NUCL_HUMAN
ID NUCL_HUMAN Reviewed; 710 AA.
AC P19338; Q53SK1; Q8NB06; Q9UCF0; Q9UDG1;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 234.
DE RecName: Full=Nucleolin;
DE AltName: Full=Protein C23;
GN Name=NCL;
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].
RC TISSUE=Retina;
RX PubMed=2737305; DOI=10.1016/0014-5793(89)80692-1;
RA Srivastava M., Fleming P.J., Pollard H.B., Burns A.L.;
RT "Cloning and sequencing of the human nucleolin cDNA.";
RL FEBS Lett. 250:99-105(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2394707; DOI=10.1016/s0021-9258(18)77205-0;
RA Srivastava M., McBride O.W., Fleming P.J., Pollard H.B., Burns A.L.;
RT "Genomic organization and chromosomal localization of the human nucleolin
RT gene.";
RL J. Biol. Chem. 265:14922-14931(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hair follicle dermal papilla;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP PROTEIN SEQUENCE OF 2-7; 349-362 AND 610-624.
RC TISSUE=Lymphoma;
RX PubMed=7718615; DOI=10.1016/0167-4889(95)00028-q;
RA Krantz S., Salazar R., Brandt R., Kellermann J., Lottspeich F.;
RT "Purification and partial amino acid sequencing of a fructosyllysine-
RT specific binding protein from cell membranes of the monocyte-like cell line
RT U937.";
RL Biochim. Biophys. Acta 1266:109-112(1995).
RN [6]
RP PROTEIN SEQUENCE OF 231-236; 349-362; 399-403; 458-461 AND 649-653.
RX PubMed=7993898; DOI=10.1021/bi00253a007;
RA Jordan P., Heid H., Kinzel V., Kubler D.;
RT "Major cell surface-located protein substrates of an ecto-protein kinase
RT are homologs of known nuclear proteins.";
RL Biochemistry 33:14696-14706(1994).
RN [7]
RP PROTEIN SEQUENCE OF 458-474, AND NUCLEOTIDE-BINDING.
RC TISSUE=Cervix carcinoma;
RX PubMed=8321232; DOI=10.1128/mcb.13.7.4301-4310.1993;
RA Ishikawa F., Matunis M.J., Dreyfuss G., Cech T.R.;
RT "Nuclear proteins that bind the pre-mRNA 3' splice site sequence r(UUAG/G)
RT and the human telomeric DNA sequence d(TTAGGG)n.";
RL Mol. Cell. Biol. 13:4301-4310(1993).
RN [8]
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH HTATSF1; CCNT1; RNA
RP POLYMERASE II; SUPT5H AND CDK9.
RX PubMed=10393184; DOI=10.1093/emboj/18.13.3688;
RA Parada C.A., Roeder R.G.;
RT "A novel RNA polymerase II-containing complex potentiates Tat-enhanced HIV-
RT 1 transcription.";
RL EMBO J. 18:3688-3701(1999).
RN [9]
RP INTERACTION WITH MDK.
RX PubMed=12147681; DOI=10.1074/jbc.m201194200;
RA Said E.A., Krust B., Nisole S., Svab J., Briand J.P., Hovanessian A.G.;
RT "The anti-HIV cytokine midkine binds the cell surface-expressed nucleolin
RT as a low affinity receptor.";
RL J. Biol. Chem. 277:37492-37502(2002).
RN [10]
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY.
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 [12]
RP INTERACTION WITH APTX.
RX PubMed=15044383; DOI=10.1093/hmg/ddh122;
RA Gueven N., Becherel O.J., Kijas A.W., Chen P., Howe O., Rudolph J.H.,
RA Gatti R., Date H., Onodera O., Taucher-Scholz G., Lavin M.F.;
RT "Aprataxin, a novel protein that protects against genotoxic stress.";
RL Hum. Mol. Genet. 13:1081-1093(2004).
RN [13]
RP INTERACTION WITH TERT.
