NUCL_MOUSE
ID NUCL_MOUSE Reviewed; 707 AA.
AC P09405; Q548M9; Q61991; Q8BQD8; Q99K50;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Nucleolin;
DE AltName: Full=Protein C23;
GN Name=Ncl; Synonyms=Nuc;
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 [GENOMIC DNA].
RC STRAIN=BALB/cJ;
RX PubMed=3137346; DOI=10.1016/0022-2836(88)90476-7;
RA Bourbon H.-M., Lapeyre B., Amalric F.;
RT "Structure of the mouse nucleolin gene. The complete sequence reveals that
RT each RNA binding domain is encoded by two independent exons.";
RL J. Mol. Biol. 200:627-638(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Egg, Lung, and 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
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 [GENOMIC DNA] OF 1-45.
RX PubMed=2906027; DOI=10.1016/0378-1119(88)90600-2;
RA Bourbon H.-M., Prudhomme M., Amalric F.;
RT "Sequence and structure of the nucleolin promoter in rodents:
RT characterization of a strikingly conserved CpG island.";
RL Gene 68:73-84(1988).
RN [5]
RP PROTEIN SEQUENCE OF 2-24.
RX PubMed=1860869; DOI=10.1016/s0021-9258(18)98743-0;
RA Pasternack M.S., Bleier K.J., McInerney T.N.;
RT "Granzyme A binding to target cell proteins. Granzyme A binds to and
RT cleaves nucleolin in vitro.";
RL J. Biol. Chem. 266:14703-14708(1991).
RN [6]
RP PROTEIN SEQUENCE OF 2-19 AND 558-567, AND FUNCTION.
RX PubMed=8065340; DOI=10.1128/mcb.14.9.6068-6074.1994;
RA Yang T.-H., Tsai W.-H., Lee Y.-M., Lei H.-Y., Lai M.-Y., Chen D.-S.,
RA Yeh N.-H., Lee S.-C.;
RT "Purification and characterization of nucleolin and its identification as a
RT transcription repressor.";
RL Mol. Cell. Biol. 14:6068-6074(1994).
RN [7]
RP PROTEIN SEQUENCE OF 327-344; 351-364; 401-412; 432-439; 460-469; 488-500;
RP 525-538; 575-586 AND 608-621, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [8]
RP IDENTIFICATION IN SWAP COMPLEX, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=9642267; DOI=10.1074/jbc.273.27.17025;
RA Borggrefe T., Wabl M., Akhmedov A.T., Jessberger R.;
RT "A B-cell-specific DNA recombination complex.";
RL J. Biol. Chem. 273:17025-17035(1998).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145 AND SER-157, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Teratocarcinoma;
RX PubMed=17622165; DOI=10.1021/pr070122r;
RA Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT cells.";
RL J. Proteome Res. 6:3174-3186(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-34; SER-40; SER-41
RP AND SER-145, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [11]
RP GLYCYLATION.
RX PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
RA Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N.,
RA Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C.;
RT "Evolutionary divergence of enzymatic mechanisms for posttranslational
RT polyglycylation.";
RL Cell 137:1076-1087(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-34; SER-40; SER-41
RP AND SER-403, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-34; SER-40; SER-41;
RP SER-145; SER-157; SER-189; SER-212; SER-303; SER-403; SER-460 AND SER-616,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [14]
RP INTERACTION WITH NVL.
RX PubMed=21474449; DOI=10.1074/jbc.m110.174680;
RA Fujiwara Y., Fujiwara K., Goda N., Iwaya N., Tenno T., Shirakawa M.,
RA Hiroaki H.;
RT "Structure and function of the N-terminal nucleolin binding domain of
RT nuclear valosin-containing protein-like 2 (NVL2) harboring a nucleolar
RT localization signal.";
RL J. Biol. Chem. 286:21732-21741(2011).
RN [15]
RP INTERACTION WITH AICDA.
