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Nuclear mitotic apparatus protein 1 (Nuclear matrix protein-22) (NMP-22) (Nuclear mitotic apparatus protein) (NuMA protein) (SP-H antigen)

 NUMA1_HUMAN             Reviewed;        2115 AA.
Q14980; H0YH75; Q14981; Q9BTE9;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
17-APR-2007, sequence version 2.
22-NOV-2017, entry version 163.
RecName: Full=Nuclear mitotic apparatus protein 1 {ECO:0000312|HGNC:HGNC:8059};
AltName: Full=Nuclear matrix protein-22 {ECO:0000303|PubMed:9730450};
Short=NMP-22 {ECO:0000303|PubMed:9730450};
AltName: Full=Nuclear mitotic apparatus protein {ECO:0000303|PubMed:1541630, ECO:0000303|PubMed:1541636};
Short=NuMA protein {ECO:0000303|PubMed:1541630, ECO:0000303|PubMed:1541636};
AltName: Full=SP-H antigen {ECO:0000303|PubMed:8408288};
Name=NUMA1 {ECO:0000312|HGNC:HGNC:8059};
Synonyms=NMP22 {ECO:0000303|PubMed:9730450},
NUMA {ECO:0000303|PubMed:1541630};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
PubMed=1541630; DOI=10.1083/jcb.116.6.1303;
Yang C.H., Lambie E.J., Snyder M.;
"NuMA: an unusually long coiled-coil related protein in the mammalian
nucleus.";
J. Cell Biol. 116:1303-1317(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND SUBCELLULAR LOCATION.
PubMed=1541636; DOI=10.1083/jcb.116.6.1395;
Compton D.A., Szilak I., Cleveland D.W.;
"Primary structure of NuMA, an intranuclear protein that defines a
novel pathway for segregation of proteins at mitosis.";
J. Cell Biol. 116:1395-1408(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8408288;
Maekawa T., Kuriyama R.;
"Primary structure and microtubule-interacting domain of the SP-H
antigen: a mitotic map located at the spindle pole characterized as a
homologous protein to NuMA.";
J. Cell Sci. 105:589-600(1993).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1576-2115 (ISOFORM 1), NUCLEOTIDE
SEQUENCE [MRNA] OF 975-1776 (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF
610-1763 (ISOFORM 4), AND ALTERNATIVE SPLICING.
PubMed=8505359;
Tang T.K., Tang C.J., Chen Y.L., Wu C.W.;
"Nuclear proteins of the bovine esophageal epithelium. II. The NuMA
gene gives rise to multiple mRNAs and gene products reactive with
monoclonal antibody W1.";
J. Cell Sci. 104:249-260(1993).
[8]
SUBCELLULAR LOCATION (ISOFORMS 3 AND 4), ALTERNATIVE SPLICING
(ISOFORMS 3 AND 4), MUTAGENESIS OF ARG-1984 AND LYS-1988, AND NUCLEAR
LOCALIZATION SIGNAL.
PubMed=7962183;
Tang T.K., Tang C.J., Chao Y.J., Wu C.W.;
"Nuclear mitotic apparatus protein (NuMA): spindle association,
nuclear targeting and differential subcellular localization of various
NuMA isoforms.";
J. Cell Sci. 107:1389-1402(1994).
[9]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-2015; THR-2055;
SER-2087 AND THR-2106, AND MUTAGENESIS OF THR-2015; THR-2055; SER-2087
AND THR-2106.
PubMed=7769006;
Compton D.A., Luo C.;
"Mutation of the predicted p34cdc2 phosphorylation sites in NuMA
impair the assembly of the mitotic spindle and block mitosis.";
J. Cell Sci. 108:621-633(1995).
[10]
USE IN DIAGNOSTIC TESTS.
PubMed=9730450; DOI=10.1016/S0090-4295(98)00219-2;
Landman J., Chang Y., Kavaler E., Droller M.J., Liu B.C.;
"Sensitivity and specificity of NMP-22, telomerase, and BTA in the
detection of human bladder cancer.";
Urology 52:398-402(1998).
[11]
SUBCELLULAR LOCATION, AND ASSOCIATION WITH THE DYNEIN-DYNACTIN
COMPLEX.
PubMed=10811826;
Merdes A., Heald R., Samejima K., Earnshaw W.C., Cleveland D.W.;
"Formation of spindle poles by dynein/dynactin-dependent transport of
NuMA.";
J. Cell Biol. 149:851-862(2000).
[12]
FUNCTION, AND INTERACTION WITH THE IMPORTIN ALPHA/IMPORTIN BETA
RECEPTOR.
