NUMA1_HUMAN
ID NUMA1_HUMAN Reviewed; 2115 AA.
AC Q14980; H0YH75; Q14981; Q9BTE9;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Nuclear mitotic apparatus protein 1 {ECO:0000312|HGNC:HGNC:8059};
DE AltName: Full=Nuclear matrix protein-22 {ECO:0000303|PubMed:9730450};
DE Short=NMP-22 {ECO:0000303|PubMed:9730450};
DE AltName: Full=Nuclear mitotic apparatus protein {ECO:0000303|PubMed:1541630, ECO:0000303|PubMed:1541636};
DE Short=NuMA protein {ECO:0000303|PubMed:1541630, ECO:0000303|PubMed:1541636};
DE AltName: Full=SP-H antigen {ECO:0000303|PubMed:8408288};
GN Name=NUMA1 {ECO:0000312|HGNC:HGNC:8059};
GN Synonyms=NMP22 {ECO:0000303|PubMed:9730450},
GN NUMA {ECO:0000303|PubMed:1541630};
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), AND SUBCELLULAR LOCATION.
RX PubMed=1541630; DOI=10.1083/jcb.116.6.1303;
RA Yang C.H., Lambie E.J., Snyder M.;
RT "NuMA: an unusually long coiled-coil related protein in the mammalian
RT nucleus.";
RL J. Cell Biol. 116:1303-1317(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND SUBCELLULAR LOCATION.
RX PubMed=1541636; DOI=10.1083/jcb.116.6.1395;
RA Compton D.A., Szilak I., Cleveland D.W.;
RT "Primary structure of NuMA, an intranuclear protein that defines a novel
RT pathway for segregation of proteins at mitosis.";
RL J. Cell Biol. 116:1395-1408(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8408288; DOI=10.1242/jcs.105.2.589;
RA Maekawa T., Kuriyama R.;
RT "Primary structure and microtubule-interacting domain of the SP-H antigen:
RT a mitotic map located at the spindle pole characterized as a homologous
RT protein to NuMA.";
RL J. Cell Sci. 105:589-600(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1576-2115 (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [MRNA] OF 975-1776 (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 610-1763
RP (ISOFORM 4), AND ALTERNATIVE SPLICING.
RX PubMed=8505359; DOI=10.1242/jcs.104.2.249;
RA Tang T.K., Tang C.J., Chen Y.L., Wu C.W.;
RT "Nuclear proteins of the bovine esophageal epithelium. II. The NuMA gene
RT gives rise to multiple mRNAs and gene products reactive with monoclonal
RT antibody W1.";
RL J. Cell Sci. 104:249-260(1993).
RN [8]
RP SUBCELLULAR LOCATION (ISOFORMS 3 AND 4), ALTERNATIVE SPLICING (ISOFORMS 3
RP AND 4), MUTAGENESIS OF ARG-1984 AND LYS-1988, AND NUCLEAR LOCALIZATION
RP SIGNAL.
RX PubMed=7962183; DOI=10.1242/jcs.107.6.1389;
RA Tang T.K., Tang C.J., Chao Y.J., Wu C.W.;
RT "Nuclear mitotic apparatus protein (NuMA): spindle association, nuclear
RT targeting and differential subcellular localization of various NuMA
RT isoforms.";
RL J. Cell Sci. 107:1389-1402(1994).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-2015; THR-2055;
RP SER-2087 AND THR-2106, AND MUTAGENESIS OF THR-2015; THR-2055; SER-2087 AND
RP THR-2106.
RX PubMed=7769006; DOI=10.1242/jcs.108.2.621;
RA Compton D.A., Luo C.;
RT "Mutation of the predicted p34cdc2 phosphorylation sites in NuMA impair the
RT assembly of the mitotic spindle and block mitosis.";
RL J. Cell Sci. 108:621-633(1995).
RN [10]
RP USE IN DIAGNOSTIC TESTS.
RX PubMed=9730450; DOI=10.1016/s0090-4295(98)00219-2;
RA Landman J., Chang Y., Kavaler E., Droller M.J., Liu B.C.;
RT "Sensitivity and specificity of NMP-22, telomerase, and BTA in the
RT detection of human bladder cancer.";
RL Urology 52:398-402(1998).
RN [11]
RP SUBCELLULAR LOCATION, AND ASSOCIATION WITH THE DYNEIN-DYNACTIN COMPLEX.
RX PubMed=10811826; DOI=10.1083/jcb.149.4.851;
RA Merdes A., Heald R., Samejima K., Earnshaw W.C., Cleveland D.W.;
RT "Formation of spindle poles by dynein/dynactin-dependent transport of
RT NuMA.";
RL J. Cell Biol. 149:851-862(2000).
RN [12]
RP FUNCTION, AND INTERACTION WITH THE IMPORTIN ALPHA/IMPORTIN BETA RECEPTOR.
RX PubMed=11163243; DOI=10.1016/s0092-8674(01)00194-5;
RA Nachury M.V., Maresca T.J., Salmon W.C., Waterman-Storer C.M., Heald R.,
RA Weis K.;
RT "Importin beta is a mitotic target of the small GTPase Ran in spindle
RT assembly.";
RL Cell 104:95-106(2001).
RN [13]
RP INTERACTION WITH GPSM2, AND SUBCELLULAR LOCATION.
RX PubMed=11781568; DOI=10.1038/ncb1201-1069;
RA Du Q., Stukenberg P.T., Macara I.G.;
RT "A mammalian partner of inscuteable binds NuMA and regulates mitotic
RT spindle organization.";
RL Nat. Cell Biol. 3:1069-1075(2001).
RN [14]
RP FUNCTION, AND INTERACTION WITH KPNB1.
RX PubMed=11229403; DOI=10.1126/science.1057661;
RA Wiese C., Wilde A., Moore M.S., Adam S.A., Merdes A., Zheng Y.;
RT "Role of importin-beta in coupling Ran to downstream targets in microtubule
RT assembly.";
RL Science 291:653-656(2001).
RN [15]
RP FUNCTION, INTERACTION WITH GPSM2 AND MICROTUBULES, SUBCELLULAR LOCATION,
RP AND DOMAINS.
RX PubMed=12445386; DOI=10.1016/s0960-9822(02)01298-8;
RA Du Q., Taylor L., Compton D.A., Macara I.G.;
RT "LGN blocks the ability of NuMA to bind and stabilize microtubules. A
RT mechanism for mitotic spindle assembly regulation.";
RL Curr. Biol. 12:1928-1933(2002).
RN [16]
RP INTERACTION WITH TNKS AND TNKS2.
RX PubMed=12080061; DOI=10.1074/jbc.m203916200;
RA Sbodio J.I., Chi N.W.;
RT "Identification of a tankyrase-binding motif shared by IRAP, TAB182, and
RT human TRF1 but not mouse TRF1. NuMA contains this RXXPDG motif and is a
RT novel tankyrase partner.";
RL J. Biol. Chem. 277:31887-31892(2002).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TUBULIN AND MICROTUBULES,
RP AND TUBULIN-BINDING DOMAIN.
RX PubMed=11956313; DOI=10.1242/jcs.115.9.1815;
RA Haren L., Merdes A.;
RT "Direct binding of NuMA to tubulin is mediated by a novel sequence motif in
RT the tail domain that bundles and stabilizes microtubules.";
RL J. Cell Sci. 115:1815-1824(2002).
RN [18]
RP FUNCTION, ADP-RIBOSYLATION, INTERACTION WITH TNKS, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16076287; DOI=10.1042/bj20050885;
RA Chang W., Dynek J.N., Smith S.;
RT "NuMA is a major acceptor of poly(ADP-ribosyl)ation by tankyrase 1 in
RT mitosis.";
RL Biochem. J. 391:177-184(2005).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1757, AND IDENTIFICATION BY
RP 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1757; SER-1769; THR-1776;
RP SER-1840 AND THR-2106, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [22]
RP FUNCTION, AND INTERACTION WITH DYNEIN-DYNACTIN COMPLEX AND RAE1.
