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Nucleophosmin (NPM) (Nucleolar phosphoprotein B23) (Nucleolar protein NO38) (Numatrin)

 NPM_HUMAN               Reviewed;         294 AA.
P06748; A8K3N7; B5BU00; D3DQL6; P08693; Q12826; Q13440; Q13441;
Q14115; Q5EU94; Q5EU95; Q5EU96; Q5EU97; Q5EU98; Q5EU99; Q6V962;
Q8WTW5; Q96AT6; Q96DC4; Q96EA5; Q9BYG9; Q9UDJ7;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 2.
25-OCT-2017, entry version 219.
RecName: Full=Nucleophosmin;
Short=NPM;
AltName: Full=Nucleolar phosphoprotein B23;
AltName: Full=Nucleolar protein NO38;
AltName: Full=Numatrin;
Name=NPM1; Synonyms=NPM;
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 1).
TISSUE=Placenta;
PubMed=2713355; DOI=10.1021/bi00429a017;
Chan W.-Y., Liu Q.R., Borjigin J., Busch H., Rennert O.M., Tease L.A.,
Chan P.-K.;
"Characterization of the cDNA encoding human nucleophosmin and studies
of its role in normal and abnormal growth.";
Biochemistry 28:1033-1039(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=B-cell lymphoma;
PubMed=2775293; DOI=10.1016/0006-291X(89)92100-1;
Li X., McNeilage L.J., Whittingham S.;
"The nucleotide sequence of a human cDNA encoding the highly conserved
nucleolar phosphoprotein B23.";
Biochem. Biophys. Res. Commun. 163:72-78(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Amnion;
PubMed=2478125; DOI=10.1016/0006-291X(89)91699-9;
Zhang X.T., Thomis D.C., Samuel C.E.;
"Isolation and characterization of a molecular cDNA clone of a human
mRNA from interferon-treated cells encoding nucleolar protein B23,
numatrin.";
Biochem. Biophys. Res. Commun. 164:176-184(1989).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=9092633; DOI=10.1093/nar/25.6.1225;
Chan P.-K., Chan F.Y., Morris S.W., Xie Z.;
"Isolation and characterization of the human nucleophosmin/B23 (NPM)
gene: identification of the YY1 binding site at the 5' enhancer
region.";
Nucleic Acids Res. 25:1225-1232(1997).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Okuwaki M., Nagata K.;
"Human homologue of Rat B23.2.";
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
INVOLVEMENT IN ACUTE MYELOGENOUS LEUKEMIA.
TISSUE=Bone marrow;
PubMed=15659725; DOI=10.1056/NEJMoa041974;
Falini B., Mecucci C., Tiacci E., Alcalay M., Rosati R.,
Pasqualucci L., La Starza R., Diverio D., Colombo E., Santucci A.,
Bigerna B., Pacini R., Pucciarini A., Liso A., Vignetti M., Fazi P.,
Meani N., Pettirossi V., Saglio G., Mandelli F., Lo-Coco F.,
Pelicci P.-G., Martelli M.F.;
"Cytoplasmic nucleophosmin in acute myelogenous leukemia with a normal
karyotype.";
N. Engl. J. Med. 352:254-266(2005).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=16574551; DOI=10.1016/S1470-2045(06)70661-1;
Bolli N., Galimberti S., Martelli M.P., Tabarrini A., Roti G.,
Mecucci C., Martelli M.F., Petrini M., Falini B.;
"Cytoplasmic nucleophosmin in myeloid sarcoma occurring 20 years after
diagnosis of acute myeloid leukaemia.";
Lancet Oncol. 7:350-352(2006).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Testis;
Lu L., Huang X.Y., Yin L.L., Xu M., Li J.M., Zhou Z.M., Sha J.H.;
"Cloning of a new transcript of nucleophosmin in testis.";
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Embryo;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[12]
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.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Bone marrow, Brain, Kidney, Lung, Prostate, Testis, and
Urinary bladder;
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).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-133, AND CHROMOSOMAL TRANSLOCATION
WITH RARA.
TISSUE=Bone marrow;
PubMed=8562957;
Redner R.L., Rush E.A., Faas S., Rudert W.A., Corey S.J.;
"The t(5;17) variant of acute promyelocytic leukemia expresses a
nucleophosmin-retinoic acid receptor fusion.";
Blood 87:882-886(1996).
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-117, AND CHROMOSOMAL TRANSLOCATION
WITH ALK.
TISSUE=T-cell lymphoma;
PubMed=8122112; DOI=10.1126/science.8122112;
Morris S.W., Kirstein M.N., Valentine M.B., Dittmer K.G.,
Shapiro D.N., Saltman D.L., Look A.T.;
"Fusion of a kinase gene, ALK, to a nucleolar protein gene, NPM, in
non-Hodgkin's lymphoma.";
Science 263:1281-1284(1994).
[16]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-117, AND CHROMOSOMAL TRANSLOCATION
WITH ALK.
TISSUE=Lymphoma;
PubMed=8633037; DOI=10.1073/pnas.93.9.4181;
Fujimoto J., Shiota M., Iwahara T., Seki N., Satoh H., Mori S.,
Yamamoto T.;
"Characterization of the transforming activity of p80, a
hyperphosphorylated protein in a Ki-1 lymphoma cell line with
chromosomal translocation t(2;5).";
Proc. Natl. Acad. Sci. U.S.A. 93:4181-4186(1996).
[17]
PROTEIN SEQUENCE OF 1-24; 33-101; 104-141; 240-248 AND 278-291,
ACETYLATION AT MET-1, PHOSPHORYLATION AT SER-125, AND IDENTIFICATION
BY MASS SPECTROMETRY.
TISSUE=Cervix carcinoma;
Bienvenut W.V., Waridel P., Quadroni M.;
Submitted (MAR-2009) to UniProtKB.
[18]
NUCLEOTIDE SEQUENCE [MRNA] OF 15-294 (ISOFORM 1).
TISSUE=Placenta;
PubMed=2602120;
Hale T.K., Mansfield B.C.;
"Nucleotide sequence of a cDNA clone representing a third allele of
human protein B23.";
Nucleic Acids Res. 17:10112-10112(1989).
[19]
PROTEIN SEQUENCE OF 33-54.
TISSUE=Colon carcinoma;
PubMed=9150948; DOI=10.1002/elps.1150180344;
Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.;
"A two-dimensional gel database of human colon carcinoma proteins.";
Electrophoresis 18:605-613(1997).
[20]
PROTEIN SEQUENCE OF 34-42; 50-67; 137-151; 218-227; 252-266 AND
277-286 (ISOFORM 1), AND INTERACTION WITH HTLV1 REX PROTEIN.
PubMed=8314759;
Adachi Y., Copeland T.D., Hatanaka M., Oroszlan S.;
"Nucleolar targeting signal of Rex protein of human T-cell leukemia
virus type I specifically binds to nucleolar shuttle protein B-23.";
J. Biol. Chem. 268:13930-13934(1993).
[21]
PROTEIN SEQUENCE OF 33-42; 213-221; 251-257 AND 268-274, FUNCTION,
INTERACTION WITH EIF2AK2, AND PHOSPHORYLATION.