PubMed=11163243;
Nachury M.V., Maresca T.J., Salmon W.C., Waterman-Storer C.M.,
Heald R., Weis K.;
"Importin beta is a mitotic target of the small GTPase Ran in spindle
assembly.";
Cell 104:95-106(2001).
[13]
INTERACTION WITH GPSM2, AND SUBCELLULAR LOCATION.
PubMed=11781568; DOI=10.1038/ncb1201-1069;
Du Q., Stukenberg P.T., Macara I.G.;
"A mammalian partner of inscuteable binds NuMA and regulates mitotic
spindle organization.";
Nat. Cell Biol. 3:1069-1075(2001).
[14]
FUNCTION, AND INTERACTION WITH KPNB1.
PubMed=11229403;
Wiese C., Wilde A., Moore M.S., Adam S.A., Merdes A., Zheng Y.;
"Role of importin-beta in coupling Ran to downstream targets in
microtubule assembly.";
Science 291:653-656(2001).
[15]
FUNCTION, INTERACTION WITH GPSM2 AND MICROTUBULES, SUBCELLULAR
LOCATION, AND DOMAINS.
PubMed=12445386;
Du Q., Taylor L., Compton D.A., Macara I.G.;
"LGN blocks the ability of NuMA to bind and stabilize microtubules. A
mechanism for mitotic spindle assembly regulation.";
Curr. Biol. 12:1928-1933(2002).
[16]
INTERACTION WITH TNKS AND TNKS2.
PubMed=12080061; DOI=10.1074/jbc.M203916200;
Sbodio J.I., Chi N.W.;
"Identification of a tankyrase-binding motif shared by IRAP, TAB182,
and human TRF1 but not mouse TRF1. NuMA contains this RXXPDG motif and
is a novel tankyrase partner.";
J. Biol. Chem. 277:31887-31892(2002).
[17]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TUBULIN AND
MICROTUBULES, AND TUBULIN-BINDING DOMAIN.
PubMed=11956313;
Haren L., Merdes A.;
"Direct binding of NuMA to tubulin is mediated by a novel sequence
motif in the tail domain that bundles and stabilizes microtubules.";
J. Cell Sci. 115:1815-1824(2002).
[18]
FUNCTION, ADP-RIBOSYLATION, INTERACTION WITH TNKS, AND SUBCELLULAR
LOCATION.
PubMed=16076287; DOI=10.1042/BJ20050428;
Chang W., Dynek J.N., Smith S.;
"NuMA is a major acceptor of poly(ADP-ribosyl)ation by tankyrase 1 in
mitosis.";
Biochem. J. 391:177-184(2005).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1757, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1757; SER-1769;
THR-1776; SER-1840 AND THR-2106, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[22]
FUNCTION, AND INTERACTION WITH DYNEIN-DYNACTIN COMPLEX AND RAE1.
PubMed=17172455; DOI=10.1073/pnas.0609582104;
Wong R.W., Blobel G., Coutavas E.;
"Rae1 interaction with NuMA is required for bipolar spindle
formation.";
Proc. Natl. Acad. Sci. U.S.A. 103:19783-19787(2006).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2077, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388; SER-395; SER-820;
SER-1601; SER-1757 AND SER-1760, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1757, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1757, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-203; THR-211;
SER-1721; SER-1724; SER-1728; SER-1757; SER-1769; SER-1772; TYR-1774;
THR-1776; SER-1788; SER-1789; SER-1792; SER-1800; THR-1804; SER-1830;
SER-1833; SER-1834; TYR-1836; SER-1840; SER-1862; SER-1887; SER-1969;
SER-1991 AND THR-2000, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[29]
FUNCTION.
PubMed=19255246; DOI=10.1083/jcb.200810091;
Silk A.D., Holland A.J., Cleveland D.W.;
"Requirements for NuMA in maintenance and establishment of mammalian
spindle poles.";
J. Cell Biol. 184:677-690(2009).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-1225; SER-1757;
SER-1769; THR-1776; SER-1788 AND SER-1800, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[31]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-379; LYS-891 AND LYS-1511,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[32]
GLYCOSYLATION AT SER-1844.
PubMed=20068230; DOI=10.1126/scisignal.2000526;
Wang Z., Udeshi N.D., Slawson C., Compton P.D., Sakabe K.,
Cheung W.D., Shabanowitz J., Hunt D.F., Hart G.W.;
"Extensive crosstalk between O-GlcNAcylation and phosphorylation
regulates cytokinesis.";
Sci. Signal. 3:RA2-RA2(2010).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-203; THR-211;
SER-271; SER-1187; SER-1225; SER-1757; SER-1769; SER-1830; SER-1862;
SER-1969; SER-1991; THR-2000 AND SER-2003, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[34]
REVIEW.