RX PubMed=17172455; DOI=10.1073/pnas.0609582104;
RA Wong R.W., Blobel G., Coutavas E.;
RT "Rae1 interaction with NuMA is required for bipolar spindle formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:19783-19787(2006).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2077, AND IDENTIFICATION BY
RP 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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388; SER-395; SER-820;
RP SER-1601; SER-1757 AND SER-1760, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1757, AND IDENTIFICATION BY
RP 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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1757, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-203; THR-211;
RP SER-1721; SER-1724; SER-1728; SER-1757; SER-1769; SER-1772; TYR-1774;
RP THR-1776; SER-1788; SER-1789; SER-1792; SER-1800; THR-1804; SER-1830;
RP SER-1833; SER-1834; TYR-1836; SER-1840; SER-1862; SER-1887; SER-1969;
RP SER-1991 AND THR-2000, 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 [28]
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 [29]
RP FUNCTION.
RX PubMed=19255246; DOI=10.1083/jcb.200810091;
RA Silk A.D., Holland A.J., Cleveland D.W.;
RT "Requirements for NuMA in maintenance and establishment of mammalian
RT spindle poles.";
RL J. Cell Biol. 184:677-690(2009).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-1225; SER-1757;
RP SER-1769; THR-1776; SER-1788 AND SER-1800, AND IDENTIFICATION BY MASS
RP 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 [31]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-379; LYS-891 AND LYS-1511, 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 [32]
RP GLYCOSYLATION AT SER-1844.
RX PubMed=20068230; DOI=10.1126/scisignal.2000526;
RA Wang Z., Udeshi N.D., Slawson C., Compton P.D., Sakabe K., Cheung W.D.,
RA Shabanowitz J., Hunt D.F., Hart G.W.;
RT "Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates
RT cytokinesis.";
RL Sci. Signal. 3:RA2-RA2(2010).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-203; THR-211;
RP SER-271; SER-1187; SER-1225; SER-1757; SER-1769; SER-1830; SER-1862;
RP SER-1969; SER-1991; THR-2000 AND SER-2003, 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 [34]
RP REVIEW.
RX PubMed=20137953; DOI=10.1016/j.tcb.2010.01.003;
RA Radulescu A.E., Cleveland D.W.;
RT "NuMA after 30 years: the matrix revisited.";
RL Trends Cell Biol. 20:214-222(2010).
RN [35]
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 [36]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1757, AND IDENTIFICATION BY
RP 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 [37]
RP FUNCTION, AND INTERACTION WITH DYNEIN-DYNACTIN COMPLEX.
RX PubMed=23027904; DOI=10.1083/jcb.201203166;
RA Kotak S., Busso C., Goenczy P.;
RT "Cortical dynein is critical for proper spindle positioning in human
RT cells.";
RL J. Cell Biol. 199:97-110(2012).
RN [38]
RP FUNCTION, INTERACTION WITH GPSM2, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP THR-1047; SER-1769; SER-1772; SER-1789 AND SER-1834 BY PLK1, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=22327364; DOI=10.1038/ncb2440;
RA Kiyomitsu T., Cheeseman I.M.;
RT "Chromosome- and spindle-pole-derived signals generate an intrinsic code
RT for spindle position and orientation.";
RL Nat. Cell Biol. 14:311-317(2012).
RN [39]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [40]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EPB41 AND EPB41L2,
RP PROBABLE PHOSPHORYLATION AT THR-2015; THR-2055 AND SER-2087 BY CDK1, AND
RP MUTAGENESIS OF THR-2015; THR-2055 AND SER-2087.
RX PubMed=23870127; DOI=10.1016/j.cell.2013.06.010;
RA Kiyomitsu T., Cheeseman I.M.;
RT "Cortical dynein and asymmetric membrane elongation coordinately position
RT the spindle in anaphase.";
RL Cell 154:391-402(2013).
RN [41]
RP FUNCTION, PHOSPHORYLATION AT THR-2015; THR-2055; SER-2087 AND THR-2106,
RP SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS
RP OF THR-2055.
RX PubMed=23921553; DOI=10.1038/emboj.2013.172;
RA Kotak S., Busso C., Goenczy P.;
RT "NuMA phosphorylation by CDK1 couples mitotic progression with cortical
RT dynein function.";
RL EMBO J. 32:2517-2529(2013).
RN [42]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-271; SER-1757;
RP SER-1769; SER-1830; SER-1834; SER-1840; SER-1844; SER-1862; SER-1887;
RP SER-1969; SER-1991; THR-2000; SER-2047; THR-2055 AND SER-2062, AND
RP 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 [43]
RP FUNCTION, INTERACTION WITH GPSM2, SUBCELLULAR LOCATION, DOMAIN, AND
RP MUTAGENESIS OF THR-2055.
RX PubMed=24109598; DOI=10.1091/mbc.e13-05-0277;
RA Seldin L., Poulson N.D., Foote H.P., Lechler T.;
RT "NuMA localization, stability, and function in spindle orientation involve
RT 4.1 and Cdk1 interactions.";
RL Mol. Biol. Cell 24:3651-3662(2013).
RN [44]
RP FUNCTION, INTERACTION WITH EPB41 AND EPB41L2, PHOSPHATIDYLINOSITOL-BINDING,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-2055.
RX PubMed=24996901; DOI=10.15252/embj.201488147;
RA Kotak S., Busso C., Goenczy P.;
RT "NuMA interacts with phosphoinositides and links the mitotic spindle with
RT the plasma membrane.";
RL EMBO J. 33:1815-1830(2014).
RN [45]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; THR-163; SER-169;
RP SER-271; SER-1225; SER-1757 AND SER-1788, AND IDENTIFICATION BY MASS
RP 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 [46]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-2055, DOMAIN,
RP PHOSPHATIDYLINOSITOL-BINDING, AND MUTAGENESIS OF THR-2055.
RX PubMed=24371089; DOI=10.1091/mbc.e13-08-0474;
RA Zheng Z., Wan Q., Meixiong G., Du Q.;
RT "Cell cycle-regulated membrane binding of NuMA contributes to efficient
RT anaphase chromosome separation.";
RL Mol. Biol. Cell 25:606-619(2014).
RN [47]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1766, AND IDENTIFICATION BY MASS
RP 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 [48]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1766, AND IDENTIFICATION BY MASS
RP 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 [49]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1766, AND IDENTIFICATION BY MASS
RP 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 [50]
RP FUNCTION, SUBUNIT, UBIQUITINATION, INTERACTION WITH ABRAXAS2; KPNB1 AND
RP DYNEIN-DYNACTIN COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=26195665; DOI=10.1083/jcb.201503039;
RA Yan K., Li L., Wang X., Hong R., Zhang Y., Yang H., Lin M., Zhang S.,
RA He Q., Zheng D., Tang J., Yin Y., Shao G.;
RT "The deubiquitinating enzyme complex BRISC is required for proper mitotic
RT spindle assembly in mammalian cells.";
RL J. Cell Biol. 210:209-224(2015).
RN [51]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25657325; DOI=10.1091/mbc.e14-09-1366;
RA Ohta S., Wood L., Toramoto I., Yagyu K., Fukagawa T., Earnshaw W.C.;
RT "CENP-32 is required to maintain centrosomal dominance in bipolar spindle
RT assembly.";
RL Mol. Biol. Cell 26:1225-1237(2015).
RN [52]
RP SUBCELLULAR LOCATION.
RX PubMed=26562023; DOI=10.1371/journal.pone.0142798;
RA Ohta S., Hamada M., Sato N., Toramoto I.;
RT "Polyglutamylated tubulin binding protein C1orf96/CSAP is involved in
RT microtubule stabilization in mitotic spindles.";
RL PLoS ONE 10:E0142798-E0142798(2015).