PubMed=12882984; DOI=10.1074/jbc.M301392200;
Pang Q., Christianson T.A., Koretsky T., Carlson H., David L.,
Keeble W., Faulkner G.R., Speckhart A., Bagby G.C.;
"Nucleophosmin interacts with and inhibits the catalytic function of
eukaryotic initiation factor 2 kinase PKR.";
J. Biol. Chem. 278:41709-41717(2003).
[22]
PROTEIN SEQUENCE OF 115-134.
PubMed=3944116;
Chan P.-K., Aldrich M.B., Cook R.G., Busch H.;
"Amino acid sequence of protein B23 phosphorylation site.";
J. Biol. Chem. 261:1868-1872(1986).
[23]
NUCLEOTIDE SEQUENCE [MRNA] OF 213-294 (ISOFORM 1), AND PROTEIN
SEQUENCE OF 227-294.
PubMed=2429957;
Chan P.-K., Chan W.-Y., Yung B.Y.M., Cook R.G., Aldrich M.B., Ku D.,
Goldknopf I.L., Busch H.;
"Amino acid sequence of a specific antigenic peptide of protein B23.";
J. Biol. Chem. 261:14335-14341(1986).
[24]
ADP-RIBOSYLATION.
PubMed=7631008;
Ramsamooj P., Notario V., Dritschilo A.;
"Modification of nucleolar protein B23 after exposure to ionizing
radiation.";
Radiat. Res. 143:158-164(1995).
[25]
CHROMOSOMAL TRANSLOCATION WITH MLF1.
PubMed=8570204;
Yoneda-Kato N., Look A.T., Kirstein M.N., Valentine M.B.,
Raimondi S.C., Cohen K.J., Carroll A.J., Morris S.W.;
"The t(3;5)(q25.1;q34) of myelodysplastic syndrome and acute myeloid
leukemia produces a novel fusion gene, NPM-MLF1.";
Oncogene 12:265-275(1996).
[26]
PHOSPHORYLATION BY CDK2.
PubMed=11051553; DOI=10.1016/S0092-8674(00)00093-3;
Okuda M., Horn H.F., Tarapore P., Tokuyama Y., Smulian A.G.,
Chan P.K., Knudsen E.S., Hofmann I.A., Snyder J.D., Bove K.E.,
Fukasawa K.;
"Nucleophosmin/B23 is a target of CDK2/cyclin E in centrosome
duplication.";
Cell 103:127-140(2000).
[27]
INTERACTION WITH HEPATITIS DELTA VIRUS S-HDAG.
PubMed=11309377; DOI=10.1074/jbc.M010087200;
Huang W.H., Yung B.Y., Syu W.J., Lee Y.H.;
"The nucleolar phosphoprotein B23 interacts with hepatitis delta
antigens and modulates the hepatitis delta virus RNA replication.";
J. Biol. Chem. 276:25166-25175(2001).
[28]
PHOSPHORYLATION AT THR-199; THR-219 AND THR-237, AND MUTAGENESIS OF
THR-199; THR-219; THR-234 AND THR-237.
PubMed=12058066; DOI=10.1091/mbc.02-03-0036;
Okuwaki M., Tsujimoto M., Nagata K.;
"The RNA binding activity of a ribosome biogenesis factor,
nucleophosmin/B23, is modulated by phosphorylation with a cell cycle-
dependent kinase and by association with its subtype.";
Mol. Biol. Cell 13:2016-2030(2002).
[29]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=12429849; DOI=10.1091/mbc.E02-05-0271;
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
Greco A., Hochstrasser D.F., Diaz J.-J.;
"Functional proteomic analysis of human nucleolus.";
Mol. Biol. Cell 13:4100-4109(2002).
[30]
REVIEW.
PubMed=12214246; DOI=10.1038/sj.onc.1205708;
Okuda M.;
"The role of nucleophosmin in centrosome duplication.";
Oncogene 21:6170-6174(2002).
[31]
SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH NEK2.
PubMed=15388344; DOI=10.1016/j.febslet.2004.08.047;
Yao J., Fu C., Ding X., Guo Z., Zenreski A., Chen Y., Ahmed K.,
Liao J., Dou Z., Yao X.;
"Nek2A kinase regulates the localization of numatrin to centrosome in
mitosis.";
FEBS Lett. 575:112-118(2004).
[32]
PHOSPHORYLATION AT SER-4 BY PLK1.
PubMed=15190079; DOI=10.1074/jbc.M403264200;
Zhang H., Shi X., Paddon H., Hampong M., Dai W., Pelech S.;
"B23/nucleophosmin serine 4 phosphorylation mediates mitotic functions
of polo-like kinase 1.";
J. Biol. Chem. 279:35726-35734(2004).
[33]
INTERACTION WITH RPGR.
PubMed=15772089; DOI=10.1093/hmg/ddi129;
Shu X., Fry A.M., Tulloch B., Manson F.D., Crabb J.W., Khanna H.,
Faragher A.J., Lennon A., He S., Trojan P., Giessl A., Wolfrum U.,
Vervoort R., Swaroop A., Wright A.F.;
"RPGR ORF15 isoform co-localizes with RPGRIP1 at centrioles and basal
bodies and interacts with nucleophosmin.";
Hum. Mol. Genet. 14:1183-1197(2005).
[34]
ACETYLATION AT LYS-212; LYS-229; LYS-230; LYS-250; LYS-257 AND
LYS-292, AND FUNCTION AS A CHAPERONE.
PubMed=16107701; DOI=10.1128/MCB.25.17.7534-7545.2005;
Swaminathan V., Kishore A.H., Febitha K.K., Kundu T.K.;
"Human histone chaperone nucleophosmin enhances acetylation-dependent
chromatin transcription.";
Mol. Cell. Biol. 25:7534-7545(2005).
[35]
SUMOYLATION AT LYS-230 AND LYS-263.
PubMed=15897463; DOI=10.1073/pnas.0502978102;
Tago K., Chiocca S., Sherr C.J.;
"Sumoylation induced by the Arf tumor suppressor: a p53-independent
function.";
Proc. Natl. Acad. Sci. U.S.A. 102:7689-7694(2005).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND THR-95, 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).
[37]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-150; LYS-154 AND LYS-212,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
"Substrate and functional diversity of lysine acetylation revealed by
a proteomics survey.";
Mol. Cell 23:607-618(2006).
[38]
FUNCTION, AND INTERACTION WITH ROCK2.
PubMed=17015463; DOI=10.1128/MCB.01383-06;
Ma Z., Kanai M., Kawamura K., Kaibuchi K., Ye K., Fukasawa K.;
"Interaction between ROCK II and nucleophosmin/B23 in the regulation
of centrosome duplication.";
Mol. Cell. Biol. 26:9016-9034(2006).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; THR-199 AND SER-254,
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).