RX PubMed=21518874; DOI=10.1073/pnas.1104423108;
RA Okazaki I.M., Okawa K., Kobayashi M., Yoshikawa K., Kawamoto S.,
RA Nagaoka H., Shinkura R., Kitawaki Y., Taniguchi H., Natsume T., Iemura S.,
RA Honjo T.;
RT "Histone chaperone Spt6 is required for class switch recombination but not
RT somatic hypermutation.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:7920-7925(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-9; LYS-15; LYS-16; LYS-96;
RP LYS-102; LYS-109; LYS-116; LYS-350; LYS-429; LYS-446; LYS-469; LYS-478;
RP LYS-522; LYS-574 AND LYS-643, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [17]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-691, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [18]
RP INTERACTION WITH LRRC34.
RX PubMed=24991885; DOI=10.1089/scd.2013.0470;
RA Luehrig S., Siamishi I., Tesmer-Wolf M., Zechner U., Engel W., Nolte J.;
RT "Lrrc34, a novel nucleolar protein, interacts with npm1 and ncl and has an
RT impact on pluripotent stem cells.";
RL Stem Cells Dev. 23:2862-2874(2014).
RN [19]
RP INTERACTION WITH ZBTB7B.
RX PubMed=28784777; DOI=10.1073/pnas.1703494114;
RA Li S., Mi L., Yu L., Yu Q., Liu T., Wang G.X., Zhao X.Y., Wu J., Lin J.D.;
RT "Zbtb7b engages the long noncoding RNA Blnc1 to drive brown and beige fat
RT development and thermogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E7111-E7120(2017).
CC -!- FUNCTION: Nucleolin is the major nucleolar protein of growing
CC eukaryotic cells. It is found associated with intranucleolar chromatin
CC and pre-ribosomal particles. It induces chromatin decondensation by
CC binding to histone H1. It is thought to play a role in pre-rRNA
CC transcription and ribosome assembly. May play a role in the process of
CC transcriptional elongation. Binds RNA oligonucleotides with 5'-UUAGGG-
CC 3' repeats more tightly than the telomeric single-stranded DNA 5'-
CC TTAGGG-3' repeats (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:8065340}.
CC -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs (By similarity). Component of the SWAP
CC complex that consists of NPM1, NCL/nucleolin, PARP1 and SWAP70
CC (PubMed:9642267). Component of a complex which is at least composed of
CC HTATSF1/Tat-SF1, the P-TEFb complex components CDK9 and CCNT1, RNA
CC polymerase II, SUPT5H, and NCL/nucleolin (By similarity). Interacts
CC with AICDA (PubMed:21518874). Interacts with APTX (By similarity).
CC Interacts with C1QBP (By similarity). Interacts with ERBB4 (By
CC similarity). Interacts (via C-terminus) with FMR1 isoform 6 (via N-
CC terminus) (By similarity). Interacts with GZF1; this interaction is
CC important for nucleolar localization of GZF1 (By similarity). Interacts
CC with NSUN2 (By similarity). Interacts with NVL (PubMed:21474449).
CC Interacts (via N-terminus domain) with SETX (By similarity). Interacts
CC (via RRM1 and C-terminal RRM4/Arg/Gly-rich domains) with TERT; the
CC interaction is important for nucleolar localization of TERT (By
CC similarity). Interacts with WDR46 (By similarity). Interacts with ZFP36
CC (By similarity). Interacts with LRRC34 (PubMed:24991885). Interacts
CC with RRP1B (By similarity). Interacts with HNRNPU; this interaction
CC occurs during mitosis (By similarity). Interacts with RIOK1; RIOK1
CC recruits NCL to PRMT5 for symmetrically methylation (By similarity).
CC Interacts with ZBTB7B (PubMed:28784777). Interacts with MDK; this
CC interaction promotes NCL clustering and lateral movements of this
CC complex into lipid rafts leading to MDK internalization (By
CC similarity). Interacts with HDGF (By similarity). Interacts with
CC ALKBH2. {ECO:0000250|UniProtKB:P19338, ECO:0000269|PubMed:21474449,
CC ECO:0000269|PubMed:21518874, ECO:0000269|PubMed:24991885,
CC ECO:0000269|PubMed:28784777, ECO:0000269|PubMed:9642267}.
CC -!- INTERACTION:
CC P09405; Q9CR42: Ankrd1; NbExp=5; IntAct=EBI-641864, EBI-8308696;
CC P09405; Q9DC51: Gnai3; NbExp=4; IntAct=EBI-641864, EBI-641852;
CC P09405; P63028: Tpt1; NbExp=4; IntAct=EBI-641864, EBI-1635228;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm {ECO:0000250}.