RN [53]
RP IDENTIFICATION IN A SPINDLE ORIENTATION COMPLEX.
RX PubMed=26766442; DOI=10.1016/j.devcel.2015.12.016;
RA Chiu C.W., Monat C., Robitaille M., Lacomme M., Daulat A.M., Macleod G.,
RA McNeill H., Cayouette M., Angers S.;
RT "SAPCD2 controls spindle orientation and asymmetric divisions by negatively
RT regulating the Galphai-LGN-NuMA ternary complex.";
RL Dev. Cell 36:50-62(2016).
RN [54]
RP FUNCTION, INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION, DOMAIN, AND
RP NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=26765568; DOI=10.7554/elife.12504;
RA Seldin L., Muroyama A., Lechler T.;
RT "NuMA-microtubule interactions are critical for spindle orientation and the
RT morphogenesis of diverse epidermal structures.";
RL Elife 5:0-0(2016).
RN [55]
RP FUNCTION, INTERACTION WITH GPSM2 AND SPAG5, AND SUBCELLULAR LOCATION.
RX PubMed=27462074; DOI=10.1074/jbc.m116.724831;
RA Chu X., Chen X., Wan Q., Zheng Z., Du Q.;
RT "Nuclear mitotic apparatus (NuMA) interacts with and regulates astrin at
RT the mitotic spindle.";
RL J. Biol. Chem. 291:20055-20067(2016).
RN [56]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1699; LYS-1766 AND LYS-1822, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [57]
RP ELECTRON MICROSCOPY, SUBUNIT, SUBCELLULAR LOCATION, AND PUTATIVE STRUCTURAL
RP FUNCTION.
RX PubMed=10075938; DOI=10.1093/emboj/18.6.1689;
RA Harborth J., Wang J., Gueth-Hallonet C., Weber K., Osborn M.;
RT "Self assembly of NuMA: multiarm oligomers as structural units of a nuclear
RT lattice.";
RL EMBO J. 18:1689-1700(1999).
RN [58]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1899-1926 IN COMPLEX WITH GPSM2,
RP FUNCTION, INTERACTION WITH GPSM2, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP GLU-1910, AND DOMAIN.
RX PubMed=21816348; DOI=10.1016/j.molcel.2011.07.011;
RA Zhu J., Wen W., Zheng Z., Shang Y., Wei Z., Xiao Z., Pan Z., Du Q.,
RA Wang W., Zhang M.;
RT "LGN/mInsc and LGN/NuMA complex structures suggest distinct functions in
RT asymmetric cell division for the Par3/mInsc/LGN and Galphai/LGN/NuMA
RT pathways.";
RL Mol. Cell 43:418-431(2011).
RN [59]
RP SUBCELLULAR LOCATION.
RX PubMed=26246606; DOI=10.1091/mbc.e15-02-0113;
RA Carvalhal S., Ribeiro S.A., Arocena M., Kasciukovic T., Temme A.,
RA Koehler K., Huebner A., Griffis E.R.;
RT "The nucleoporin ALADIN regulates Aurora A localization to ensure robust
RT mitotic spindle formation.";
RL Mol. Biol. Cell 26:3424-3438(2015).
CC -!- FUNCTION: Microtubule (MT)-binding protein that plays a role in the
CC formation and maintenance of the spindle poles and the alignement and
CC the segregation of chromosomes during mitotic cell division
CC (PubMed:7769006, PubMed:17172455, PubMed:19255246, PubMed:24996901,
CC PubMed:26195665, PubMed:27462074). Functions to tether the minus ends
CC of MTs at the spindle poles, which is critical for the establishment
CC and maintenance of the spindle poles (PubMed:12445386,
CC PubMed:11956313). Plays a role in the establishment of the mitotic
CC spindle orientation during metaphase and elongation during anaphase in
CC a dynein-dynactin-dependent manner (PubMed:23870127, PubMed:24109598,
CC PubMed:24996901, PubMed:26765568). In metaphase, part of a ternary
CC complex composed of GPSM2 and G(i) alpha proteins, that regulates the
CC recruitment and anchorage of the dynein-dynactin complex in the mitotic
CC cell cortex regions situated above the two spindle poles, and hence
CC regulates the correct oritentation of the mitotic spindle
CC (PubMed:23027904, PubMed:22327364, PubMed:23921553). During anaphase,
CC mediates the recruitment and accumulation of the dynein-dynactin
CC complex at the cell membrane of the polar cortical region through
CC direct association with phosphatidylinositol 4,5-bisphosphate
CC (PI(4,5)P2), and hence participates in the regulation of the spindle
CC elongation and chromosome segregation (PubMed:22327364,
CC PubMed:23921553, PubMed:24996901, PubMed:24371089). Binds also to other
CC polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate
CC (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol
CC triphosphate (PIP3), in vitro (PubMed:24996901, PubMed:24371089). Also
CC required for proper orientation of the mitotic spindle during
CC asymmetric cell divisions (PubMed:21816348). Plays a role in mitotic MT
CC aster assembly (PubMed:11163243, PubMed:11229403, PubMed:12445386).
CC Involved in anastral spindle assembly (PubMed:25657325). Positively
CC regulates TNKS protein localization to spindle poles in mitosis
CC (PubMed:16076287). Highly abundant component of the nuclear matrix
CC where it may serve a non-mitotic structural role, occupies the majority
CC of the nuclear volume (PubMed:10075938). Required for epidermal
CC differentiation and hair follicle morphogenesis (By similarity).
CC {ECO:0000250|UniProtKB:E9Q7G0, ECO:0000269|PubMed:11163243,
CC ECO:0000269|PubMed:11229403, ECO:0000269|PubMed:11956313,
CC ECO:0000269|PubMed:12445386, ECO:0000269|PubMed:16076287,
CC ECO:0000269|PubMed:17172455, ECO:0000269|PubMed:19255246,
CC ECO:0000269|PubMed:22327364, ECO:0000269|PubMed:23027904,
CC ECO:0000269|PubMed:23870127, ECO:0000269|PubMed:23921553,
CC ECO:0000269|PubMed:24109598, ECO:0000269|PubMed:24371089,
CC ECO:0000269|PubMed:24996901, ECO:0000269|PubMed:25657325,
CC ECO:0000269|PubMed:26195665, ECO:0000269|PubMed:26765568,
CC ECO:0000269|PubMed:27462074, ECO:0000269|PubMed:7769006,
CC ECO:0000305|PubMed:10075938, ECO:0000305|PubMed:21816348}.
CC -!- SUBUNIT: Homodimer (PubMed:10075938). Also forms multiarm oligomers by
CC association of C-terminal tail domains, oligomers may further assemble
CC to form a hexagonal nuclear lattice-like network (PubMed:10075938).