[40]
INTERACTION WITH NSUN2.
PubMed=17215513; DOI=10.1091/mbc.E06-11-1021;
Sakita-Suto S., Kanda A., Suzuki F., Sato S., Takata T., Tatsuka M.;
"Aurora-B regulates RNA methyltransferase NSUN2.";
Mol. Biol. Cell 18:1107-1117(2007).
[41]
INTERACTION WITH SENP3, AND MUTAGENESIS OF LYS-263.
PubMed=18259216; DOI=10.1038/embor.2008.3;
Haindl M., Harasim T., Eick D., Muller S.;
"The nucleolar SUMO-specific protease SENP3 reverses SUMO modification
of nucleophosmin and is required for rRNA processing.";
EMBO Rep. 9:273-279(2008).
[42]
INTERACTION WITH SENP3, AND SUBCELLULAR LOCATION.
PubMed=19015314; DOI=10.1083/jcb.200807185;
Yun C., Wang Y., Mukhopadhyay D., Backlund P., Kolli N., Yergey A.,
Wilkinson K.D., Dasso M.;
"Nucleolar protein B23/nucleophosmin regulates the vertebrate SUMO
pathway through SENP3 and SENP5 proteases.";
J. Cell Biol. 183:589-595(2008).
[43]
REVIEW.
PubMed=18024471; DOI=10.1093/jb/mvm222;
Okuwaki M.;
"The structure and functions of NPM1/Nucleophosmin/B23, a
multifunctional nucleolar acidic protein.";
J. Biochem. 143:441-448(2008).
[44]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-125 AND THR-279,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[45]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-125, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[46]
FUNCTION.
PubMed=18809582; DOI=10.1128/MCB.01548-07;
Maggi L.B. Jr., Kuchenruether M., Dadey D.Y., Schwope R.M.,
Grisendi S., Townsend R.R., Pandolfi P.P., Weber J.D.;
"Nucleophosmin serves as a rate-limiting nuclear export chaperone for
the Mammalian ribosome.";
Mol. Cell. Biol. 28:7050-7065(2008).
[47]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; THR-75; THR-95;
SER-125; SER-139; THR-234; THR-237 AND SER-243, 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).
[48]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, 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).
[49]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND 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).
[50]
FUNCTION, INTERACTION WITH APEX1, IDENTIFICATION BY MASS SPECTROMETRY,
AND SUBCELLULAR LOCATION.
PubMed=19188445; DOI=10.1128/MCB.01337-08;
Vascotto C., Fantini D., Romanello M., Cesaratto L., Deganuto M.,
Leonardi A., Radicella J.P., Kelley M.R., D'Ambrosio C., Scaloni A.,
Quadrifoglio F., Tell G.;
"APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in
the rRNA quality control process.";
Mol. Cell. Biol. 29:1834-1854(2009).
[51]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[52]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-125, 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).
[53]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-32; LYS-150; LYS-257;
LYS-267 AND LYS-273, ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-257
(ISOFORM 3), 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).
[54]
INTERACTION WITH CEBPA.
PubMed=20075868; DOI=10.1038/emboj.2009.404;
Muller C., Bremer A., Schreiber S., Eichwald S., Calkhoven C.F.;
"Nucleolar retention of a translational C/EBPalpha isoform stimulates
rDNA transcription and cell size.";
EMBO J. 29:897-909(2010).
[55]
SUBCELLULAR LOCATION, AND INTERACTION WITH RPS10.
PubMed=20159986; DOI=10.1074/jbc.M110.103911;
Ren J., Wang Y., Liang Y., Zhang Y., Bao S., Xu Z.;
"Methylation of ribosomal protein S10 by protein-arginine
methyltransferase 5 regulates ribosome biogenesis.";
J. Biol. Chem. 285:12695-12705(2010).
[56]
FUNCTION, PHOSPHORYLATION AT SER-4 BY PLK2, AND MUTAGENESIS OF SER-4;
THR-95; SER-125 AND THR-199.
PubMed=20352051; DOI=10.1371/journal.pone.0009849;
Krause A., Hoffmann I.;
"Polo-like kinase 2-dependent phosphorylation of NPM/B23 on serine 4
triggers centriole duplication.";
PLoS ONE 5:E9849-E9849(2010).
[57]
PHOSPHORYLATION AT THR-199 BY CDK6.
PubMed=20333249; DOI=10.1371/journal.ppat.1000818;
Sarek G., Jaerviluoma A., Moore H.M., Tojkander S., Vartia S.,
Biberfeld P., Laiho M., Ojala P.M.;
"Nucleophosmin phosphorylation by v-cyclin-CDK6 controls KSHV
latency.";
PLoS Pathog. 6:E1000818-E1000818(2010).
[58]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-4; SER-10; SER-70; THR-95; SER-125; SER-137;
SER-139; THR-199; SER-242; SER-243; SER-260 AND THR-279,
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254 (ISOFORM 3), 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).
[59]
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).
[60]
FUNCTION, AND INTERACTION WITH BRCA2.
PubMed=21084279; DOI=10.1158/0008-5472.CAN-10-0030;
Wang H.F., Takenaka K., Nakanishi A., Miki Y.;
"BRCA2 and nucleophosmin coregulate centrosome amplification and form
a complex with the Rho effector kinase ROCK2.";
Cancer Res. 71:68-77(2011).
[61]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CENPW.
PubMed=22002061; DOI=10.1074/jbc.M111.228411;
Chun Y., Park B., Koh W., Lee S., Cheon Y., Kim R., Che L., Lee S.;
"New centromeric component CENP-W is an RNA-associated nuclear matrix
protein that interacts with nucleophosmin/B23 protein.";
J. Biol. Chem. 286:42758-42769(2011).
[62]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-4; SER-70; SER-125; SER-227; SER-243 AND
SER-254, 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).
[63]
FUNCTION, INTERACTION WITH ATF5, AND SUBCELLULAR LOCATION.
PubMed=22528486; DOI=10.1074/jbc.M112.363622;
Liu X., Liu D., Qian D., Dai J., An Y., Jiang S., Stanley B., Yang J.,
Wang B., Liu X., Liu D.X.;
"Nucleophosmin (NPM1/B23) interacts with activating transcription
factor 5 (ATF5) protein and promotes proteasome- and caspase-dependent
ATF5 degradation in hepatocellular carcinoma cells.";
J. Biol. Chem. 287:19599-19609(2012).
[64]
INTERACTION WITH DDX31.
PubMed=23019224; DOI=10.1158/0008-5472.CAN-12-1645;
Fukawa T., Ono M., Matsuo T., Uehara H., Miki T., Nakamura Y.,
Kanayama H.O., Katagiri T.;
"DDX31 regulates the p53-HDM2 pathway and rRNA gene transcription
through its interaction with NPM1 in renal cell carcinomas.";
Cancer Res. 72:5867-5877(2012).