CC Note=Localized in cytoplasmic mRNP granules containing untranslated
CC mRNAs. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in B-cells that have been induced to
CC switch to various Ig isotypes. {ECO:0000269|PubMed:9642267}.
CC -!- PTM: Some glutamate residues are glycylated by TTLL8. This modification
CC occurs exclusively on glutamate residues and results in a glycine chain
CC on the gamma-carboxyl group.
CC -!- PTM: Symmetrically methylated by PRMT5. {ECO:0000250|UniProtKB:P19338}.
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DR EMBL; X07699; CAA30538.1; -; Genomic_DNA.
DR EMBL; AF318184; AAK07920.1; -; mRNA.
DR EMBL; AK050958; BAC34476.1; -; mRNA.
DR EMBL; AK083307; BAC38858.1; -; mRNA.
DR EMBL; AK144894; BAE26119.1; -; mRNA.
DR EMBL; AK161706; BAE36542.1; -; mRNA.
DR EMBL; AK163275; BAE37270.1; -; mRNA.
DR EMBL; BC005460; AAH05460.1; -; mRNA.
DR EMBL; M22089; AAA39841.1; -; Genomic_DNA.
DR CCDS; CCDS35646.1; -.
DR PIR; A29958; DNMS.
DR RefSeq; NP_035010.3; NM_010880.3.
DR AlphaFoldDB; P09405; -.
DR SMR; P09405; -.
DR BioGRID; 201706; 89.
DR CORUM; P09405; -.
DR IntAct; P09405; 18.
DR MINT; P09405; -.
DR STRING; 10090.ENSMUSP00000027438; -.
DR iPTMnet; P09405; -.
DR PhosphoSitePlus; P09405; -.
DR SwissPalm; P09405; -.
DR REPRODUCTION-2DPAGE; P09405; -.
DR EPD; P09405; -.
DR jPOST; P09405; -.
DR MaxQB; P09405; -.
DR PaxDb; P09405; -.
DR PeptideAtlas; P09405; -.
DR PRIDE; P09405; -.
DR ProteomicsDB; 291922; -.
DR TopDownProteomics; P09405; -.
DR Antibodypedia; 3779; 871 antibodies from 42 providers.
DR DNASU; 17975; -.
DR Ensembl; ENSMUST00000027438; ENSMUSP00000027438; ENSMUSG00000026234.
DR GeneID; 17975; -.
DR KEGG; mmu:17975; -.
DR UCSC; uc007bvl.1; mouse.
DR CTD; 4691; -.
DR MGI; MGI:97286; Ncl.
DR VEuPathDB; HostDB:ENSMUSG00000026234; -.
DR eggNOG; KOG0123; Eukaryota.
DR GeneTree; ENSGT00940000157437; -.
DR HOGENOM; CLU_026300_1_0_1; -.
DR InParanoid; P09405; -.
DR OMA; GYVQYSS; -.
DR OrthoDB; 1174365at2759; -.
DR PhylomeDB; P09405; -.
DR TreeFam; TF328499; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 17975; 29 hits in 77 CRISPR screens.
DR ChiTaRS; Ncl; mouse.
DR PRO; PR:P09405; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P09405; protein.
DR Bgee; ENSMUSG00000026234; Expressed in embryonic post-anal tail and 96 other tissues.
DR ExpressionAtlas; P09405; baseline and differential.
DR Genevisible; P09405; MM.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0001533; C:cornified envelope; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0001651; C:dense fibrillar component; ISO:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0044547; F:DNA topoisomerase binding; ISO:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:1990631; F:ErbB-4 class receptor binding; ISO:MGI.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0043236; F:laminin binding; ISO:MGI.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0042134; F:rRNA primary transcript binding; ISO:MGI.
DR GO; GO:0035368; F:selenocysteine insertion sequence binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; ISO:MGI.
DR GO; GO:0042162; F:telomeric DNA binding; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; ISO:MGI.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IDA:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:MGI.
DR GO; GO:0006897; P:endocytosis; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:MGI.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:1901838; P:positive regulation of transcription of nucleolar large rRNA by RNA polymerase I; ISO:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:MGI.
