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Nucleolar and coiled-body phosphoprotein 1 (140 kDa nucleolar phosphoprotein) (Nopp140) (Hepatitis C virus NS5A-transactivated protein 13) (HCV NS5A-transactivated protein 13) (Nucleolar 130 kDa protein) (Nucleolar phosphoprotein p130)

 NOLC1_HUMAN             Reviewed;         699 AA.
Q14978; Q15030; Q5VV70; Q9BUV3;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
17-APR-2007, sequence version 2.
05-DEC-2018, entry version 185.
RecName: Full=Nucleolar and coiled-body phosphoprotein 1 {ECO:0000305};
AltName: Full=140 kDa nucleolar phosphoprotein {ECO:0000303|PubMed:10567578};
Short=Nopp140 {ECO:0000303|PubMed:10567578};
AltName: Full=Hepatitis C virus NS5A-transactivated protein 13;
Short=HCV NS5A-transactivated protein 13;
AltName: Full=Nucleolar 130 kDa protein {ECO:0000303|PubMed:7657714};
AltName: Full=Nucleolar phosphoprotein p130 {ECO:0000303|PubMed:7657714};
Name=NOLC1 {ECO:0000312|HGNC:HGNC:15608};
Synonyms=KIAA0035 {ECO:0000303|PubMed:7584026}, NS5ATP13;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), SUBCELLULAR LOCATION, AND
PHOSPHORYLATION.
TISSUE=Leukemia;
PubMed=7657714;
Pai C.-Y., Chen H.-K., Sheu H.-L., Yeh N.-H.;
"Cell-cycle-dependent alterations of a highly phosphorylated nucleolar
protein p130 are associated with nucleologenesis.";
J. Cell Sci. 108:1911-1920(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Ying Z.L., Hong D., Jun C.;
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-699 (ISOFORM BETA), AND
VARIANT PRO-456.
TISSUE=Bone marrow;
PubMed=7584026; DOI=10.1093/dnares/1.1.27;
Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y.,
Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.;
"Prediction of the coding sequences of unidentified human genes. I.
The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by
analysis of randomly sampled cDNA clones from human immature myeloid
cell line KG-1.";
DNA Res. 1:27-35(1994).
[7]
ALTERNATIVE SPLICING.
PubMed=8630004; DOI=10.1006/bbrc.1996.0639;
Pai C.-Y., Yeh N.-H.;
"Cell proliferation-dependent expression of two isoforms of the
nucleolar phosphoprotein p130.";
Biochem. Biophys. Res. Commun. 221:581-587(1996).
[8]
FUNCTION.
PubMed=9016786; DOI=10.1006/bbrc.1996.5966;
Chen H.-K., Yeh N.-H.;
"The nucleolar phosphoprotein P130 is a GTPase/ATPase with intrinsic
property to form large complexes triggered by F- and Mg2+.";
Biochem. Biophys. Res. Commun. 230:370-375(1997).
[9]
FUNCTION, AND INTERACTION WITH RPA194.
PubMed=10567578; DOI=10.1128/MCB.19.12.8536;
Chen H.-K., Pai C.-Y., Huang J.-Y., Yeh N.-H.;
"Human Nopp140, which interacts with RNA polymerase I: implications
for rRNA gene transcription and nucleolar structural organization.";
Mol. Cell. Biol. 19:8536-8546(1999).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-607 AND THR-610, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538; SER-563 AND
SER-698, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-607; THR-610; SER-643
AND SER-698, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508; SER-538; THR-607;
THR-610 AND SER-643, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-90; SER-91;
SER-366; SER-508; SER-580; SER-582; SER-686 AND SER-698, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-698, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33; LYS-415 AND LYS-663, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397; SER-508; SER-538;
SER-563; SER-580; SER-582; SER-643 AND SER-698, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397; SER-538; SER-622;
SER-643 AND SER-698, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-188; SER-397; SER-456;
SER-508; SER-538; THR-607; THR-610; SER-643 AND SER-698, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; SER-363 AND
SER-698, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[24]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-683, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[25]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-67 AND LYS-193, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[26]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-415 AND LYS-572, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[27]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-67 AND LYS-604, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[28]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-67 AND LYS-193, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[29]
FUNCTION, UBIQUITINATION, AND SUBUNIT.
