RTF2_MOUSE
ID RTF2_MOUSE Reviewed; 307 AA.
AC Q99K95; A2APA0; Q543D3; Q80X88; Q9CV27;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Replication termination factor 2 {ECO:0000305};
DE Short=RTF2;
DE AltName: Full=Replication termination factor 2 domain-containing protein 1;
GN Name=Rtf2 {ECO:0000312|MGI:MGI:1913654}; Synonyms=Rtfdc1;
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=Bone marrow, Forelimb, Skin, and Tongue;
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 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Mammary 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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and Spleen;
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: Replication termination factor which is a component of the
CC elongating replisome. Required for ATR pathway signaling upon DNA
CC damage and has a positive activity during DNA replication. Might
CC function to facilitate fork pausing at replication fork barriers like
CC the rDNA. May be globally required to stimulate ATR signaling after the
CC fork stalls or encounters a lesion. Interacts with nascent DNA.
CC {ECO:0000250|UniProtKB:Q9BY42}.
CC -!- SUBUNIT: Interacts with DDI2; probably also interacts with DDI1.
CC {ECO:0000250|UniProtKB:Q9BY42}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q9BY42}.
CC Note=Localizes at the replication fork. {ECO:0000250|UniProtKB:Q9BY42}.
CC -!- PTM: Undergoes proteasomal degradation, via DDI1 and DDI2. Removal from
CC stalled replisomes and degradation are required for genome stability.
CC {ECO:0000250|UniProtKB:Q9BY42}.
CC -!- SIMILARITY: Belongs to the rtf2 family. {ECO:0000305}.
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DR EMBL; AK009901; BAB26573.1; -; mRNA.
DR EMBL; AK028792; BAC26123.1; -; mRNA.
DR EMBL; AK053258; BAC35324.1; -; mRNA.
DR EMBL; AK077823; BAC37024.1; -; mRNA.
DR EMBL; AK153121; BAE31736.1; -; mRNA.
DR EMBL; AK167287; BAE39393.1; -; mRNA.
DR EMBL; AL833787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004803; AAH04803.1; -; mRNA.
DR EMBL; BC049072; AAH49072.2; -; mRNA.
DR CCDS; CCDS17132.1; -.
DR RefSeq; NP_079818.1; NM_025542.2.
DR AlphaFoldDB; Q99K95; -.
DR BioGRID; 211448; 9.
DR IntAct; Q99K95; 6.
DR STRING; 10090.ENSMUSP00000029005; -.
DR iPTMnet; Q99K95; -.
DR PhosphoSitePlus; Q99K95; -.
DR SwissPalm; Q99K95; -.
DR EPD; Q99K95; -.
DR MaxQB; Q99K95; -.
DR PaxDb; Q99K95; -.
DR PRIDE; Q99K95; -.
DR ProteomicsDB; 260951; -.
DR Antibodypedia; 28888; 163 antibodies from 18 providers.
DR Ensembl; ENSMUST00000029005; ENSMUSP00000029005; ENSMUSG00000027502.
DR GeneID; 66404; -.
DR KEGG; mmu:66404; -.
DR UCSC; uc008ocw.1; mouse.
DR CTD; 51507; -.
DR MGI; MGI:1913654; Rtf2.
DR VEuPathDB; HostDB:ENSMUSG00000027502; -.
DR eggNOG; KOG3113; Eukaryota.
DR GeneTree; ENSGT00390000010923; -.
DR HOGENOM; CLU_048955_1_0_1; -.
DR InParanoid; Q99K95; -.
DR OMA; EVCHKCG; -.
DR OrthoDB; 1385322at2759; -.
DR PhylomeDB; Q99K95; -.
DR TreeFam; TF314621; -.
DR BioGRID-ORCS; 66404; 25 hits in 76 CRISPR screens.
DR ChiTaRS; Rtfdc1; mouse.
DR PRO; PR:Q99K95; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q99K95; protein.
DR Bgee; ENSMUSG00000027502; Expressed in spermatid and 265 other tissues.
DR Genevisible; Q99K95; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005657; C:replication fork; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0072711; P:cellular response to hydroxyurea; ISS:UniProtKB.
DR GO; GO:1902979; P:mitotic DNA replication termination; IEA:InterPro.
DR GO; GO:0097752; P:regulation of DNA stability; ISS:UniProtKB.
DR CDD; cd16653; RING-like_Rtf2; 1.
DR InterPro; IPR006735; Rtf2.
DR InterPro; IPR027799; Rtf2_RING-finger.
DR PANTHER; PTHR12775; PTHR12775; 1.
PE 1: Evidence at protein level;
KW Chromosome; Phosphoprotein; Reference proteome.
FT CHAIN 1..307
FT /note="Replication termination factor 2"
FT /id="PRO_0000079428"
FT REGION 193..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BY42"
SQ SEQUENCE 307 AA; 33935 MW; 94348165CC98B005 CRC64;
MGCDGGTIPK RHELVKGPKK VEKVDKDAEL VAQWNYCTLS QEILRRPIVA CELGRLYNKD
AVIEFLLDKS AEKALGKAAS HIRSIKNVTE LRLSDNPAWE GDKGNTKGDK HDDLQRARFI
CPVVGLEMNG RHRFCFLRCC GCVFSERALK EIKAEVCHTC GAAFQEEDII VLNGTKEDVE
MLKKRMEERR LRAKLEKKTK KPKTATECAS KPGTTQDSAG PSKVKSGKPE EADPDPREKK
STPAPRGAAT NGSASGKVGK PPCGALKRSI ADSEESETYK SIFTSHSSAK RSKEESAHWV
THTSYCF