PubMed=20137953; DOI=10.1016/j.tcb.2010.01.003;
Radulescu A.E., Cleveland D.W.;
"NuMA after 30 years: the matrix revisited.";
Trends Cell Biol. 20:214-222(2010).
[35]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1757, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[37]
FUNCTION, AND INTERACTION WITH DYNEIN-DYNACTIN COMPLEX.
PubMed=23027904; DOI=10.1083/jcb.201203166;
Kotak S., Busso C., Goenczy P.;
"Cortical dynein is critical for proper spindle positioning in human
cells.";
J. Cell Biol. 199:97-110(2012).
[38]
FUNCTION, INTERACTION WITH GPSM2, SUBCELLULAR LOCATION,
PHOSPHORYLATION AT THR-1047; SER-1769; SER-1772; SER-1789 AND SER-1834
BY PLK1, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=22327364; DOI=10.1038/ncb2440;
Kiyomitsu T., Cheeseman I.M.;
"Chromosome- and spindle-pole-derived signals generate an intrinsic
code for spindle position and orientation.";
Nat. Cell Biol. 14:311-317(2012).
[39]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[40]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EPB41 AND EPB41L2,
PROBABLE PHOSPHORYLATION AT THR-2015; THR-2055 AND SER-2087 BY CDK1,
AND MUTAGENESIS OF THR-2015; THR-2055 AND SER-2087.
PubMed=23870127; DOI=10.1016/j.cell.2013.06.010;
Kiyomitsu T., Cheeseman I.M.;
"Cortical dynein and asymmetric membrane elongation coordinately
position the spindle in anaphase.";
Cell 154:391-402(2013).
[41]
FUNCTION, PHOSPHORYLATION AT THR-2015; THR-2055; SER-2087 AND
THR-2106, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY,
AND MUTAGENESIS OF THR-2055.
PubMed=23921553; DOI=10.1038/emboj.2013.172;
Kotak S., Busso C., Goenczy P.;
"NuMA phosphorylation by CDK1 couples mitotic progression with
cortical dynein function.";
EMBO J. 32:2517-2529(2013).
[42]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-271; SER-1757;
SER-1769; SER-1830; SER-1834; SER-1840; SER-1844; SER-1862; SER-1887;
SER-1969; SER-1991; THR-2000; SER-2047; THR-2055 AND SER-2062, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[43]
FUNCTION, INTERACTION WITH GPSM2, SUBCELLULAR LOCATION, DOMAIN, AND
MUTAGENESIS OF THR-2055.
PubMed=24109598; DOI=10.1091/mbc.E13-05-0277;
Seldin L., Poulson N.D., Foote H.P., Lechler T.;
"NuMA localization, stability, and function in spindle orientation
involve 4.1 and Cdk1 interactions.";
Mol. Biol. Cell 24:3651-3662(2013).
[44]
FUNCTION, INTERACTION WITH EPB41 AND EPB41L2,
PHOSPHATIDYLINOSITOL-BINDING, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
THR-2055.
PubMed=24996901; DOI=10.15252/embj.201488147;
Kotak S., Busso C., Goenczy P.;
"NuMA interacts with phosphoinositides and links the mitotic spindle
with the plasma membrane.";
EMBO J. 33:1815-1830(2014).
[45]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; THR-163; SER-169;
SER-271; SER-1225; SER-1757 AND SER-1788, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[46]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-2055, DOMAIN,
PHOSPHATIDYLINOSITOL-BINDING, AND MUTAGENESIS OF THR-2055.
PubMed=24371089; DOI=10.1091/mbc.E13-08-0474;
Zheng Z., Wan Q., Meixiong G., Du Q.;
"Cell cycle-regulated membrane binding of NuMA contributes to
efficient anaphase chromosome separation.";
Mol. Biol. Cell 25:606-619(2014).
[47]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1766, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[48]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1766, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[49]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1766, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[50]
FUNCTION, SUBUNIT, UBIQUITINATION, INTERACTION WITH ABRAXAS2; KPNB1
AND DYNEIN-DYNACTIN COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, AND
SUBCELLULAR LOCATION.
PubMed=26195665; DOI=10.1083/jcb.201503039;
Yan K., Li L., Wang X., Hong R., Zhang Y., Yang H., Lin M., Zhang S.,
He Q., Zheng D., Tang J., Yin Y., Shao G.;
"The deubiquitinating enzyme complex BRISC is required for proper
mitotic spindle assembly in mammalian cells.";
J. Cell Biol. 210:209-224(2015).
[51]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=25657325; DOI=10.1091/mbc.E14-09-1366;
Ohta S., Wood L., Toramoto I., Yagyu K., Fukagawa T., Earnshaw W.C.;
"CENP-32 is required to maintain centrosomal dominance in bipolar
spindle assembly.";
Mol. Biol. Cell 26:1225-1237(2015).