PubMed=26399832; DOI=10.1038/nature14978;
Werner A., Iwasaki S., McGourty C.A., Medina-Ruiz S., Teerikorpi N.,
Fedrigo I., Ingolia N.T., Rape M.;
"Cell-fate determination by ubiquitin-dependent regulation of
translation.";
Nature 525:523-527(2015).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[31]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-67; LYS-76; LYS-186;
LYS-193; LYS-342; LYS-347; LYS-390; LYS-396; LYS-401; LYS-407;
LYS-415; LYS-440; LYS-452; LYS-505; LYS-579; LYS-604; LYS-613;
LYS-647; LYS-663 AND LYS-695, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Nucleolar protein that acts as a regulator of RNA
polymerase I by connecting RNA polymerase I with enzymes
responsible for ribosomal processing and modification
(PubMed:10567578, PubMed:26399832). Required for neural crest
specification: following monoubiquitination by the BCR(KBTBD8)
complex, associates with TCOF1 and acts as a platform to connect
RNA polymerase I with enzymes responsible for ribosomal processing
and modification, leading to remodel the translational program of
differentiating cells in favor of neural crest specification
(PubMed:26399832). Involved in nucleologenesis, possibly by
playing a role in the maintenance of the fundamental structure of
the fibrillar center and dense fibrillar component in the
nucleolus (PubMed:9016786). It has intrinsic GTPase and ATPase
activities (PubMed:9016786). {ECO:0000269|PubMed:10567578,
ECO:0000269|PubMed:26399832, ECO:0000269|PubMed:9016786}.
-!- SUBUNIT: Heterodimer; heterodimerizes with TCOF1 following
monoubiquitination (PubMed:26399832). Interacts with RNA
polymerase I 194 kDa subunit (RPA194) and with casein kinase-II
(PubMed:10567578). Interacts with DKC1/NAP57, NOP58 and
fibrillarin (By similarity). {ECO:0000250|UniProtKB:P41777,
ECO:0000269|PubMed:10567578, ECO:0000269|PubMed:26399832}.
-!- INTERACTION:
P49407:ARRB1; NbExp=3; IntAct=EBI-396155, EBI-743313;
P32121:ARRB2; NbExp=3; IntAct=EBI-396155, EBI-714559;
P04591:gag (xeno); NbExp=2; IntAct=EBI-396155, EBI-6179719;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:7657714}. Cytoplasm
{ECO:0000269|PubMed:7657714}. Note=Shuttles between the nucleolus
and the cytoplasm. At telophase it begins to assemble into
granular-like pre-nucleolar bodies which are subsequently
relocated to nucleoli at the early G1-phase.
{ECO:0000269|PubMed:7657714}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=Alpha;
IsoId=Q14978-1; Sequence=Displayed;
Name=Beta;
IsoId=Q14978-2; Sequence=VSP_004338;
Name=3;
IsoId=Q14978-3; Sequence=VSP_035415;
-!- PTM: Undergoes rapid and massive phosphorylation/dephosphorylation
cycles on CK2 and PKC sites. NOLC1 is one of the mostly
phosphorylated proteins in the cell. {ECO:0000269|PubMed:7657714}.
-!- PTM: Ubiquitinated. Monoubiquitination by the BCR(KBTBD8) complex
promotes the formation of a NOLC1-TCOF1 complex that acts as a
platform to connect RNA polymerase I with enzymes responsible for
ribosomal processing and modification, leading to remodel the
translational program of differentiating cells in favor of neural
crest specification (PubMed:26399832).
{ECO:0000269|PubMed:26399832}.
-!- SIMILARITY: Belongs to the NOLC1 family. {ECO:0000305}.
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EMBL; Z34289; CAA84063.1; -; mRNA.
EMBL; AY820769; AAV67777.1; -; mRNA.
EMBL; AL500527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471066; EAW49714.1; -; Genomic_DNA.
EMBL; CH471066; EAW49715.1; -; Genomic_DNA.