[65]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[66]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-10; SER-43;
SER-70; THR-95; SER-125; SER-139; THR-234; THR-237; SER-242; SER-243;
SER-254 AND SER-260, 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).
[67]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-243, 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).
[68]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-27; LYS-32; LYS-248 AND
LYS-250, 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).
[69]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-32; LYS-248; LYS-257 AND
LYS-267, 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).
[70]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MYC AND NOP53.
PubMed=25956029; DOI=10.1016/j.ajpath.2015.03.016;
Kim J.Y., Cho Y.E., Park J.H.;
"The nucleolar protein GLTSCR2 is an upstream negative regulator of
the oncogenic Nucleophosmin-MYC axis.";
Am. J. Pathol. 185:2061-2068(2015).
[71]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-32 AND LYS-215, 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).
[72]
SUBUNIT, SUBCELLULAR LOCATION, AND UBIQUITINATION.
PubMed=25818168; DOI=10.1111/jcmm.12474;
Kim J.Y., Cho Y.E., An Y.M., Kim S.H., Lee Y.G., Park J.H., Lee S.;
"GLTSCR2 is an upstream negative regulator of nucleophosmin in
cervical cancer.";
J. Cell. Mol. Med. 19:1245-1252(2015).
[73]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-32, 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).
[74]
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).
[75]
ADP-RIBOSYLATION AT SER-207.
PubMed=28190768; DOI=10.1016/j.molcel.2017.01.003;
Bonfiglio J.J., Fontana P., Zhang Q., Colby T., Gibbs-Seymour I.,
Atanassov I., Bartlett E., Zaja R., Ahel I., Matic I.;
"Serine ADP-ribosylation depends on HPF1.";
Mol. Cell 0:0-0(2017).
[76]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-32; LYS-141; LYS-150;
LYS-215; LYS-248; LYS-250; LYS-257; LYS-263; LYS-267 AND LYS-273, 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).
[77]
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 9-124.
PubMed=17879352; DOI=10.1002/prot.21504;
Lee H.H., Kim H.S., Kang J.Y., Lee B.I., Ha J.Y., Yoon H.J., Lim S.O.,
Jung G., Suh S.W.;
"Crystal structure of human nucleophosmin-core reveals plasticity of
the pentamer-pentamer interface.";
Proteins 69:672-678(2007).
[78]
STRUCTURE BY NMR OF 243-294, AND MUTAGENESIS OF LYS-248; LYS-250;
PHE-268; PHE-276; TRP-288 AND TRP-290.
PubMed=18511415; DOI=10.1074/jbc.M801706200;
Grummitt C.G., Townsley F.M., Johnson C.M., Warren A.J., Bycroft M.;
"Structural consequences of nucleophosmin mutations in acute myeloid
leukemia.";
J. Biol. Chem. 283:23326-23332(2008).
-!- FUNCTION: Involved in diverse cellular processes such as ribosome
biogenesis, centrosome duplication, protein chaperoning, histone
assembly, cell proliferation, and regulation of tumor suppressors
p53/TP53 and ARF. Binds ribosome presumably to drive ribosome
nuclear export. Associated with nucleolar ribonucleoprotein
structures and bind single-stranded nucleic acids. Acts as a
chaperonin for the core histones H3, H2B and H4. Stimulates APEX1
endonuclease activity on apurinic/apyrimidinic (AP) double-
stranded DNA but inhibits APEX1 endonuclease activity on AP
single-stranded RNA. May exert a control of APEX1 endonuclease
activity within nucleoli devoted to repair AP on rDNA and the
removal of oxidized rRNA molecules. In concert with BRCA2,
regulates centrosome duplication. Regulates centriole duplication:
phosphorylation by PLK2 is able to trigger centriole replication.
Negatively regulates the activation of EIF2AK2/PKR and suppresses
apoptosis through inhibition of EIF2AK2/PKR autophosphorylation.
Antagonizes the inhibitory effect of ATF5 on cell proliferation
and relieves ATF5-induced G2/M blockade (PubMed:22528486). In
complex with MYC enhances the transcription of MYC target genes
(PubMed:25956029). {ECO:0000269|PubMed:12882984,
ECO:0000269|PubMed:16107701, ECO:0000269|PubMed:17015463,
ECO:0000269|PubMed:18809582, ECO:0000269|PubMed:19188445,
ECO:0000269|PubMed:20352051, ECO:0000269|PubMed:21084279,
ECO:0000269|PubMed:22002061, ECO:0000269|PubMed:22528486,
ECO:0000269|PubMed:25956029}.
-!- SUBUNIT: Decamer formed by two pentameric rings associated in a
head-to-head fashion (By similarity). Disulfide-linked dimers
under certain conditions (PubMed:25818168). The SWAP complex
consists of NPM1, NCL, PARP1 and SWAP70 (By similarity). Interacts
with NSUN2 and SENP3. Interacts with hepatitis delta virus S-HDAg.
Interacts with HTLV1 Rex protein (via N-terminal nuclear
localization signal). Interacts with the methylated form of RPS10.
Interacts (via N-terminal domain) with APEX1; the interaction is
RNA-dependent and decreases in hydrogen peroxide-damaged cells.
Interacts with isoform 1 of NEK2. Interacts with ROCK2 and BRCA2.
Interacts with RPGR. Interacts with CENPW. Interacts with
EIF2AK2/PKR. Interacts with CEBPA (isoform 4) (PubMed:20075868).
Interacts with DDX31; this interaction prevents interaction
between NPM1 and HDM2 (PubMed:23019224). Interacts with MYC;
competitive with NOP53 (PubMed:25956029). Interacts with NOP53;
the interaction is direct and competitive with MYC
(PubMed:25956029). Interacts with LRRC34 (By similarity).
{ECO:0000250|UniProtKB:Q61937, ECO:0000269|PubMed:11309377,
ECO:0000269|PubMed:12882984, ECO:0000269|PubMed:15388344,
ECO:0000269|PubMed:15772089, ECO:0000269|PubMed:17015463,
ECO:0000269|PubMed:17215513, ECO:0000269|PubMed:18259216,
ECO:0000269|PubMed:19015314, ECO:0000269|PubMed:19188445,
ECO:0000269|PubMed:20075868, ECO:0000269|PubMed:20159986,
ECO:0000269|PubMed:21084279, ECO:0000269|PubMed:22002061,
ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:23019224,
ECO:0000269|PubMed:25818168, ECO:0000269|PubMed:25956029,
ECO:0000269|PubMed:8314759}.