[52]
SUBCELLULAR LOCATION.
PubMed=26562023; DOI=10.1371/journal.pone.0142798;
Ohta S., Hamada M., Sato N., Toramoto I.;
"Polyglutamylated tubulin binding protein C1orf96/CSAP is involved in
microtubule stabilization in mitotic spindles.";
PLoS ONE 10:E0142798-E0142798(2015).
[53]
IDENTIFICATION IN A SPINDLE ORIENTATION COMPLEX.
PubMed=26766442; DOI=10.1016/j.devcel.2015.12.016;
Chiu C.W., Monat C., Robitaille M., Lacomme M., Daulat A.M.,
Macleod G., McNeill H., Cayouette M., Angers S.;
"SAPCD2 controls spindle orientation and asymmetric divisions by
negatively regulating the Galphai-LGN-NuMA ternary complex.";
Dev. Cell 36:50-62(2016).
[54]
FUNCTION, INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION, DOMAIN,
AND NUCLEAR LOCALIZATION SIGNAL.
PubMed=26765568; DOI=10.7554/eLife.12504;
Seldin L., Muroyama A., Lechler T.;
"NuMA-microtubule interactions are critical for spindle orientation
and the morphogenesis of diverse epidermal structures.";
Elife 5:0-0(2016).
[55]
FUNCTION, INTERACTION WITH GPSM2 AND SPAG5, AND SUBCELLULAR LOCATION.
PubMed=27462074; DOI=10.1074/jbc.M116.724831;
Chu X., Chen X., Wan Q., Zheng Z., Du Q.;
"Nuclear mitotic apparatus (NuMA) interacts with and regulates astrin
at the mitotic spindle.";
J. Biol. Chem. 291:20055-20067(2016).
[56]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1699; LYS-1766 AND LYS-1822,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[57]
ELECTRON MICROSCOPY, SUBUNIT, SUBCELLULAR LOCATION, AND PUTATIVE
STRUCTURAL FUNCTION.
PubMed=10075938; DOI=10.1093/emboj/18.6.1689;
Harborth J., Wang J., Gueth-Hallonet C., Weber K., Osborn M.;
"Self assembly of NuMA: multiarm oligomers as structural units of a
nuclear lattice.";
EMBO J. 18:1689-1700(1999).
[58]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1899-1926 IN COMPLEX WITH
GPSM2, FUNCTION, INTERACTION WITH GPSM2, SUBCELLULAR LOCATION,
MUTAGENESIS OF GLU-1910, AND DOMAIN.
PubMed=21816348; DOI=10.1016/j.molcel.2011.07.011;
Zhu J., Wen W., Zheng Z., Shang Y., Wei Z., Xiao Z., Pan Z., Du Q.,
Wang W., Zhang M.;
"LGN/mInsc and LGN/NuMA complex structures suggest distinct functions
in asymmetric cell division for the Par3/mInsc/LGN and
Galphai/LGN/NuMA pathways.";
Mol. Cell 43:418-431(2011).
-!- FUNCTION: Microtubule (MT)-binding protein that plays a role in
the formation and maintenance of the spindle poles and the
alignement and the segregation of chromosomes during mitotic cell
division (PubMed:7769006, PubMed:17172455, PubMed:19255246,
PubMed:24996901, PubMed:26195665, PubMed:27462074). Functions to
tether the minus ends of MTs at the spindle poles, which is
critical for the establishment and maintenance of the spindle
poles (PubMed:12445386, PubMed:11956313). Plays a role in the
establishment of the mitotic spindle orientation during metaphase
and elongation during anaphase in a dynein-dynactin-dependent
manner (PubMed:23870127, PubMed:24109598, PubMed:24996901,
PubMed:26765568). In metaphase, part of a ternary complex composed
of GPSM2 and G(i) alpha proteins, that regulates the recruitment
and anchorage of the dynein-dynactin complex in the mitotic cell
cortex regions situated above the two spindle poles, and hence
regulates the correct oritentation of the mitotic spindle
(PubMed:23027904, PubMed:22327364, PubMed:23921553). During
anaphase, mediates the recruitment and accumulation of the dynein-
dynactin complex at the cell membrane of the polar cortical region
through direct association with phosphatidylinositol 4,5-
bisphosphate (PI(4,5)P2), and hence participates in the regulation
of the spindle elongation and chromosome segregation
(PubMed:22327364, PubMed:23921553, PubMed:24996901,
PubMed:24371089). Binds also to other polyanionic
phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP),
lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate
(PIP3), in vitro (PubMed:24996901, PubMed:24371089). Also required
for proper orientation of the mitotic spindle during asymmetric
cell divisions (PubMed:21816348). Plays a role in mitotic MT aster
assembly (PubMed:11163243, PubMed:11229403, PubMed:12445386).