DR GO; GO:2000232; P:regulation of rRNA processing; ISO:MGI.
DR CDD; cd12403; RRM1_NCL; 1.
DR CDD; cd12405; RRM3_NCL; 1.
DR CDD; cd12406; RRM4_NCL; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR InterPro; IPR034230; Nucleolin_RRM1.
DR InterPro; IPR034234; Nucleolin_RRM3.
DR InterPro; IPR034235; Nucleolin_RRM4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 4.
DR SMART; SM00360; RRM; 4.
DR SUPFAM; SSF54928; SSF54928; 4.
DR PROSITE; PS50102; RRM; 4.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; RNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1860869,
FT ECO:0000269|PubMed:8065340"
FT CHAIN 2..707
FT /note="Nucleolin"
FT /id="PRO_0000081693"
FT REPEAT 58..65
FT /note="1"
FT REPEAT 75..82
FT /note="2"
FT REPEAT 83..90
FT /note="3"
FT REPEAT 91..98
FT /note="4"
FT REPEAT 99..104
FT /note="5; truncated"
FT REPEAT 105..112
FT /note="6"
FT REPEAT 120..127
FT /note="7"
FT REPEAT 128..135
FT /note="8"
FT DOMAIN 309..385
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 395..468
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 487..561
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 569..644
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..135
FT /note="8 X 8 AA tandem repeats of X-T-P-X-K-K-X-X"
FT REGION 639..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..43
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..170
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..216
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..273
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 15
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 16
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 69
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 76
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 84
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 92
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 96
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 99
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 102
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 106
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 109
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 116
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 121
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 124
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:17622165, ECO:0007744|PubMed:21183079"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17622165,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 220
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 320
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 350
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 369
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 379
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 400
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 407
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 429
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 446
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 469
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 478
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 514
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 522
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 569
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 574
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 577
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 643
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 653
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 657
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 663
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 667
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 670
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 676
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 678
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 684
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 688
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 691
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 691
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 299
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 299
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 326
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 326
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 372
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 379
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 514
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 574
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 586
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 586
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 621
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CONFLICT 155
FT /note="D -> E (in Ref. 3; AAH05460)"
FT /evidence="ECO:0000305"
FT CONFLICT 203..204
FT /note="DD -> EE (in Ref. 3; AAH05460)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="D -> E (in Ref. 3; AAH05460)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 707 AA; 76723 MW; EE2CE2ACDBF54CD4 CRC64;
MVKLAKAGKT HGEAKKMAPP PKEVEEDSED EEMSEDEDDS SGEEEVVIPQ KKGKKATTTP
AKKVVVSQTK KAAVPTPAKK AAVTPGKKAV ATPAKKNITP AKVIPTPGKK GAAQAKALVP
TPGKKGAATP AKGAKNGKNA KKEDSDEDED EEDEDDSDED EDDEEEDEFE PPIVKGVKPA
KAAPAAPASE DEEDDEDEDD EEDDDEEEED DSEEEVMEIT TAKGKKTPAK VVPMKAKSVA
EEEDDEEEDE DDEDEDDEEE DDEDDDEEEE EEEPVKAAPG KRKKEMTKQK EAPEAKKQKV
EGSEPTTPFN LFIGNLNPNK SVNELKFAIS ELFAKNDLAV VDVRTGTNRK FGYVDFESAE
DLEKALELTG LKVFGNEIKL EKPKGRDSKK VRAARTLLAK NLSFNITEDE LKEVFEDAME
IRLVSQDGKS KGIAYIEFKS EADAEKNLEE KQGAEIDGRS VSLYYTGEKG QRQERTGKTS
TWSGESKTLV LSNLSYSATK ETLEEVFEKA TFIKVPQNPH GKPKGYAFIE FASFEDAKEA
LNSCNKMEIE GRTIRLELQG SNSRSQPSKT LFVKGLSEDT TEETLKESFE GSVRARIVTD
RETGSSKGFG FVDFNSEEDA KAAKEAMEDG EIDGNKVTLD WAKPKGEGGF GGRGGGRGGF
GGRGGGRGGR GGFGGRGRGG FGGRGGFRGG RGGGGDFKPQ GKKTKFE