-!- INTERACTION:
Q98147:- (xeno); NbExp=2; IntAct=EBI-78579, EBI-626601;
O14965:AURKA; NbExp=3; IntAct=EBI-78579, EBI-448680;
Q96GD4:AURKB; NbExp=5; IntAct=EBI-78579, EBI-624291;
Q8N726:CDKN2A; NbExp=2; IntAct=EBI-78579, EBI-625922;
P49450-1:CENPA; NbExp=3; IntAct=EBI-354150, EBI-15826012;
P10176:COX8A; NbExp=3; IntAct=EBI-78579, EBI-3904738;
Q10570:CPSF1; NbExp=2; IntAct=EBI-78579, EBI-347859;
P19525:EIF2AK2; NbExp=3; IntAct=EBI-78579, EBI-640775;
Q9BZQ8:FAM129A; NbExp=7; IntAct=EBI-78579, EBI-6916466;
Q13547:HDAC1; NbExp=2; IntAct=EBI-78579, EBI-301834;
Q92769:HDAC2; NbExp=2; IntAct=EBI-78579, EBI-301821;
Q9BXL5:HEMGN; NbExp=7; IntAct=EBI-78579, EBI-3916399;
P24938:L2 (xeno); NbExp=4; IntAct=EBI-78579, EBI-7481199;
P68951:L2 (xeno); NbExp=5; IntAct=EBI-78579, EBI-7481182;
P0DOE7:M (xeno); NbExp=3; IntAct=EBI-78579, EBI-10042882;
Q00987:MDM2; NbExp=5; IntAct=EBI-78579, EBI-389668;
Q86SE8:NPM2; NbExp=5; IntAct=EBI-78579, EBI-6658150;
Q8IZL8:PELP1; NbExp=3; IntAct=EBI-78579, EBI-716449;
B1Q2W9:pre-C/C (xeno); NbExp=8; IntAct=EBI-78579, EBI-9081051;
Q9H4L4:SENP3; NbExp=6; IntAct=EBI-78579, EBI-2880236;
P63165:SUMO1; NbExp=3; IntAct=EBI-354150, EBI-80140;
P05549:TFAP2A; NbExp=6; IntAct=EBI-78579, EBI-347351;
P04637:TP53; NbExp=6; IntAct=EBI-78579, EBI-366083;
Q14669:TRIP12; NbExp=2; IntAct=EBI-354150, EBI-308443;
P63104:YWHAZ; NbExp=2; IntAct=EBI-78579, EBI-347088;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:25818168,
ECO:0000269|PubMed:25956029}. Nucleus, nucleoplasm
{ECO:0000269|PubMed:25818168}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome. Note=Generally
nucleolar, but is translocated to the nucleoplasm in case of serum
starvation or treatment with anticancer drugs. Has been found in
the cytoplasm in patients with primary acute myelogenous leukemia
(AML), but not with secondary AML. Can shuttle between cytoplasm
and nucleus. Co- localizes with the methylated form of RPS10 in
the granular component (GC) region of the nucleolus. Colocalized
with nucleolin and APEX1 in nucleoli. Isoform 1 of NEK2 is
required for its localization to the centrosome during mitosis.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P06748-1; Sequence=Displayed;
Name=2;
IsoId=P06748-2; Sequence=VSP_003616;
Name=3;
IsoId=P06748-3; Sequence=VSP_043599;
Note=Contains a N6-acetyllysine at position 257. Contains a
phosphoserine at position 254. {ECO:0000244|PubMed:19608861,
ECO:0000244|PubMed:20068231};
-!- PTM: Acetylated at C-terminal lysine residues, thereby increasing
affinity to histones. {ECO:0000269|PubMed:16107701,
ECO:0000269|Ref.17}.
-!- PTM: ADP-ribosylated.
-!- PTM: Phosphorylated at Ser-4 by PLK1 and PLK2. Phosphorylation at
Ser-4 by PLK2 in S phase is required for centriole duplication and
is sufficient to trigger centriole replication. Phosphorylation at
Ser-4 by PLK1 takes place during mitosis. Phosphorylated by CDK2
at Ser-125 and Thr-199. Phosphorylation at Thr-199 may trigger
initiation of centrosome duplication. Phosphorylated by CDK1 at
Thr-199, Thr-219, Thr-234 and Thr-237 during cell mitosis. When
these four sites are phosphorated, RNA-binding activity seem to be
abolished. May be phosphorylated at Ser-70 by NEK2. The Thr-199
phosphorylated form has higher affinity for ROCK2. CDK6 triggers
Thr-199 phosphorylation when complexed to Kaposi's sarcoma
herpesvirus (KSHV) V-cyclin, leading to viral reactivation by
reducing viral LANA levels. {ECO:0000269|PubMed:11051553,
ECO:0000269|PubMed:12058066, ECO:0000269|PubMed:12882984,
ECO:0000269|PubMed:15190079, ECO:0000269|PubMed:15388344,
ECO:0000269|PubMed:20333249, ECO:0000269|PubMed:20352051,
ECO:0000269|Ref.17}.
-!- PTM: Sumoylated by ARF. {ECO:0000269|PubMed:15897463}.
-!- PTM: May be ubiquitinated. Ubiquitination leads to proteasomal
degradation. {ECO:0000269|PubMed:25818168}.
-!- DISEASE: Note=A chromosomal aberration involving NPM1 is found in
a form of non-Hodgkin lymphoma. Translocation t(2;5)(p23;q35) with
ALK. The resulting chimeric NPM1-ALK protein homodimerize and the
kinase becomes constitutively activated.
{ECO:0000269|PubMed:8122112, ECO:0000269|PubMed:8633037}.
-!- DISEASE: Note=A chromosomal aberration involving NPM1 is found in
a form of acute promyelocytic leukemia. Translocation
t(5;17)(q32;q11) with RARA. {ECO:0000269|PubMed:8562957}.
-!- DISEASE: Note=A chromosomal aberration involving NPM1 is a cause
of myelodysplastic syndrome (MDS). Translocation t(3;5)(q25.1;q34)
with MLF1. {ECO:0000269|PubMed:8570204}.
-!- DISEASE: Note=Defects in NPM1 are associated with acute
myelogenous leukemia (AML). Mutations in exon 12 affecting the C-
terminus of the protein are associated with an aberrant
cytoplasmic location. {ECO:0000269|PubMed:15659725}.
-!- SIMILARITY: Belongs to the nucleoplasmin family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/NPM1ID22.html";
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EMBL; M23613; AAA36380.1; -; mRNA.
EMBL; M28699; AAA58386.1; -; mRNA.
EMBL; M26697; AAA36385.1; -; mRNA.
EMBL; U89321; AAB94739.1; -; Genomic_DNA.
EMBL; U89309; AAB94739.1; JOINED; Genomic_DNA.
EMBL; U89310; AAB94739.1; JOINED; Genomic_DNA.
EMBL; U89311; AAB94739.1; JOINED; Genomic_DNA.
EMBL; U89313; AAB94739.1; JOINED; Genomic_DNA.
EMBL; U89314; AAB94739.1; JOINED; Genomic_DNA.
EMBL; U89317; AAB94739.1; JOINED; Genomic_DNA.
EMBL; U89319; AAB94739.1; JOINED; Genomic_DNA.
EMBL; AB042278; BAB40600.1; -; mRNA.
EMBL; AY740634; AAW67752.1; -; mRNA.
EMBL; AY740635; AAW67753.1; -; mRNA.
