RHNO1_HUMAN
ID RHNO1_HUMAN Reviewed; 238 AA.
AC Q9BSD3; B7Z989;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=RAD9, HUS1, RAD1-interacting nuclear orphan protein 1;
DE AltName: Full=RAD9, RAD1, HUS1-interacting nuclear orphan protein;
GN Name=RHNO1; Synonyms=C12orf32, RHINO; ORFNames=HKMT1188;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hepatoblastoma;
RX PubMed=15221005; DOI=10.1038/sj.onc.1207782;
RA Yamada S., Ohira M., Horie H., Ando K., Takayasu H., Suzuki Y., Sugano S.,
RA Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y., Ando H., Suita S.,
RA Kaneko M., Sasaki F., Hashizume K., Ohnuma N., Nakagawara A.;
RT "Expression profiling and differential screening between hepatoblastomas
RT and the corresponding normal livers: identification of high expression of
RT the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas.";
RL Oncogene 23:5901-5911(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreas;
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 [5]
RP INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=20811708; DOI=10.3892/ijo_00000737;
RA Kim J.W., Fukukawa C., Ueda K., Nishidate T., Katagiri T., Nakamura Y.;
RT "Involvement of C12orf32 overexpression in breast carcinogenesis.";
RL Int. J. Oncol. 37:861-867(2010).
RN [6]
RP FUNCTION, INTERACTION WITH RAD9A; RAD18; TOPBP1 AND UBE2N, MUTAGENESIS OF
RP 55-SER--PHE-61, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21659603; DOI=10.1126/science.1203430;
RA Cotta-Ramusino C., McDonald E.R. III, Hurov K., Sowa M.E., Harper J.W.,
RA Elledge S.J.;
RT "A DNA damage response screen identifies RHINO, a 9-1-1 and TopBP1
RT interacting protein required for ATR signaling.";
RL Science 332:1313-1317(2011).
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.
CC {ECO:0000269|PubMed:21659603}.
CC -!- SUBUNIT: Interacts with RAD9A, RAD18, TOPBP1 and UBE2N.
CC {ECO:0000269|PubMed:21659603}.
CC -!- INTERACTION:
CC Q9BSD3; Q9Y5Z0: BACE2; NbExp=3; IntAct=EBI-9658624, EBI-11282723;
CC Q9BSD3; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-9658624, EBI-11524452;
CC Q9BSD3; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-9658624, EBI-3867333;
CC Q9BSD3; Q08379: GOLGA2; NbExp=3; IntAct=EBI-9658624, EBI-618309;
CC Q9BSD3; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-9658624, EBI-10171774;
CC Q9BSD3; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-9658624, EBI-10172052;
CC Q9BSD3; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-9658624, EBI-741037;
CC Q9BSD3; Q9UBB9: TFIP11; NbExp=6; IntAct=EBI-9658624, EBI-1105213;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20811708}. Chromosome
CC {ECO:0000269|PubMed:20811708}. Note=Localizes to sites of DNA damage in
CC a H2AX-independent manner.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BSD3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BSD3-2; Sequence=VSP_045307;
CC -!- TISSUE SPECIFICITY: Weakly expressed in testis, prostate, ovary, thymus
CC and small intestine. Expressed strongly in breast cancer cells.
CC {ECO:0000269|PubMed:20811708}.
CC -!- INDUCTION: Up-regulated in breast cancer cells.
CC {ECO:0000269|PubMed:20811708}.
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DR EMBL; AB073599; BAD38639.1; -; mRNA.
DR EMBL; AK304613; BAH14225.1; -; mRNA.
DR EMBL; AC005911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005106; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS58199.1; -. [Q9BSD3-2]
DR CCDS; CCDS8518.1; -. [Q9BSD3-1]
DR RefSeq; NP_001239428.1; NM_001252499.2. [Q9BSD3-1]
DR RefSeq; NP_001239429.1; NM_001252500.2. [Q9BSD3-2]
DR RefSeq; NP_001244026.1; NM_001257097.1. [Q9BSD3-1]
DR RefSeq; NP_001244027.1; NM_001257098.1. [Q9BSD3-1]
DR PDB; 6J8Y; X-ray; 2.40 A; D=45-64.
DR PDBsum; 6J8Y; -.
DR AlphaFoldDB; Q9BSD3; -.
DR SMR; Q9BSD3; -.
DR BioGRID; 123729; 23.
DR CORUM; Q9BSD3; -.
DR IntAct; Q9BSD3; 13.
DR STRING; 9606.ENSP00000479598; -.
