NOLC1_HUMAN
ID NOLC1_HUMAN Reviewed; 699 AA.
AC Q14978; Q15030; Q5VV70; Q9BUV3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Nucleolar and coiled-body phosphoprotein 1 {ECO:0000305};
DE AltName: Full=140 kDa nucleolar phosphoprotein {ECO:0000303|PubMed:10567578};
DE Short=Nopp140 {ECO:0000303|PubMed:10567578};
DE AltName: Full=Hepatitis C virus NS5A-transactivated protein 13;
DE Short=HCV NS5A-transactivated protein 13;
DE AltName: Full=Nucleolar 130 kDa protein {ECO:0000303|PubMed:7657714};
DE AltName: Full=Nucleolar phosphoprotein p130 {ECO:0000303|PubMed:7657714};
GN Name=NOLC1 {ECO:0000312|HGNC:HGNC:15608};
GN Synonyms=KIAA0035 {ECO:0000303|PubMed:7584026}, NS5ATP13;
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] (ISOFORM ALPHA), SUBCELLULAR LOCATION, AND
RP PHOSPHORYLATION.
RC TISSUE=Leukemia;
RX PubMed=7657714; DOI=10.1242/jcs.108.5.1911;
RA Pai C.-Y., Chen H.-K., Sheu H.-L., Yeh N.-H.;
RT "Cell-cycle-dependent alterations of a highly phosphorylated nucleolar
RT protein p130 are associated with nucleologenesis.";
RL J. Cell Sci. 108:1911-1920(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Ying Z.L., Hong D., Jun C.;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Lung;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-699 (ISOFORM BETA), AND VARIANT
RP PRO-456.
RC TISSUE=Bone marrow;
RX PubMed=7584026; DOI=10.1093/dnares/1.1.27;
RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S.,
RA Nagase T., Seki N., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. I. The
RT coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of
RT randomly sampled cDNA clones from human immature myeloid cell line KG-1.";
RL DNA Res. 1:27-35(1994).
RN [7]
RP ALTERNATIVE SPLICING.
RX PubMed=8630004; DOI=10.1006/bbrc.1996.0639;
RA Pai C.-Y., Yeh N.-H.;
RT "Cell proliferation-dependent expression of two isoforms of the nucleolar
RT phosphoprotein p130.";
RL Biochem. Biophys. Res. Commun. 221:581-587(1996).
RN [8]
RP FUNCTION.
RX PubMed=9016786; DOI=10.1006/bbrc.1996.5966;
RA Chen H.-K., Yeh N.-H.;
RT "The nucleolar phosphoprotein P130 is a GTPase/ATPase with intrinsic
RT property to form large complexes triggered by F- and Mg2+.";
RL Biochem. Biophys. Res. Commun. 230:370-375(1997).
RN [9]
RP FUNCTION, AND INTERACTION WITH RPA194.
RX PubMed=10567578; DOI=10.1128/mcb.19.12.8536;
RA Chen H.-K., Pai C.-Y., Huang J.-Y., Yeh N.-H.;
RT "Human Nopp140, which interacts with RNA polymerase I: implications for
RT rRNA gene transcription and nucleolar structural organization.";
RL Mol. Cell. Biol. 19:8536-8546(1999).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-607 AND THR-610, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538; SER-563 AND SER-698, AND
RP IDENTIFICATION BY 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-607; THR-610; SER-643 AND
RP SER-698, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508; SER-538; THR-607;
RP THR-610 AND SER-643, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-90; SER-91; SER-366;
RP SER-508; SER-580; SER-582; SER-686 AND SER-698, AND IDENTIFICATION BY MASS
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-698, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33; LYS-415 AND LYS-663, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397; SER-508; SER-538;
RP SER-563; SER-580; SER-582; SER-643 AND SER-698, AND IDENTIFICATION BY MASS
RP 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 [20]
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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397; SER-538; SER-622;
RP SER-643 AND SER-698, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-188; SER-397; SER-456;
RP SER-508; SER-538; THR-607; THR-610; SER-643 AND SER-698, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; SER-363 AND SER-698, AND
RP IDENTIFICATION BY 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 [24]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-683, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
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 [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-67 AND LYS-193, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-415 AND LYS-572, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [27]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-67 AND LYS-604, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [28]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-67 AND LYS-193, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [29]
RP FUNCTION, UBIQUITINATION, AND SUBUNIT.
RX PubMed=26399832; DOI=10.1038/nature14978;
RA Werner A., Iwasaki S., McGourty C.A., Medina-Ruiz S., Teerikorpi N.,
RA Fedrigo I., Ingolia N.T., Rape M.;
RT "Cell-fate determination by ubiquitin-dependent regulation of
RT translation.";
RL Nature 525:523-527(2015).
