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 05-OCT-2016, entry version 89. DE RecName: Full=TIMELESS-interacting protein; GN Name=Tipin; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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 RT project: 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 CC replication and the maintenance of replication fork stability. CC Important for cell survival after DNA damage or replication CC stress. May be specifically required for the ATR-CHEK1 pathway in CC the replication checkpoint induced by hydroxyurea or ultraviolet CC light. Forms a complex with TIMELESS and this complex regulates CC DNA replication processes under both normal and stress conditions, CC stabilizes replication forks and influences both CHEK1 CC phosphorylation and the intra-S phase checkpoint in response to CC genotoxic stress. {ECO:0000269|PubMed:17141802}. CC -!- SUBUNIT: Interacts with MCM6 and MCM7 (By similarity). Interacts CC with TIMELESS, which impairs TIMELESS self-association. Interacts CC with RPA2 and PRDX2. {ECO:0000250, ECO:0000269|PubMed:12875843, CC ECO:0000269|PubMed:17141802}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12875843}. CC Nucleus {ECO:0000269|PubMed:12875843}. CC -!- TISSUE SPECIFICITY: Expressed in brain. CC {ECO:0000269|PubMed:12875843}. CC -!- DEVELOPMENTAL STAGE: Expression peaks between E11 and E15. At CC E7.5, expressed in germ cell layers. At E14.5, expressed at CC highest levels in thymus, liver, gastrointestinal tract, lung and CC the rapidly 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 UniGene; Mm.196219; -. DR ProteinModelPortal; Q91WA1; -. DR SMR; Q91WA1; 71-127, 87-144, 192-216. DR BioGrid; 211238; 30. DR IntAct; Q91WA1; 28. DR STRING; 10090.ENSMUSP00000034964; -. DR iPTMnet; Q91WA1; -. DR PhosphoSite; Q91WA1; -. DR EPD; Q91WA1; -. DR MaxQB; Q91WA1; -. DR PaxDb; Q91WA1; -. DR PeptideAtlas; Q91WA1; -. DR PRIDE; Q91WA1; -. DR Ensembl; ENSMUST00000034964; ENSMUSP00000034964; ENSMUSG00000032397. DR GeneID; 66131; -. DR KEGG; mmu:66131; -. DR UCSC; uc009qbr.1; mouse. DR CTD; 54962; -. DR MGI; MGI:1921571; Tipin. DR eggNOG; KOG3004; Eukaryota. DR eggNOG; ENOG4111VXN; LUCA. DR GeneTree; ENSGT00390000005764; -. DR HOGENOM; HOG000154594; -. DR HOVERGEN; HBG061130; -. DR InParanoid; Q91WA1; -. DR KO; K10904; -. DR OMA; DILDNPC; -. DR OrthoDB; EOG091G0H5F; -. DR PhylomeDB; Q91WA1; -. DR TreeFam; TF313290; -. DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends. DR PRO; PR:Q91WA1; -. DR Proteomes; UP000000589; Chromosome 9. DR Bgee; ENSMUSG00000032397; -. DR CleanEx; MM_TIPIN; -. DR Genevisible; Q91WA1; MM. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0000790; C:nuclear chromatin; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0044770; P:cell cycle phase transition; ISS:BHF-UCL. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0000077; P:DNA damage checkpoint; IMP:MGI. DR GO; GO:0000076; P:DNA replication checkpoint; ISS:UniProtKB. DR GO; GO:0031573; P:intra-S DNA damage checkpoint; ISS:UniProtKB. DR GO; GO:0007067; P:mitotic nuclear division; IEA:UniProtKB-KW. DR GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB. DR GO; GO:0048478; P:replication fork protection; IEA:InterPro. DR GO; GO:0009411; P:response to UV; IMP:MGI. DR InterPro; IPR012923; Csm3. DR Pfam; PF07962; Swi3; 1. DR ProDom; PD089639; Swi3; 1. PE 1: Evidence at protein level; KW Cell cycle; Cell division; Complete proteome; Cytoplasm; DNA damage; KW Mitosis; Nucleus; Phosphoprotein; Reference proteome. FT CHAIN 1 278 TIMELESS-interacting protein. FT /FTId=PRO_0000305254. FT REGION 64 140 Interaction with TIMELESS. {ECO:0000250}. FT MOD_RES 191 191 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9BVW5}. FT MOD_RES 219 219 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9BVW5}. FT MOD_RES 233 233 Phosphothreonine. FT {ECO:0000250|UniProtKB:Q9BVW5}. FT CONFLICT 67 67 T -> A (in Ref. 1; BAB22798). FT {ECO:0000305}. FT CONFLICT 265 265 C -> F (in Ref. 2; AAH16211). FT {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 //