NPM_HUMAN
ID NPM_HUMAN Reviewed; 294 AA.
AC P06748; A8K3N7; B5BU00; D3DQL6; P08693; Q12826; Q13440; Q13441; Q14115;
AC Q5EU94; Q5EU95; Q5EU96; Q5EU97; Q5EU98; Q5EU99; Q6V962; Q8WTW5; Q96AT6;
AC Q96DC4; Q96EA5; Q9BYG9; Q9UDJ7;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 254.
DE RecName: Full=Nucleophosmin;
DE Short=NPM;
DE AltName: Full=Nucleolar phosphoprotein B23;
DE AltName: Full=Nucleolar protein NO38;
DE AltName: Full=Numatrin;
GN Name=NPM1; Synonyms=NPM;
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 1).
RC TISSUE=Placenta;
RX PubMed=2713355; DOI=10.1021/bi00429a017;
RA Chan W.-Y., Liu Q.R., Borjigin J., Busch H., Rennert O.M., Tease L.A.,
RA Chan P.-K.;
RT "Characterization of the cDNA encoding human nucleophosmin and studies of
RT its role in normal and abnormal growth.";
RL Biochemistry 28:1033-1039(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=B-cell lymphoma;
RX PubMed=2775293; DOI=10.1016/0006-291x(89)92100-1;
RA Li X., McNeilage L.J., Whittingham S.;
RT "The nucleotide sequence of a human cDNA encoding the highly conserved
RT nucleolar phosphoprotein B23.";
RL Biochem. Biophys. Res. Commun. 163:72-78(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Amnion;
RX PubMed=2478125; DOI=10.1016/0006-291x(89)91699-9;
RA Zhang X.T., Thomis D.C., Samuel C.E.;
RT "Isolation and characterization of a molecular cDNA clone of a human mRNA
RT from interferon-treated cells encoding nucleolar protein B23, numatrin.";
RL Biochem. Biophys. Res. Commun. 164:176-184(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=9092633; DOI=10.1093/nar/25.6.1225;
RA Chan P.-K., Chan F.Y., Morris S.W., Xie Z.;
RT "Isolation and characterization of the human nucleophosmin/B23 (NPM) gene:
RT identification of the YY1 binding site at the 5' enhancer region.";
RL Nucleic Acids Res. 25:1225-1232(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Okuwaki M., Nagata K.;
RT "Human homologue of Rat B23.2.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP INVOLVEMENT IN ACUTE MYELOGENOUS LEUKEMIA.
RC TISSUE=Bone marrow;
RX PubMed=15659725; DOI=10.1056/nejmoa041974;
RA Falini B., Mecucci C., Tiacci E., Alcalay M., Rosati R., Pasqualucci L.,
RA La Starza R., Diverio D., Colombo E., Santucci A., Bigerna B., Pacini R.,
RA Pucciarini A., Liso A., Vignetti M., Fazi P., Meani N., Pettirossi V.,
RA Saglio G., Mandelli F., Lo-Coco F., Pelicci P.-G., Martelli M.F.;
RT "Cytoplasmic nucleophosmin in acute myelogenous leukemia with a normal
RT karyotype.";
RL N. Engl. J. Med. 352:254-266(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=16574551; DOI=10.1016/s1470-2045(06)70661-1;
RA Bolli N., Galimberti S., Martelli M.P., Tabarrini A., Roti G., Mecucci C.,
RA Martelli M.F., Petrini M., Falini B.;
RT "Cytoplasmic nucleophosmin in myeloid sarcoma occurring 20 years after
RT diagnosis of acute myeloid leukaemia.";
RL Lancet Oncol. 7:350-352(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RA Lu L., Huang X.Y., Yin L.L., Xu M., Li J.M., Zhou Z.M., Sha J.H.;
RT "Cloning of a new transcript of nucleophosmin in testis.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [12]
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 [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Bone marrow, Brain, Kidney, Lung, Prostate, Testis, and
RC Urinary bladder;
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 [14]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-133, AND CHROMOSOMAL TRANSLOCATION WITH
RP RARA.
RC TISSUE=Bone marrow;
RX PubMed=8562957;
RA Redner R.L., Rush E.A., Faas S., Rudert W.A., Corey S.J.;
RT "The t(5;17) variant of acute promyelocytic leukemia expresses a
RT nucleophosmin-retinoic acid receptor fusion.";
RL Blood 87:882-886(1996).
RN [15]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-117, AND CHROMOSOMAL TRANSLOCATION WITH
RP ALK.
RC TISSUE=T-cell lymphoma;
RX PubMed=8122112; DOI=10.1126/science.8122112;
RA Morris S.W., Kirstein M.N., Valentine M.B., Dittmer K.G., Shapiro D.N.,
RA Saltman D.L., Look A.T.;
RT "Fusion of a kinase gene, ALK, to a nucleolar protein gene, NPM, in non-
RT Hodgkin's lymphoma.";
RL Science 263:1281-1284(1994).
RN [16]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-117, AND CHROMOSOMAL TRANSLOCATION WITH
RP ALK.
RC TISSUE=Lymphoma;
RX PubMed=8633037; DOI=10.1073/pnas.93.9.4181;
RA Fujimoto J., Shiota M., Iwahara T., Seki N., Satoh H., Mori S.,
RA Yamamoto T.;
RT "Characterization of the transforming activity of p80, a
RT hyperphosphorylated protein in a Ki-1 lymphoma cell line with chromosomal
RT translocation t(2;5).";
RL Proc. Natl. Acad. Sci. U.S.A. 93:4181-4186(1996).
RN [17]
RP PROTEIN SEQUENCE OF 1-24; 33-101; 104-141; 240-248 AND 278-291, ACETYLATION
RP AT MET-1, PHOSPHORYLATION AT SER-125, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [18]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 15-294 (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=2602120;
RA Hale T.K., Mansfield B.C.;
RT "Nucleotide sequence of a cDNA clone representing a third allele of human
RT protein B23.";
RL Nucleic Acids Res. 17:10112-10112(1989).
RN [19]
RP PROTEIN SEQUENCE OF 33-54.
RC TISSUE=Colon carcinoma;
RX PubMed=9150948; DOI=10.1002/elps.1150180344;
RA Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.;
RT "A two-dimensional gel database of human colon carcinoma proteins.";
RL Electrophoresis 18:605-613(1997).
RN [20]
RP PROTEIN SEQUENCE OF 34-42; 50-67; 137-151; 218-227; 252-266 AND 277-286
RP (ISOFORM 1), AND INTERACTION WITH HTLV1 REX PROTEIN (MICROBIAL INFECTION).
RX PubMed=8314759; DOI=10.1016/s0021-9258(19)85191-8;
RA Adachi Y., Copeland T.D., Hatanaka M., Oroszlan S.;
RT "Nucleolar targeting signal of Rex protein of human T-cell leukemia virus
RT type I specifically binds to nucleolar shuttle protein B-23.";
RL J. Biol. Chem. 268:13930-13934(1993).
RN [21]
RP PROTEIN SEQUENCE OF 33-42; 213-221; 251-257 AND 268-274, FUNCTION,
RP INTERACTION WITH EIF2AK2, AND PHOSPHORYLATION.
RX PubMed=12882984; DOI=10.1074/jbc.m301392200;
RA Pang Q., Christianson T.A., Koretsky T., Carlson H., David L., Keeble W.,
RA Faulkner G.R., Speckhart A., Bagby G.C.;
RT "Nucleophosmin interacts with and inhibits the catalytic function of
RT eukaryotic initiation factor 2 kinase PKR.";
RL J. Biol. Chem. 278:41709-41717(2003).
