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Protein

RAD9, HUS1, RAD1-interacting nuclear orphan protein 1

Gene

RHNO1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in DNA damage response (DDR) signaling upon genotoxic stresses such as ionizing radiation (IR) during the S phase. Recruited to sites of DNA damage through interaction with the 9-1-1 cell-cycle checkpoint response complex and TOPBP1 in a ATR-dependent manner. Required for the progression of the G1 to S phase transition. Plays a role in the stimulation of CHEK1 phosphorylation.1 Publication

GO - Biological processi

  • cellular response to ionizing radiation Source: UniProtKB
  • cellular response to UV Source: UniProtKB
  • DNA damage checkpoint Source: UniProtKB
  • DNA replication Source: Reactome
  • positive regulation of G0 to G1 transition Source: UniProtKB
  • recombinational repair Source: UniProtKB
  • regulation of signal transduction by p53 class mediator Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Cell cycle, DNA damage

Enzyme and pathway databases

ReactomeiR-HSA-5685938. HDR through Single Strand Annealing (SSA).
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-69473. G2/M DNA damage checkpoint.

Names & Taxonomyi

Protein namesi
Recommended name:
RAD9, HUS1, RAD1-interacting nuclear orphan protein 1
Alternative name(s):
RAD9, RAD1, HUS1-interacting nuclear orphan protein
Gene namesi
Name:RHNO1
Synonyms:C12orf32, RHINO
ORF Names:HKMT1188
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:28206. RHNO1.

Subcellular locationi

  • Nucleus 1 Publication
  • Chromosome 1 Publication

  • Note: Localizes to sites of DNA damage in a H2AX-independent manner.

GO - Cellular componenti

  • chromosome Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi55 – 617SWVSPDF → AAAAAAA: Inhibits binding to the 9-1-1 complex. Does not inhibit interaction with TOPBP1. Inhibits localizion to sites of DNA damage. 1 Publication

Polymorphism and mutation databases

BioMutaiRHNO1.
DMDMi74739410.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 238238RAD9, HUS1, RAD1-interacting nuclear orphan protein 1PRO_0000263105Add
BLAST

Proteomic databases

MaxQBiQ9BSD3.
PaxDbiQ9BSD3.
PeptideAtlasiQ9BSD3.
PRIDEiQ9BSD3.

PTM databases

iPTMnetiQ9BSD3.
PhosphoSiteiQ9BSD3.

Expressioni

Tissue specificityi

Weakly expressed in testis, prostate, ovary, thymus and small intestine. Expressed strongly in breast cancer cells.1 Publication

Inductioni

Up-regulated in breast cancer cells.1 Publication

Gene expression databases

BgeeiQ9BSD3.
CleanExiHS_C12orf32.
ExpressionAtlasiQ9BSD3. baseline and differential.
GenevisibleiQ9BSD3. HS.

Organism-specific databases

HPAiHPA038682.

Interactioni

Subunit structurei

Interacts with RAD9A, RAD18, TOPBP1 and UBE2N.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
GOLGA2Q083793EBI-9658624,EBI-618309
KRTAP10-9P604113EBI-9658624,EBI-10172052
LZTS2Q9BRK43EBI-9658624,EBI-741037
TFIP11Q9UBB93EBI-9658624,EBI-1105213

Protein-protein interaction databases

BioGridi123729. 13 interactions.
IntActiQ9BSD3. 5 interactions.
STRINGi9606.ENSP00000438590.

Structurei

3D structure databases

ProteinModelPortaliQ9BSD3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiENOG410IZA4. Eukaryota.
ENOG410XXDT. LUCA.
GeneTreeiENSGT00390000003219.
HOVERGENiHBG059694.
InParanoidiQ9BSD3.
OMAiLLFHQQP.
PhylomeDBiQ9BSD3.
TreeFamiTF336053.

Family and domain databases

InterProiIPR029293. RHNO1.
[Graphical view]
PfamiPF15319. RHINO. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BSD3-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPPRKKRRQP SQKAPLLFHQ QPLEGPKHSC ASTQLPITHT RQVPSKPIDH
60 70 80 90 100
STITSWVSPD FDTAAGSLFP AYQKHQNRAR HSSRKPTTSK FPHLTFESPQ
110 120 130 140 150
SSSSETLGIP LIRECPSESE KDVSRRPLVP VLSPQSCGNM SVQALQSLPY
160 170 180 190 200
VFIPPDIQTP ESSSVKEELI PQDQKENSLL SCTLHTGTPN SPEPGPVLVK
210 220 230
DTPEDKYGIK VTWRRRQHLL AYLRERGKLS RSQFLVKS
Length:238
Mass (Da):26,709
Last modified:June 1, 2001 - v1
Checksum:iC405083C6F6E4CAD
GO
Isoform 2 (identifier: Q9BSD3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     43-56: Missing.