CC Associates with the dynein-dynactin complex; this association promotes
CC the transport and accumulation of NUMA1 at the mitotic spindle poles
CC that is inhibited by the BRISC complex in a PLK1-dependent manner
CC (PubMed:10811826, PubMed:17172455, PubMed:23027904, PubMed:22327364,
CC PubMed:26195665). Part of a spindle orientation complex at least
CC composed of GNAI1, GPSM2 and NUMA1 (PubMed:26766442). Interacts (via C-
CC terminus) with microtubules (MTs); this interaction is direct and
CC promotes both MT bundle formation and stability in a dynein-dynactin
CC complex- and CDK1-independent manner (PubMed:12445386, PubMed:11956313,
CC PubMed:26765568). Interacts with EPB41 and EPB41L2; these interactions
CC are negatively regulated by CDK1 during metaphase and are important for
CC anaphase-specific localization of NUMA1 in symmetrically dividing cells
CC (PubMed:23870127, PubMed:24996901). Interacts (via C-terminus) with
CC GPSM2 (via TPR repeats); this interaction is direct, prevented by
CC competitive binding of INSC, is inhibited in a PLK1-dependent manner,
CC blocks the association of NUMA1 with MTs and inhibits NUMA1-induced MT
CC bundle formation, prevents the association of NUMA1 with SPAG5, induces
CC mitotic spindle pole localization of GPSM2, both metaphase cell cortex
CC localization of NUMA1 and mitotic spindle organization
CC (PubMed:11781568, PubMed:12445386, PubMed:22327364, PubMed:24109598,
CC PubMed:27462074, PubMed:21816348). Does not interact with GPSM2 during
CC anaphase (PubMed:23870127). Interacts (via C-terminus) with the nuclear
CC importin alpha/importin beta receptor; this interaction is inhibited by
CC RanGTP (PubMed:11163243). Interacts (via C-terminus) with KPNB1; this
CC interaction is inhibited by RanGTP and the BRISC complex
CC (PubMed:11229403, PubMed:26195665). Interacts with ABRAXAS2 and the
CC BRISC complex; these interactions regulate mitotic spindle assembly
CC (PubMed:26195665). Interacts (via N-terminal end of the coiled-coil
CC domain) with RAE1; this interaction promotes mitotic spindle formation
CC (PubMed:17172455). Interacts (via C-terminus) with SPAG5 (via C-
CC terminus); this interaction promotes the recruitment of SPAG5 to the
CC MTs at spindle poles in a dynein-dynactin-dependent manner and
CC regulates mitotic spindle organization and proper chromosome alignment
CC during mitosis (PubMed:27462074). Interacts with TNKS; this interaction
CC occurs at the onset of mitosis (PubMed:12080061, PubMed:16076287).
CC Interacts with TNKS2 (PubMed:12080061). Interacts with tubulin
CC (PubMed:11956313). Interacts with KHDC3L (via C-terminus) (By
CC similarity). {ECO:0000250|UniProtKB:E9Q7G0,
CC ECO:0000269|PubMed:10075938, ECO:0000269|PubMed:10811826,
CC ECO:0000269|PubMed:11163243, ECO:0000269|PubMed:11229403,
CC ECO:0000269|PubMed:11781568, ECO:0000269|PubMed:11956313,
CC ECO:0000269|PubMed:12080061, ECO:0000269|PubMed:12445386,
CC ECO:0000269|PubMed:16076287, ECO:0000269|PubMed:17172455,
CC ECO:0000269|PubMed:21816348, ECO:0000269|PubMed:22327364,
CC ECO:0000269|PubMed:23027904, ECO:0000269|PubMed:23870127,
CC ECO:0000269|PubMed:24109598, ECO:0000269|PubMed:24996901,
CC ECO:0000269|PubMed:26195665, ECO:0000269|PubMed:26765568,
CC ECO:0000269|PubMed:26766442, ECO:0000269|PubMed:27462074}.
CC -!- INTERACTION:
CC Q14980; Q2TAC2: CCDC57; NbExp=3; IntAct=EBI-521611, EBI-2808286;
CC Q14980; Q53SE7: FLJ13057; NbExp=3; IntAct=EBI-521611, EBI-10172181;
CC Q14980; P63096: GNAI1; NbExp=4; IntAct=EBI-521611, EBI-618639;
CC Q14980; P81274: GPSM2; NbExp=6; IntAct=EBI-521611, EBI-618655;
CC Q14980; P78406: RAE1; NbExp=6; IntAct=EBI-521611, EBI-724495;
CC Q14980; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-521611, EBI-750109;
CC Q14980; O95271: TNKS; NbExp=2; IntAct=EBI-521611, EBI-1105254;
CC Q14980; Q9H2K2: TNKS2; NbExp=4; IntAct=EBI-521611, EBI-4398527;
CC Q14980-2; Q8VDU0: Gpsm2; Xeno; NbExp=2; IntAct=EBI-10981450, EBI-7575403;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1541630,
CC ECO:0000269|PubMed:23921553, ECO:0000269|PubMed:27462074}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:10811826}. Nucleus matrix
CC {ECO:0000269|PubMed:10075938, ECO:0000269|PubMed:11956313,
CC ECO:0000269|PubMed:1541636, ECO:0000269|PubMed:7962183}. Chromosome
CC {ECO:0000269|PubMed:1541630}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11956313, ECO:0000269|PubMed:12445386,
CC ECO:0000269|PubMed:26765568}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:10811826,
CC ECO:0000269|PubMed:1541630, ECO:0000269|PubMed:1541636,
CC ECO:0000269|PubMed:25657325, ECO:0000269|PubMed:26562023,
CC ECO:0000269|PubMed:26765568}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:10811826, ECO:0000269|PubMed:11781568,
CC ECO:0000269|PubMed:11956313, ECO:0000269|PubMed:12445386,
CC ECO:0000269|PubMed:1541630, ECO:0000269|PubMed:1541636,
CC ECO:0000269|PubMed:16076287, ECO:0000269|PubMed:21816348,
CC ECO:0000269|PubMed:22327364, ECO:0000269|PubMed:23870127,
CC ECO:0000269|PubMed:23921553, ECO:0000269|PubMed:24109598,
CC ECO:0000269|PubMed:24996901, ECO:0000269|PubMed:25657325,
CC ECO:0000269|PubMed:26195665, ECO:0000269|PubMed:26246606,
CC ECO:0000269|PubMed:26562023, ECO:0000269|PubMed:27462074,
CC ECO:0000269|PubMed:7769006, ECO:0000269|PubMed:7962183}. Cytoplasm,
CC cell cortex {ECO:0000269|PubMed:21816348, ECO:0000269|PubMed:22327364,
CC ECO:0000269|PubMed:23870127, ECO:0000269|PubMed:23921553,
CC ECO:0000269|PubMed:24109598, ECO:0000269|PubMed:24996901}. Cell
CC membrane {ECO:0000269|PubMed:24371089, ECO:0000269|PubMed:24996901};
CC Lipid-anchor {ECO:0000269|PubMed:24371089,
CC ECO:0000269|PubMed:24996901}; Cytoplasmic side
CC {ECO:0000269|PubMed:24371089, ECO:0000269|PubMed:24996901}. Lateral
CC cell membrane {ECO:0000250|UniProtKB:E9Q7G0}. Note=Mitotic cell cycle-
CC dependent shuttling protein that relocalizes from the interphase
CC nucleus to the spindle poles and cell cortex (PubMed:1541636,
CC PubMed:10811826). The localization to the spindle poles is regulated by
CC AAAS (PubMed:26246606). In interphase, resides in the nuclear matrix
CC (PubMed:1541630, PubMed:1541636, PubMed:23921553). In prophase,
CC restricted to the interchromatin or condensed chromosome space
CC (PubMed:10811826). In prometaphase, after nuclear envelope disassembly,
CC forms aggregates both in the spindle midzone and at duplicated
CC centrosomes and astral microtubules (MTs) of the bipolar spindle
CC apparatus (PubMed:10811826). Translocates from the spindle midzone
CC towards the spindle poles along spindle fibers in a MT- and dynein-
CC dynactin-dependent manner until the anaphase onset (PubMed:1541636,
CC PubMed:10811826). In metaphase, recruited to the polar cortical region
CC in a GPSM2- and GNAI1-dependent manner (PubMed:23870127,
CC PubMed:24109598, PubMed:24996901). Excluded from the metaphase
CC equatorial cortical region in a RanGTP-dependent manner
CC (PubMed:22327364, PubMed:23870127). Phosphorylation on Thr-2055 by CDK1
CC results in its localization at spindle poles in metaphase, but not at
CC the cell cortex (PubMed:23921553). In anaphase, recruited and anchored
CC at the cell membrane of the polar cortical region in a EPB41-,
CC EPB41L2-, phosphatidylinositol-dependent and GPSM2- and G(i) alpha
CC proteins-independent manner (PubMed:23870127, PubMed:24996901,
CC PubMed:24109598, PubMed:24371089). Excluded from the anaphase
CC equatorial region of the cell cortex in a RACGAP1- and KIF23-dependent
CC and RanGTP-independent manner (PubMed:24996901). Associated with astral
CC MTs emanating from the spindle poles during anaphase (PubMed:12445386,
CC PubMed:24996901). Nonphosphorylated Thr-2055 localizes at the cell
CC cortex, weakly during metaphase and more prominently during anaphase in
CC a phosphatase PPP2CA-dependent manner (PubMed:23921553). As mitosis
CC progresses it reassociates with telophase chromosomes very early during
CC nuclear reformation, before substantial accumulation of lamins on
CC chromosomal surfaces is evident (PubMed:1541636). Localizes to the tips
CC of cortical MTs in prometaphase (PubMed:26765568). Localizes along MTs
CC and specifically to both MT plus and minus ends (PubMed:26765568).
