RRP1_HUMAN
ID RRP1_HUMAN Reviewed; 461 AA.
AC P56182; Q9NST5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Ribosomal RNA processing protein 1 homolog A;
DE AltName: Full=Novel nuclear protein 1;
DE Short=NNP-1;
DE AltName: Full=Nucleolar protein Nop52;
DE AltName: Full=RRP1-like protein;
GN Name=RRP1; Synonyms=D21S2056E, NNP1, NOP52, RRP1A;
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 [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Kidney;
RX PubMed=9192856; DOI=10.1006/geno.1997.4755;
RA Jansen E., Meulemans S.M.P., Orlans I.C.R., Van de Ven W.J.M.;
RT "The NNP-1 gene (D21S2056E), which encodes a novel nuclear protein, maps in
RT close proximity to the cystatin B gene within the EPM1 and APECED critical
RT region on 21q22.3.";
RL Genomics 42:336-341(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Small intestine;
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 103-461, AND VARIANT ARG-326.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP FUNCTION.
RX PubMed=10341208; DOI=10.1242/jcs.112.12.1889;
RA Savino T.M., Bastos R., Jansen E., Hernandez-Verdun D.;
RT "The nucleolar antigen Nop52, the human homologue of the yeast ribosomal
RT RNA processing RRP1, is recruited at late stages of nucleologenesis.";
RL J. Cell Sci. 112:1889-1900(1999).
RN [6]
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 [7]
RP INTERACTION WITH RRP1B.
RX PubMed=20926688; DOI=10.1091/mbc.e10-04-0287;
RA Chamousset D., De Wever V., Moorhead G.B., Chen Y., Boisvert F.M.,
RA Lamond A.I., Trinkle-Mulcahy L.;
RT "RRP1B targets PP1 to mammalian cell nucleoli and is associated with pre-
RT 60S ribosomal subunits.";
RL Mol. Biol. Cell 21:4212-4226(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-412, 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 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 [10]
RP INTERACTION WITH C1QBP.
RX PubMed=21536856; DOI=10.1074/mcp.m110.006148;
RA Yoshikawa H., Komatsu W., Hayano T., Miura Y., Homma K., Izumikawa K.,
RA Ishikawa H., Miyazawa N., Tachikawa H., Yamauchi Y., Isobe T.,
RA Takahashi N.;
RT "Splicing factor 2-associated protein p32 participates in ribosome
RT biogenesis by regulating the binding of Nop52 and fibrillarin to
RT preribosome particles.";
RL Mol. Cell. Proteomics 10:0-0(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247; SER-250 AND SER-251, AND
RP IDENTIFICATION BY 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
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).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP METHYLATION AT GLN-427, AND MUTAGENESIS OF GLN-427.
RX PubMed=26797129; DOI=10.1074/jbc.m115.711952;
RA Kusevic D., Kudithipudi S., Jeltsch A.;
RT "Substrate specificity of the HEMK2 protein glutamine methyltransferase and
RT identification of novel substrates.";
RL J. Biol. Chem. 291:6124-6133(2016).
CC -!- FUNCTION: Plays a critical role in the generation of 28S rRNA.
CC {ECO:0000269|PubMed:10341208}.
CC -!- SUBUNIT: Interacts with C1QBP (PubMed:21536856). Interacts with RRP1B
CC (PubMed:20926688). {ECO:0000269|PubMed:20926688,
CC ECO:0000269|PubMed:21536856}.
CC -!- INTERACTION:
CC P56182; Q14684: RRP1B; NbExp=2; IntAct=EBI-2880285, EBI-372051;
CC P56182; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-2880285, EBI-12023934;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849,
CC ECO:0000269|PubMed:9192856}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in fetal and adult tissues.
CC {ECO:0000269|PubMed:9192856}.
CC -!- PTM: Methylated at Gln-427 by N6AMT1. {ECO:0000269|PubMed:26797129}.
CC -!- SIMILARITY: Belongs to the RRP1 family. {ECO:0000305}.
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DR EMBL; U79775; AAC51625.1; -; mRNA.
DR EMBL; AP001752; BAA95542.1; -; Genomic_DNA.
DR EMBL; BC000380; AAH00380.1; -; mRNA.
DR EMBL; AL137757; CAB70909.1; -; mRNA.
DR CCDS; CCDS42951.1; -.
DR PIR; T46485; T46485.
DR RefSeq; NP_003674.1; NM_003683.5.
DR AlphaFoldDB; P56182; -.
DR SMR; P56182; -.
DR BioGRID; 114137; 134.
DR IntAct; P56182; 45.
DR MINT; P56182; -.