Involved in anastral spindle assembly (PubMed:25657325).
Positively regulates TNKS protein localization to spindle poles in
mitosis (PubMed:16076287). Highly abundant component of the
nuclear matrix where it may serve a non-mitotic structural role,
occupies the majority of the nuclear volume (PubMed:10075938).
Required for epidermal differentiation and hair follicle
morphogenesis (By similarity). {ECO:0000250|UniProtKB:E9Q7G0,
ECO:0000269|PubMed:11163243, ECO:0000269|PubMed:11229403,
ECO:0000269|PubMed:11956313, ECO:0000269|PubMed:12445386,
ECO:0000269|PubMed:16076287, ECO:0000269|PubMed:17172455,
ECO:0000269|PubMed:19255246, ECO:0000269|PubMed:22327364,
ECO:0000269|PubMed:23027904, ECO:0000269|PubMed:23870127,
ECO:0000269|PubMed:23921553, ECO:0000269|PubMed:24109598,
ECO:0000269|PubMed:24371089, ECO:0000269|PubMed:24996901,
ECO:0000269|PubMed:25657325, ECO:0000269|PubMed:26195665,
ECO:0000269|PubMed:26765568, ECO:0000269|PubMed:27462074,
ECO:0000269|PubMed:7769006, ECO:0000305|PubMed:10075938,
ECO:0000305|PubMed:21816348}.
-!- SUBUNIT: Homodimer (PubMed:10075938). Also forms multiarm
oligomers by association of C-terminal tail domains, oligomers may
further assemble to form a hexagonal nuclear lattice-like network
(PubMed:10075938). Associates with the dynein-dynactin complex;
this association promotes the transport and accumulation of NUMA1
at the mitotic spindle poles that is inhibited by the BRISC
complex in a PLK1-dependent manner (PubMed:10811826,
PubMed:17172455, PubMed:23027904, PubMed:22327364,
PubMed:26195665). Part of a spindle orientation complex at least
composed of GNAI1, GPSM2 and NUMA1 (PubMed:26766442). Interacts
(via C-terminus) with microtubules (MTs); this interaction is
direct and promotes both MT bundle formation and stability in a
dynein-dynactin complex- and CDK1-independent manner
(PubMed:12445386, PubMed:11956313, PubMed:26765568). Interacts
with EPB41 and EPB41L2; these interactions are negatively
regulated by CDK1 during metaphase and are important for anaphase-
specific localization of NUMA1 in symmetrically dividing cells
(PubMed:23870127, PubMed:24996901). Interacts (via C-terminus)
with GPSM2 (via TPR repeats); this interaction is direct,
prevented by competitive binding of INSC, is inhibited in a PLK1-
dependent manner, blocks the association of NUMA1 with MTs and
inhibits NUMA1-induced MT bundle formation, prevents the
association of NUMA1 with SPAG5, induces mitotic spindle pole
localization of GPSM2, both metaphase cell cortex localization of
NUMA1 and mitotic spindle organization (PubMed:11781568,
PubMed:12445386, PubMed:22327364, PubMed:24109598,
PubMed:27462074, PubMed:21816348). Does not interact with GPSM2
during anaphase (PubMed:23870127). Interacts (via C-terminus) with
the nuclear importin alpha/importin beta receptor; this
interaction is inhibited by RanGTP (PubMed:11163243). Interacts
(via C-terminus) with KPNB1; this interaction is inhibited by
RanGTP and the BRISC complex (PubMed:11229403, PubMed:26195665).
Interacts with ABRAXAS2 and the BRISC complex; these interactions
regulate mitotic spindle assembly (PubMed:26195665). Interacts
(via N-terminal end of the coiled-coil domain) with RAE1; this
interaction promotes mitotic spindle formation (PubMed:17172455).
Interacts (via C-terminus) with SPAG5 (via C-terminus); this
interaction promotes the recruitment of SPAG5 to the MTs at
spindle poles in a dynein-dynactin-dependent manner and regulates
mitotic spindle organization and proper chromosome alignment
during mitosis (PubMed:27462074). Interacts with TNKS; this
interaction occurs at the onset of mitosis (PubMed:12080061,
PubMed:16076287). Interacts with TNKS2 (PubMed:12080061).