RN [22]
RP PROTEIN SEQUENCE OF 115-134.
RX PubMed=3944116; DOI=10.1016/s0021-9258(17)36022-2;
RA Chan P.-K., Aldrich M.B., Cook R.G., Busch H.;
RT "Amino acid sequence of protein B23 phosphorylation site.";
RL J. Biol. Chem. 261:1868-1872(1986).
RN [23]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 213-294 (ISOFORM 1), AND PROTEIN SEQUENCE OF
RP 227-294.
RX PubMed=2429957; DOI=10.1016/s0021-9258(18)67023-1;
RA Chan P.-K., Chan W.-Y., Yung B.Y.M., Cook R.G., Aldrich M.B., Ku D.,
RA Goldknopf I.L., Busch H.;
RT "Amino acid sequence of a specific antigenic peptide of protein B23.";
RL J. Biol. Chem. 261:14335-14341(1986).
RN [24]
RP ADP-RIBOSYLATION.
RX PubMed=7631008; DOI=10.2307/3579152;
RA Ramsamooj P., Notario V., Dritschilo A.;
RT "Modification of nucleolar protein B23 after exposure to ionizing
RT radiation.";
RL Radiat. Res. 143:158-164(1995).
RN [25]
RP CHROMOSOMAL TRANSLOCATION WITH MLF1.
RX PubMed=8570204;
RA Yoneda-Kato N., Look A.T., Kirstein M.N., Valentine M.B., Raimondi S.C.,
RA Cohen K.J., Carroll A.J., Morris S.W.;
RT "The t(3;5)(q25.1;q34) of myelodysplastic syndrome and acute myeloid
RT leukemia produces a novel fusion gene, NPM-MLF1.";
RL Oncogene 12:265-275(1996).
RN [26]
RP PHOSPHORYLATION BY CDK2.
RX PubMed=11051553; DOI=10.1016/s0092-8674(00)00093-3;
RA Okuda M., Horn H.F., Tarapore P., Tokuyama Y., Smulian A.G., Chan P.K.,
RA Knudsen E.S., Hofmann I.A., Snyder J.D., Bove K.E., Fukasawa K.;
RT "Nucleophosmin/B23 is a target of CDK2/cyclin E in centrosome
RT duplication.";
RL Cell 103:127-140(2000).
RN [27]
RP INTERACTION WITH HEPATITIS DELTA VIRUS S-HDAG (MICROBIAL INFECTION).
RX PubMed=11309377; DOI=10.1074/jbc.m010087200;
RA Huang W.H., Yung B.Y., Syu W.J., Lee Y.H.;
RT "The nucleolar phosphoprotein B23 interacts with hepatitis delta antigens
RT and modulates the hepatitis delta virus RNA replication.";
RL J. Biol. Chem. 276:25166-25175(2001).
RN [28]
RP PHOSPHORYLATION AT THR-199; THR-219 AND THR-237, AND MUTAGENESIS OF
RP THR-199; THR-219; THR-234 AND THR-237.
RX PubMed=12058066; DOI=10.1091/mbc.02-03-0036;
RA Okuwaki M., Tsujimoto M., Nagata K.;
RT "The RNA binding activity of a ribosome biogenesis factor,
RT nucleophosmin/B23, is modulated by phosphorylation with a cell cycle-
RT dependent kinase and by association with its subtype.";
RL Mol. Biol. Cell 13:2016-2030(2002).
RN [29]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [30]
RP REVIEW.
RX PubMed=12214246; DOI=10.1038/sj.onc.1205708;
RA Okuda M.;
RT "The role of nucleophosmin in centrosome duplication.";
RL Oncogene 21:6170-6174(2002).
RN [31]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [32]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH NEK2.
RX PubMed=15388344; DOI=10.1016/j.febslet.2004.08.047;
RA Yao J., Fu C., Ding X., Guo Z., Zenreski A., Chen Y., Ahmed K., Liao J.,
RA Dou Z., Yao X.;
RT "Nek2A kinase regulates the localization of numatrin to centrosome in
RT mitosis.";
RL FEBS Lett. 575:112-118(2004).
RN [33]
RP PHOSPHORYLATION AT SER-4 BY PLK1.
RX PubMed=15190079; DOI=10.1074/jbc.m403264200;
RA Zhang H., Shi X., Paddon H., Hampong M., Dai W., Pelech S.;
RT "B23/nucleophosmin serine 4 phosphorylation mediates mitotic functions of
RT polo-like kinase 1.";
RL J. Biol. Chem. 279:35726-35734(2004).
RN [34]
RP INTERACTION WITH RPGR.
RX PubMed=15772089; DOI=10.1093/hmg/ddi129;
RA Shu X., Fry A.M., Tulloch B., Manson F.D., Crabb J.W., Khanna H.,
RA Faragher A.J., Lennon A., He S., Trojan P., Giessl A., Wolfrum U.,
RA Vervoort R., Swaroop A., Wright A.F.;
RT "RPGR ORF15 isoform co-localizes with RPGRIP1 at centrioles and basal
RT bodies and interacts with nucleophosmin.";
RL Hum. Mol. Genet. 14:1183-1197(2005).
RN [35]
RP ACETYLATION AT LYS-212; LYS-229; LYS-230; LYS-250; LYS-257 AND LYS-292, AND
RP FUNCTION AS A CHAPERONE.
RX PubMed=16107701; DOI=10.1128/mcb.25.17.7534-7545.2005;
RA Swaminathan V., Kishore A.H., Febitha K.K., Kundu T.K.;
RT "Human histone chaperone nucleophosmin enhances acetylation-dependent
RT chromatin transcription.";
RL Mol. Cell. Biol. 25:7534-7545(2005).
RN [36]
RP SUMOYLATION AT LYS-230 AND LYS-263.
RX PubMed=15897463; DOI=10.1073/pnas.0502978102;
RA Tago K., Chiocca S., Sherr C.J.;
RT "Sumoylation induced by the Arf tumor suppressor: a p53-independent
RT function.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:7689-7694(2005).
RN [37]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND THR-95, 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 [38]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-150; LYS-154 AND LYS-212, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y.,
RA Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT "Substrate and functional diversity of lysine acetylation revealed by a
RT proteomics survey.";
RL Mol. Cell 23:607-618(2006).
RN [39]
RP FUNCTION, AND INTERACTION WITH ROCK2.
RX PubMed=17015463; DOI=10.1128/mcb.01383-06;
RA Ma Z., Kanai M., Kawamura K., Kaibuchi K., Ye K., Fukasawa K.;
RT "Interaction between ROCK II and nucleophosmin/B23 in the regulation of
RT centrosome duplication.";
RL Mol. Cell. Biol. 26:9016-9034(2006).
RN [40]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; THR-199 AND SER-254, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [41]
RP INTERACTION WITH NSUN2.
RX PubMed=17215513; DOI=10.1091/mbc.e06-11-1021;
RA Sakita-Suto S., Kanda A., Suzuki F., Sato S., Takata T., Tatsuka M.;
RT "Aurora-B regulates RNA methyltransferase NSUN2.";
RL Mol. Biol. Cell 18:1107-1117(2007).
RN [42]
RP INTERACTION WITH SENP3, AND MUTAGENESIS OF LYS-263.
RX PubMed=18259216; DOI=10.1038/embor.2008.3;
RA Haindl M., Harasim T., Eick D., Muller S.;
RT "The nucleolar SUMO-specific protease SENP3 reverses SUMO modification of
RT nucleophosmin and is required for rRNA processing.";
RL EMBO Rep. 9:273-279(2008).
