RRP36_HUMAN
ID RRP36_HUMAN Reviewed; 259 AA.
AC Q96EU6; Q9BRF6; Q9P0C8;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Ribosomal RNA processing protein 36 homolog;
GN Name=RRP36; Synonyms=C6orf153; ORFNames=HSPC253;
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 MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=B-cell, and 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 80-259 (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RA Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L.,
RA Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
RT "Human partial CDS from CD34+ stem cells.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION AS A MENINGIOMA ANTIGEN.
RX PubMed=15983380; DOI=10.1073/pnas.0500404102;
RA Comtesse N., Zippel A., Walle S., Monz D., Backes C., Fischer U., Mayer J.,
RA Ludwig N., Hildebrandt A., Keller A., Steudel W.-I., Lenhof H.-P.,
RA Meese E.;
RT "Complex humoral immune response against a benign tumor: frequent antibody
RT response against specific antigens as diagnostic targets.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:9601-9606(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=20038530; DOI=10.1128/mcb.00999-09;
RA Gerus M., Bonnart C., Caizergues-Ferrer M., Henry Y., Henras A.K.;
RT "Evolutionarily conserved function of RRP36 in early cleavages of the pre-
RT rRNA and production of the 40S ribosomal subunit.";
RL Mol. Cell. Biol. 30:1130-1144(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Involved in the early processing steps of the pre-rRNA in the
CC maturation pathway leading to the 18S rRNA.
CC {ECO:0000269|PubMed:20038530}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:20038530}.
CC Note=Concentrated in the fibrillar region of the nucleolus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96EU6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96EU6-2; Sequence=VSP_020884;
CC -!- MISCELLANEOUS: Meningioma antigen.
CC -!- SIMILARITY: Belongs to the RRP36 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH06293.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL136304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006293; AAH06293.2; ALT_INIT; mRNA.
DR EMBL; BC011933; AAH11933.1; -; mRNA.
DR EMBL; AF161371; AAF28931.1; -; mRNA.
DR CCDS; CCDS34453.1; -. [Q96EU6-1]
DR RefSeq; NP_001316633.1; NM_001329704.1.
DR RefSeq; NP_149103.1; NM_033112.3. [Q96EU6-1]
DR AlphaFoldDB; Q96EU6; -.
DR BioGRID; 124584; 53.
DR IntAct; Q96EU6; 14.
DR MINT; Q96EU6; -.
DR STRING; 9606.ENSP00000244496; -.
DR iPTMnet; Q96EU6; -.
DR PhosphoSitePlus; Q96EU6; -.
DR BioMuta; RRP36; -.
DR DMDM; 74751848; -.
DR EPD; Q96EU6; -.
DR jPOST; Q96EU6; -.
DR MassIVE; Q96EU6; -.
DR MaxQB; Q96EU6; -.
DR PaxDb; Q96EU6; -.
DR PeptideAtlas; Q96EU6; -.
DR PRIDE; Q96EU6; -.
DR ProteomicsDB; 76450; -. [Q96EU6-1]
DR ProteomicsDB; 76451; -. [Q96EU6-2]
DR Antibodypedia; 30248; 77 antibodies from 20 providers.
DR DNASU; 88745; -.
DR Ensembl; ENST00000244496.6; ENSP00000244496.5; ENSG00000124541.7. [Q96EU6-1]
DR GeneID; 88745; -.
DR KEGG; hsa:88745; -.
DR MANE-Select; ENST00000244496.6; ENSP00000244496.5; NM_033112.4; NP_149103.1.
DR UCSC; uc003otp.2; human. [Q96EU6-1]
DR CTD; 88745; -.
DR GeneCards; RRP36; -.
DR HGNC; HGNC:21374; RRP36.
DR HPA; ENSG00000124541; Low tissue specificity.
DR MIM; 613475; gene.
DR neXtProt; NX_Q96EU6; -.
DR OpenTargets; ENSG00000124541; -.
DR PharmGKB; PA165618219; -.
DR VEuPathDB; HostDB:ENSG00000124541; -.
DR eggNOG; KOG3190; Eukaryota.
DR GeneTree; ENSGT00530000064271; -.
DR HOGENOM; CLU_048802_4_0_1; -.
DR InParanoid; Q96EU6; -.
DR OMA; RWHIKQN; -.
DR OrthoDB; 1471490at2759; -.
DR PhylomeDB; Q96EU6; -.
DR TreeFam; TF315154; -.
DR PathwayCommons; Q96EU6; -.
DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q96EU6; -.
DR BioGRID-ORCS; 88745; 239 hits in 1088 CRISPR screens.
DR ChiTaRS; RRP36; human.
DR GenomeRNAi; 88745; -.
DR Pharos; Q96EU6; Tbio.
DR PRO; PR:Q96EU6; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q96EU6; protein.
DR Bgee; ENSG00000124541; Expressed in tibialis anterior and 173 other tissues.
DR ExpressionAtlas; Q96EU6; baseline and differential.
DR Genevisible; Q96EU6; HS.
DR GO; GO:0030686; C:90S preribosome; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000469; P:cleavage involved in rRNA processing; IEA:InterPro.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IDA:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IDA:UniProtKB.
DR InterPro; IPR009292; RRP36.
DR PANTHER; PTHR21738; PTHR21738; 1.
DR Pfam; PF06102; RRP36; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Nucleus; Phosphoprotein;
KW Reference proteome; Ribosome biogenesis; rRNA processing.
FT CHAIN 1..259
FT /note="Ribosomal RNA processing protein 36 homolog"
FT /id="PRO_0000252157"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 157..205
FT /evidence="ECO:0000255"
FT MOTIF 241..244
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 18..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..251
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 18..23
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020884"
FT VARIANT 78
FT /note="A -> G (in dbSNP:rs3749903)"
FT /id="VAR_027786"
FT CONFLICT 88
FT /note="V -> F (in Ref. 3; AAF28931)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 259 AA; 29823 MW; 8388ED8B7306CF8E CRC64;
MPGANYRAGA GAGAGARRPR GARDREEDGG GLEPAAVARD LLRGTSNMSF EELLELQSQV
GTKTYKQLVA GNSPKKQASR PPIQNACVAD KHRPLEMSAK IRVPFLRQVV PISKKVARDP
RFDDLSGEYN PEVFDKTYQF LNDIRAKEKE LVKKQLKKHL SGEEHEKLQQ LLQRMEQQEM
AQQERKQQQE LHLALKQERR AQAQQGHRPY FLKKSEQRQL ALAEKFKELK RSKKLENFLS
RKRRRNAGKD RRHLPLSKE
