NOP2_MOUSE
ID NOP2_MOUSE Reviewed; 793 AA.
AC Q922K7; Q3U4W9;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Probable 28S rRNA (cytosine-C(5))-methyltransferase;
DE EC=2.1.1.-;
DE AltName: Full=Nucleolar protein 1;
DE AltName: Full=Nucleolar protein 2 homolog;
DE AltName: Full=Proliferating-cell nucleolar antigen p120;
DE AltName: Full=Proliferation-associated nucleolar protein p120;
GN Name=Nop2; Synonyms=Nol1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1394192;
RA Valdez B.C., Perlaky L., Saijo Y., Henning D., Zhu C., Busch R.K.,
RA Zhang W.W., Busch H.;
RT "A region of antisense RNA from human p120 cDNA with high homology to mouse
RT p120 cDNA inhibits NIH 3T3 proliferation.";
RL Cancer Res. 52:5681-5686(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 1-731.
RC STRAIN=NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-169 AND SER-179, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP CITRULLINATION AT ARG-86 AND ARG-148.
RX PubMed=24463520; DOI=10.1038/nature12942;
RA Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S.,
RA Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C.,
RA Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.;
RT "Citrullination regulates pluripotency and histone H1 binding to
RT chromatin.";
RL Nature 507:104-108(2014).
CC -!- FUNCTION: Involved in ribosomal large subunit assembly. S-adenosyl-L-
CC methionine-dependent methyltransferase that specifically methylates the
CC C(5) position of cytosine 4447 in 28S rRNA. May play a role in the
CC regulation of the cell cycle and the increased nucleolar activity that
CC is associated with the cell proliferation.
CC {ECO:0000250|UniProtKB:P46087}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cytidine in 28S rRNA + S-adenosyl-L-methionine = a 5-
CC methylcytidine in 28S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:47788, Rhea:RHEA-COMP:11915, Rhea:RHEA-COMP:11916,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC -!- SUBUNIT: Interacts with MCRS1. Interacts with WDR46. Interacts with
CC RRP1B. {ECO:0000250|UniProtKB:P46087}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000255|PROSITE-ProRule:PRU01023}.
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DR EMBL; BC007151; AAH07151.1; -; mRNA.
DR EMBL; AK154006; BAE32311.1; -; mRNA.
DR PIR; A48998; A48998.
DR AlphaFoldDB; Q922K7; -.
DR SMR; Q922K7; -.
DR CORUM; Q922K7; -.
DR IntAct; Q922K7; 2.
DR MINT; Q922K7; -.
DR STRING; 10090.ENSMUSP00000047123; -.
DR iPTMnet; Q922K7; -.
DR PhosphoSitePlus; Q922K7; -.
DR SwissPalm; Q922K7; -.
DR EPD; Q922K7; -.
DR MaxQB; Q922K7; -.
DR PaxDb; Q922K7; -.
DR PeptideAtlas; Q922K7; -.
DR PRIDE; Q922K7; -.
DR ProteomicsDB; 293941; -.
DR MGI; MGI:107891; Nop2.
DR eggNOG; KOG1122; Eukaryota.
DR InParanoid; Q922K7; -.
DR PhylomeDB; Q922K7; -.
DR ChiTaRS; Nop2; mouse.
DR PRO; PR:Q922K7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q922K7; protein.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009383; F:rRNA (cytosine-C5-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0001825; P:blastocyst formation; IMP:MGI.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0000027; P:ribosomal large subunit assembly; ISS:UniProtKB.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR InterPro; IPR031341; Methyltr_RsmF_N.
DR InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR InterPro; IPR011023; Nop2p.
DR InterPro; IPR012586; P120R_rpt.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR023273; RCMT_NOP2.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22807; PTHR22807; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR Pfam; PF17125; Methyltr_RsmF_N; 1.
DR Pfam; PF08062; P120R; 2.
DR PRINTS; PR02008; RCMTFAMILY.
DR PRINTS; PR02012; RCMTNOP2.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00446; nop2p; 1.
DR PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Citrullination; Isopeptide bond; Methyltransferase; Nucleus;
KW Phosphoprotein; Reference proteome; Ribosome biogenesis; RNA-binding;
KW rRNA processing; S-adenosyl-L-methionine; Transferase; Ubl conjugation.
FT CHAIN 1..793
FT /note="Probable 28S rRNA (cytosine-C(5))-methyltransferase"
FT /id="PRO_0000279585"
FT REGION 1..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..135
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 502
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 377..383
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 401
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 428
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 445
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46087"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46087"
FT MOD_RES 86
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:24463520"
FT MOD_RES 148
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:24463520"
FT MOD_RES 169
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 634
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P46087"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46087"
FT MOD_RES 713
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46087"
FT MOD_RES 767
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46087"
FT MOD_RES 782
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46087"
FT MOD_RES 793
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46087"
FT CROSSLNK 72
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P46087"
FT CROSSLNK 257
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P46087"
FT CROSSLNK 601
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P46087"
FT CONFLICT 160
FT /note="A -> T (in Ref. 3; BAE32311)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="L -> A (in Ref. 3; BAE32311)"
FT /evidence="ECO:0000305"
FT CONFLICT 708
FT /note="P -> PP (in Ref. 3; BAE32311)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 793 AA; 86752 MW; CB3B52A01A2E753F CRC64;
MGRKLDPTKK EKRGPGRKAR KQKGAETELV RFLPAAGDEN SKRLSSRARK RAAKRRAGSV
DVPKPNKSPG IKTLPGELSK GAVQARGKKR PAPIQNSDGD EEEDSGEDDV VTQGDLWGSE
DSDEDMVDDY GAASNSEDEE EKLLPIERAA LKQKAQDATA GVLWNEEDTD EDEDDDGVSP
ESHPRKDDKA EGDLQINVED EEAFVLPPAG ETDQDGQAPD LQRVHKRIQD IVGVLRDFGA
QREEGRSRAE YLSRLQKDLA TYYSYGDFLL SKLMELFPLS ELIEFLEANE VPRPITLRTN
TLKTRRRDLA QLLINRGVNL DPLGKWSKSG LVVYDSSVPI GATPEYLAGH YMLQGASSML
PVMALAPQEH ERILDMCCAP GGKTSYIAQL MKNTGVILAN DANADRLKSV VGNLHRLGVT
NTIISHYDGR QFPKVVGGFD RVLLDAPCSG TGVISKDPAV KTNKDEKDIQ RCAHLQKELL
LSAIDSVNAA SKTGGYLVYC TCSITVEENE WVVDYALKKR NVRLVPTGLD FGQEGFTRFQ
ARRFHPTLRS TRRFYPHTHN MDGFFIAKFK KFSNSIPQPH AGNSAAATPT EPDLKDQVTP
KSENGSQPTK KARGAVKAKQ QLLRQPHSKK PFQKLNGIAK GPGLSTEPSV PDAQVSTRPS
QSAGNADVNS KRKRSEKLKQ RGPKWKPSKE AAVPKPSAPS RVEDSGTPVP TPSEIRAAPR
PKDCAPSLGK AKKKQKGKQQ LAQQPANGAA PLKEDAVSKG PSAPFVSPHS STRPPPAKRR
KSMTKGNSQP LLS