RN [43]
RP INTERACTION WITH SENP3, AND SUBCELLULAR LOCATION.
RX PubMed=19015314; DOI=10.1083/jcb.200807185;
RA Yun C., Wang Y., Mukhopadhyay D., Backlund P., Kolli N., Yergey A.,
RA Wilkinson K.D., Dasso M.;
RT "Nucleolar protein B23/nucleophosmin regulates the vertebrate SUMO pathway
RT through SENP3 and SENP5 proteases.";
RL J. Cell Biol. 183:589-595(2008).
RN [44]
RP REVIEW.
RX PubMed=18024471; DOI=10.1093/jb/mvm222;
RA Okuwaki M.;
RT "The structure and functions of NPM1/Nucleophosmin/B23, a multifunctional
RT nucleolar acidic protein.";
RL J. Biochem. 143:441-448(2008).
RN [45]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-125 AND THR-279, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [46]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-125, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [47]
RP FUNCTION.
RX PubMed=18809582; DOI=10.1128/mcb.01548-07;
RA Maggi L.B. Jr., Kuchenruether M., Dadey D.Y., Schwope R.M., Grisendi S.,
RA Townsend R.R., Pandolfi P.P., Weber J.D.;
RT "Nucleophosmin serves as a rate-limiting nuclear export chaperone for the
RT Mammalian ribosome.";
RL Mol. Cell. Biol. 28:7050-7065(2008).
RN [48]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; THR-75; THR-95; SER-125;
RP SER-139; THR-234; THR-237 AND SER-243, 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 [49]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, 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 [50]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [51]
RP INTERACTION WITH RRP1B.
RX PubMed=19710015; DOI=10.1074/jbc.m109.023457;
RA Crawford N.P., Yang H., Mattaini K.R., Hunter K.W.;
RT "The metastasis efficiency modifier ribosomal RNA processing 1 homolog B
RT (RRP1B) is a chromatin-associated factor.";
RL J. Biol. Chem. 284:28660-28673(2009).
RN [52]
RP SUBCELLULAR LOCATION, UBIQUITINATION, AND DEUBIQUITINATION BY USP36.
RX PubMed=19208757; DOI=10.1242/jcs.044461;
RA Endo A., Matsumoto M., Inada T., Yamamoto A., Nakayama K.I., Kitamura N.,
RA Komada M.;
RT "Nucleolar structure and function are regulated by the deubiquitylating
RT enzyme USP36.";
RL J. Cell Sci. 122:678-686(2009).
RN [53]
RP FUNCTION, INTERACTION WITH APEX1, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19188445; DOI=10.1128/mcb.01337-08;
RA Vascotto C., Fantini D., Romanello M., Cesaratto L., Deganuto M.,
RA Leonardi A., Radicella J.P., Kelley M.R., D'Ambrosio C., Scaloni A.,
RA Quadrifoglio F., Tell G.;
RT "APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in the
RT rRNA quality control process.";
RL Mol. Cell. Biol. 29:1834-1854(2009).
RN [54]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [55]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-125, AND
RP IDENTIFICATION BY 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 [56]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-32; LYS-150; LYS-257; LYS-267 AND
RP LYS-273, ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-257 (ISOFORM 3), 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 [57]
RP INTERACTION WITH CEBPA.
RX PubMed=20075868; DOI=10.1038/emboj.2009.404;
RA Muller C., Bremer A., Schreiber S., Eichwald S., Calkhoven C.F.;
RT "Nucleolar retention of a translational C/EBPalpha isoform stimulates rDNA
RT transcription and cell size.";
RL EMBO J. 29:897-909(2010).
RN [58]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH RPS10.
RX PubMed=20159986; DOI=10.1074/jbc.m110.103911;
RA Ren J., Wang Y., Liang Y., Zhang Y., Bao S., Xu Z.;
RT "Methylation of ribosomal protein S10 by protein-arginine methyltransferase
RT 5 regulates ribosome biogenesis.";
RL J. Biol. Chem. 285:12695-12705(2010).
RN [59]
RP INTERACTION WITH RRP1B.
RX PubMed=20926688; DOI=10.1091/mbc.e10-04-0287;
RA Chamousset D., De Wever V., Moorhead G.B., Chen Y., Boisvert F.M.,
RA Lamond A.I., Trinkle-Mulcahy L.;
RT "RRP1B targets PP1 to mammalian cell nucleoli and is associated with pre-
RT 60S ribosomal subunits.";
RL Mol. Biol. Cell 21:4212-4226(2010).
RN [60]
RP FUNCTION, PHOSPHORYLATION AT SER-4 BY PLK2, AND MUTAGENESIS OF SER-4;
RP THR-95; SER-125 AND THR-199.
RX PubMed=20352051; DOI=10.1371/journal.pone.0009849;
RA Krause A., Hoffmann I.;
RT "Polo-like kinase 2-dependent phosphorylation of NPM/B23 on serine 4
RT triggers centriole duplication.";
RL PLoS ONE 5:E9849-E9849(2010).
RN [61]
RP PHOSPHORYLATION AT THR-199 BY CDK6.
RX PubMed=20333249; DOI=10.1371/journal.ppat.1000818;
RA Sarek G., Jaerviluoma A., Moore H.M., Tojkander S., Vartia S.,
RA Biberfeld P., Laiho M., Ojala P.M.;
RT "Nucleophosmin phosphorylation by v-cyclin-CDK6 controls KSHV latency.";
RL PLoS Pathog. 6:E1000818-E1000818(2010).
RN [62]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-4; SER-10; SER-70; THR-95; SER-125; SER-137; SER-139;
RP THR-199; SER-242; SER-243; SER-260 AND THR-279, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-254 (ISOFORM 3), 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 [63]
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 [64]
RP FUNCTION, AND INTERACTION WITH BRCA2.
RX PubMed=21084279; DOI=10.1158/0008-5472.can-10-0030;
RA Wang H.F., Takenaka K., Nakanishi A., Miki Y.;
RT "BRCA2 and nucleophosmin coregulate centrosome amplification and form a
RT complex with the Rho effector kinase ROCK2.";
RL Cancer Res. 71:68-77(2011).
RN [65]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CENPW.
RX PubMed=22002061; DOI=10.1074/jbc.m111.228411;
RA Chun Y., Park B., Koh W., Lee S., Cheon Y., Kim R., Che L., Lee S.;
RT "New centromeric component CENP-W is an RNA-associated nuclear matrix
RT protein that interacts with nucleophosmin/B23 protein.";
RL J. Biol. Chem. 286:42758-42769(2011).
RN [66]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-4; SER-70; SER-125; SER-227; SER-243 AND SER-254, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [67]
RP FUNCTION, INTERACTION WITH ATF5, AND SUBCELLULAR LOCATION.
RX PubMed=22528486; DOI=10.1074/jbc.m112.363622;
RA Liu X., Liu D., Qian D., Dai J., An Y., Jiang S., Stanley B., Yang J.,
RA Wang B., Liu X., Liu D.X.;
RT "Nucleophosmin (NPM1/B23) interacts with activating transcription factor 5
RT (ATF5) protein and promotes proteasome- and caspase-dependent ATF5
RT degradation in hepatocellular carcinoma cells.";
RL J. Biol. Chem. 287:19599-19609(2012).
RN [68]
RP INTERACTION WITH DDX31.