RX PubMed=15371412; DOI=10.1074/jbc.m407643200;
RA Khurts S., Masutomi K., Delgermaa L., Arai K., Oishi N., Mizuno H.,
RA Hayashi N., Hahn W.C., Murakami S.;
RT "Nucleolin interacts with telomerase.";
RL J. Biol. Chem. 279:51508-51515(2004).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145; SER-153 AND SER-563, 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-580, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145; SER-153; SER-184 AND
RP SER-206, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate cancer
RT cells: identification of phosphoproteins in the LNCaP cell line.";
RL Electrophoresis 28:2027-2034(2007).
RN [17]
RP INTERACTION WITH GZF1, AND SUBCELLULAR LOCATION.
RX PubMed=17674968; DOI=10.1016/j.yexcr.2007.07.003;
RA Dambara A., Morinaga T., Fukuda N., Yamakawa Y., Kato T., Enomoto A.,
RA Asai N., Murakumo Y., Matsuo S., Takahashi M.;
RT "Nucleolin modulates the subcellular localization of GDNF-inducible zinc
RT finger protein 1 and its roles in transcription and cell proliferation.";
RL Exp. Cell Res. 313:3755-3766(2007).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-76 AND THR-121, 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 [19]
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 [20]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=17289661; DOI=10.1074/mcp.m600346-mcp200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; THR-69; SER-184; SER-206
RP AND THR-214, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [23]
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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-34 AND THR-301, 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 [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-9; LYS-102; LYS-116; LYS-124;
RP LYS-318; LYS-377; LYS-398; LYS-403; LYS-513; LYS-572; LYS-577 AND LYS-646,
RP AND 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 [26]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ERBB4, AND
RP SUBCELLULAR LOCATION.
RX PubMed=20858735; DOI=10.1158/1541-7786.mcr-10-0042;
RA Gilmore-Hebert M., Ramabhadran R., Stern D.F.;
RT "Interactions of ErbB4 and Kap1 connect the growth factor and DNA damage
RT response pathways.";
RL Mol. Cancer Res. 8:1388-1398(2010).
RN [27]
RP INTERACTION WITH ZFP36.
RX PubMed=20221403; DOI=10.1371/journal.pone.0009588;
RA Kedar V.P., Darby M.K., Williams J.G., Blackshear P.J.;
RT "Phosphorylation of human tristetraprolin in response to its interaction
RT with the Cbl interacting protein CIN85.";
RL PLoS ONE 5:E9588-E9588(2010).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-34; SER-67; THR-69;
RP THR-76; THR-84; THR-92; THR-99; THR-106; THR-113; THR-121; SER-145; SER-563
RP AND SER-619, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [29]
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 [30]
RP SUBUNIT, INTERACTION WITH RIOK1, AND METHYLATION BY PRTM5.
RX PubMed=21081503; DOI=10.1074/jbc.m110.148486;
RA Guderian G., Peter C., Wiesner J., Sickmann A., Schulze-Osthoff K.,
RA Fischer U., Grimmler M.;
RT "RioK1, a new interactor of protein arginine methyltransferase 5 (PRMT5),
RT competes with pICln for binding and modulates PRMT5 complex composition and
RT substrate specificity.";
RL J. Biol. Chem. 286:1976-1986(2011).
RN [31]
RP INTERACTION WITH NVL.
RX PubMed=21474449; DOI=10.1074/jbc.m110.174680;
RA Fujiwara Y., Fujiwara K., Goda N., Iwaya N., Tenno T., Shirakawa M.,
RA Hiroaki H.;
RT "Structure and function of the N-terminal nucleolin binding domain of
RT nuclear valosin-containing protein-like 2 (NVL2) harboring a nucleolar
RT localization signal.";
RL J. Biol. Chem. 286:21732-21741(2011).
RN [32]
RP INTERACTION WITH HNRNPU.
RX PubMed=21242313; DOI=10.1242/jcs.063347;
RA Ma N., Matsunaga S., Morimoto A., Sakashita G., Urano T., Uchiyama S.,
RA Fukui K.;
RT "The nuclear scaffold protein SAF-A is required for kinetochore-microtubule
RT attachment and contributes to the targeting of Aurora-A to mitotic
RT spindles.";
RL J. Cell Sci. 124:394-404(2011).
