRDX2, AND FUNCTION. RX PubMed=17141802; DOI=10.1016/j.jmb.2006.10.097; RA Gotter A.L., Suppa C., Emanuel B.S.; RT "Mammalian TIMELESS and Tipin are evolutionarily conserved replication RT fork-associated factors."; RL J. Mol. Biol. 366:36-52(2007). CC -!- FUNCTION: Plays an important role in the control of DNA replication and CC the maintenance of replication fork stability. Important for cell CC survival after DNA damage or replication stress. May be specifically CC required for the ATR-CHEK1 pathway in the replication checkpoint CC induced by hydroxyurea or ultraviolet light. Forms a complex with CC TIMELESS and this complex regulates DNA replication processes under CC both normal and stress conditions, stabilizes replication forks and CC influences both CHEK1 phosphorylation and the intra-S phase checkpoint CC in response to genotoxic stress. {ECO:0000269|PubMed:17141802}. CC -!- SUBUNIT: Interacts with MCM6 and MCM7 (By similarity). Interacts with CC TIMELESS, which impairs TIMELESS self-association. Interacts with RPA2 CC and PRDX2. {ECO:0000250, ECO:0000269|PubMed:12875843, CC ECO:0000269|PubMed:17141802}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12875843}. Nucleus CC {ECO:0000269|PubMed:12875843}. CC -!- TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:12875843}. CC -!- DEVELOPMENTAL STAGE: Expression peaks between 11 dpc and 15 dpc. At 7.5 CC dpc, expressed in germ cell layers. At 14.5 dpc, expressed at highest CC levels in thymus, liver, gastrointestinal tract, lung and the rapidly CC proliferating ventricular zone of the brain. CC {ECO:0000269|PubMed:12875843}. CC -!- SIMILARITY: Belongs to the CSM3 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK003451; BAB22798.1; -; mRNA. DR EMBL; AK003802; BAB23004.1; -; mRNA. DR EMBL; AK011357; BAB27565.1; -; mRNA. DR EMBL; AK038111; BAC29931.1; -; mRNA. DR EMBL; BC016211; AAH16211.1; -; mRNA. DR EMBL; BK001385; DAA01364.1; -; mRNA. DR CCDS; CCDS23279.1; -. DR RefSeq; NP_001311485.1; NM_001324556.1. DR RefSeq; NP_001311486.1; NM_001324557.1. DR RefSeq; NP_001311487.1; NM_001324558.1. DR RefSeq; NP_079648.1; NM_025372.4. DR RefSeq; XP_006511403.1; XM_006511340.3. DR AlphaFoldDB; Q91WA1; -. DR SMR; Q91WA1; -. DR BioGRID; 211238; 31. DR IntAct; Q91WA1; 28. DR STRING; 10090.ENSMUSP00000034964; -. DR iPTMnet; Q91WA1; -. DR PhosphoSitePlus; Q91WA1; -. DR EPD; Q91WA1; -. DR MaxQB; Q91WA1; -. DR PaxDb; Q91WA1; -. DR PeptideAtlas; Q91WA1; -. DR PRIDE; Q91WA1; -. DR ProteomicsDB; 259454; -. DR Antibodypedia; 26122; 336 antibodies from 25 providers. DR DNASU; 66131; -. DR Ensembl; ENSMUST00000034964; ENSMUSP00000034964; ENSMUSG00000032397. DR Ensembl; ENSMUST00000216594; ENSMUSP00000149833; ENSMUSG00000032397. DR GeneID; 66131; -. DR KEGG; mmu:66131; -. DR UCSC; uc009qbr.1; mouse. DR CTD; 54962; -. DR MGI; MGI:1921571; Tipin. DR VEuPathDB; HostDB:ENSMUSG00000032397; -. DR eggNOG; KOG3004; Eukaryota. DR GeneTree; ENSGT00390000005764; -. DR HOGENOM; CLU_074595_0_0_1; -. DR InParanoid; Q91WA1; -. DR OMA; IIHEDFI; -. DR OrthoDB; 1505397at2759; -. DR PhylomeDB; Q91WA1; -. DR TreeFam; TF313290; -. DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends. DR BioGRID-ORCS; 66131; 17 hits in 74 CRISPR screens. DR ChiTaRS; Tipin; mouse. DR PRO; PR:Q91WA1; -. DR Proteomes; UP000000589; Chromosome 9. DR RNAct; Q91WA1; protein. DR Bgee; ENSMUSG00000032397; Expressed in heart and 315 other tissues. DR ExpressionAtlas; Q91WA1; baseline and differential. DR Genevisible; Q91WA1; MM. DR GO; GO:0000785; C:chromatin; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0031298; C:replication fork protection complex; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IBA:GO_Central. DR GO; GO:0044770; P:cell cycle phase transition; ISS:UniProtKB. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0000077; P:DNA damage checkpoint signaling; IMP:MGI. DR GO; GO:0000076; P:DNA replication checkpoint signaling; ISS:UniProtKB. DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; ISS:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB. DR GO; GO:0043111; P:replication fork arrest; IBA:GO_Central. DR GO; GO:0048478; P:replication fork protection; IBA:GO_Central. DR GO; GO:0009411; P:response to UV; IMP:MGI. DR InterPro; IPR012923; Csm3. DR InterPro; IPR040038; TIPIN/Csm3/Swi3. DR PANTHER; PTHR13220; PTHR13220; 1. DR Pfam; PF07962; Swi3; 1. PE 1: Evidence at protein level; KW Cell cycle; Cell division; Cytoplasm; DNA damage; Mitosis; Nucleus; KW Phosphoprotein; Reference proteome. FT CHAIN 1..278 FT /note="TIMELESS-interacting protein" FT /id="PRO_0000305254" FT REGION 1..59 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 64..140 FT /note="Interaction with TIMELESS" FT /evidence="ECO:0000250" FT REGION 155..197 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 216..278 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 171..193 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 255..278 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 191 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9BVW5" FT MOD_RES 219 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9BVW5" FT MOD_RES 233 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9BVW5" FT CONFLICT 67 FT /note="T -> A (in Ref. 1; BAB22798)" FT /evidence="ECO:0000305" FT CONFLICT 265 FT /note="C -> F (in Ref. 2; AAH16211)" FT /evidence="ECO:0000305" SQ SEQUENCE 278 AA; 31498 MW; 769F56BBDF2763C9 CRC64; MLEQEENGLF EIPDYEHVED ETFPPFPPPA SPERDPADAE PEEGSGSGVP VPPKRTVKRN LPKLDATRLT SERGLPALRH VFDKTKFKGK GHEAEDLKTL IRHMEHWAHR LFPKLQFEDF IDRVENLGNK KEVQTCLKRI RLDLPIVHED FVNNNDEVGE ANGPDVSATG FDPFLTSSSD SRKFASEPTR SLTEEQQQRI ERNKQLALER RQAKLLSNSQ SLENDVTVEE NSTGEDQEES NGLNIDTADG PHDVPFASTH EEEQCKAEET QLDHTNLD //