Interacts with tubulin (PubMed:11956313).
{ECO:0000269|PubMed:10075938, ECO:0000269|PubMed:10811826,
ECO:0000269|PubMed:11163243, ECO:0000269|PubMed:11229403,
ECO:0000269|PubMed:11781568, ECO:0000269|PubMed:11956313,
ECO:0000269|PubMed:12080061, ECO:0000269|PubMed:12445386,
ECO:0000269|PubMed:16076287, ECO:0000269|PubMed:17172455,
ECO:0000269|PubMed:21816348, ECO:0000269|PubMed:22327364,
ECO:0000269|PubMed:23027904, ECO:0000269|PubMed:23870127,
ECO:0000269|PubMed:24109598, ECO:0000269|PubMed:24996901,
ECO:0000269|PubMed:26195665, ECO:0000269|PubMed:26765568,
ECO:0000269|PubMed:26766442, ECO:0000269|PubMed:27462074}.
-!- INTERACTION:
Q2TAC2:CCDC57; NbExp=3; IntAct=EBI-521611, EBI-2808286;
Q53SE7:FLJ13057; NbExp=3; IntAct=EBI-521611, EBI-10172181;
P63096:GNAI1; NbExp=4; IntAct=EBI-521611, EBI-618639;
P81274:GPSM2; NbExp=6; IntAct=EBI-521611, EBI-618655;
Q8VDU0:Gpsm2 (xeno); NbExp=2; IntAct=EBI-10981450, EBI-7575403;
P78406:RAE1; NbExp=6; IntAct=EBI-521611, EBI-724495;
Q9NYB0:TERF2IP; NbExp=2; IntAct=EBI-521611, EBI-750109;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1541630,
ECO:0000269|PubMed:23921553, ECO:0000269|PubMed:27462074}.
Nucleus, nucleoplasm {ECO:0000269|PubMed:10811826}. Nucleus matrix
{ECO:0000269|PubMed:10075938, ECO:0000269|PubMed:11956313,
ECO:0000269|PubMed:1541636, ECO:0000269|PubMed:7962183}.
Chromosome {ECO:0000269|PubMed:1541630}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:11956313, ECO:0000269|PubMed:12445386,
ECO:0000269|PubMed:26765568}. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:10811826,
ECO:0000269|PubMed:1541630, ECO:0000269|PubMed:1541636,
ECO:0000269|PubMed:25657325, ECO:0000269|PubMed:26562023,
ECO:0000269|PubMed:26765568}. Cytoplasm, cytoskeleton, spindle
pole {ECO:0000269|PubMed:10811826, ECO:0000269|PubMed:11781568,
ECO:0000269|PubMed:11956313, ECO:0000269|PubMed:12445386,
ECO:0000269|PubMed:1541630, ECO:0000269|PubMed:1541636,
ECO:0000269|PubMed:16076287, ECO:0000269|PubMed:21816348,
ECO:0000269|PubMed:22327364, ECO:0000269|PubMed:23870127,
ECO:0000269|PubMed:23921553, ECO:0000269|PubMed:24109598,
ECO:0000269|PubMed:24996901, ECO:0000269|PubMed:25657325,
ECO:0000269|PubMed:26195665, ECO:0000269|PubMed:26562023,
ECO:0000269|PubMed:27462074, ECO:0000269|PubMed:7769006,
ECO:0000269|PubMed:7962183}. Cytoplasm, cell cortex
{ECO:0000269|PubMed:21816348, ECO:0000269|PubMed:22327364,
ECO:0000269|PubMed:23870127, ECO:0000269|PubMed:23921553,
ECO:0000269|PubMed:24109598, ECO:0000269|PubMed:24996901}. Cell
membrane {ECO:0000269|PubMed:24371089,
ECO:0000269|PubMed:24996901}; Lipid-anchor
{ECO:0000269|PubMed:24371089, ECO:0000269|PubMed:24996901};
Cytoplasmic side {ECO:0000269|PubMed:24371089,
ECO:0000269|PubMed:24996901}. Lateral cell membrane
{ECO:0000250|UniProtKB:E9Q7G0}. Note=Mitotic cell cycle-dependent
shuttling protein that relocalizes from the interphase nucleus to
the spindle poles and cell cortex (PubMed:1541636,
PubMed:10811826). In interphase, resides in the nuclear matrix
(PubMed:1541630, PubMed:1541636, PubMed:23921553). In prophase,
restricted to the interchromatin or condensed chromosome space
(PubMed:10811826). In prometaphase, after nuclear envelope
disassembly, forms aggregates both in the spindle midzone and at
duplicated centrosomes and astral microtubules (MTs) of the
bipolar spindle apparatus (PubMed:10811826). Translocates from the
spindle midzone towards the spindle poles along spindle fibers in
a MT- and dynein-dynactin-dependent manner until the anaphase
onset (PubMed:1541636, PubMed:10811826). In metaphase, recruited
to the polar cortical region in a GPSM2- and GNAI1-dependent
manner (PubMed:23870127, PubMed:24109598, PubMed:24996901).