RN [33]
RP INTERACTION WITH SETX.
RX PubMed=21700224; DOI=10.1016/j.molcel.2011.04.026;
RA Skourti-Stathaki K., Proudfoot N.J., Gromak N.;
RT "Human senataxin resolves RNA/DNA hybrids formed at transcriptional pause
RT sites to promote Xrn2-dependent termination.";
RL Mol. Cell 42:794-805(2011).
RN [34]
RP INTERACTION WITH C1QBP.
RX PubMed=21536856; DOI=10.1074/mcp.m110.006148;
RA Yoshikawa H., Komatsu W., Hayano T., Miura Y., Homma K., Izumikawa K.,
RA Ishikawa H., Miyazawa N., Tachikawa H., Yamauchi Y., Isobe T.,
RA Takahashi N.;
RT "Splicing factor 2-associated protein p32 participates in ribosome
RT biogenesis by regulating the binding of Nop52 and fibrillarin to
RT preribosome particles.";
RL Mol. Cell. Proteomics 10:0-0(2011).
RN [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; THR-69; SER-563; SER-580
RP AND SER-619, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [36]
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 [37]
RP INTERACTION WITH WDR46.
RX PubMed=23848194; DOI=10.1111/gtc.12077;
RA Hirai Y., Louvet E., Oda T., Kumeta M., Watanabe Y., Horigome T.,
RA Takeyasu K.;
RT "Nucleolar scaffold protein, WDR46, determines the granular compartmental
RT localization of nucleolin and DDX21.";
RL Genes Cells 18:780-797(2013).
RN [38]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; THR-76; THR-121; SER-145;
RP SER-153; SER-184; SER-206; SER-356; THR-367; THR-405; SER-458; SER-460;
RP SER-563; SER-580 AND SER-619, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [39]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-42; SER-67; SER-184;
RP SER-580; SER-591 AND SER-619, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [40]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [41]
RP INTERACTION WITH FMR1.
RX PubMed=24658146; DOI=10.1371/journal.pone.0091465;
RA Taha M.S., Nouri K., Milroy L.G., Moll J.M., Herrmann C., Brunsveld L.,
RA Piekorz R.P., Ahmadian M.R.;
RT "Subcellular fractionation and localization studies reveal a direct
RT interaction of the fragile X mental retardation protein (FMRP) with
RT nucleolin.";
RL PLoS ONE 9:E91465-E91465(2014).
RN [42]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-297; LYS-324 AND LYS-589, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [43]
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 [44]
RP INTERACTION WITH HDGF.
RX PubMed=26845719; DOI=10.1515/hsz-2015-0273;
RA Nuesse J., Mirastschijski U., Waespy M., Oetjen J., Brandes N., Rebello O.,
RA Paroni F., Kelm S., Dietz F.;
RT "Two new isoforms of the human hepatoma-derived growth factor interact with
RT components of the cytoskeleton.";
RL Biol. Chem. 397:417-436(2016).
RN [45]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-324; LYS-370; LYS-377; LYS-513;
RP LYS-577; LYS-589 AND LYS-624, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [46]
RP STRUCTURE BY NMR OF 478-566.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RRM_1 domain of NCL protein.";
RL Submitted (JUN-2006) to the PDB data bank.
CC -!- FUNCTION: Nucleolin is the major nucleolar protein of growing
CC eukaryotic cells. It is found associated with intranucleolar chromatin
CC and pre-ribosomal particles. It induces chromatin decondensation by
CC binding to histone H1. It is thought to play a role in pre-rRNA
CC transcription and ribosome assembly. May play a role in the process of
CC transcriptional elongation. Binds RNA oligonucleotides with 5'-UUAGGG-
CC 3' repeats more tightly than the telomeric single-stranded DNA 5'-
CC TTAGGG-3' repeats. {ECO:0000269|PubMed:10393184}.