RX PubMed=23019224; DOI=10.1158/0008-5472.can-12-1645;
RA Fukawa T., Ono M., Matsuo T., Uehara H., Miki T., Nakamura Y.,
RA Kanayama H.O., Katagiri T.;
RT "DDX31 regulates the p53-HDM2 pathway and rRNA gene transcription through
RT its interaction with NPM1 in renal cell carcinomas.";
RL Cancer Res. 72:5867-5877(2012).
RN [69]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [70]
RP INTERACTION WITH NPM3.
RX PubMed=22362753; DOI=10.1093/nar/gks162;
RA Okuwaki M., Sumi A., Hisaoka M., Saotome-Nakamura A., Akashi S.,
RA Nishimura Y., Nagata K.;
RT "Function of homo- and hetero-oligomers of human
RT nucleoplasmin/nucleophosmin family proteins NPM1, NPM2 and NPM3 during
RT sperm chromatin remodeling.";
RL Nucleic Acids Res. 40:4861-4878(2012).
RN [71]
RP INTERACTION WITH ALKBH2.
RX PubMed=23972994; DOI=10.1016/j.celrep.2013.07.027;
RA Li P., Gao S., Wang L., Yu F., Li J., Wang C., Li J., Wong J.;
RT "ABH2 couples regulation of ribosomal DNA transcription with DNA alkylation
RT repair.";
RL Cell Rep. 4:817-829(2013).
RN [72]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-10; SER-43; SER-70;
RP THR-95; SER-125; SER-139; THR-234; THR-237; SER-242; SER-243; SER-254 AND
RP SER-260, AND IDENTIFICATION 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 [73]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-243, 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 [74]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-27; LYS-32; LYS-248 AND LYS-250,
RP AND 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 [75]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-32; LYS-248; LYS-257 AND LYS-267,
RP AND 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 [76]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MYC AND NOP53.
RX PubMed=25956029; DOI=10.1016/j.ajpath.2015.03.016;
RA Kim J.Y., Cho Y.E., Park J.H.;
RT "The nucleolar protein GLTSCR2 is an upstream negative regulator of the
RT oncogenic Nucleophosmin-MYC axis.";
RL Am. J. Pathol. 185:2061-2068(2015).
RN [77]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-32 AND LYS-215, 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 [78]
RP SUBUNIT, SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=25818168; DOI=10.1111/jcmm.12474;
RA Kim J.Y., Cho Y.E., An Y.M., Kim S.H., Lee Y.G., Park J.H., Lee S.;
RT "GLTSCR2 is an upstream negative regulator of nucleophosmin in cervical
RT cancer.";
RL J. Cell. Mol. Med. 19:1245-1252(2015).
RN [79]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-32, AND IDENTIFICATION BY MASS
RP 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 [80]
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 [81]
RP ADP-RIBOSYLATION AT SER-207.
RX PubMed=28190768; DOI=10.1016/j.molcel.2017.01.003;
RA Bonfiglio J.J., Fontana P., Zhang Q., Colby T., Gibbs-Seymour I.,
RA Atanassov I., Bartlett E., Zaja R., Ahel I., Matic I.;
RT "Serine ADP-ribosylation depends on HPF1.";
RL Mol. Cell 0:0-0(2017).
RN [82]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-32; LYS-141; LYS-150; LYS-215;
RP LYS-248; LYS-250; LYS-257; LYS-263; LYS-267 AND LYS-273, AND IDENTIFICATION
RP 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).
RN [83]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 9-124.
RX PubMed=17879352; DOI=10.1002/prot.21504;
RA Lee H.H., Kim H.S., Kang J.Y., Lee B.I., Ha J.Y., Yoon H.J., Lim S.O.,
RA Jung G., Suh S.W.;
RT "Crystal structure of human nucleophosmin-core reveals plasticity of the
RT pentamer-pentamer interface.";
RL Proteins 69:672-678(2007).
RN [84]
RP STRUCTURE BY NMR OF 243-294, AND MUTAGENESIS OF LYS-248; LYS-250; LYS-267;
RP PHE-268; PHE-276; TRP-288 AND TRP-290.
RX PubMed=18511415; DOI=10.1074/jbc.m801706200;
RA Grummitt C.G., Townsley F.M., Johnson C.M., Warren A.J., Bycroft M.;
RT "Structural consequences of nucleophosmin mutations in acute myeloid
RT leukemia.";
RL J. Biol. Chem. 283:23326-23332(2008).
CC -!- FUNCTION: Involved in diverse cellular processes such as ribosome
CC biogenesis, centrosome duplication, protein chaperoning, histone
CC assembly, cell proliferation, and regulation of tumor suppressors
CC p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear
CC export. Associated with nucleolar ribonucleoprotein structures and bind
CC single-stranded nucleic acids. Acts as a chaperonin for the core
CC histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on
CC apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1
CC endonuclease activity on AP single-stranded RNA. May exert a control of
CC APEX1 endonuclease activity within nucleoli devoted to repair AP on
CC rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2,
CC regulates centrosome duplication. Regulates centriole duplication:
CC phosphorylation by PLK2 is able to trigger centriole replication.
CC Negatively regulates the activation of EIF2AK2/PKR and suppresses
CC apoptosis through inhibition of EIF2AK2/PKR autophosphorylation.
CC Antagonizes the inhibitory effect of ATF5 on cell proliferation and
CC relieves ATF5-induced G2/M blockade (PubMed:22528486). In complex with
CC MYC enhances the transcription of MYC target genes (PubMed:25956029).
CC May act as chaperonin or cotransporter in the nucleolar localization of
CC transcription termination factor TTF1 (By similarity).
CC {ECO:0000250|UniProtKB:Q61937, ECO:0000269|PubMed:12882984,
CC ECO:0000269|PubMed:16107701, ECO:0000269|PubMed:17015463,
CC ECO:0000269|PubMed:18809582, ECO:0000269|PubMed:19188445,
CC ECO:0000269|PubMed:20352051, ECO:0000269|PubMed:21084279,
CC ECO:0000269|PubMed:22002061, ECO:0000269|PubMed:22528486,
CC ECO:0000269|PubMed:25956029}.
CC -!- SUBUNIT: Decamer formed by two pentameric rings associated in a head-
CC to-head fashion (By similarity). Disulfide-linked dimers under certain
CC conditions (PubMed:25818168). The SWAP complex consists of NPM1, NCL,
CC PARP1 and SWAP70 (By similarity). Interacts with NSUN2 and SENP3.
CC Interacts with the methylated form of RPS10. Interacts (via N-terminal
CC domain) with APEX1; the interaction is RNA-dependent and decreases in
CC hydrogen peroxide-damaged cells. Interacts with isoform 1 of NEK2.
CC Interacts with ROCK2 and BRCA2. Interacts with RPGR. Interacts with
CC CENPW. Interacts with EIF2AK2/PKR. Interacts with CEBPA (isoform 4)
CC (PubMed:20075868). Interacts with DDX31; this interaction prevents
CC interaction between NPM1 and HDM2 (PubMed:23019224). Interacts with
CC MYC; competitive with NOP53 (PubMed:25956029). Interacts with NOP53;
CC the interaction is direct and competitive with MYC (PubMed:25956029).
CC Interacts with LRRC34 (By similarity). Interacts with RRP1B
CC (PubMed:19710015, PubMed:20926688). Interacts with NPM3
CC (PubMed:22362753). Interacts with ALKBH2 (PubMed:23972994). Interacts
CC with TTF1 (via C-terminal region) (By similarity).