RN [30]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [31]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-67; LYS-76; LYS-186; LYS-193;
RP LYS-342; LYS-347; LYS-390; LYS-396; LYS-401; LYS-407; LYS-415; LYS-440;
RP LYS-452; LYS-505; LYS-579; LYS-604; LYS-613; LYS-647; LYS-663 AND LYS-695,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Nucleolar protein that acts as a regulator of RNA polymerase
CC I by connecting RNA polymerase I with enzymes responsible for ribosomal
CC processing and modification (PubMed:10567578, PubMed:26399832).
CC Required for neural crest specification: following monoubiquitination
CC by the BCR(KBTBD8) complex, associates with TCOF1 and acts as a
CC platform to connect RNA polymerase I with enzymes responsible for
CC ribosomal processing and modification, leading to remodel the
CC translational program of differentiating cells in favor of neural crest
CC specification (PubMed:26399832). Involved in nucleologenesis, possibly
CC by playing a role in the maintenance of the fundamental structure of
CC the fibrillar center and dense fibrillar component in the nucleolus
CC (PubMed:9016786). It has intrinsic GTPase and ATPase activities
CC (PubMed:9016786). {ECO:0000269|PubMed:10567578,
CC ECO:0000269|PubMed:26399832, ECO:0000269|PubMed:9016786}.
CC -!- SUBUNIT: Heterodimer; heterodimerizes with TCOF1 following
CC monoubiquitination (PubMed:26399832). Interacts with RNA polymerase I
CC 194 kDa subunit (RPA194) and with casein kinase-II (PubMed:10567578).
CC Interacts with DKC1/NAP57, NOP58 and fibrillarin (By similarity).
CC {ECO:0000250|UniProtKB:P41777, ECO:0000269|PubMed:10567578,
CC ECO:0000269|PubMed:26399832}.
CC -!- INTERACTION:
CC Q14978; P49407: ARRB1; NbExp=3; IntAct=EBI-396155, EBI-743313;
CC Q14978; P32121: ARRB2; NbExp=3; IntAct=EBI-396155, EBI-714559;
CC Q14978; PRO_0000038593 [P04591]: gag; Xeno; NbExp=2; IntAct=EBI-396155, EBI-6179719;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:7657714}.
CC Cytoplasm {ECO:0000269|PubMed:7657714}. Note=Shuttles between the
CC nucleolus and the cytoplasm. At telophase it begins to assemble into
CC granular-like pre-nucleolar bodies which are subsequently relocated to
CC nucleoli at the early G1-phase. {ECO:0000269|PubMed:7657714}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Alpha;
CC IsoId=Q14978-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=Q14978-2; Sequence=VSP_004338;
CC Name=3;
CC IsoId=Q14978-3; Sequence=VSP_035415;
CC -!- PTM: Undergoes rapid and massive phosphorylation/dephosphorylation
CC cycles on CK2 and PKC sites. NOLC1 is one of the mostly phosphorylated
CC proteins in the cell. {ECO:0000269|PubMed:7657714}.
CC -!- PTM: Ubiquitinated. Monoubiquitination by the BCR(KBTBD8) complex
CC promotes the formation of a NOLC1-TCOF1 complex that acts as a platform
CC to connect RNA polymerase I with enzymes responsible for ribosomal
CC processing and modification, leading to remodel the translational
CC program of differentiating cells in favor of neural crest specification
CC (PubMed:26399832). {ECO:0000269|PubMed:26399832}.
CC -!- PTM: Pyrophosphorylated by 5-diphosphoinositol pentakisphosphate (5-
CC IP7). Serine pyrophosphorylation is achieved by Mg(2+)-dependent, but
CC enzyme independent transfer of a beta-phosphate from a inositol
CC pyrophosphate to a pre-phosphorylated serine residue.
CC {ECO:0000250|UniProtKB:E9Q5C9}.
CC -!- SIMILARITY: Belongs to the NOLC1 family. {ECO:0000305}.
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DR EMBL; Z34289; CAA84063.1; -; mRNA.
DR EMBL; AY820769; AAV67777.1; -; mRNA.
DR EMBL; AL500527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49714.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49715.1; -; Genomic_DNA.
DR EMBL; BC001883; AAH01883.1; -; mRNA.
DR EMBL; D21262; BAA04803.1; -; mRNA.
DR CCDS; CCDS65925.1; -. [Q14978-3]
DR CCDS; CCDS65926.1; -. [Q14978-2]
DR CCDS; CCDS7530.1; -. [Q14978-1]
DR PIR; I38073; I38073.
