TIPIN_MOUSE
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 03-AUG-2022, entry version 116.
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}.
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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; 363 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 fetal liver hematopoietic progenitor cell and 258 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