CC {ECO:0000250|UniProtKB:Q61937, ECO:0000269|PubMed:12882984,
CC ECO:0000269|PubMed:15388344, ECO:0000269|PubMed:15772089,
CC ECO:0000269|PubMed:17015463, ECO:0000269|PubMed:17215513,
CC ECO:0000269|PubMed:18259216, ECO:0000269|PubMed:19015314,
CC ECO:0000269|PubMed:19188445, ECO:0000269|PubMed:19710015,
CC ECO:0000269|PubMed:20075868, ECO:0000269|PubMed:20159986,
CC ECO:0000269|PubMed:20926688, ECO:0000269|PubMed:21084279,
CC ECO:0000269|PubMed:22002061, ECO:0000269|PubMed:22362753,
CC ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:23019224,
CC ECO:0000269|PubMed:23972994, ECO:0000269|PubMed:25818168,
CC ECO:0000269|PubMed:25956029}.
CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis delta virus S-
CC HDAg. {ECO:0000269|PubMed:11309377}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HTLV1 Rex protein (via N-
CC terminal nuclear localization signal). {ECO:0000269|PubMed:8314759}.
CC -!- INTERACTION:
CC P06748; O14965: AURKA; NbExp=3; IntAct=EBI-78579, EBI-448680;
CC P06748; Q96GD4: AURKB; NbExp=5; IntAct=EBI-78579, EBI-624291;
CC P06748; Q8N726: CDKN2A; NbExp=2; IntAct=EBI-78579, EBI-625922;
CC P06748; P10176: COX8A; NbExp=3; IntAct=EBI-78579, EBI-3904738;
CC P06748; Q10570: CPSF1; NbExp=2; IntAct=EBI-78579, EBI-347859;
CC P06748; P19525: EIF2AK2; NbExp=3; IntAct=EBI-78579, EBI-640775;
CC P06748; Q13547: HDAC1; NbExp=2; IntAct=EBI-78579, EBI-301834;
CC P06748; Q92769: HDAC2; NbExp=2; IntAct=EBI-78579, EBI-301821;
CC P06748; Q9BXL5: HEMGN; NbExp=7; IntAct=EBI-78579, EBI-3916399;
CC P06748; Q92876: KLK6; NbExp=3; IntAct=EBI-78579, EBI-2432309;
CC P06748; Q71RC2: LARP4; NbExp=2; IntAct=EBI-78579, EBI-2878091;
CC P06748; Q00987: MDM2; NbExp=5; IntAct=EBI-78579, EBI-389668;
CC P06748; Q9BZQ8: NIBAN1; NbExp=7; IntAct=EBI-78579, EBI-6916466;
CC P06748; Q86SE8: NPM2; NbExp=6; IntAct=EBI-78579, EBI-6658150;
CC P06748; Q86SE8-2: NPM2; NbExp=5; IntAct=EBI-78579, EBI-12193061;
CC P06748; Q8IZL8: PELP1; NbExp=3; IntAct=EBI-78579, EBI-716449;
CC P06748; Q96BK5: PINX1; NbExp=11; IntAct=EBI-78579, EBI-721782;
CC P06748; P62753: RPS6; NbExp=3; IntAct=EBI-78579, EBI-356625;
CC P06748; Q9H4L4: SENP3; NbExp=6; IntAct=EBI-78579, EBI-2880236;
CC P06748; O14746: TERT; NbExp=5; IntAct=EBI-78579, EBI-1772203;
CC P06748; P05549: TFAP2A; NbExp=6; IntAct=EBI-78579, EBI-347351;
CC P06748; P04637: TP53; NbExp=6; IntAct=EBI-78579, EBI-366083;
CC P06748; P63104: YWHAZ; NbExp=2; IntAct=EBI-78579, EBI-347088;
CC P06748; Q64364: Cdkn2a; Xeno; NbExp=2; IntAct=EBI-78579, EBI-1202287;
CC P06748; P24938: L2; Xeno; NbExp=4; IntAct=EBI-78579, EBI-7481199;
CC P06748; P68951: L2; Xeno; NbExp=5; IntAct=EBI-78579, EBI-7481182;
CC P06748; P0DOE7: M; Xeno; NbExp=3; IntAct=EBI-78579, EBI-10042882;
CC P06748; Q6UPD4: NP; Xeno; NbExp=4; IntAct=EBI-78579, EBI-25616456;
CC P06748; P03427: PB2; Xeno; NbExp=3; IntAct=EBI-78579, EBI-8430745;
CC P06748; B1Q2W9: pre-C/C; Xeno; NbExp=8; IntAct=EBI-78579, EBI-9081051;
CC P06748; Q98147; Xeno; NbExp=2; IntAct=EBI-78579, EBI-626601;
CC P06748-1; P49450-1: CENPA; NbExp=3; IntAct=EBI-354150, EBI-15826012;
CC P06748-1; P63165: SUMO1; NbExp=3; IntAct=EBI-354150, EBI-80140;
CC P06748-1; P04637: TP53; NbExp=3; IntAct=EBI-354150, EBI-366083;
CC P06748-1; Q14669: TRIP12; NbExp=2; IntAct=EBI-354150, EBI-308443;
CC P06748-2; Q86SE8-2: NPM2; NbExp=4; IntAct=EBI-354154, EBI-12193061;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:19208757,
CC ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:25818168,
CC ECO:0000269|PubMed:25956029}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:25818168}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:14654843}.
CC Note=Generally nucleolar, but is translocated to the nucleoplasm in
CC case of serum starvation or treatment with anticancer drugs. Has been
CC found in the cytoplasm in patients with primary acute myelogenous
CC leukemia (AML), but not with secondary AML. Can shuttle between
CC cytoplasm and nucleus. Co- localizes with the methylated form of RPS10
CC in the granular component (GC) region of the nucleolus. Colocalized
CC with nucleolin and APEX1 in nucleoli. Isoform 1 of NEK2 is required for
CC its localization to the centrosome during mitosis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P06748-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P06748-2; Sequence=VSP_003616;
CC Name=3;
CC IsoId=P06748-3; Sequence=VSP_043599;
CC -!- PTM: Acetylated at C-terminal lysine residues, thereby increasing
CC affinity to histones. {ECO:0000269|PubMed:16107701,
CC ECO:0000269|Ref.17}.
CC -!- PTM: ADP-ribosylated.
CC -!- PTM: Phosphorylated at Ser-4 by PLK1 and PLK2. Phosphorylation at Ser-4
CC by PLK2 in S phase is required for centriole duplication and is
CC sufficient to trigger centriole replication. Phosphorylation at Ser-4
CC by PLK1 takes place during mitosis. Phosphorylated by CDK2 at Ser-125
CC and Thr-199. Phosphorylation at Thr-199 may trigger initiation of
CC centrosome duplication. Phosphorylated by CDK1 at Thr-199, Thr-219,
CC Thr-234 and Thr-237 during cell mitosis. When these four sites are
CC phosphorated, RNA-binding activity seem to be abolished. May be
CC phosphorylated at Ser-70 by NEK2. The Thr-199 phosphorylated form has
CC higher affinity for ROCK2. CDK6 triggers Thr-199 phosphorylation when
CC complexed to Kaposi's sarcoma herpesvirus (KSHV) V-cyclin, leading to
CC viral reactivation by reducing viral LANA levels.
CC {ECO:0000269|PubMed:11051553, ECO:0000269|PubMed:12058066,
CC ECO:0000269|PubMed:12882984, ECO:0000269|PubMed:15190079,
CC ECO:0000269|PubMed:15388344, ECO:0000269|PubMed:20333249,
CC ECO:0000269|PubMed:20352051, ECO:0000269|Ref.17}.