DR iPTMnet; Q9BSD3; -.
DR PhosphoSitePlus; Q9BSD3; -.
DR BioMuta; RHNO1; -.
DR DMDM; 74739410; -.
DR MassIVE; Q9BSD3; -.
DR MaxQB; Q9BSD3; -.
DR PaxDb; Q9BSD3; -.
DR PeptideAtlas; Q9BSD3; -.
DR PRIDE; Q9BSD3; -.
DR Antibodypedia; 48896; 8 antibodies from 4 providers.
DR DNASU; 83695; -.
DR Ensembl; ENST00000461997.5; ENSP00000438828.1; ENSG00000171792.11. [Q9BSD3-2]
DR Ensembl; ENST00000489288.7; ENSP00000438590.1; ENSG00000171792.11. [Q9BSD3-1]
DR Ensembl; ENST00000618250.4; ENSP00000479598.1; ENSG00000171792.11. [Q9BSD3-1]
DR GeneID; 83695; -.
DR KEGG; hsa:83695; -.
DR MANE-Select; ENST00000489288.7; ENSP00000438590.1; NM_001252499.3; NP_001239428.1.
DR UCSC; uc001qlh.5; human. [Q9BSD3-1]
DR CTD; 83695; -.
DR DisGeNET; 83695; -.
DR GeneCards; RHNO1; -.
DR HGNC; HGNC:28206; RHNO1.
DR HPA; ENSG00000171792; Low tissue specificity.
DR MIM; 614085; gene.
DR neXtProt; NX_Q9BSD3; -.
DR OpenTargets; ENSG00000171792; -.
DR VEuPathDB; HostDB:ENSG00000171792; -.
DR eggNOG; ENOG502S7M3; Eukaryota.
DR GeneTree; ENSGT00390000003219; -.
DR HOGENOM; CLU_075584_0_0_1; -.
DR InParanoid; Q9BSD3; -.
DR OMA; VCPQFET; -.
DR OrthoDB; 1140824at2759; -.
DR PhylomeDB; Q9BSD3; -.
DR TreeFam; TF336053; -.
DR PathwayCommons; Q9BSD3; -.
DR Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
DR Reactome; R-HSA-9709570; Impaired BRCA2 binding to RAD51.
DR SignaLink; Q9BSD3; -.
DR BioGRID-ORCS; 83695; 18 hits in 1067 CRISPR screens.
DR ChiTaRS; RHNO1; human.
DR GenomeRNAi; 83695; -.
DR Pharos; Q9BSD3; Tbio.
DR PRO; PR:Q9BSD3; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9BSD3; protein.
DR Bgee; ENSG00000171792; Expressed in ventricular zone and 166 other tissues.
DR ExpressionAtlas; Q9BSD3; baseline and differential.
DR Genevisible; Q9BSD3; HS.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0071479; P:cellular response to ionizing radiation; IDA:UniProtKB.
DR GO; GO:0034644; P:cellular response to UV; IDA:UniProtKB.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0070318; P:positive regulation of G0 to G1 transition; IMP:UniProtKB.
DR GO; GO:0000725; P:recombinational repair; IMP:UniProtKB.
DR InterPro; IPR029293; RHNO1.
DR PANTHER; PTHR35541; PTHR35541; 1.
DR Pfam; PF15319; RHINO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Chromosome; DNA damage;
KW Nucleus; Reference proteome.
FT CHAIN 1..238
FT /note="RAD9, HUS1, RAD1-interacting nuclear orphan protein
FT 1"
FT /id="PRO_0000263105"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 43..56
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045307"
FT MUTAGEN 55..61
FT /note="SWVSPDF->AAAAAAA: Inhibits binding to the 9-1-1
FT complex. Does not inhibit interaction with TOPBP1. Inhibits
FT localizion to sites of DNA damage."
FT /evidence="ECO:0000269|PubMed:21659603"
SQ SEQUENCE 238 AA; 26709 MW; C405083C6F6E4CAD CRC64;
MPPRKKRRQP SQKAPLLFHQ QPLEGPKHSC ASTQLPITHT RQVPSKPIDH STITSWVSPD
FDTAAGSLFP AYQKHQNRAR HSSRKPTTSK FPHLTFESPQ SSSSETLGIP LIRECPSESE
KDVSRRPLVP VLSPQSCGNM SVQALQSLPY VFIPPDIQTP ESSSVKEELI PQDQKENSLL
SCTLHTGTPN SPEPGPVLVK DTPEDKYGIK VTWRRRQHLL AYLRERGKLS RSQFLVKS