CC Accumulates also at MT tips near the cell periphery (PubMed:26765568).
CC Colocalizes with GPSM2 at mitotic spindle poles during mitosis
CC (PubMed:11781568, PubMed:21816348). Colocalizes with SPAG5 at mitotic
CC spindle at prometaphase and at mitotic spindle poles at metaphase and
CC anaphase (PubMed:27462074). Colocalizes with ABRO1 at mitotic spindle
CC poles (PubMed:26195665). Colocalized with TNKS from prophase through to
CC anaphase in mitosis (PubMed:16076287). Colocalizes with tubulin alpha
CC (PubMed:12445386). CCSAP is essential for its centrosomal localization
CC (PubMed:26562023). In horizontally retinal progenitor dividing cells,
CC localized to the lateral cortical region (By similarity).
CC {ECO:0000250|UniProtKB:E9Q7G0, ECO:0000269|PubMed:10811826,
CC ECO:0000269|PubMed:11781568, ECO:0000269|PubMed:12445386,
CC ECO:0000269|PubMed:1541630, ECO:0000269|PubMed:1541636,
CC ECO:0000269|PubMed:16076287, ECO:0000269|PubMed:21816348,
CC ECO:0000269|PubMed:22327364, ECO:0000269|PubMed:23870127,
CC ECO:0000269|PubMed:23921553, ECO:0000269|PubMed:24109598,
CC ECO:0000269|PubMed:24371089, ECO:0000269|PubMed:24996901,
CC ECO:0000269|PubMed:26195665, ECO:0000269|PubMed:26246606,
CC ECO:0000269|PubMed:26562023, ECO:0000269|PubMed:26765568,
CC ECO:0000269|PubMed:27462074}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, cytosol
CC {ECO:0000269|PubMed:7962183}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:7962183}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000269|PubMed:7962183}. Note=During
CC interphase, mainly clustered at the centrosomal region in the cytosol.
CC After entry into mitosis, detected at mitotic spindle poles.
CC {ECO:0000269|PubMed:7962183}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm, cytosol
CC {ECO:0000269|PubMed:7962183}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:7962183}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000269|PubMed:7962183}. Note=During
CC interphase, mainly clustered at the centrosomal region in the cytosol.
CC After entry into mitosis, detected at mitotic spindle poles.
CC {ECO:0000269|PubMed:7962183}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=Numa-1, p230;
CC IsoId=Q14980-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14980-2; Sequence=VSP_012910;
CC Name=3; Synonyms=Numa-m {ECO:0000303|PubMed:7962183}, p195;
CC IsoId=Q14980-3; Sequence=VSP_044378;
CC Name=4; Synonyms=Numa-s {ECO:0000303|PubMed:7962183}, p194;
CC IsoId=Q14980-4; Sequence=VSP_044379;
CC Name=5;
CC IsoId=Q14980-5; Sequence=VSP_054146;
CC -!- DOMAIN: The C-terminal tubulin-binding domain mediates direct binding
CC to microtubules, independently of dynein-dynactin complex, and induces
CC their bundling and stabilization (PubMed:11956313). The 4.1-binding
CC domain is necessary for its cortical stability and spindle orientation
CC (PubMed:24109598). {ECO:0000269|PubMed:11956313,
CC ECO:0000269|PubMed:24109598}.
CC -!- PTM: Phosphorylation and dephosphorylation on Thr-2055 regulates the
CC extent of cortical NUMA1 and the dynein-dynactin complex localization
CC during mitotic metaphase and anaphase (PubMed:23921553). In metaphase,
CC phosphorylation on Thr-2055 occurs in a kinase CDK1-dependent manner;
CC this phosphorylation maintains low levels of cortical dynein-dynactin
CC complex at metaphase, and hence proper spindle positioning
CC (PubMed:7769006, PubMed:23921553, PubMed:24371089). In anaphase,
CC dephosphorylated on Thr-2055 by phosphatase PPP2CA; this
CC dephosphorylation stimulates its membrane association and with the
CC dynein-dynactin complex its enrichment at the cell cortex, and hence
CC robust spindle elongation (PubMed:23921553, PubMed:24371089). Probably
CC also phosphorylated on Thr-2015 and Ser-2087 by CDK1; these
CC phosphorylations may regulate its cell cortex recruitment during
CC metaphase and anaphase (PubMed:23870127). Phosphorylated on Thr-1047,
CC Ser-1769, Ser-1772, Ser-1789 and Ser-1834 by PLK1; these
CC phosphorylations induce cortical dynein-dynactin complex dissociation
CC from the NUMA1-GPSM2 complex and negatively regulates cortical dynein-
CC dynactin complex localization (PubMed:22327364).
CC {ECO:0000269|PubMed:22327364, ECO:0000269|PubMed:23870127,
CC ECO:0000269|PubMed:23921553, ECO:0000269|PubMed:24371089,
CC ECO:0000269|PubMed:7769006}.
CC -!- PTM: ADP-ribosylated by TNKS at the onset of mitosis; ADP-ribosylation
CC is not required for its localization to spindle poles
CC (PubMed:16076287). {ECO:0000269|PubMed:16076287}.
CC -!- PTM: O-glycosylated during cytokinesis at sites identical or close to
CC phosphorylation sites, this interferes with the phosphorylation status
CC (PubMed:20068230). {ECO:0000269|PubMed:20068230}.
CC -!- PTM: Ubiquitinated with 'Lys-63'-linked polyubiquitin chains.
CC Deubiquitination by the BRISC complex is important for the
CC incorporation of NUMA1 into mitotic spindle poles and normal spindle
CC pole function, probably by modulating interactions between NUMA1,
CC dynein-dynactin complex and importin-beta.
CC {ECO:0000269|PubMed:26195665}.
CC -!- MISCELLANEOUS: Also known as nuclear matrix protein-22/NMP-22/NMP22, an
CC antigen used in diagnostic tests of bladder cancer.
CC {ECO:0000269|PubMed:9730450}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA77670.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/NUMAID119.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; Z14227; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; Z14228; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; Z14229; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; Z11583; CAA77669.1; -; mRNA.
DR EMBL; Z11584; CAA77670.1; ALT_FRAME; mRNA.
DR EMBL; AP002490; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW74826.1; -; Genomic_DNA.
DR EMBL; BC004165; AAH04165.1; -; mRNA.
DR CCDS; CCDS31633.1; -. [Q14980-1]
DR CCDS; CCDS66156.1; -. [Q14980-2]
DR PIR; A42184; A42184.
DR RefSeq; NP_001273490.1; NM_001286561.1. [Q14980-2]
DR RefSeq; NP_006176.2; NM_006185.3. [Q14980-1]
DR RefSeq; XP_006718627.1; XM_006718564.1. [Q14980-1]
DR PDB; 3RO2; X-ray; 2.30 A; B=1899-1926.