CC -!- PTM: Sumoylated by ARF. {ECO:0000269|PubMed:15897463}.
CC -!- PTM: Ubiquitinated. Ubiquitination leads to proteasomal degradation.
CC Deubiquitinated by USP36 (PubMed:19208757).
CC {ECO:0000269|PubMed:19208757, ECO:0000269|PubMed:25818168}.
CC -!- DISEASE: Note=A chromosomal aberration involving NPM1 is found in a
CC form of non-Hodgkin lymphoma. Translocation t(2;5)(p23;q35) with ALK.
CC The resulting chimeric NPM1-ALK protein homodimerize and the kinase
CC becomes constitutively activated. {ECO:0000269|PubMed:8122112,
CC ECO:0000269|PubMed:8633037}.
CC -!- DISEASE: Note=A chromosomal aberration involving NPM1 is found in a
CC form of acute promyelocytic leukemia. Translocation t(5;17)(q32;q11)
CC with RARA. {ECO:0000269|PubMed:8562957}.
CC -!- DISEASE: Note=A chromosomal aberration involving NPM1 is a cause of
CC myelodysplastic syndrome (MDS). Translocation t(3;5)(q25.1;q34) with
CC MLF1. {ECO:0000269|PubMed:8570204}.
CC -!- DISEASE: Note=Defects in NPM1 are associated with acute myelogenous
CC leukemia (AML). Mutations in exon 12 affecting the C-terminus of the
CC protein are associated with an aberrant cytoplasmic location.
CC {ECO:0000269|PubMed:15659725}.
CC -!- SIMILARITY: Belongs to the nucleoplasmin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/NPM1ID22.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M23613; AAA36380.1; -; mRNA.
DR EMBL; M28699; AAA58386.1; -; mRNA.
DR EMBL; M26697; AAA36385.1; -; mRNA.
DR EMBL; U89321; AAB94739.1; -; Genomic_DNA.
DR EMBL; U89309; AAB94739.1; JOINED; Genomic_DNA.
DR EMBL; U89310; AAB94739.1; JOINED; Genomic_DNA.
DR EMBL; U89311; AAB94739.1; JOINED; Genomic_DNA.
DR EMBL; U89313; AAB94739.1; JOINED; Genomic_DNA.
DR EMBL; U89314; AAB94739.1; JOINED; Genomic_DNA.
DR EMBL; U89317; AAB94739.1; JOINED; Genomic_DNA.
DR EMBL; U89319; AAB94739.1; JOINED; Genomic_DNA.
DR EMBL; AB042278; BAB40600.1; -; mRNA.
DR EMBL; AY740634; AAW67752.1; -; mRNA.
DR EMBL; AY740635; AAW67753.1; -; mRNA.
DR EMBL; AY740636; AAW67754.1; -; mRNA.
DR EMBL; AY740637; AAW67755.1; -; mRNA.
DR EMBL; AY740638; AAW67756.1; -; mRNA.
DR EMBL; AY740639; AAW67757.1; -; mRNA.
DR EMBL; AY740640; AAW67758.1; -; mRNA.
DR EMBL; DQ303464; ABC40399.1; -; mRNA.
DR EMBL; AY347529; AAQ24860.1; -; mRNA.
DR EMBL; BT007011; AAP35657.1; -; mRNA.
DR EMBL; AK290652; BAF83341.1; -; mRNA.
DR EMBL; AB451236; BAG70050.1; -; mRNA.
DR EMBL; AB451361; BAG70175.1; -; mRNA.
DR EMBL; CH471062; EAW61443.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61446.1; -; Genomic_DNA.
DR EMBL; BC002398; AAH02398.1; -; mRNA.
DR EMBL; BC008495; AAH08495.1; -; mRNA.
DR EMBL; BC009623; AAH09623.1; -; mRNA.
DR EMBL; BC012566; AAH12566.1; -; mRNA.
DR EMBL; BC014349; AAH14349.1; -; mRNA.
DR EMBL; BC016716; AAH16716.1; -; mRNA.
DR EMBL; BC016768; AAH16768.1; -; mRNA.
DR EMBL; BC016824; AAH16824.1; -; mRNA.
DR EMBL; BC021668; AAH21668.1; -; mRNA.
DR EMBL; BC021983; AAH21983.1; -; mRNA.
DR EMBL; BC050628; AAH50628.1; -; mRNA.
DR EMBL; BC107754; AAI07755.1; -; mRNA.
DR EMBL; U41742; AAB00112.1; ALT_TERM; mRNA.
DR EMBL; U41743; AAB00113.1; ALT_TERM; mRNA.
DR EMBL; U04946; AAA58698.1; ALT_TERM; mRNA.
DR EMBL; D45915; BAA08343.1; ALT_TERM; mRNA.
DR EMBL; X16934; CAA34809.1; -; mRNA.
DR EMBL; J02590; AAA36473.1; -; mRNA.
DR EMBL; M31004; AAA36474.1; -; mRNA.
DR CCDS; CCDS43399.1; -. [P06748-3]
DR CCDS; CCDS4376.1; -. [P06748-1]
DR CCDS; CCDS4377.1; -. [P06748-2]
DR PIR; A33423; A32915.
DR PIR; I38491; I38491.
DR RefSeq; NP_001032827.1; NM_001037738.2. [P06748-3]
DR RefSeq; NP_002511.1; NM_002520.6. [P06748-1]
DR RefSeq; NP_954654.1; NM_199185.3. [P06748-2]
DR PDB; 2LLH; NMR; -; A=225-294.
DR PDB; 2P1B; X-ray; 2.75 A; A/B/C/D/E/F/G/H/I/J=9-122.
DR PDB; 2VXD; NMR; -; A=243-294.
DR 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.
DR PDBsum; 2LLH; -.
DR PDBsum; 2P1B; -.
DR PDBsum; 2VXD; -.
DR PDBsum; 5EHD; -.
DR AlphaFoldDB; P06748; -.
DR BMRB; P06748; -.
DR SMR; P06748; -.
DR BioGRID; 110929; 912.
DR CORUM; P06748; -.
DR DIP; DIP-30932N; -.
DR IntAct; P06748; 435.
DR MINT; P06748; -.
DR STRING; 9606.ENSP00000296930; -.
DR BindingDB; P06748; -.
DR ChEMBL; CHEMBL5178; -.
DR DrugBank; DB11638; Artenimol.
DR DrugCentral; P06748; -.
DR GlyGen; P06748; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; P06748; -.
DR MetOSite; P06748; -.
DR PhosphoSitePlus; P06748; -.
DR SwissPalm; P06748; -.
DR BioMuta; NPM1; -.
DR DMDM; 114762; -.
DR DOSAC-COBS-2DPAGE; P06748; -.
DR REPRODUCTION-2DPAGE; IPI00549248; -.
DR SWISS-2DPAGE; P06748; -.
DR EPD; P06748; -.
DR jPOST; P06748; -.
DR MassIVE; P06748; -.
DR MaxQB; P06748; -.
DR PaxDb; P06748; -.
DR PeptideAtlas; P06748; -.
DR PRIDE; P06748; -.
DR ProteomicsDB; 51927; -. [P06748-1]
DR ProteomicsDB; 51928; -. [P06748-2]
DR ProteomicsDB; 51929; -. [P06748-3]
DR TopDownProteomics; P06748-1; -. [P06748-1]
DR TopDownProteomics; P06748-2; -. [P06748-2]
DR TopDownProteomics; P06748-3; -. [P06748-3]
DR Antibodypedia; 1828; 1302 antibodies from 48 providers.
