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 28-JUL-2009, entry version 38. 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. 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 MEDLINE=22758615; 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: Required for normal progression of S-phase. Important CC for cell survival after DNA damage or replication stress. May be CC specifically required for the ATR-CHK1 pathway in the replication CC checkpoint induced by hydroxyurea or ultraviolet light. CC -!- SUBUNIT: Interacts with MCM6 and MCM7 (By similarity). Interacts CC with TIMELESS, which impairs TIMELESS self-association. Interacts CC with RPA2 and PRDX2. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- TISSUE SPECIFICITY: Expressed in brain. 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 -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By CC similarity). CC -!- SIMILARITY: Belongs to the CSM3 family. 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 IPI; IPI00471129; -. DR RefSeq; NP_079648.1; -. DR UniGene; Mm.196219; -. DR PhosphoSite; Q91WA1; -. DR PRIDE; Q91WA1; -. DR Ensembl; ENSMUST00000034964; ENSMUSP00000034964; ENSMUSG00000032397; Mus musculus. DR GeneID; 66131; -. DR KEGG; mmu:66131; -. DR UCSC; uc009qbr.1; mouse. DR MGI; MGI:1921571; Tipin. DR HOGENOM; Q91WA1; -. DR HOVERGEN; Q91WA1; -. DR OMA; Q91WA1; IDLPDYE. DR NextBio; 320724; -. DR ArrayExpress; Q91WA1; -. DR Bgee; Q91WA1; -. DR CleanEx; MM_TIPIN; -. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0000790; C:nuclear chromatin; ISS:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:MGI. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. 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:mitosis; IEA:UniProtKB-KW. DR GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB. DR GO; GO:0033261; P:regulation of S phase; ISS:UniProtKB. DR GO; GO:0048478; P:replication fork protection; IEA:InterPro. DR InterPro; IPR012923; Swi3. DR Pfam; PF07962; Swi3; 1. PE 1: Evidence at protein level; KW Cell cycle; Cell division; Cytoplasm; DNA damage; Mitosis; Nucleus; KW Phosphoprotein. FT CHAIN 1 278 TIMELESS-interacting protein. FT /FTId=PRO_0000305254. FT REGION 64 140 Interaction with TIMELESS (By FT similarity). FT MOD_RES 191 191 Phosphoserine (By similarity). FT MOD_RES 219 219 Phosphoserine (By similarity). FT CONFLICT 67 67 T -> A (in Ref. 1; BAB22798). FT CONFLICT 265 265 C -> F (in Ref. 2; AAH16211). 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 //