DR PDB; 5GXW; X-ray; 2.39 A; B=1984-2010.
DR PDB; 6HC2; X-ray; 4.31 A; B/D/F/H/J/L/N/P/R/T/V/X=1860-1928.
DR PDB; 6QJA; X-ray; 1.54 A; A/B/C/D=1-153.
DR PDBsum; 3RO2; -.
DR PDBsum; 5GXW; -.
DR PDBsum; 6HC2; -.
DR PDBsum; 6QJA; -.
DR AlphaFoldDB; Q14980; -.
DR SMR; Q14980; -.
DR BioGRID; 110980; 210.
DR CORUM; Q14980; -.
DR DIP; DIP-32937N; -.
DR ELM; Q14980; -.
DR IntAct; Q14980; 86.
DR MINT; Q14980; -.
DR STRING; 9606.ENSP00000377298; -.
DR CarbonylDB; Q14980; -.
DR GlyConnect; 2887; 1 O-Linked glycan (1 site).
DR GlyGen; Q14980; 7 sites, 1 O-linked glycan (7 sites).
DR iPTMnet; Q14980; -.
DR MetOSite; Q14980; -.
DR PhosphoSitePlus; Q14980; -.
DR SwissPalm; Q14980; -.
DR BioMuta; NUMA1; -.
DR DMDM; 145559510; -.
DR CPTAC; CPTAC-937; -.
DR EPD; Q14980; -.
DR jPOST; Q14980; -.
DR MassIVE; Q14980; -.
DR MaxQB; Q14980; -.
DR PaxDb; Q14980; -.
DR PeptideAtlas; Q14980; -.
DR PRIDE; Q14980; -.
DR ProteomicsDB; 38621; -.
DR ProteomicsDB; 60272; -. [Q14980-1]
DR ProteomicsDB; 60273; -. [Q14980-2]
DR ProteomicsDB; 78989; -.
DR Antibodypedia; 16895; 437 antibodies from 38 providers.
DR CPTC; Q14980; 1 antibody.
DR DNASU; 4926; -.
DR Ensembl; ENST00000351960.10; ENSP00000260051.8; ENSG00000137497.19. [Q14980-5]
DR Ensembl; ENST00000358965.10; ENSP00000351851.6; ENSG00000137497.19. [Q14980-2]
DR Ensembl; ENST00000393695.8; ENSP00000377298.4; ENSG00000137497.19. [Q14980-1]
DR Ensembl; ENST00000613205.4; ENSP00000480172.1; ENSG00000137497.19. [Q14980-5]
DR Ensembl; ENST00000620566.4; ENSP00000478624.1; ENSG00000137497.19. [Q14980-2]
DR GeneID; 4926; -.
DR KEGG; hsa:4926; -.
DR MANE-Select; ENST00000393695.8; ENSP00000377298.4; NM_006185.4; NP_006176.2.
DR UCSC; uc001ork.3; human. [Q14980-1]
DR CTD; 4926; -.
DR DisGeNET; 4926; -.
DR GeneCards; NUMA1; -.
DR HGNC; HGNC:8059; NUMA1.
DR HPA; ENSG00000137497; Low tissue specificity.
DR MalaCards; NUMA1; -.
DR MIM; 164009; gene.
DR neXtProt; NX_Q14980; -.
DR OpenTargets; ENSG00000137497; -.
DR Orphanet; 520; Acute promyelocytic leukemia.
DR PharmGKB; PA31844; -.
DR VEuPathDB; HostDB:ENSG00000137497; -.
DR eggNOG; ENOG502QTDA; Eukaryota.
DR GeneTree; ENSGT00950000183078; -.
DR HOGENOM; CLU_006666_1_0_1; -.
DR InParanoid; Q14980; -.
DR OMA; QCRRQQE; -.
DR OrthoDB; 524033at2759; -.
DR PhylomeDB; Q14980; -.
DR TreeFam; TF334442; -.
DR PathwayCommons; Q14980; -.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-68875; Mitotic Prophase.
DR SignaLink; Q14980; -.
DR SIGNOR; Q14980; -.
DR BioGRID-ORCS; 4926; 459 hits in 1086 CRISPR screens.
DR ChiTaRS; NUMA1; human.
DR GeneWiki; Nuclear_mitotic_apparatus_protein_1; -.
DR GenomeRNAi; 4926; -.
DR Pharos; Q14980; Tbio.
DR PRO; PR:Q14980; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q14980; protein.
DR Bgee; ENSG00000137497; Expressed in right uterine tube and 205 other tissues.
DR ExpressionAtlas; Q14980; baseline and differential.
DR Genevisible; Q14980; HS.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0099738; C:cell cortex region; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0055028; C:cortical microtubule; IDA:UniProtKB.
DR GO; GO:1905720; C:cytoplasmic microtubule bundle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:InterPro.
DR GO; GO:0097575; C:lateral cell cortex; ISS:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0097427; C:microtubule bundle; IDA:UniProtKB.
DR GO; GO:0036449; C:microtubule minus-end; IDA:UniProtKB.
DR GO; GO:0035371; C:microtubule plus-end; IDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR GO; GO:0061673; C:mitotic spindle astral microtubule; IDA:UniProtKB.
DR GO; GO:1990023; C:mitotic spindle midzone; IDA:UniProtKB.
DR GO; GO:0097431; C:mitotic spindle pole; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0016363; C:nuclear matrix; 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:UniProtKB.
DR GO; GO:0005819; C:spindle; TAS:ProtInc.
DR GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0031616; C:spindle pole centrosome; IDA:UniProtKB.
DR GO; GO:0097718; F:disordered domain specific binding; IMP:CAFA.
DR GO; GO:0070840; F:dynein complex binding; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0051011; F:microtubule minus-end binding; IDA:UniProtKB.
DR GO; GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IMP:CAFA.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; TAS:ProtInc.
DR GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
DR GO; GO:0055048; P:anastral spindle assembly; IMP:UniProtKB.
DR GO; GO:0030953; P:astral microtubule organization; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IDA:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:Ensembl.
DR GO; GO:0001578; P:microtubule bundle formation; IMP:UniProtKB.
DR GO; GO:0006997; P:nucleus organization; TAS:ProtInc.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISS:UniProtKB.
DR GO; GO:0051984; P:positive regulation of chromosome segregation; IMP:UniProtKB.
DR GO; GO:1905820; P:positive regulation of chromosome separation; IMP:UniProtKB.
DR GO; GO:0051798; P:positive regulation of hair follicle development; ISS:UniProtKB.
DR GO; GO:0032388; P:positive regulation of intracellular transport; IMP:UniProtKB.
DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; ISS:UniProtKB.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:UniProtKB.
DR GO; GO:1902846; P:positive regulation of mitotic spindle elongation; IMP:UniProtKB.
DR GO; GO:1904778; P:positive regulation of protein localization to cell cortex; IMP:UniProtKB.
DR GO; GO:1902365; P:positive regulation of protein localization to spindle pole body; IDA:UniProtKB.
DR GO; GO:1905832; P:positive regulation of spindle assembly; IMP:UniProtKB.
DR GO; GO:0090235; P:regulation of metaphase plate congression; IMP:UniProtKB.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IDA:UniProtKB.
DR InterPro; IPR026650; NUMA1.