Excluded from the metaphase equatorial cortical region in a
RanGTP-dependent manner (PubMed:22327364, PubMed:23870127).
Phosphorylation on Thr-2055 by CDK1 results in its localization at
spindle poles in metaphase, but not at the cell cortex
(PubMed:23921553). In anaphase, recruited and anchored at the cell
membrane of the polar cortical region in a EPB41-, EPB41L2-,
phosphatidylinositol-dependent and GPSM2- and G(i) alpha proteins-
independent manner (PubMed:23870127, PubMed:24996901,
PubMed:24109598, PubMed:24371089). Excluded from the anaphase
equatorial region of the cell cortex in a RACGAP1- and KIF23-
dependent and RanGTP-independent manner (PubMed:24996901).
Associated with astral MTs emanating from the spindle poles during
anaphase (PubMed:12445386, PubMed:24996901). Nonphosphorylated
Thr-2055 localizes at the cell cortex, weakly during metaphase and
more prominently during anaphase in a phosphatase PPP2CA-dependent
manner (PubMed:23921553). As mitosis progresses it reassociates
with telophase chromosomes very early during nuclear reformation,
before substantial accumulation of lamins on chromosomal surfaces
is evident (PubMed:1541636). Localizes to the tips of cortical MTs
in prometaphase (PubMed:26765568). Localizes along MTs and
specifically to both MT plus and minus ends (PubMed:26765568).
Accumulates also at MT tips near the cell periphery
(PubMed:26765568). Colocalizes with GPSM2 at mitotic spindle poles
during mitosis (PubMed:11781568, PubMed:21816348). Colocalizes
with SPAG5 at mitotic spindle at prometaphase and at mitotic
spindle poles at metaphase and anaphase (PubMed:27462074).
Colocalizes with ABRO1 at mitotic spindle poles (PubMed:26195665).
Colocalized with TNKS from prophase through to anaphase in mitosis
(PubMed:16076287). Colocalizes with tubulin alpha
(PubMed:12445386). CCSAP is essential for its centrosomal
localization (PubMed:26562023). In horizontally retinal progenitor
dividing cells, localized to the lateral cortical region (By
similarity). {ECO:0000250|UniProtKB:E9Q7G0,
ECO:0000269|PubMed:10811826, ECO:0000269|PubMed:11781568,
ECO:0000269|PubMed:12445386, ECO:0000269|PubMed:1541630,
ECO:0000269|PubMed:1541636, ECO:0000269|PubMed:16076287,
ECO:0000269|PubMed:21816348, ECO:0000269|PubMed:22327364,
ECO:0000269|PubMed:23870127, ECO:0000269|PubMed:23921553,
ECO:0000269|PubMed:24109598, ECO:0000269|PubMed:24371089,
ECO:0000269|PubMed:24996901, ECO:0000269|PubMed:26195665,
ECO:0000269|PubMed:26562023, ECO:0000269|PubMed:26765568,
ECO:0000269|PubMed:27462074}.
-!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm, cytosol
{ECO:0000269|PubMed:7962183}. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:7962183}.
Cytoplasm, cytoskeleton, spindle pole
{ECO:0000269|PubMed:7962183}. Note=During interphase, mainly
clustered at the centrosomal region in the cytosol. After entry
into mitosis, detected at mitotic spindle poles.
{ECO:0000269|PubMed:7962183}.
-!- SUBCELLULAR LOCATION: Isoform 4: Cytoplasm, cytosol
{ECO:0000269|PubMed:7962183}. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:7962183}.
Cytoplasm, cytoskeleton, spindle pole
{ECO:0000269|PubMed:7962183}. Note=During interphase, mainly
clustered at the centrosomal region in the cytosol. After entry
into mitosis, detected at mitotic spindle poles.