CC -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs (PubMed:17289661). Component of the SWAP
CC complex that consists of NPM1, NCL/nucleolin, PARP1 and SWAP70 (By
CC similarity). Component of a complex which is at least composed of
CC HTATSF1/Tat-SF1, the P-TEFb complex components CDK9 and CCNT1, RNA
CC polymerase II, SUPT5H, and NCL/nucleolin (PubMed:10393184). Interacts
CC with AICDA (By similarity). Interacts with APTX (PubMed:15044383).
CC Interacts with C1QBP (PubMed:21536856). Interacts with ERBB4
CC (PubMed:20858735). Interacts (via C-terminus) with FMR1 isoform 6 (via
CC N-terminus) (PubMed:24658146). Interacts with GZF1; this interaction is
CC important for nucleolar localization of GZF1 (PubMed:17674968).
CC Interacts with NSUN2 (PubMed:17215513). Interacts with NVL
CC (PubMed:21474449). Interacts (via N-terminus domain) with SETX
CC (PubMed:21700224). Interacts (via RRM1 and C-terminal RRM4/Arg/Gly-rich
CC domains) with TERT; the interaction is important for nucleolar
CC localization of TERT (PubMed:15371412). Interacts with WDR46
CC (PubMed:23848194). Interacts with ZFP36 (PubMed:20221403). Interacts
CC with LRRC34 (By similarity). Interacts with RRP1B (PubMed:19710015).
CC Interacts with HNRNPU; this interaction occurs during mitosis
CC (PubMed:21242313). Interacts with RIOK1; RIOK1 recruits NCL to PRMT5
CC for symmetrically methylation (PubMed:21081503). Interacts with ZBTB7B
CC (By similarity). Interacts with MDK; this interaction promotes NCL
CC clustering and lateral movements of this complex into lipid rafts
CC leading to MDK internalization (PubMed:12147681). Interacts with HDGF
CC (isoform 1) (PubMed:26845719). Interacts with ALKBH2.
CC {ECO:0000250|UniProtKB:P09405, ECO:0000269|PubMed:10393184,
CC ECO:0000269|PubMed:12147681, ECO:0000269|PubMed:15044383,
CC ECO:0000269|PubMed:15371412, ECO:0000269|PubMed:17215513,
CC ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:17674968,
CC ECO:0000269|PubMed:19710015, ECO:0000269|PubMed:20221403,
CC ECO:0000269|PubMed:20858735, ECO:0000269|PubMed:21081503,
CC ECO:0000269|PubMed:21242313, ECO:0000269|PubMed:21474449,
CC ECO:0000269|PubMed:21536856, ECO:0000269|PubMed:21700224,
CC ECO:0000269|PubMed:23848194, ECO:0000269|PubMed:23972994,
CC ECO:0000269|PubMed:24658146, ECO:0000269|PubMed:26845719}.
CC -!- INTERACTION:
CC P19338; Q9Y6D6: ARFGEF1; NbExp=5; IntAct=EBI-346967, EBI-1044254;
CC P19338; P49407: ARRB1; NbExp=3; IntAct=EBI-346967, EBI-743313;
CC P19338; P32121: ARRB2; NbExp=3; IntAct=EBI-346967, EBI-714559;
CC P19338; PRO_0000005794 [P39060]: COL18A1; NbExp=12; IntAct=EBI-346967, EBI-2566375;
CC P19338; Q00987: MDM2; NbExp=8; IntAct=EBI-346967, EBI-389668;
CC P19338; P35579: MYH9; NbExp=3; IntAct=EBI-346967, EBI-350338;
CC P19338; P19338: NCL; NbExp=5; IntAct=EBI-346967, EBI-346967;
CC P19338; Q9UQ80: PA2G4; NbExp=2; IntAct=EBI-346967, EBI-924893;
CC P19338; Q06710: PAX8; NbExp=2; IntAct=EBI-346967, EBI-2683132;
CC P19338; P61586: RHOA; NbExp=3; IntAct=EBI-346967, EBI-446668;
CC P19338; P04637: TP53; NbExp=2; IntAct=EBI-346967, EBI-366083;
CC P19338; P63104: YWHAZ; NbExp=2; IntAct=EBI-346967, EBI-347088;
CC P19338; Q9CR42: Ankrd1; Xeno; NbExp=2; IntAct=EBI-346967, EBI-8308696;
CC P19338; Q8AZK7: EBNA-LP; Xeno; NbExp=2; IntAct=EBI-346967, EBI-1185167;
CC P19338; PRO_0000037577 [P27958]; Xeno; NbExp=4; IntAct=EBI-346967, EBI-6904388;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm. Note=Localized in
CC cytoplasmic mRNP granules containing untranslated mRNAs.