DR DNASU; 4869; -.
DR Ensembl; ENST00000296930.10; ENSP00000296930.5; ENSG00000181163.14. [P06748-1]
DR Ensembl; ENST00000351986.10; ENSP00000341168.6; ENSG00000181163.14. [P06748-2]
DR Ensembl; ENST00000393820.2; ENSP00000377408.2; ENSG00000181163.14. [P06748-3]
DR Ensembl; ENST00000517671.5; ENSP00000428755.1; ENSG00000181163.14. [P06748-1]
DR Ensembl; ENST00000678280.1; ENSP00000503235.1; ENSG00000181163.14. [P06748-3]
DR GeneID; 4869; -.
DR KEGG; hsa:4869; -.
DR MANE-Select; ENST00000296930.10; ENSP00000296930.5; NM_002520.7; NP_002511.1.
DR UCSC; uc003mbh.4; human. [P06748-1]
DR CTD; 4869; -.
DR DisGeNET; 4869; -.
DR GeneCards; NPM1; -.
DR HGNC; HGNC:7910; NPM1.
DR HPA; ENSG00000181163; Low tissue specificity.
DR MalaCards; NPM1; -.
DR MIM; 164040; gene.
DR neXtProt; NX_P06748; -.
DR OpenTargets; ENSG00000181163; -.
DR Orphanet; 98834; Acute myeloblastic leukemia with maturation.
DR Orphanet; 98833; Acute myeloblastic leukemia without maturation.
DR Orphanet; 402026; Acute myeloid leukemia with NPM1 somatic mutations.
DR Orphanet; 520; Acute promyelocytic leukemia.
DR Orphanet; 1775; Dyskeratosis congenita.
DR Orphanet; 98842; Lymphomatoid papulosis.
DR Orphanet; 300865; Primary cutaneous anaplastic large cell lymphoma.
DR PharmGKB; PA31712; -.
DR VEuPathDB; HostDB:ENSG00000181163; -.
DR eggNOG; KOG0488; Eukaryota.
DR GeneTree; ENSGT00940000153052; -.
DR HOGENOM; CLU_058838_0_0_1; -.
DR InParanoid; P06748; -.
DR OMA; KEYFWCA; -.
DR PhylomeDB; P06748; -.
DR TreeFam; TF327704; -.
DR PathwayCommons; P06748; -.
DR Reactome; R-HSA-180746; Nuclear import of Rev protein.
DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-HSA-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR Reactome; R-HSA-8869496; TFAP2A acts as a transcriptional repressor during retinoic acid induced cell differentiation.
DR Reactome; R-HSA-9700645; ALK mutants bind TKIs.
DR Reactome; R-HSA-9725370; Signaling by ALK fusions and activated point mutants.
DR Reactome; R-HSA-9725371; Nuclear events stimulated by ALK signaling in cancer.
DR SignaLink; P06748; -.
DR SIGNOR; P06748; -.
DR BioGRID-ORCS; 4869; 528 hits in 1019 CRISPR screens.
DR ChiTaRS; NPM1; human.
DR EvolutionaryTrace; P06748; -.
DR GeneWiki; NPM1; -.
DR GenomeRNAi; 4869; -.
DR Pharos; P06748; Tbio.
DR PRO; PR:P06748; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P06748; protein.
DR Bgee; ENSG00000181163; Expressed in calcaneal tendon and 189 other tissues.
DR ExpressionAtlas; P06748; baseline and differential.
DR Genevisible; P06748; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0001652; C:granular component; IEA:Ensembl.
DR GO; GO:0015934; C:large ribosomal subunit; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0032993; C:protein-DNA complex; IDA:CAFA.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0015935; C:small ribosomal subunit; IEA:Ensembl.
DR GO; GO:0031616; C:spindle pole centrosome; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:CAFA.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:CAFA.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0051059; F:NF-kappaB binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
DR GO; GO:0043023; F:ribosomal large subunit binding; IDA:MGI.
DR GO; GO:0043024; F:ribosomal small subunit binding; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IEA:Ensembl.
DR GO; GO:0030957; F:Tat protein binding; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IDA:UniProtKB.
DR GO; GO:0006884; P:cell volume homeostasis; IEA:Ensembl.
DR GO; GO:0034644; P:cellular response to UV; IDA:CAFA.
DR GO; GO:0090398; P:cellular senescence; IMP:GO_Central.
DR GO; GO:0007098; P:centrosome cycle; IMP:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; TAS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0010826; P:negative regulation of centrosome duplication; IMP:UniProtKB.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IEA:Ensembl.
DR GO; GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IDA:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB.
DR GO; GO:1902751; P:positive regulation of cell cycle G2/M phase transition; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0010825; P:positive regulation of centrosome duplication; IEA:Ensembl.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IEA:Ensembl.
DR GO; GO:1904751; P:positive regulation of protein localization to nucleolus; IEA:Ensembl.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:CAFA.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; IDA:UniProtKB.
DR GO; GO:0008104; P:protein localization; IDA:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0001558; P:regulation of cell growth; IEA:Ensembl.
DR GO; GO:0046599; P:regulation of centriole replication; IMP:UniProtKB.
DR GO; GO:0010824; P:regulation of centrosome duplication; IBA:GO_Central.
DR GO; GO:0043516; P:regulation of DNA damage response, signal transduction by p53 class mediator; IEA:Ensembl.
DR GO; GO:0060735; P:regulation of eIF2 alpha phosphorylation by dsRNA; IDA:UniProtKB.
DR GO; GO:0032071; P:regulation of endodeoxyribonuclease activity; IDA:UniProtKB.
DR GO; GO:0060699; P:regulation of endoribonuclease activity; IDA:UniProtKB.
DR GO; GO:1902629; P:regulation of mRNA stability involved in cellular response to UV; IMP:UniProtKB.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IBA:GO_Central.
DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; IBA:GO_Central.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IBA:GO_Central.
DR GO; GO:0000056; P:ribosomal small subunit export from nucleus; IBA:GO_Central.
DR GO; GO:0042255; P:ribosome assembly; TAS:UniProtKB.
DR GO; GO:0006407; P:rRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR DisProt; DP01474; -.
DR IDEAL; IID00295; -.
DR InterPro; IPR032569; NPM1_C.
DR InterPro; IPR004301; Nucleoplasmin.
DR InterPro; IPR024057; Nucleoplasmin_core_dom.
DR InterPro; IPR036824; Nucleoplasmin_core_dom_sf.
DR PANTHER; PTHR22747; PTHR22747; 1.
DR Pfam; PF16276; NPM1-C; 1.
DR Pfam; PF03066; Nucleoplasmin; 1.
DR SUPFAM; SSF69203; SSF69203; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ADP-ribosylation; Alternative splicing;
KW Chaperone; Chromosomal rearrangement; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Disulfide bond; Host-virus interaction;
KW Isopeptide bond; Nucleus; Phosphoprotein; Proto-oncogene;
KW Reference proteome; RNA-binding; Ubl conjugation.