DR STRING; 9606.ENSP00000417464; -.
DR GlyGen; P56182; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P56182; -.
DR PhosphoSitePlus; P56182; -.
DR SwissPalm; P56182; -.
DR BioMuta; RRP1; -.
DR DMDM; 2829451; -.
DR SWISS-2DPAGE; P56182; -.
DR EPD; P56182; -.
DR jPOST; P56182; -.
DR MassIVE; P56182; -.
DR MaxQB; P56182; -.
DR PaxDb; P56182; -.
DR PeptideAtlas; P56182; -.
DR PRIDE; P56182; -.
DR ProteomicsDB; 56901; -.
DR Antibodypedia; 5231; 169 antibodies from 25 providers.
DR DNASU; 8568; -.
DR Ensembl; ENST00000497547.2; ENSP00000417464.1; ENSG00000160214.13.
DR GeneID; 8568; -.
DR KEGG; hsa:8568; -.
DR MANE-Select; ENST00000497547.2; ENSP00000417464.1; NM_003683.6; NP_003674.1.
DR UCSC; uc002zds.3; human.
DR CTD; 8568; -.
DR DisGeNET; 8568; -.
DR GeneCards; RRP1; -.
DR HGNC; HGNC:18785; RRP1.
DR HPA; ENSG00000160214; Low tissue specificity.
DR MIM; 610653; gene.
DR neXtProt; NX_P56182; -.
DR OpenTargets; ENSG00000160214; -.
DR PharmGKB; PA162402091; -.
DR VEuPathDB; HostDB:ENSG00000160214; -.
DR eggNOG; KOG3911; Eukaryota.
DR GeneTree; ENSGT00390000011821; -.
DR HOGENOM; CLU_022876_2_0_1; -.
DR InParanoid; P56182; -.
DR OMA; QTMIREW; -.
DR OrthoDB; 1337189at2759; -.
DR PhylomeDB; P56182; -.
DR TreeFam; TF315294; -.
DR PathwayCommons; P56182; -.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; P56182; -.
DR BioGRID-ORCS; 8568; 682 hits in 1083 CRISPR screens.
DR ChiTaRS; RRP1; human.
DR GeneWiki; RRP1; -.
DR GenomeRNAi; 8568; -.
DR Pharos; P56182; Tbio.
DR PRO; PR:P56182; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; P56182; protein.
DR Bgee; ENSG00000160214; Expressed in tendon of biceps brachii and 184 other tissues.
DR ExpressionAtlas; P56182; baseline and differential.
DR Genevisible; P56182; HS.
DR GO; GO:0005694; C:chromosome; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR InterPro; IPR010301; RRP1-like.
DR PANTHER; PTHR13026; PTHR13026; 1.
DR Pfam; PF05997; Nop52; 1.
PE 1: Evidence at protein level;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; rRNA processing.
FT CHAIN 1..461
FT /note="Ribosomal RNA processing protein 1 homolog A"
FT /id="PRO_0000096887"
FT REGION 239..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 412
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 427
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000269|PubMed:26797129"
FT VARIANT 194
FT /note="I -> V (in dbSNP:rs34224504)"
FT /id="VAR_053894"
FT VARIANT 326
FT /note="K -> R (in dbSNP:rs915770)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_053895"
FT MUTAGEN 427
FT /note="Q->R: Abolishes methylation by N6AMT1."
FT /evidence="ECO:0000269|PubMed:26797129"
SQ SEQUENCE 461 AA; 52839 MW; C6F204EF4161AEAE CRC64;
MVSRVQLPPE IQLAQRLAGN EQVTRDRAVR KLRKYIVART QRAAGGFTHD ELLKVWKGLF
YCMWMQDKPL LQEELGRTIS QLVHAFQTTE AQHLFLQAFW QTMNREWTGI DRLRLDKFYM
LMRMVLNESL KVLKMQGWEE RQIEELLELL MTEILHPSSQ APNGVKSHFI EIFLEELTKV
GAEELTADQN LKFIDPFCRI AARTKDSLVL NNITRGIFET IVEQAPLAIE DLLNELDTQD
EEVASDSDES SEGGERGDAL SQKRSEKPPA GSICRAEPEA GEEQAGDDRD SGGPVLQFDY
EAVANRLFEM ASRQSTPSQN RKRLYKVIRK LQDLAGGIFP EDEIPEKACR RLLEGRRQKK
TKKQKRLLRL QQERGKGEKE PPSPGMERKR SRRRGVGADP EARAEAGEQP GTAERALLRD
QPRGRGQRGA RQRRRTPRPL TSARAKAANV QEPEKKKKRR E