CC -!- PTM: Some glutamate residues are glycylated by TTLL8. This modification
CC occurs exclusively on glutamate residues and results in a glycine chain
CC on the gamma-carboxyl group (By similarity). {ECO:0000250}.
CC -!- PTM: Symmetrically methylated by PRMT5. {ECO:0000269|PubMed:21081503}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC03738.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
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DR EMBL; M60858; AAA59954.1; -; Genomic_DNA.
DR EMBL; AK091742; BAC03738.1; ALT_SEQ; mRNA.
DR EMBL; AC017104; AAY24247.1; -; Genomic_DNA.
DR CCDS; CCDS33397.1; -.
DR PIR; A35804; A35804.
DR PIR; S53728; S53728.
DR RefSeq; NP_005372.2; NM_005381.2.
DR PDB; 2FC8; NMR; -; A=564-652.
DR PDB; 2FC9; NMR; -; A=478-565.
DR PDB; 2KRR; NMR; -; A=300-466.
DR PDBsum; 2FC8; -.
DR PDBsum; 2FC9; -.
DR PDBsum; 2KRR; -.
DR AlphaFoldDB; P19338; -.
DR SMR; P19338; -.
DR BioGRID; 110771; 620.
DR CORUM; P19338; -.
DR DIP; DIP-89N; -.
DR ELM; P19338; -.
DR IntAct; P19338; 183.
DR MINT; P19338; -.
DR STRING; 9606.ENSP00000318195; -.
DR ChEMBL; CHEMBL4295725; -.
DR MoonProt; P19338; -.
DR GlyGen; P19338; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; P19338; -.
DR MetOSite; P19338; -.
DR PhosphoSitePlus; P19338; -.
DR SwissPalm; P19338; -.
DR BioMuta; NCL; -.
DR DMDM; 90110781; -.
DR DOSAC-COBS-2DPAGE; P19338; -.
DR SWISS-2DPAGE; P19338; -.
DR CPTAC; CPTAC-936; -.
DR EPD; P19338; -.
DR jPOST; P19338; -.
DR MassIVE; P19338; -.
DR MaxQB; P19338; -.
DR PaxDb; P19338; -.
DR PeptideAtlas; P19338; -.
DR PRIDE; P19338; -.
DR ProteomicsDB; 53647; -.
DR TopDownProteomics; P19338; -.
DR ABCD; P19338; 5 sequenced antibodies.
DR Antibodypedia; 3779; 871 antibodies from 42 providers.
DR DNASU; 4691; -.
DR Ensembl; ENST00000322723.9; ENSP00000318195.4; ENSG00000115053.17.
DR GeneID; 4691; -.
DR KEGG; hsa:4691; -.
DR MANE-Select; ENST00000322723.9; ENSP00000318195.4; NM_005381.3; NP_005372.2.
DR UCSC; uc002vru.4; human.
DR CTD; 4691; -.
DR DisGeNET; 4691; -.
DR GeneCards; NCL; -.
DR HGNC; HGNC:7667; NCL.
DR HPA; ENSG00000115053; Low tissue specificity.
DR MIM; 164035; gene.
DR neXtProt; NX_P19338; -.
DR OpenTargets; ENSG00000115053; -.
DR PharmGKB; PA31469; -.
DR VEuPathDB; HostDB:ENSG00000115053; -.
DR eggNOG; KOG0123; Eukaryota.
DR GeneTree; ENSGT00940000157437; -.
DR HOGENOM; CLU_026300_1_0_1; -.
DR InParanoid; P19338; -.
DR OrthoDB; 1479417at2759; -.
DR PhylomeDB; P19338; -.
DR TreeFam; TF328499; -.
DR PathwayCommons; P19338; -.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; P19338; -.