EMBL; AY740636; AAW67754.1; -; mRNA.
EMBL; AY740637; AAW67755.1; -; mRNA.
EMBL; AY740638; AAW67756.1; -; mRNA.
EMBL; AY740639; AAW67757.1; -; mRNA.
EMBL; AY740640; AAW67758.1; -; mRNA.
EMBL; DQ303464; ABC40399.1; -; mRNA.
EMBL; AY347529; AAQ24860.1; -; mRNA.
EMBL; BT007011; AAP35657.1; -; mRNA.
EMBL; AK290652; BAF83341.1; -; mRNA.
EMBL; AB451236; BAG70050.1; -; mRNA.
EMBL; AB451361; BAG70175.1; -; mRNA.
EMBL; CH471062; EAW61443.1; -; Genomic_DNA.
EMBL; CH471062; EAW61446.1; -; Genomic_DNA.
EMBL; BC002398; AAH02398.1; -; mRNA.
EMBL; BC008495; AAH08495.1; -; mRNA.
EMBL; BC009623; AAH09623.1; -; mRNA.
EMBL; BC012566; AAH12566.1; -; mRNA.
EMBL; BC014349; AAH14349.1; -; mRNA.
EMBL; BC016716; AAH16716.1; -; mRNA.
EMBL; BC016768; AAH16768.1; -; mRNA.
EMBL; BC016824; AAH16824.1; -; mRNA.
EMBL; BC021668; AAH21668.1; -; mRNA.
EMBL; BC021983; AAH21983.1; -; mRNA.
EMBL; BC050628; AAH50628.1; -; mRNA.
EMBL; BC107754; AAI07755.1; -; mRNA.
EMBL; U41742; AAB00112.1; ALT_TERM; mRNA.
EMBL; U41743; AAB00113.1; ALT_TERM; mRNA.
EMBL; U04946; AAA58698.1; ALT_TERM; mRNA.
EMBL; D45915; BAA08343.1; ALT_TERM; mRNA.
EMBL; X16934; CAA34809.1; -; mRNA.
EMBL; J02590; AAA36473.1; -; mRNA.
EMBL; M31004; AAA36474.1; -; mRNA.
CCDS; CCDS43399.1; -. [P06748-3]
CCDS; CCDS4376.1; -. [P06748-1]
CCDS; CCDS4377.1; -. [P06748-2]
PIR; A33423; A32915.
PIR; I38491; I38491.
RefSeq; NP_001032827.1; NM_001037738.2. [P06748-3]
RefSeq; NP_002511.1; NM_002520.6. [P06748-1]
RefSeq; NP_954654.1; NM_199185.3. [P06748-2]
UniGene; Hs.557550; -.
PDB; 2LLH; NMR; -; A=225-294.
PDB; 2P1B; X-ray; 2.75 A; A/B/C/D/E/F/G/H/I/J=9-122.
PDB; 2VXD; NMR; -; A=243-294.
PDB; 5EHD; X-ray; 2.55 A; A/B/C/D/E/F/G/H/I/J/a/b/c/d/e/f/g/h/i/j=9-124.
PDBsum; 2LLH; -.
PDBsum; 2P1B; -.
PDBsum; 2VXD; -.
PDBsum; 5EHD; -.
ProteinModelPortal; P06748; -.
SMR; P06748; -.
BioGrid; 110929; 588.
CORUM; P06748; -.
DIP; DIP-30932N; -.
IntAct; P06748; 271.
MINT; MINT-4938330; -.
STRING; 9606.ENSP00000296930; -.
BindingDB; P06748; -.
ChEMBL; CHEMBL5178; -.
iPTMnet; P06748; -.
PhosphoSitePlus; P06748; -.
SwissPalm; P06748; -.
BioMuta; NPM1; -.
DMDM; 114762; -.
DOSAC-COBS-2DPAGE; P06748; -.
REPRODUCTION-2DPAGE; IPI00549248; -.
SWISS-2DPAGE; P06748; -.
EPD; P06748; -.
MaxQB; P06748; -.
PaxDb; P06748; -.
PeptideAtlas; P06748; -.
PRIDE; P06748; -.
TopDownProteomics; P06748-1; -. [P06748-1]
TopDownProteomics; P06748-2; -. [P06748-2]
TopDownProteomics; P06748-3; -. [P06748-3]
DNASU; 4869; -.
Ensembl; ENST00000296930; ENSP00000296930; ENSG00000181163. [P06748-1]
Ensembl; ENST00000351986; ENSP00000341168; ENSG00000181163. [P06748-2]
Ensembl; ENST00000393820; ENSP00000377408; ENSG00000181163. [P06748-3]
Ensembl; ENST00000517671; ENSP00000428755; ENSG00000181163. [P06748-1]
GeneID; 4869; -.
KEGG; hsa:4869; -.
UCSC; uc003mbh.4; human. [P06748-1]
CTD; 4869; -.
DisGeNET; 4869; -.
EuPathDB; HostDB:ENSG00000181163.13; -.
GeneCards; NPM1; -.
HGNC; HGNC:7910; NPM1.
HPA; CAB012983; -.
HPA; HPA011384; -.
MalaCards; NPM1; -.
MIM; 164040; gene.
neXtProt; NX_P06748; -.
OpenTargets; ENSG00000181163; -.
Orphanet; 98834; Acute myeloblastic leukemia with maturation.
Orphanet; 98833; Acute myeloblastic leukemia without maturation.
Orphanet; 402026; Acute myeloid leukemia with NPM1 somatic mutations.
Orphanet; 520; Acute promyelocytic leukemia.
PharmGKB; PA31712; -.
eggNOG; ENOG410IHZM; Eukaryota.
eggNOG; ENOG4111IKX; LUCA.
GeneTree; ENSGT00440000034554; -.
HOGENOM; HOG000013061; -.
HOVERGEN; HBG001860; -.
InParanoid; P06748; -.
KO; K11276; -.
OMA; VEACICS; -.
OrthoDB; EOG091G0NLY; -.
PhylomeDB; P06748; -.
TreeFam; TF327704; -.
Reactome; R-HSA-180746; Nuclear import of Rev protein.
Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
Reactome; R-HSA-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
Reactome; R-HSA-8869496; TFAP2A acts as a transcriptional repressor during retinoic acid induced cell differentiation.
SIGNOR; P06748; -.
ChiTaRS; NPM1; human.
EvolutionaryTrace; P06748; -.
GeneWiki; NPM1; -.
GenomeRNAi; 4869; -.
PMAP-CutDB; P06748; -.
PRO; PR:P06748; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000181163; -.
ExpressionAtlas; P06748; baseline and differential.
Genevisible; P06748; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0001652; C:granular component; IEA:Ensembl.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:MGI.
GO; GO:0015934; C:large ribosomal subunit; IEA:Ensembl.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:CAFA.
GO; GO:0032993; C:protein-DNA complex; IDA:CAFA.
GO; GO:0015935; C:small ribosomal subunit; IEA:Ensembl.
