RHNO1_MOUSE
ID RHNO1_MOUSE Reviewed; 235 AA.
AC Q8K3A4; Q3U0N5; Q3UK55; Q99JS2;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=RAD9, HUS1, RAD1-interacting nuclear orphan protein 1;
GN Name=Rhno1;
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=BALB/cJ, DBA/2J, and NOD; TISSUE=Spleen;
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=Mammary gland, and Mammary tumor;
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).
CC -!- FUNCTION: Plays a role in DNA damage response (DDR) signaling upon
CC genotoxic stresses such as ionizing radiation (IR) during the S phase.
CC Recruited to sites of DNA damage through interaction with the 9-1-1
CC cell-cycle checkpoint response complex and TOPBP1 in a ATR-dependent
CC manner. Required for the progression of the G1 to S phase transition.
CC Plays a role in the stimulation of CHEK1 phosphorylation (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RAD9A, RAD18, TOPBP1 and UBE2N. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC Note=Localizes to sites of DNA damage in a H2AX-independent manner.
CC {ECO:0000250}.
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DR EMBL; AK146167; BAE26947.1; -; mRNA.
DR EMBL; AK156717; BAE33817.1; -; mRNA.
DR EMBL; AK168313; BAE40253.1; -; mRNA.
DR EMBL; BC005726; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC027368; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS85164.1; -.
DR AlphaFoldDB; Q8K3A4; -.
DR IntAct; Q8K3A4; 1.
DR STRING; 10090.ENSMUSP00000114836; -.
DR PaxDb; Q8K3A4; -.
DR PRIDE; Q8K3A4; -.
DR MGI; MGI:1915315; Rhno1.
DR eggNOG; ENOG502S7M3; Eukaryota.
DR InParanoid; Q8K3A4; -.
DR PhylomeDB; Q8K3A4; -.
DR Reactome; R-MMU-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
DR ChiTaRS; Rhno1; mouse.
DR PRO; PR:Q8K3A4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8K3A4; protein.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0071479; P:cellular response to ionizing radiation; ISO:MGI.
DR GO; GO:0034644; P:cellular response to UV; ISO:MGI.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; ISO:MGI.
DR GO; GO:0070318; P:positive regulation of G0 to G1 transition; ISO:MGI.
DR GO; GO:0000725; P:recombinational repair; ISO:MGI.
DR InterPro; IPR029293; RHNO1.
DR PANTHER; PTHR35541; PTHR35541; 1.
DR Pfam; PF15319; RHINO; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Chromosome; DNA damage; Nucleus; Reference proteome.
FT CHAIN 1..235
FT /note="RAD9, HUS1, RAD1-interacting nuclear orphan protein
FT 1"
FT /id="PRO_0000263106"
FT REGION 75..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 25
FT /note="P -> T (in Ref. 1; BAE26947)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="W -> R (in Ref. 1; BAE26947)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="H -> N (in Ref. 1; BAE33817)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 235 AA; 26820 MW; 0948EF99D20AE90C CRC64;
MPPKKRRRQS QKAQLLFHQQ PLEGPKHHYE SCQQPITHTV QVPSKPIDQS TVTSWVSPQF
DRAAESRFLI HWKPHRDQAR RPTRRSTCKF PRLTFESPQS SSSETLLLSN RVQPQNSEKD
PPRRPLVPLF SPQSCGELSV HVPHSLPHVF APPDIQTPDS SVRDDPISPD QKENSFPSCI
LGPGTPSSPE PGPVLVKDTP EEKYGIKVTW RRRRHLFAYL KEKGKLDGSQ FLVKI