Show »
Length:224
Mass (Da):25,160
Checksum:iA87E082158162395
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei43 – 5614Missing in isoform 2. 1 PublicationVSP_045307Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB073599 mRNA. Translation: BAD38639.1.
AK304613 mRNA. Translation: BAH14225.1.
AC005911 Genomic DNA. No translation available.
BC005106 mRNA. No translation available.
CCDSiCCDS58199.1. [Q9BSD3-2]
CCDS8518.1. [Q9BSD3-1]
RefSeqiNP_001239428.1. NM_001252499.2. [Q9BSD3-1]
NP_001239429.1. NM_001252500.2. [Q9BSD3-2]
NP_001244026.1. NM_001257097.1. [Q9BSD3-1]
NP_001244027.1. NM_001257098.1. [Q9BSD3-1]
UniGeneiHs.198853.

Genome annotation databases

EnsembliENST00000461997; ENSP00000438828; ENSG00000171792. [Q9BSD3-2]
ENST00000489288; ENSP00000438590; ENSG00000171792. [Q9BSD3-1]
ENST00000618250; ENSP00000479598; ENSG00000171792. [Q9BSD3-1]
GeneIDi83695.
KEGGihsa:83695.
UCSCiuc001qlh.5. human. [Q9BSD3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB073599 mRNA. Translation: BAD38639.1.
AK304613 mRNA. Translation: BAH14225.1.
AC005911 Genomic DNA. No translation available.
BC005106 mRNA. No translation available.
CCDSiCCDS58199.1. [Q9BSD3-2]
CCDS8518.1. [Q9BSD3-1]
RefSeqiNP_001239428.1. NM_001252499.2. [Q9BSD3-1]
NP_001239429.1. NM_001252500.2. [Q9BSD3-2]
NP_001244026.1. NM_001257097.1. [Q9BSD3-1]
NP_001244027.1. NM_001257098.1. [Q9BSD3-1]
UniGeneiHs.198853.

3D structure databases

ProteinModelPortaliQ9BSD3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123729. 13 interactions.
IntActiQ9BSD3. 5 interactions.
STRINGi9606.ENSP00000438590.

PTM databases

iPTMnetiQ9BSD3.
PhosphoSiteiQ9BSD3.

Polymorphism and mutation databases

BioMutaiRHNO1.
DMDMi74739410.

Proteomic databases

MaxQBiQ9BSD3.
PaxDbiQ9BSD3.
PeptideAtlasiQ9BSD3.
PRIDEiQ9BSD3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000461997; ENSP00000438828; ENSG00000171792. [Q9BSD3-2]
ENST00000489288; ENSP00000438590; ENSG00000171792. [Q9BSD3-1]
ENST00000618250; ENSP00000479598; ENSG00000171792. [Q9BSD3-1]
GeneIDi83695.
KEGGihsa:83695.
UCSCiuc001qlh.5. human. [Q9BSD3-1]

Organism-specific databases

CTDi83695.
GeneCardsiRHNO1.
HGNCiHGNC:28206. RHNO1.
HPAiHPA038682.
MIMi614085. gene.
neXtProtiNX_Q9BSD3.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IZA4. Eukaryota.
ENOG410XXDT. LUCA.
GeneTreeiENSGT00390000003219.
HOVERGENiHBG059694.
InParanoidiQ9BSD3.
OMAiLLFHQQP.
PhylomeDBiQ9BSD3.
TreeFamiTF336053.

Enzyme and pathway databases

ReactomeiR-HSA-5685938. HDR through Single Strand Annealing (SSA).
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-69473. G2/M DNA damage checkpoint.

Miscellaneous databases

GenomeRNAii83695.
PROiQ9BSD3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BSD3.
CleanExiHS_C12orf32.
ExpressionAtlasiQ9BSD3. baseline and differential.
GenevisibleiQ9BSD3. HS.

Family and domain databases

InterProiIPR029293. RHNO1.
[Graphical view]
PfamiPF15319. RHINO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas."
    Yamada S., Ohira M., Horie H., Ando K., Takayasu H., Suzuki Y., Sugano S., Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y., Ando H., Suita S., Kaneko M., Sasaki F., Hashizume K., Ohnuma N., Nakagawara A.
    Oncogene 23:5901-5911(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Hepatoblastoma.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Uterus.
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Pancreas.
  5. "Involvement of C12orf32 overexpression in breast carcinogenesis."
    Kim J.W., Fukukawa C., Ueda K., Nishidate T., Katagiri T., Nakamura Y.
    Int. J. Oncol. 37:861-867(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "A DNA damage response screen identifies RHINO, a 9-1-1 and TopBP1 interacting protein required for ATR signaling."
    Cotta-Ramusino C., McDonald E.R. III, Hurov K., Sowa M.E., Harper J.W., Elledge S.J.
    Science 332:1313-1317(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAD9A; RAD18; TOPBP1 AND UBE2N, MUTAGENESIS OF 55-SER--PHE-61, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiRHNO1_HUMAN
AccessioniPrimary (citable) accession number: Q9BSD3
Secondary accession number(s): B7Z989
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.