EMBL; BC001883; AAH01883.1; -; mRNA.
EMBL; D21262; BAA04803.1; -; mRNA.
CCDS; CCDS65925.1; -. [Q14978-3]
CCDS; CCDS65926.1; -. [Q14978-2]
CCDS; CCDS7530.1; -. [Q14978-1]
PIR; I38073; I38073.
RefSeq; NP_001271317.1; NM_001284388.1. [Q14978-2]
RefSeq; NP_001271318.1; NM_001284389.1. [Q14978-3]
RefSeq; NP_004732.2; NM_004741.4. [Q14978-1]
UniGene; Hs.523238; -.
ProteinModelPortal; Q14978; -.
BioGrid; 114654; 140.
CORUM; Q14978; -.
IntAct; Q14978; 51.
MINT; Q14978; -.
STRING; 9606.ENSP00000359024; -.
iPTMnet; Q14978; -.
PhosphoSitePlus; Q14978; -.
SwissPalm; Q14978; -.
BioMuta; NOLC1; -.
DMDM; 145559503; -.
EPD; Q14978; -.
MaxQB; Q14978; -.
PaxDb; Q14978; -.
PeptideAtlas; Q14978; -.
PRIDE; Q14978; -.
ProteomicsDB; 60269; -.
ProteomicsDB; 60270; -. [Q14978-2]
ProteomicsDB; 60271; -. [Q14978-3]
DNASU; 9221; -.
Ensembl; ENST00000405356; ENSP00000385410; ENSG00000166197. [Q14978-2]
Ensembl; ENST00000488254; ENSP00000475080; ENSG00000166197. [Q14978-3]
Ensembl; ENST00000605788; ENSP00000474710; ENSG00000166197. [Q14978-1]
GeneID; 9221; -.
KEGG; hsa:9221; -.
UCSC; uc001kuo.4; human. [Q14978-1]
CTD; 9221; -.
DisGeNET; 9221; -.
EuPathDB; HostDB:ENSG00000166197.16; -.
GeneCards; NOLC1; -.
H-InvDB; HIX0009150; -.
HGNC; HGNC:15608; NOLC1.
HPA; CAB032654; -.
HPA; HPA037366; -.
HPA; HPA050388; -.
MIM; 602394; gene.
neXtProt; NX_Q14978; -.
OpenTargets; ENSG00000166197; -.
PharmGKB; PA31679; -.
eggNOG; KOG2992; Eukaryota.
eggNOG; ENOG4111U5P; LUCA.
GeneTree; ENSGT00730000111092; -.
HOGENOM; HOG000113823; -.
HOVERGEN; HBG075370; -.
InParanoid; Q14978; -.
OMA; DEPPKNQ; -.
OrthoDB; EOG091G127U; -.
PhylomeDB; Q14978; -.
TreeFam; TF341730; -.
SIGNOR; Q14978; -.
ChiTaRS; NOLC1; human.
GeneWiki; Nucleolar_phosphoprotein_p130; -.
GenomeRNAi; 9221; -.
PRO; PR:Q14978; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000166197; Expressed in 240 organ(s), highest expression level in middle temporal gyrus.
CleanEx; HS_NOLC1; -.
ExpressionAtlas; Q14978; baseline and differential.
Genevisible; Q14978; HS.
GO; GO:0031428; C:box C/D snoRNP complex; IEA:Ensembl.
GO; GO:0031429; C:box H/ACA snoRNP complex; IEA:Ensembl.
GO; GO:0015030; C:Cajal body; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0034512; F:box C/D snoRNA binding; IEA:Ensembl.
GO; GO:0062064; F:box C/D snoRNP complex binding; IEA:Ensembl.
GO; GO:0034513; F:box H/ACA snoRNA binding; IEA:Ensembl.
GO; GO:0062065; F:box H/ACA snoRNP complex binding; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; IEA:Ensembl.
GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:Ensembl.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0008139; F:nuclear localization sequence binding; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0001042; F:RNA polymerase I core binding; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IEA:Ensembl.
GO; GO:0033979; P:box H/ACA snoRNA metabolic process; IEA:Ensembl.
