RPF2_HUMAN
ID RPF2_HUMAN Reviewed; 306 AA.
AC Q9H7B2; Q5VXN1; Q8N4A1;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 09-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Ribosome production factor 2 homolog;
DE AltName: Full=Brix domain-containing protein 1;
DE AltName: Full=Ribosome biogenesis protein RPF2 homolog;
GN Name=RPF2; Synonyms=BXDC1;
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 GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-253.
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 [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=19170763; DOI=10.1111/j.1365-2443.2008.01262.x;
RA Hirano Y., Ishii K., Kumeta M., Furukawa K., Takeyasu K., Horigome T.;
RT "Proteomic and targeted analytical identification of BXDC1 and EBNA1BP2 as
RT dynamic scaffold proteins in the nucleolus.";
RL Genes Cells 14:155-166(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP FUNCTION.
RX PubMed=24120868; DOI=10.1016/j.celrep.2013.08.049;
RA Sloan K.E., Bohnsack M.T., Watkins N.J.;
RT "The 5S RNP couples p53 homeostasis to ribosome biogenesis and nucleolar
RT stress.";
RL Cell Rep. 5:237-247(2013).
CC -!- FUNCTION: Involved in ribosomal large subunit assembly. May regulate
CC the localization of the 5S RNP/5S ribonucleoprotein particle to the
CC nucleolus. {ECO:0000269|PubMed:24120868}.
CC -!- INTERACTION:
CC Q9H7B2; Q15700: DLG2; NbExp=3; IntAct=EBI-1051960, EBI-80426;
CC Q9H7B2; Q15050: RRS1; NbExp=2; IntAct=EBI-1051960, EBI-749186;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849,
CC ECO:0000269|PubMed:19170763}. Note=Associated with the nucleolus in an
CC RNA-dependent manner.
CC -!- SIMILARITY: Belongs to the RPF2 family. {ECO:0000305}.
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DR EMBL; AL357515; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48303.1; -; Genomic_DNA.
DR EMBL; BC035314; AAH35314.1; -; mRNA.
DR EMBL; AK024740; BAB14983.1; -; mRNA.
DR CCDS; CCDS5088.1; -.
DR RefSeq; NP_115570.1; NM_032194.2.
DR AlphaFoldDB; Q9H7B2; -.
DR SMR; Q9H7B2; -.
DR BioGRID; 123917; 266.
DR IntAct; Q9H7B2; 77.
DR MINT; Q9H7B2; -.
DR STRING; 9606.ENSP00000402338; -.
DR GlyGen; Q9H7B2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H7B2; -.
DR PhosphoSitePlus; Q9H7B2; -.
DR SwissPalm; Q9H7B2; -.
DR BioMuta; RPF2; -.
DR DMDM; 30581070; -.
DR SWISS-2DPAGE; Q9H7B2; -.
DR EPD; Q9H7B2; -.
DR jPOST; Q9H7B2; -.
DR MassIVE; Q9H7B2; -.
DR MaxQB; Q9H7B2; -.
DR PaxDb; Q9H7B2; -.
DR PeptideAtlas; Q9H7B2; -.
DR PRIDE; Q9H7B2; -.
DR ProteomicsDB; 81095; -.
DR Antibodypedia; 19293; 165 antibodies from 25 providers.
DR DNASU; 84154; -.
DR Ensembl; ENST00000441448.7; ENSP00000402338.2; ENSG00000197498.13.
DR GeneID; 84154; -.
DR KEGG; hsa:84154; -.
DR MANE-Select; ENST00000441448.7; ENSP00000402338.2; NM_032194.3; NP_115570.1.
DR UCSC; uc003pun.5; human.
DR CTD; 84154; -.
DR DisGeNET; 84154; -.
DR GeneCards; RPF2; -.
DR HGNC; HGNC:20870; RPF2.
DR HPA; ENSG00000197498; Low tissue specificity.
DR MIM; 618471; gene.
DR neXtProt; NX_Q9H7B2; -.
DR OpenTargets; ENSG00000197498; -.
DR PharmGKB; PA165618192; -.
DR VEuPathDB; HostDB:ENSG00000197498; -.
DR eggNOG; KOG3031; Eukaryota.
DR GeneTree; ENSGT00390000007279; -.
DR InParanoid; Q9H7B2; -.
DR OMA; GCKIPRI; -.
DR OrthoDB; 974865at2759; -.
DR PhylomeDB; Q9H7B2; -.
DR TreeFam; TF314371; -.
DR PathwayCommons; Q9H7B2; -.
DR SignaLink; Q9H7B2; -.
DR BioGRID-ORCS; 84154; 748 hits in 1082 CRISPR screens.
DR ChiTaRS; RPF2; human.
DR GenomeRNAi; 84154; -.
DR Pharos; Q9H7B2; Tbio.
DR PRO; PR:Q9H7B2; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9H7B2; protein.
DR Bgee; ENSG00000197498; Expressed in tibialis anterior and 189 other tissues.
DR ExpressionAtlas; Q9H7B2; baseline and differential.
DR Genevisible; Q9H7B2; HS.
DR GO; GO:0005694; C:chromosome; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0008097; F:5S rRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:1902570; P:protein localization to nucleolus; IMP:UniProtKB.
DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; IMP:UniProtKB.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:UniProtKB.
DR InterPro; IPR007109; Brix.
DR InterPro; IPR039770; Rpf2.
DR PANTHER; PTHR12728; PTHR12728; 1.
DR Pfam; PF04427; Brix; 1.
DR SMART; SM00879; Brix; 1.
DR PROSITE; PS50833; BRIX; 1.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome; Ribosome biogenesis.
FT CHAIN 1..306
FT /note="Ribosome production factor 2 homolog"
FT /id="PRO_0000120223"
FT DOMAIN 31..234
FT /note="Brix"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00034"
FT REGION 270..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 41
FT /note="A -> G (in dbSNP:rs9320350)"
FT /id="VAR_033639"
FT VARIANT 60
FT /note="G -> S (in dbSNP:rs6909298)"
FT /id="VAR_033640"
FT CONFLICT 253
FT /note="N -> K (in Ref. 4; BAB14983)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 306 AA; 35583 MW; 377F53E1371A0BB1 CRC64;
MDTLDRVVKP KTKRAKRFLE KREPKLNENI KNAMLIKGGN ANATVTKVLK DVYALKKPYG
VLYKKKNITR PFEDQTSLEF FSKKSDCSLF MFGSHNKKRP NNLVIGRMYD YHVLDMIELG
IENFVSLKDI KNSKCPEGTK PMLIFAGDDF DVTEDYRRLK SLLIDFFRGP TVSNIRLAGL
EYVLHFTALN GKIYFRSYKL LLKKSGCRTP RIELEEMGPS LDLVLRRTHL ASDDLYKLSM
KMPKALKPKK KKNISHDTFG TTYGRIHMQK QDLSKLQTRK MKGLKKRPAE RITEDHEKKS
KRIKKN