DR PANTHER; PTHR18902:SF24; PTHR18902:SF24; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ADP-ribosylation; Alternative splicing;
KW Cell cycle; Cell division; Cell membrane; Chromosome; Chromosome partition;
KW Coiled coil; Cytoplasm; Cytoskeleton; Glycoprotein; Isopeptide bond;
KW Lipid-binding; Lipoprotein; Membrane; Microtubule; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..2115
FT /note="Nuclear mitotic apparatus protein 1"
FT /id="PRO_0000057998"
FT REGION 1..212
FT /note="Head (Globular)"
FT REGION 549..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1090..1225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1275..1296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1699..1876
FT /note="Membrane-binding domain 1"
FT /evidence="ECO:0000269|PubMed:24996901"
FT REGION 1700..2115
FT /note="Tail (Globular)"
FT REGION 1734..1761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1788..1810
FT /note="4.1-binding domain"
FT /evidence="ECO:0000269|PubMed:24109598,
FT ECO:0000269|PubMed:24996901"
FT REGION 1826..1901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1882..1985
FT /note="Tubulin-binding domain"
FT /evidence="ECO:0000269|PubMed:11956313,
FT ECO:0000269|PubMed:12445386"
FT REGION 1892..1926
FT /note="GPSM2-binding domain"
FT /evidence="ECO:0000269|PubMed:11781568,
FT ECO:0000269|PubMed:12445386, ECO:0000269|PubMed:21816348,
FT ECO:0000269|PubMed:24109598"
FT REGION 1955..2115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1981..2060
FT /note="Membrane-binding domain 2"
FT /evidence="ECO:0000269|PubMed:24371089"
FT COILED 213..1699
FT /evidence="ECO:0000255"
FT MOTIF 1742..1748
FT /note="Tankyrase-binding domain"
FT /evidence="ECO:0000269|PubMed:12080061"
FT MOTIF 1984..1989
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:26765568,
FT ECO:0000269|PubMed:7962183"
FT COMPBIAS 549..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..953
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1013
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1734..1756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1830..1862
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1873..1895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1964..1987
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2014..2028
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2029..2058
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2073..2100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 163
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 211
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 379
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 820
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 891
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1047
FT /note="Phosphothreonine; by PLK1"
FT /evidence="ECO:0000269|PubMed:22327364"
FT MOD_RES 1187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 1511
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1601
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 1721
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1724
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1728
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1757
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1760
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 1769
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000269|PubMed:22327364,
FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1772
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000269|PubMed:22327364,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 1774
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1776
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332"
FT MOD_RES 1788
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT MOD_RES 1789
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000269|PubMed:22327364,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 1792
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1800
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 1804
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1830
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1833
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1834
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000269|PubMed:22327364,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 1836
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1840
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 1844
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1862
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1887
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1969
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1991
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 2000
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 2003
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 2015
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:23921553,
FT ECO:0000269|PubMed:7769006"
FT MOD_RES 2047
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2055
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:23921553,
FT ECO:0000269|PubMed:7769006, ECO:0007744|PubMed:23186163"
FT MOD_RES 2062
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2077
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17924679"
FT MOD_RES 2087
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:23921553,
FT ECO:0000269|PubMed:7769006"
FT MOD_RES 2106
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:23921553,
FT ECO:0000269|PubMed:7769006, ECO:0007744|PubMed:16964243"
FT CARBOHYD 1844
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000269|PubMed:20068230"
FT CROSSLNK 1699
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1766
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 1766
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:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1822
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 414..1549
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054146"
FT VAR_SEQ 1536..1549
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1541636"
FT /id="VSP_012910"
FT VAR_SEQ 1725..2115
FT /note="LDLSCEEGTPLSITSKLPRTQPDGTSVPGEPASPISQRLPPKVESLESLYFT
FT PIPARSQAPLESSLDSLGDVFLDSGRKTRSARRRTTQIINITMTKKLDVEEPDSANSSF
FT YSTRSAPASQASLRATSSTQSLARLGSPDYGNSALLSLPGYRPTTRSSARRSQAGVSSG
FT APPGRNSFYMGTCQDEPEQLDDWNRIAELQQRNRVCPPHLKTCYPLESRPSLSLGTITD
FT EEMKTGDPQETLRRASMQPIQIAEGTGITTRQQRKRVSLEPHQGPGTPESKKATSCFPR
FT PMTPRDRHEGRKQSTTEAQKKAAPASTKQADRRQSMAFSILNTPKKLGNSLLRRGASKK
FT ALSKASPNTRSGTRRSPRIATTTASAATAAAIGATPRAKGKAKH -> SQANSSQTPRD
FT SDACPHPGLVPGPSLAPSRSWPRGPGAWTVWALSLPCLLFS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8505359"
FT /id="VSP_044378"
FT VAR_SEQ 1739..2115
FT /note="SKLPRTQPDGTSVPGEPASPISQRLPPKVESLESLYFTPIPARSQAPLESSL
FT DSLGDVFLDSGRKTRSARRRTTQIINITMTKKLDVEEPDSANSSFYSTRSAPASQASLR
FT ATSSTQSLARLGSPDYGNSALLSLPGYRPTTRSSARRSQAGVSSGAPPGRNSFYMGTCQ
FT DEPEQLDDWNRIAELQQRNRVCPPHLKTCYPLESRPSLSLGTITDEEMKTGDPQETLRR
FT ASMQPIQIAEGTGITTRQQRKRVSLEPHQGPGTPESKKATSCFPRPMTPRDRHEGRKQS
FT TTEAQKKAAPASTKQADRRQSMAFSILNTPKKLGNSLLRRGASKKALSKASPNTRSGTR
FT RSPRIATTTASAATAAAIGATPRAKGKAKH -> RSGGSLPPYVCLWSACCLSGCILVR
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:8505359"
FT /id="VSP_044379"
FT VARIANT 242
FT /note="K -> R (in dbSNP:rs34239655)"
FT /id="VAR_031679"
FT VARIANT 794
FT /note="A -> G (in dbSNP:rs3750913)"
FT /id="VAR_031680"
FT VARIANT 1153
FT /note="E -> D (in dbSNP:rs34311364)"
FT /id="VAR_031681"
FT VARIANT 1825
FT /note="V -> M (in dbSNP:rs7949430)"
FT /id="VAR_031682"
FT VARIANT 1836
FT /note="Y -> H (in dbSNP:rs35586429)"
FT /id="VAR_031683"
FT VARIANT 2049
FT /note="A -> T (in dbSNP:rs5743685)"
FT /id="VAR_051248"
FT MUTAGEN 1910
FT /note="E->A: Abolishes interaction with GPSM2."
FT /evidence="ECO:0000269|PubMed:21816348"
FT MUTAGEN 1984
FT /note="R->G: No effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:7962183"
FT MUTAGEN 1988
FT /note="K->E: Abolishes nuclear localization."
FT /evidence="ECO:0000269|PubMed:7962183"
FT MUTAGEN 2015
FT /note="T->A: Abolishes association with the mitotic
FT spindle. Increases premature accumulation at the cell
FT cortex during metaphase; when associated with A-2055 and A-
FT 2087."
FT /evidence="ECO:0000269|PubMed:23870127,
FT ECO:0000269|PubMed:7769006"
FT MUTAGEN 2055
FT /note="T->A: Increases premature accumulation at the cell
FT membrane of the polar cortical region in prophase and
FT metaphase. Reduces association with the mitotic spindle.
FT Increased randomization of spindle orientation. Increases
FT premature accumulation at the cell cortex during metaphase;
FT when associated with A-2015 and A-2087."
FT /evidence="ECO:0000269|PubMed:23870127,
FT ECO:0000269|PubMed:23921553, ECO:0000269|PubMed:24109598,
FT ECO:0000269|PubMed:24371089, ECO:0000269|PubMed:24996901,
FT ECO:0000269|PubMed:7769006"
FT MUTAGEN 2055
FT /note="T->D: Increases localization at the spindle poles.
FT Decreases localization at the cell cortex."
FT /evidence="ECO:0000269|PubMed:24109598"
FT MUTAGEN 2055
FT /note="T->E: Absence of cell membrane association even in
FT anaphase. Increased localization at spindle poles and
FT chromosome congression defects. Does not localize to the
FT cortex in either metaphase or anaphase. Increased
FT randomization of spindle orientation."