DR RefSeq; NP_001271317.1; NM_001284388.1. [Q14978-2]
DR RefSeq; NP_001271318.1; NM_001284389.1. [Q14978-3]
DR RefSeq; NP_004732.2; NM_004741.4. [Q14978-1]
DR AlphaFoldDB; Q14978; -.
DR SMR; Q14978; -.
DR BioGRID; 114654; 242.
DR CORUM; Q14978; -.
DR IntAct; Q14978; 91.
DR MINT; Q14978; -.
DR STRING; 9606.ENSP00000385410; -.
DR DrugBank; DB00997; Doxorubicin.
DR GlyGen; Q14978; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q14978; -.
DR PhosphoSitePlus; Q14978; -.
DR SwissPalm; Q14978; -.
DR BioMuta; NOLC1; -.
DR DMDM; 145559503; -.
DR EPD; Q14978; -.
DR jPOST; Q14978; -.
DR MassIVE; Q14978; -.
DR MaxQB; Q14978; -.
DR PaxDb; Q14978; -.
DR PeptideAtlas; Q14978; -.
DR PRIDE; Q14978; -.
DR ProteomicsDB; 60269; -. [Q14978-1]
DR ProteomicsDB; 60270; -. [Q14978-2]
DR ProteomicsDB; 60271; -. [Q14978-3]
DR Antibodypedia; 31392; 292 antibodies from 33 providers.
DR DNASU; 9221; -.
DR Ensembl; ENST00000405356.5; ENSP00000385410.1; ENSG00000166197.17. [Q14978-2]
DR Ensembl; ENST00000488254.6; ENSP00000475080.1; ENSG00000166197.17. [Q14978-3]
DR Ensembl; ENST00000605788.6; ENSP00000474710.2; ENSG00000166197.17. [Q14978-1]
DR GeneID; 9221; -.
DR KEGG; hsa:9221; -.
DR MANE-Select; ENST00000605788.6; ENSP00000474710.2; NM_004741.5; NP_004732.2.
DR UCSC; uc001kuo.4; human. [Q14978-1]
DR CTD; 9221; -.
DR DisGeNET; 9221; -.
DR GeneCards; NOLC1; -.
DR HGNC; HGNC:15608; NOLC1.
DR HPA; ENSG00000166197; Low tissue specificity.
DR MIM; 602394; gene.
DR neXtProt; NX_Q14978; -.
DR OpenTargets; ENSG00000166197; -.
DR PharmGKB; PA31679; -.
DR VEuPathDB; HostDB:ENSG00000166197; -.
DR eggNOG; KOG2992; Eukaryota.
DR GeneTree; ENSGT00730000111092; -.
DR HOGENOM; CLU_014527_0_0_1; -.
DR InParanoid; Q14978; -.
DR OMA; RESGCQG; -.
DR OrthoDB; 1610147at2759; -.
DR PhylomeDB; Q14978; -.
DR TreeFam; TF341730; -.
DR PathwayCommons; Q14978; -.
DR SignaLink; Q14978; -.
DR SIGNOR; Q14978; -.
DR BioGRID-ORCS; 9221; 463 hits in 1097 CRISPR screens.
DR ChiTaRS; NOLC1; human.
DR GeneWiki; Nucleolar_phosphoprotein_p130; -.
DR GenomeRNAi; 9221; -.
DR Pharos; Q14978; Tbio.
DR PRO; PR:Q14978; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q14978; protein.
DR Bgee; ENSG00000166197; Expressed in middle temporal gyrus and 204 other tissues.
DR ExpressionAtlas; Q14978; baseline and differential.
DR Genevisible; Q14978; HS.
DR GO; GO:0031428; C:box C/D RNP complex; IEA:Ensembl.
DR GO; GO:0031429; C:box H/ACA snoRNP complex; IEA:Ensembl.
DR GO; GO:0015030; C:Cajal body; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0034512; F:box C/D RNA binding; IEA:Ensembl.
DR GO; GO:0062064; F:box C/D snoRNP complex binding; IEA:Ensembl.
DR GO; GO:0034513; F:box H/ACA snoRNA binding; IEA:Ensembl.
DR GO; GO:0062065; F:box H/ACA snoRNP complex binding; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0008139; F:nuclear localization sequence binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0001093; F:TFIIB-class transcription factor binding; IEA:Ensembl.
DR GO; GO:0033979; P:box H/ACA RNA metabolic process; IEA:Ensembl.
DR GO; GO:0000278; P:mitotic cell cycle; TAS:ProtInc.
DR GO; GO:0014032; P:neural crest cell development; IMP:UniProtKB.
DR GO; GO:0014029; P:neural crest formation; IMP:UniProtKB.
DR GO; GO:0007000; P:nucleolus organization; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0042306; P:regulation of protein import into nucleus; IEA:Ensembl.