GO; GO:0031616; C:spindle pole centrosome; IDA:UniProtKB.
GO; GO:0033613; F:activating transcription factor binding; IPI:CAFA.
GO; GO:0001047; F:core promoter binding; IDA:CAFA.
GO; GO:0042393; F:histone binding; IDA:UniProtKB.
GO; GO:0051059; F:NF-kappaB binding; IDA:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IMP:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004860; F:protein kinase inhibitor activity; IDA:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
GO; GO:0043023; F:ribosomal large subunit binding; IDA:MGI.
GO; GO:0043024; F:ribosomal small subunit binding; IDA:MGI.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0001105; F:RNA polymerase II transcription coactivator activity; IDA:CAFA.
GO; GO:0019843; F:rRNA binding; IEA:Ensembl.
GO; GO:0030957; F:Tat protein binding; IDA:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0051082; F:unfolded protein binding; IDA:UniProtKB.
GO; GO:0007569; P:cell aging; IMP:UniProtKB.
GO; GO:0016049; P:cell growth; IEA:Ensembl.
GO; GO:0006884; P:cell volume homeostasis; IEA:Ensembl.
GO; GO:0034644; P:cellular response to UV; IDA:CAFA.
GO; GO:0034080; P:CENP-A containing nucleosome assembly; TAS:Reactome.
GO; GO:0007098; P:centrosome cycle; IMP:UniProtKB.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
GO; GO:0006281; P:DNA repair; IDA:UniProtKB.
GO; GO:0006886; P:intracellular protein transport; TAS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0010826; P:negative regulation of centrosome duplication; IMP:UniProtKB.
GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IEA:Ensembl.
GO; GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; IDA:UniProtKB.
GO; GO:0006913; P:nucleocytoplasmic transport; IDA:UniProtKB.
GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB.
GO; GO:1902751; P:positive regulation of cell cycle G2/M phase transition; IDA:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0010825; P:positive regulation of centrosome duplication; IEA:Ensembl.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:0045860; P:positive regulation of protein kinase activity; IEA:Ensembl.
GO; GO:1904751; P:positive regulation of protein localization to nucleolus; IEA:Ensembl.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:CAFA.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0045727; P:positive regulation of translation; IDA:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
GO; GO:0008104; P:protein localization; IDA:UniProtKB.
GO; GO:0051259; P:protein oligomerization; IDA:MGI.
GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
GO; GO:0046599; P:regulation of centriole replication; IMP:UniProtKB.
GO; GO:0043516; P:regulation of DNA damage response, signal transduction by p53 class mediator; IEA:Ensembl.
GO; GO:0060735; P:regulation of eIF2 alpha phosphorylation by dsRNA; IDA:UniProtKB.
GO; GO:0032071; P:regulation of endodeoxyribonuclease activity; IDA:UniProtKB.
GO; GO:0060699; P:regulation of endoribonuclease activity; IDA:UniProtKB.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006950; P:response to stress; IMP:UniProtKB.
GO; GO:0042273; P:ribosomal large subunit biogenesis; IEA:Ensembl.
GO; GO:0000055; P:ribosomal large subunit export from nucleus; IEA:Ensembl.
GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:Ensembl.
GO; GO:0000056; P:ribosomal small subunit export from nucleus; IEA:Ensembl.
GO; GO:0042255; P:ribosome assembly; TAS:UniProtKB.
GO; GO:0006407; P:rRNA export from nucleus; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR032569; NPM1_C.
InterPro; IPR004301; Nucleoplasmin.
InterPro; IPR024057; Nucleoplasmin_core_dom.
InterPro; IPR036824; Nucleoplasmin_core_dom_sf.
PANTHER; PTHR22747; PTHR22747; 1.
Pfam; PF16276; NPM1-C; 1.
Pfam; PF03066; Nucleoplasmin; 1.
SUPFAM; SSF69203; SSF69203; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ADP-ribosylation; Alternative splicing;
Chaperone; Chromosomal rearrangement; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; Disulfide bond;
Host-virus interaction; Isopeptide bond; Nucleus; Phosphoprotein;
Proto-oncogene; Reference proteome; RNA-binding; Ubl conjugation.
CHAIN 1 294 Nucleophosmin.
/FTId=PRO_0000219481.
REGION 1 186 Required for interaction with SENP3.
REGION 1 117 Necessary for interaction with APEX1.
{ECO:0000269|PubMed:19188445}.
REGION 243 294 Required for nucleolar localization.
MOTIF 152 157 Nuclear localization signal.
{ECO:0000255}.
MOTIF 191 197 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 1 9 Met-rich.
COMPBIAS 120 132 Asp/Glu-rich (acidic).
COMPBIAS 161 188 Asp/Glu-rich (highly acidic).
SITE 55 55 Interaction between pentamers.
{ECO:0000250}.
SITE 80 80 Interaction between pentamers.
{ECO:0000250}.
SITE 175 176 Breakpoint for translocation to form
NPM1-MLF1. {ECO:0000269|PubMed:8570204}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895,
ECO:0000269|Ref.17}.
MOD_RES 4 4 Phosphoserine; by PLK1 and PLK2.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15190079,
ECO:0000269|PubMed:20352051}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 32 32 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 43 43 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 67 67 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q61937}.
MOD_RES 70 70 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 75 75 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 95 95 Phosphothreonine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 125 125 Phosphoserine; by CDK2.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|Ref.17}.
MOD_RES 137 137 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 139 139 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 150 150 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:16916647,
ECO:0000244|PubMed:19608861}.
MOD_RES 154 154 N6-acetyllysine.
{ECO:0000244|PubMed:16916647}.
MOD_RES 199 199 Phosphothreonine; by CDK1, CDK2 and CDK6.
{ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:12058066,
ECO:0000269|PubMed:20333249}.
MOD_RES 207 207 ADP-ribosylserine.
{ECO:0000269|PubMed:28190768}.
MOD_RES 212 212 N6-acetyllysine.
{ECO:0000244|PubMed:16916647,
ECO:0000269|PubMed:16107701}.
MOD_RES 219 219 Phosphothreonine; by CDK1.
{ECO:0000305|PubMed:12058066}.
MOD_RES 227 227 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 229 229 N6-acetyllysine.
{ECO:0000269|PubMed:16107701}.
MOD_RES 230 230 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:16107701}.
MOD_RES 234 234 Phosphothreonine; by CDK1.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 237 237 Phosphothreonine; by CDK1.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:12058066}.
MOD_RES 242 242 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 243 243 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 250 250 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:16107701}.
MOD_RES 254 254 Phosphoserine.
{ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 257 257 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861,
ECO:0000269|PubMed:16107701}.
MOD_RES 260 260 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 267 267 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 267 267 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q61937}.
MOD_RES 273 273 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 279 279 Phosphothreonine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:20068231}.
MOD_RES 292 292 N6-acetyllysine.
{ECO:0000269|PubMed:16107701}.
CROSSLNK 27 27 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447}.