FT /evidence="ECO:0000269|PubMed:23921553,
FT ECO:0000269|PubMed:24371089"
FT MUTAGEN 2087
FT /note="S->A: Abolishes association with the mitotic
FT spindle. Increases premature accumulation at the cell
FT cortex during metaphase; when associated with A-2015 and A-
FT 2055."
FT /evidence="ECO:0000269|PubMed:23870127,
FT ECO:0000269|PubMed:7769006"
FT MUTAGEN 2106
FT /note="T->A: Abolishes association with the mitotic
FT spindle."
FT /evidence="ECO:0000269|PubMed:7769006"
FT CONFLICT 772
FT /note="Q -> L (in Ref. 2; CAA77670)"
FT /evidence="ECO:0000305"
FT CONFLICT 815..816
FT /note="ER -> DG (in Ref. 2; CAA77670)"
FT /evidence="ECO:0000305"
FT CONFLICT 873
FT /note="E -> K (in Ref. 2; CAA77670)"
FT /evidence="ECO:0000305"
FT CONFLICT 1589
FT /note="L -> F (in Ref. 2; CAA77670)"
FT /evidence="ECO:0000305"
FT CONFLICT 1637
FT /note="S -> T (in Ref. 3; Z14227/Z14228)"
FT /evidence="ECO:0000305"
FT CONFLICT 1682
FT /note="S -> T (in Ref. 3; Z14227/Z14228)"
FT /evidence="ECO:0000305"
FT CONFLICT 1798
FT /note="L -> Q (in Ref. 3; CAA77669)"
FT /evidence="ECO:0000305"
FT HELIX 5..17
FT /evidence="ECO:0007829|PDB:6QJA"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:6QJA"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:6QJA"
FT HELIX 34..44
FT /evidence="ECO:0007829|PDB:6QJA"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:6QJA"
FT HELIX 57..70
FT /evidence="ECO:0007829|PDB:6QJA"
FT HELIX 84..88
FT /evidence="ECO:0007829|PDB:6QJA"
FT HELIX 92..107
FT /evidence="ECO:0007829|PDB:6QJA"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:6QJA"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:6QJA"
FT HELIX 121..137
FT /evidence="ECO:0007829|PDB:6QJA"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:6QJA"
FT HELIX 143..152
FT /evidence="ECO:0007829|PDB:6QJA"
FT TURN 1917..1919
FT /evidence="ECO:0007829|PDB:3RO2"
FT HELIX 1920..1922
FT /evidence="ECO:0007829|PDB:3RO2"
FT STRAND 1995..1997
FT /evidence="ECO:0007829|PDB:5GXW"
SQ SEQUENCE 2115 AA; 238260 MW; DE734EC85B812CC7 CRC64;
MTLHATRGAA LLSWVNSLHV ADPVEAVLQL QDCSIFIKII DRIHGTEEGQ QILKQPVSER
LDFVCSFLQK NRKHPSSPEC LVSAQKVLEG SELELAKMTM LLLYHSTMSS KSPRDWEQFE
YKIQAELAVI LKFVLDHEDG LNLNEDLENF LQKAPVPSTC SSTFPEELSP PSHQAKREIR
FLELQKVASS SSGNNFLSGS PASPMGDILQ TPQFQMRRLK KQLADERSNR DELELELAEN
RKLLTEKDAQ IAMMQQRIDR LALLNEKQAA SPLEPKELEE LRDKNESLTM RLHETLKQCQ
DLKTEKSQMD RKINQLSEEN GDLSFKLREF ASHLQQLQDA LNELTEEHSK ATQEWLEKQA
QLEKELSAAL QDKKCLEEKN EILQGKLSQL EEHLSQLQDN PPQEKGEVLG DVLQLETLKQ
EAATLAANNT QLQARVEMLE TERGQQEAKL LAERGHFEEE KQQLSSLITD LQSSISNLSQ
AKEELEQASQ AHGARLTAQV ASLTSELTTL NATIQQQDQE LAGLKQQAKE KQAQLAQTLQ
QQEQASQGLR HQVEQLSSSL KQKEQQLKEV AEKQEATRQD HAQQLATAAE EREASLRERD
AALKQLEALE KEKAAKLEIL QQQLQVANEA RDSAQTSVTQ AQREKAELSR KVEELQACVE
TARQEQHEAQ AQVAELELQL RSEQQKATEK ERVAQEKDQL QEQLQALKES LKVTKGSLEE
EKRRAADALE EQQRCISELK AETRSLVEQH KRERKELEEE RAGRKGLEAR LQQLGEAHQA
ETEVLRRELA EAMAAQHTAE SECEQLVKEV AAWRERYEDS QQEEAQYGAM FQEQLMTLKE
ECEKARQELQ EAKEKVAGIE SHSELQISRQ QNELAELHAN LARALQQVQE KEVRAQKLAD
DLSTLQEKMA ATSKEVARLE TLVRKAGEQQ ETASRELVKE PARAGDRQPE WLEEQQGRQF
CSTQAALQAM EREAEQMGNE LERLRAALME SQGQQQEERG QQEREVARLT QERGRAQADL
ALEKAARAEL EMRLQNALNE QRVEFATLQE ALAHALTEKE GKDQELAKLR GLEAAQIKEL
EELRQTVKQL KEQLAKKEKE HASGSGAQSE AAGRTEPTGP KLEALRAEVS KLEQQCQKQQ
EQADSLERSL EAERASRAER DSALETLQGQ LEEKAQELGH SQSALASAQR ELAAFRTKVQ
DHSKAEDEWK AQVARGRQEA ERKNSLISSL EEEVSILNRQ VLEKEGESKE LKRLVMAESE
KSQKLEERLR LLQAETASNS ARAAERSSAL REEVQSLREE AEKQRVASEN LRQELTSQAE
RAEELGQELK AWQEKFFQKE QALSTLQLEH TSTQALVSEL LPAKHLCQQL QAEQAAAEKR
HREELEQSKQ AAGGLRAELL RAQRELGELI PLRQKVAEQE RTAQQLRAEK ASYAEQLSML
KKAHGLLAEE NRGLGERANL GRQFLEVELD QAREKYVQEL AAVRADAETR LAEVQREAQS
TARELEVMTA KYEGAKVKVL EERQRFQEER QKLTAQVEQL EVFQREQTKQ VEELSKKLAD
SDQASKVQQQ KLKAVQAQGG ESQQEAQRLQ AQLNELQAQL SQKEQAAEHY KLQMEKAKTH
YDAKKQQNQE LQEQLRSLEQ LQKENKELRA EAERLGHELQ QAGLKTKEAE QTCRHLTAQV
RSLEAQVAHA DQQLRDLGKF QVATDALKSR EPQAKPQLDL SIDSLDLSCE EGTPLSITSK
LPRTQPDGTS VPGEPASPIS QRLPPKVESL ESLYFTPIPA RSQAPLESSL DSLGDVFLDS
GRKTRSARRR TTQIINITMT KKLDVEEPDS ANSSFYSTRS APASQASLRA TSSTQSLARL
GSPDYGNSAL LSLPGYRPTT RSSARRSQAG VSSGAPPGRN SFYMGTCQDE PEQLDDWNRI
AELQQRNRVC PPHLKTCYPL ESRPSLSLGT ITDEEMKTGD PQETLRRASM QPIQIAEGTG
ITTRQQRKRV SLEPHQGPGT PESKKATSCF PRPMTPRDRH EGRKQSTTEA QKKAAPASTK
QADRRQSMAF SILNTPKKLG NSLLRRGASK KALSKASPNT RSGTRRSPRI ATTTASAATA
AAIGATPRAK GKAKH