FT CHAIN 1..294
FT /note="Nucleophosmin"
FT /id="PRO_0000219481"
FT REGION 1..186
FT /note="Required for interaction with SENP3"
FT REGION 1..117
FT /note="Necessary for interaction with APEX1"
FT /evidence="ECO:0000269|PubMed:19188445"
FT REGION 120..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..294
FT /note="Required for nucleolar localization"
FT MOTIF 152..157
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 191..197
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 162..186
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 55
FT /note="Interaction between pentamers"
FT /evidence="ECO:0000250"
FT SITE 80
FT /note="Interaction between pentamers"
FT /evidence="ECO:0000250"
FT SITE 175..176
FT /note="Breakpoint for translocation to form NPM1-MLF1"
FT /evidence="ECO:0000269|PubMed:8570204"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.17, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 4
FT /note="Phosphoserine; by PLK1 and PLK2"
FT /evidence="ECO:0000269|PubMed:15190079,
FT ECO:0000269|PubMed:20352051, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 32
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 67
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q61937"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 75
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 95
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 125
FT /note="Phosphoserine; by CDK2"
FT /evidence="ECO:0000269|Ref.17, ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 150
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:16916647,
FT ECO:0007744|PubMed:19608861"
FT MOD_RES 154
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:16916647"
FT MOD_RES 199
FT /note="Phosphothreonine; by CDK1, CDK2 and CDK6"
FT /evidence="ECO:0000269|PubMed:12058066,
FT ECO:0000269|PubMed:20333249, ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 207
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000269|PubMed:28190768"
FT MOD_RES 212
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:16107701,
FT ECO:0007744|PubMed:16916647"
FT MOD_RES 219
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000305|PubMed:12058066"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 229
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:16107701"
FT MOD_RES 230
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16107701"
FT MOD_RES 234
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 237
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:12058066,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 250
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16107701"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 257
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16107701,
FT ECO:0007744|PubMed:19608861"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 267
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 267
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q61937"
FT MOD_RES 273
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 279
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 292
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:16107701"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT CROSSLNK 32
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 32
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 150
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 215
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 230
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT CROSSLNK 248
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 248
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733"
FT CROSSLNK 250
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 257
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 257
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 263
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000269|PubMed:15897463"
FT CROSSLNK 263
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 267
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 267
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 273
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 195..223
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_003616"
FT VAR_SEQ 258..294
FT /note="GGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKSL -> AH (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.5"
FT /id="VSP_043599"
FT MUTAGEN 4
FT /note="S->A: Abolishes phosphorylation by PLK2 and impairs
FT centriole duplication."
FT /evidence="ECO:0000269|PubMed:20352051"
FT MUTAGEN 4
FT /note="S->D,E: Mimicks phosphorylation state, inducing
FT accumulation of centrioles."
FT /evidence="ECO:0000269|PubMed:20352051"
FT MUTAGEN 95
FT /note="T->A: Does not affect phosphorylation by PLK2."
FT /evidence="ECO:0000269|PubMed:20352051"
FT MUTAGEN 125
FT /note="S->A: Does not affect phosphorylation by PLK2."
FT /evidence="ECO:0000269|PubMed:20352051"
FT MUTAGEN 199
FT /note="T->A: Partial loss of phosphorylation. Does not
FT affect phosphorylation by PLK2."
FT /evidence="ECO:0000269|PubMed:12058066,
FT ECO:0000269|PubMed:20352051"
FT MUTAGEN 219
FT /note="T->A: Partial loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:12058066"
FT MUTAGEN 234
FT /note="T->A: Partial loss of phosphorylation; when
FT associated with A-237."
FT /evidence="ECO:0000269|PubMed:12058066"
FT MUTAGEN 237
FT /note="T->A: Partial loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:12058066"
FT MUTAGEN 248
FT /note="K->A: Partial destabilization of the structure."
FT /evidence="ECO:0000269|PubMed:18511415"
FT MUTAGEN 250
FT /note="K->A: Increase in the stabilization of the
FT structure."
FT /evidence="ECO:0000269|PubMed:18511415"
FT MUTAGEN 263
FT /note="K->A: Increase in the stabilization of the structure
FT and partial delocalization to the nucleoplasm. Complete
FT delocalization to the nucleoplasm; when associated with A-
FT 267."
FT /evidence="ECO:0000269|PubMed:18259216"
FT MUTAGEN 263
FT /note="K->R: No change in the sumoylation level."
FT /evidence="ECO:0000269|PubMed:18259216"
FT MUTAGEN 267
FT /note="K->A: Increase in the stabilization of the structure
FT and complete delocalization to the nucleoplasm. Complete
FT delocalization to the nucleoplasm; when associated with A-
FT 263."
FT /evidence="ECO:0000269|PubMed:18511415"
FT MUTAGEN 268
FT /note="F->A: Complete destabilization of the structure and
FT loss of nucleolus localization; when associated with A-
FT 276."
FT /evidence="ECO:0000269|PubMed:18511415"
FT MUTAGEN 276
FT /note="F->A: Complete destabilization of the structure and
FT loss of nucleolus localization; when associated with A-
FT 268."
FT /evidence="ECO:0000269|PubMed:18511415"
FT MUTAGEN 288
FT /note="W->A: Complete destabilization of the structure;
FT when associated with A-290."
FT /evidence="ECO:0000269|PubMed:18511415"
FT MUTAGEN 290
FT /note="W->A: Partial destabilization of the structure.
FT Complete destabilization of the structure; when associated
FT with A-288."
FT /evidence="ECO:0000269|PubMed:18511415"
FT CONFLICT 80
FT /note="K -> E (in Ref. 13; AAH21983)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="E -> D (in Ref. 22; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="Missing (in Ref. 6; AAW67758)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="D -> G (in Ref. 13; AAH16768)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="D -> N (in Ref. 11; BAG70175/BAG70050)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="D -> P (in Ref. 23; AAA36473/AAA36474)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="S -> L (in Ref. 21; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="P -> S (in Ref. 23; AAA36473)"
FT /evidence="ECO:0000305"
FT CONFLICT 219..221
FT /note="TPR -> SSS (in Ref. 23; AAA36473)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="Q -> R (in Ref. 8; AAQ24860)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="Y -> C (in Ref. 13; AAH16768)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="L -> F (in Ref. 13; AAH12566)"
FT /evidence="ECO:0000305"
FT CONFLICT 288..294
FT /note="WQWRKSL -> CLAVEEVSLRK (in Ref. 6; AAW67752/
FT AAW67755)"
FT /evidence="ECO:0000305"
FT CONFLICT 288..294
FT /note="WQWRKSL -> CMAVEEVSLRK (in Ref. 6; AAW67753 and 7;
FT ABC40399)"
FT /evidence="ECO:0000305"
FT CONFLICT 288..294
FT /note="WQWRKSL -> CVAVEEVSLRK (in Ref. 6; AAW67754)"
FT /evidence="ECO:0000305"
FT CONFLICT 290..294
FT /note="WRKSL -> SLAQVSLRK (in Ref. 6; AAW67756)"
FT /evidence="ECO:0000305"
FT CONFLICT 290..294
FT /note="WRKSL -> SLEKVSLRK (in Ref. 6; AAW67757)"
FT /evidence="ECO:0000305"
FT STRAND 15..24
FT /evidence="ECO:0007829|PDB:5EHD"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:5EHD"
FT STRAND 40..49
FT /evidence="ECO:0007829|PDB:5EHD"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:5EHD"
FT STRAND 71..80
FT /evidence="ECO:0007829|PDB:5EHD"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:5EHD"
FT STRAND 84..94
FT /evidence="ECO:0007829|PDB:5EHD"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:5EHD"
FT STRAND 109..117
FT /evidence="ECO:0007829|PDB:5EHD"
FT HELIX 244..257
FT /evidence="ECO:0007829|PDB:2LLH"
FT HELIX 265..275
FT /evidence="ECO:0007829|PDB:2LLH"
FT HELIX 281..292
FT /evidence="ECO:0007829|PDB:2LLH"
FT MOD_RES P06748-3:254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES P06748-3:257
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
SQ 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