DR SIGNOR; P19338; -.
DR BioGRID-ORCS; 4691; 684 hits in 1091 CRISPR screens.
DR ChiTaRS; NCL; human.
DR EvolutionaryTrace; P19338; -.
DR GenomeRNAi; 4691; -.
DR Pharos; P19338; Tbio.
DR PRO; PR:P19338; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P19338; protein.
DR Bgee; ENSG00000115053; Expressed in ventricular zone and 98 other tissues.
DR ExpressionAtlas; P19338; baseline and differential.
DR Genevisible; P19338; HS.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0005694; C:chromosome; IDA:HPA.
DR GO; GO:0001533; C:cornified envelope; IEA:Ensembl.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0044547; F:DNA topoisomerase binding; IPI:CAFA.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:CAFA.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IDA:UniProtKB.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0017148; P:negative regulation of translation; IMP:CAFA.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:1901838; P:positive regulation of transcription of nucleolar large rRNA by RNA polymerase I; IMP:UniProtKB.
DR CDD; cd12403; RRM1_NCL; 1.
DR CDD; cd12405; RRM3_NCL; 1.
DR CDD; cd12406; RRM4_NCL; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR InterPro; IPR034230; Nucleolin_RRM1.
DR InterPro; IPR034234; Nucleolin_RRM3.
DR InterPro; IPR034235; Nucleolin_RRM4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR Pfam; PF00076; RRM_1; 4.
DR SMART; SM00360; RRM; 4.
DR SMART; SM00361; RRM_1; 2.
DR SUPFAM; SSF54928; SSF54928; 3.
DR PROSITE; PS50102; RRM; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW DNA-binding; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7718615"
FT CHAIN 2..710
FT /note="Nucleolin"
FT /id="PRO_0000081691"
FT REPEAT 58..65
FT /note="1"
FT REPEAT 75..82
FT /note="2"
FT REPEAT 83..90
FT /note="3"
FT REPEAT 91..98
FT /note="4"
FT REPEAT 99..104
FT /note="5; truncated"
FT REPEAT 105..112
FT /note="6"
FT REPEAT 120..127
FT /note="7"
FT REPEAT 128..135
FT /note="8"
FT DOMAIN 307..383
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 393..466
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 486..560
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 572..647
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..135
FT /note="8 X 8 AA tandem repeats of X-T-P-X-K-K-X-X"
FT REGION 640..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..43
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..171
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..210
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..272
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 15
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 16
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 67
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 69
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 76
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 84
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 92
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 96
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 99
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 102
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 106
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 109
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 113
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 116
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 121
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 124
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17487921, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17487921, ECO:0007744|PubMed:23186163"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17487921,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17487921,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 214
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 301
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 318
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 348
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 367
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 377
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 398
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 403
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 405
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 427
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 444
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 467
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 477
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 513