CROSSLNK 32 32 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 32 32 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 141 141 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 150 150 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 215 215 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 230 230 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
CROSSLNK 248 248 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 248 248 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 250 250 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 257 257 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 257 257 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:28112733}.
CROSSLNK 263 263 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000269|PubMed:15897463}.
CROSSLNK 263 263 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 267 267 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 267 267 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 273 273 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
VAR_SEQ 195 223 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_003616.
VAR_SEQ 258 294 GGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKSL ->
AH (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.5}.
/FTId=VSP_043599.
MUTAGEN 4 4 S->A: Abolishes phosphorylation by PLK2
and impairs centriole duplication.
{ECO:0000269|PubMed:20352051}.
MUTAGEN 4 4 S->D,E: Mimicks phosphorylation state,
inducing accumulation of centrioles.
{ECO:0000269|PubMed:20352051}.
MUTAGEN 95 95 T->A: Does not affect phosphorylation by
PLK2. {ECO:0000269|PubMed:20352051}.
MUTAGEN 125 125 S->A: Does not affect phosphorylation by
PLK2. {ECO:0000269|PubMed:20352051}.
MUTAGEN 199 199 T->A: Partial loss of phosphorylation.
Does not affect phosphorylation by PLK2.
{ECO:0000269|PubMed:12058066,
ECO:0000269|PubMed:20352051}.
MUTAGEN 219 219 T->A: Partial loss of phosphorylation.
{ECO:0000269|PubMed:12058066}.
MUTAGEN 234 234 T->A: Partial loss of phosphorylation;
when associated with A-237.
{ECO:0000269|PubMed:12058066}.
MUTAGEN 237 237 T->A: Partial loss of phosphorylation.
{ECO:0000269|PubMed:12058066}.
MUTAGEN 248 248 K->A: Partial destabilization of the
structure. {ECO:0000269|PubMed:18511415}.
MUTAGEN 250 250 K->A: Increase in the stabilization of
the structure.
{ECO:0000269|PubMed:18511415}.
MUTAGEN 263 263 K->A: Increase in the stabilization of
the structure and partial delocalization
to the nucleoplasm. Complete
delocalization to the nucleoplasm; when
associated with A-267.
{ECO:0000269|PubMed:18259216}.
MUTAGEN 263 263 K->R: No change in the sumoylation level.
{ECO:0000269|PubMed:18259216}.
MUTAGEN 267 267 K->A: Increase in the stabilization of
the structure and complete delocalization
to the nucleoplasm. Complete
delocalization to the nucleoplasm; when
associated with A-263.
MUTAGEN 268 268 F->A: Complete destabilization of the
structure and loss of nucleolus
localization; when associated with A-276.
{ECO:0000269|PubMed:18511415}.
MUTAGEN 276 276 F->A: Complete destabilization of the
structure and loss of nucleolus
localization; when associated with A-268.
{ECO:0000269|PubMed:18511415}.
MUTAGEN 288 288 W->A: Complete destabilization of the
structure; when associated with A-290.
{ECO:0000269|PubMed:18511415}.
MUTAGEN 290 290 W->A: Partial destabilization of the
structure. Complete destabilization of
the structure; when associated with A-
288. {ECO:0000269|PubMed:18511415}.
CONFLICT 80 80 K -> E (in Ref. 13; AAH21983).
{ECO:0000305}.
CONFLICT 129 129 E -> D (in Ref. 22; AA sequence).
{ECO:0000305}.
CONFLICT 168 168 Missing (in Ref. 6; AAW67758).
{ECO:0000305}.
CONFLICT 178 178 D -> G (in Ref. 13; AAH16768).
{ECO:0000305}.
CONFLICT 183 183 D -> N (in Ref. 11; BAG70175/BAG70050).
{ECO:0000305}.
CONFLICT 213 213 D -> P (in Ref. 23; AAA36473/AAA36474).
{ECO:0000305}.
CONFLICT 214 214 S -> L (in Ref. 21; AA sequence).
{ECO:0000305}.
CONFLICT 216 216 P -> S (in Ref. 23; AAA36473).
{ECO:0000305}.
CONFLICT 219 221 TPR -> SSS (in Ref. 23; AAA36473).
{ECO:0000305}.
CONFLICT 231 231 Q -> R (in Ref. 8; AAQ24860).
{ECO:0000305}.
CONFLICT 271 271 Y -> C (in Ref. 13; AAH16768).
{ECO:0000305}.
CONFLICT 287 287 L -> F (in Ref. 13; AAH12566).
{ECO:0000305}.
CONFLICT 288 294 WQWRKSL -> CLAVEEVSLRK (in Ref. 6;
AAW67752/AAW67755). {ECO:0000305}.
CONFLICT 288 294 WQWRKSL -> CMAVEEVSLRK (in Ref. 6;
AAW67753 and 7; ABC40399). {ECO:0000305}.
CONFLICT 288 294 WQWRKSL -> CVAVEEVSLRK (in Ref. 6;
AAW67754). {ECO:0000305}.
CONFLICT 290 294 WRKSL -> SLAQVSLRK (in Ref. 6; AAW67756).
{ECO:0000305}.
CONFLICT 290 294 WRKSL -> SLEKVSLRK (in Ref. 6; AAW67757).
{ECO:0000305}.
STRAND 15 24 {ECO:0000244|PDB:5EHD}.
STRAND 29 31 {ECO:0000244|PDB:5EHD}.
STRAND 40 49 {ECO:0000244|PDB:5EHD}.
STRAND 58 65 {ECO:0000244|PDB:5EHD}.
STRAND 71 80 {ECO:0000244|PDB:5EHD}.
TURN 81 83 {ECO:0000244|PDB:5EHD}.
STRAND 84 94 {ECO:0000244|PDB:5EHD}.
STRAND 96 104 {ECO:0000244|PDB:5EHD}.
STRAND 109 117 {ECO:0000244|PDB:5EHD}.
HELIX 244 257 {ECO:0000244|PDB:2LLH}.
HELIX 265 275 {ECO:0000244|PDB:2LLH}.
HELIX 281 292 {ECO:0000244|PDB:2LLH}.
SEQUENCE 294 AA; 32575 MW; 620BC7BA2E4A0054 CRC64;
MEDSMDMDMS PLRPQNYLFG CELKADKDYH FKVDNDENEH QLSLRTVSLG AGAKDELHIV
EAEAMNYEGS PIKVTLATLK MSVQPTVSLG GFEITPPVVL RLKCGSGPVH ISGQHLVAVE
EDAESEDEEE EDVKLLSISG KRSAPGGGSK VPQKKVKLAA DEDDDDDDEE DDDEDDDDDD
FDDEEAEEKA PVKKSIRDTP AKNAQKSNQN GKDSKPSSTP RSKGQESFKK QEKTPKTPKG
PSSVEDIKAK MQASIEKGGS LPKVEAKFIN YVKNCFRMTD QEAIQDLWQW RKSL


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