DR GO; GO:0006417; P:regulation of translation; IMP:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IEA:Ensembl.
DR GO; GO:0006364; P:rRNA processing; TAS:ProtInc.
DR DisProt; DP01178; -.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR007718; Srp40_C.
DR Pfam; PF05022; SRP40_C; 1.
DR PROSITE; PS50896; LISH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cytoplasm; GTP-binding;
KW Isopeptide bond; Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..699
FT /note="Nucleolar and coiled-body phosphoprotein 1"
FT /id="PRO_0000096942"
FT DOMAIN 10..42
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT REPEAT 84..95
FT /note="Acidic serine cluster 1"
FT REPEAT 125..136
FT /note="Acidic serine cluster 2"
FT REPEAT 167..178
FT /note="Acidic serine cluster 3"
FT REPEAT 221..232
FT /note="Acidic serine cluster 4"
FT REPEAT 264..275
FT /note="Acidic serine cluster 5"
FT REPEAT 325..336
FT /note="Acidic serine cluster 6"
FT REPEAT 363..375
FT /note="Acidic serine cluster 7"
FT REPEAT 425..436
FT /note="Acidic serine cluster 8"
FT REPEAT 470..481
FT /note="Acidic serine cluster 9"
FT REPEAT 519..529
FT /note="Acidic serine cluster 10"
FT REPEAT 555..566
FT /note="Acidic serine cluster 11"
FT REGION 65..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..566
FT /note="11 X 12 AA approximate repeats of an acidic serine
FT cluster"
FT REGION 204..382
FT /note="Interaction with RPA194"
FT MOTIF 68..82
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 384..587
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 601..617
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 161..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..305
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..637
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 33
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 91
FT /note="Diphosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9Q5C9"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 188
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 415
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 607
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 610
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 622
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 663
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 683
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT CROSSLNK 67
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 76
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 186
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 193
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 342
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 347
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 390
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 396
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 401
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 407
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 415
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 415
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 440
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 452
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 505
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 572
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 579
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 604
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 613
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 647
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 663
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 695
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 58..59
FT /note="LK -> LNR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_035415"
FT VAR_SEQ 241
FT /note="K -> KVWTITSVRAE (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:7584026"
FT /id="VSP_004338"
FT VARIANT 412
FT /note="G -> V (in dbSNP:rs11191224)"
FT /id="VAR_031677"
FT VARIANT 456
FT /note="S -> P (in dbSNP:rs1049455)"
FT /evidence="ECO:0000269|PubMed:7584026"
FT /id="VAR_031678"
FT CONFLICT 3
FT /note="D -> A (in Ref. 6; BAA04803)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="S -> R (in Ref. 1; CAA84063)"
FT /evidence="ECO:0000305"
FT CONFLICT 291..292
FT /note="SV -> YA (in Ref. 1; CAA84063)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 699 AA; 73603 MW; 7C5C4F25677E2E61 CRC64;
MADAGIRRVV PSDLYPLVLG FLRDNQLSEV ANKFAKATGA TQQDANASSL LDIYSFWLKS
AKVPERKLQA NGPVAKKAKK KASSSDSEDS SEEEEEVQGP PAKKAAVPAK RVGLPPGKAA
AKASESSSSE ESSDDDDEED QKKQPVQKGV KPQAKAAKAP PKKAKSSDSD SDSSSEDEPP
KNQKPKITPV TVKAQTKAPP KPARAAPKIA NGKAASSSSS SSSSSSSDDS EEEKAAATPK
KTVPKKQVVA KAPVKAATTP TRKSSSSEDS SSDEEEEQKK PMKNKPGPYS SVPPPSAPPP
KKSLGTQPPK KAVEKQQPVE SSEDSSDESD SSSEEEKKPP TKAVVSKATT KPPPAKKAAE
SSSDSSDSDS SEDDEAPSKP AGTTKNSSNK PAVTTKSPAV KPAAAPKQPV GGGQKLLTRK
ADSSSSEEES SSSEEEKTKK MVATTKPKAT AKAALSLPAK QAPQGSRDSS SDSDSSSSEE
EEEKTSKSAV KKKPQKVAGG AAPSKPASAK KGKAESSNSS SSDDSSEEEE EKLKGKGSPR
PQAPKANGTS ALTAQNGKAA KNSEEEEEEK KKAAVVVSKS GSLKKRKQNE AAKEAETPQA
KKIKLQTPNT FPKRKKGEKR ASSPFRRVRE EEIEVDSRVA DNSFDAKRGA AGDWGERANQ
VLKFTKGKSF RHEKTKKKRG SYRGGSISVQ VNSIKFDSE