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 521
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 572
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 577
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 646
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 656
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 660
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 666
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 670
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 673
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 679
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 681
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 687
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 691
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 694
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 694
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 324
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 324
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 370
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 377
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 513
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 577
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 589
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 589
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 624
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 68
FT /note="P -> L (in dbSNP:rs11542691)"
FT /id="VAR_046353"
FT VARIANT 122
FT /note="P -> L (in dbSNP:rs11542687)"
FT /id="VAR_046354"
FT VARIANT 174
FT /note="A -> V (in dbSNP:rs11542689)"
FT /id="VAR_046355"
FT CONFLICT 549
FT /note="E -> G (in Ref. 3; BAC03738)"
FT /evidence="ECO:0000305"
FT CONFLICT 623..626
FT /note="Missing (in Ref. 2; AAA59954)"
FT /evidence="ECO:0000305"
FT CONFLICT 625..627
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:2KRR"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:2KRR"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:2KRR"
FT HELIX 321..333
FT /evidence="ECO:0007829|PDB:2KRR"
FT STRAND 338..343
FT /evidence="ECO:0007829|PDB:2KRR"
FT STRAND 345..356
FT /evidence="ECO:0007829|PDB:2KRR"
FT HELIX 357..365
FT /evidence="ECO:0007829|PDB:2KRR"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:2KRR"
FT HELIX 388..391
FT /evidence="ECO:0007829|PDB:2KRR"
FT STRAND 394..399
FT /evidence="ECO:0007829|PDB:2KRR"
FT HELIX 406..413
FT /evidence="ECO:0007829|PDB:2KRR"
FT STRAND 416..424
FT /evidence="ECO:0007829|PDB:2KRR"
FT STRAND 427..435
FT /evidence="ECO:0007829|PDB:2KRR"
FT HELIX 439..442
FT /evidence="ECO:0007829|PDB:2KRR"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:2KRR"
FT HELIX 446..449
FT /evidence="ECO:0007829|PDB:2KRR"
FT STRAND 460..463
FT /evidence="ECO:0007829|PDB:2KRR"
FT STRAND 486..492
FT /evidence="ECO:0007829|PDB:2FC9"
FT HELIX 499..505
FT /evidence="ECO:0007829|PDB:2FC9"
FT STRAND 510..513
FT /evidence="ECO:0007829|PDB:2FC9"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:2FC9"
FT STRAND 524..529
FT /evidence="ECO:0007829|PDB:2FC9"
FT HELIX 533..542
FT /evidence="ECO:0007829|PDB:2FC9"
FT STRAND 544..548
FT /evidence="ECO:0007829|PDB:2FC9"
FT STRAND 551..557
FT /evidence="ECO:0007829|PDB:2FC9"
FT STRAND 565..568
FT /evidence="ECO:0007829|PDB:2FC8"
FT STRAND 572..577
FT /evidence="ECO:0007829|PDB:2FC8"
FT HELIX 585..590
FT /evidence="ECO:0007829|PDB:2FC8"
FT STRAND 596..602
FT /evidence="ECO:0007829|PDB:2FC8"
FT STRAND 604..606
FT /evidence="ECO:0007829|PDB:2FC8"
FT STRAND 608..616
FT /evidence="ECO:0007829|PDB:2FC8"
FT HELIX 620..630
FT /evidence="ECO:0007829|PDB:2FC8"
FT STRAND 641..644
FT /evidence="ECO:0007829|PDB:2FC8"
FT STRAND 650..652
FT /evidence="ECO:0007829|PDB:2FC8"
SQ SEQUENCE 710 AA; 76614 MW; C97F6E34E5CA6727 CRC64;
MVKLAKAGKN QGDPKKMAPP PKEVEEDSED EEMSEDEEDD SSGEEVVIPQ KKGKKAAATS
AKKVVVSPTK KVAVATPAKK AAVTPGKKAA ATPAKKTVTP AKAVTTPGKK GATPGKALVA
TPGKKGAAIP AKGAKNGKNA KKEDSDEEED DDSEEDEEDD EDEDEDEDEI EPAAMKAAAA
APASEDEDDE DDEDDEDDDD DEEDDSEEEA METTPAKGKK AAKVVPVKAK NVAEDEDEEE
DDEDEDDDDD EDDEDDDDED DEEEEEEEEE EPVKEAPGKR KKEMAKQKAA PEAKKQKVEG
TEPTTAFNLF VGNLNFNKSA PELKTGISDV FAKNDLAVVD VRIGMTRKFG YVDFESAEDL
EKALELTGLK VFGNEIKLEK PKGKDSKKER DARTLLAKNL PYKVTQDELK EVFEDAAEIR
LVSKDGKSKG IAYIEFKTEA DAEKTFEEKQ GTEIDGRSIS LYYTGEKGQN QDYRGGKNST
WSGESKTLVL SNLSYSATEE TLQEVFEKAT FIKVPQNQNG KSKGYAFIEF ASFEDAKEAL
NSCNKREIEG RAIRLELQGP RGSPNARSQP SKTLFVKGLS EDTTEETLKE SFDGSVRARI
VTDRETGSSK GFGFVDFNSE EDAKAAKEAM EDGEIDGNKV TLDWAKPKGE GGFGGRGGGR
GGFGGRGGGR GGRGGFGGRG RGGFGGRGGF RGGRGGGGDH KPQGKKTKFE