GO; GO:0000278; P:mitotic cell cycle; TAS:ProtInc.
GO; GO:0014032; P:neural crest cell development; IMP:UniProtKB.
GO; GO:0014029; P:neural crest formation; IMP:UniProtKB.
GO; GO:0007000; P:nucleolus organization; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0042306; P:regulation of protein import into nucleus; IEA:Ensembl.
GO; GO:0006417; P:regulation of translation; IMP:UniProtKB.
GO; GO:0006970; P:response to osmotic stress; IEA:Ensembl.
GO; GO:0006364; P:rRNA processing; TAS:ProtInc.
InterPro; IPR006594; LisH.
InterPro; IPR039191; Srp40/Nopp140.
InterPro; IPR007718; Srp40_C.
PANTHER; PTHR23216; PTHR23216; 1.
Pfam; PF05022; SRP40_C; 1.
PROSITE; PS50896; LISH; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; GTP-binding; Isopeptide bond; Methylation;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Ubl conjugation.
CHAIN 1 699 Nucleolar and coiled-body phosphoprotein
1.
/FTId=PRO_0000096942.
DOMAIN 10 42 LisH. {ECO:0000255|PROSITE-
ProRule:PRU00126}.
REPEAT 84 95 Acidic serine cluster 1.
REPEAT 125 136 Acidic serine cluster 2.
REPEAT 167 178 Acidic serine cluster 3.
REPEAT 221 232 Acidic serine cluster 4.
REPEAT 264 275 Acidic serine cluster 5.
REPEAT 325 336 Acidic serine cluster 6.
REPEAT 363 375 Acidic serine cluster 7.
REPEAT 425 436 Acidic serine cluster 8.
REPEAT 470 481 Acidic serine cluster 9.
REPEAT 519 529 Acidic serine cluster 10.
REPEAT 555 566 Acidic serine cluster 11.
REGION 84 566 11 X 12 AA approximate repeats of an
acidic serine cluster.
REGION 204 382 Interaction with RPA194.
MOTIF 68 82 Nuclear localization signal.
{ECO:0000255}.
MOTIF 384 587 Nuclear localization signal.
{ECO:0000255}.
MOTIF 601 617 Nuclear localization signal.
{ECO:0000255}.
MOD_RES 33 33 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 87 87 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 90 90 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 91 91 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 188 188 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 362 362 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 363 363 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 366 366 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 397 397 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 415 415 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 456 456 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 508 508 Phosphoserine.
{ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 538 538 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 563 563 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:20068231}.
MOD_RES 580 580 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 582 582 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 607 607 Phosphothreonine.
{ECO:0000244|PubMed:15144186,
ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:23186163}.
MOD_RES 610 610 Phosphothreonine.
{ECO:0000244|PubMed:15144186,
ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:23186163}.
MOD_RES 622 622 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 643 643 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 663 663 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 683 683 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 686 686 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 698 698 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
CROSSLNK 67 67 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 76 76 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 186 186 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 193 193 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 342 342 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 347 347 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 390 390 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 396 396 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 401 401 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 407 407 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 415 415 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 415 415 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 440 440 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 452 452 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 505 505 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 572 572 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 579 579 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 604 604 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 613 613 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 647 647 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 663 663 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 695 695 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 58 59 LK -> LNR (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.2}.
/FTId=VSP_035415.
VAR_SEQ 241 241 K -> KVWTITSVRAE (in isoform Beta).
{ECO:0000303|PubMed:7584026}.
/FTId=VSP_004338.
VARIANT 412 412 G -> V (in dbSNP:rs11191224).
/FTId=VAR_031677.
VARIANT 456 456 S -> P (in dbSNP:rs1049455).
{ECO:0000269|PubMed:7584026}.
/FTId=VAR_031678.
CONFLICT 3 3 D -> A (in Ref. 6; BAA04803).
{ECO:0000305}.
CONFLICT 133 133 S -> R (in Ref. 1; CAA84063).
{ECO:0000305}.
CONFLICT 291 292 SV -> YA (in Ref. 1; CAA84063).
{ECO:0000305}.
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


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