{ECO:0000269|PubMed:7962183}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=Numa-1, p230;
IsoId=Q14980-1; Sequence=Displayed;
Name=2;
IsoId=Q14980-2; Sequence=VSP_012910;
Note=No experimental confirmation available.;
Name=3; Synonyms=Numa-m {ECO:0000303|PubMed:7962183}, p195;
IsoId=Q14980-3; Sequence=VSP_044378;
Name=4; Synonyms=Numa-s {ECO:0000303|PubMed:7962183}, p194;
IsoId=Q14980-4; Sequence=VSP_044379;
Name=5;
IsoId=Q14980-5; Sequence=VSP_054146;
Note=No experimental confirmation available.;
-!- DOMAIN: The C-terminal tubulin-binding domain mediates direct
binding to microtubules, independently of dynein-dynactin complex,
and induces their bundling and stabilization (PubMed:11956313).
The 4.1-binding domain is necessary for its cortical stability and
spindle orientation (PubMed:24109598).
{ECO:0000269|PubMed:11956313, ECO:0000269|PubMed:24109598}.
-!- PTM: Phosphorylation and dephosphorylation on Thr-2055 regulates
the extent of cortical NUMA1 and the dynein-dynactin complex
localization during mitotic metaphase and anaphase
(PubMed:23921553). In metaphase, phosphorylation on Thr-2055
occurs in a kinase CDK1-dependent manner; this phosphorylation
maintains low levels of cortical dynein-dynactin complex at
metaphase, and hence proper spindle positioning (PubMed:7769006,
PubMed:23921553, PubMed:24371089). In anaphase, dephosphorylated
on Thr-2055 by phosphatase PPP2CA; this dephosphorylation
stimulates its membrane association and with the dynein-dynactin
complex its enrichment at the cell cortex, and hence robust
spindle elongation (PubMed:23921553, PubMed:24371089). Probably
also phosphorylated on Thr-2015 and Ser-2087 by CDK1; these
phosphorylations may regulate its cell cortex recruitment during
metaphase and anaphase (PubMed:23870127). Phosphorylated on Thr-
1047, Ser-1769, Ser-1772, Ser-1789 and Ser-1834 by PLK1; these
phosphorylations induce cortical dynein-dynactin complex
dissociation from the NUMA1-GPSM2 complex and negatively regulates
cortical dynein-dynactin complex localization (PubMed:22327364).
{ECO:0000269|PubMed:22327364, ECO:0000269|PubMed:23870127,
ECO:0000269|PubMed:23921553, ECO:0000269|PubMed:24371089,
ECO:0000269|PubMed:7769006}.
-!- PTM: ADP-ribosylated by TNKS at the onset of mitosis; ADP-
ribosylation is not required for its localization to spindle poles
(PubMed:16076287). {ECO:0000269|PubMed:16076287}.
-!- PTM: O-glycosylated during cytokinesis at sites identical or close
to phosphorylation sites, this interferes with the phosphorylation
status (PubMed:20068230). {ECO:0000269|PubMed:20068230}.
-!- PTM: Ubiquitinated with 'Lys-63'-linked polyubiquitin chains.
Deubiquitination by the BRISC complex is important for the
incorporation of NUMA1 into mitotic spindle poles and normal
spindle pole function, probably by modulating interactions between
NUMA1, dynein-dynactin complex and importin-beta.
{ECO:0000269|PubMed:26195665}.
-!- MISCELLANEOUS: Also known as nuclear matrix protein-22/NMP-
22/NMP22, an antigen used in diagnostic tests of bladder cancer.
{ECO:0000269|PubMed:9730450}.
-!- SEQUENCE CAUTION:
Sequence=CAA77670.1; Type=Frameshift; Positions=1270, 1299; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/NUMAID119.html";
-----------------------------------------------------------------------
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EMBL; Z14227; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; Z14228; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; Z14229; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; Z11583; CAA77669.1; -; mRNA.
EMBL; Z11584; CAA77670.1; ALT_FRAME; mRNA.
EMBL; AP002490; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471076; EAW74826.1; -; Genomic_DNA.
EMBL; BC004165; AAH04165.1; -; mRNA.
CCDS; CCDS31633.1; -. [Q14980-1]
CCDS; CCDS66156.1; -. [Q14980-2]
PIR; A42184; A42184.
RefSeq; NP_001273490.1; NM_001286561.1. [Q14980-2]
RefSeq; NP_006176.2; NM_006185.3. [Q14980-1]
RefSeq; XP_006718627.1; XM_006718564.1. [Q14980-1]
UniGene; Hs.325978; -.
UniGene; Hs.591967; -.
PDB; 3RO2; X-ray; 2.30 A; B=1899-1926.
PDB; 5GXW; X-ray; 2.39 A; B=1984-2010.
PDBsum; 3RO2; -.
PDBsum; 5GXW; -.
ProteinModelPortal; Q14980; -.
SMR; Q14980; -.
BioGrid; 110980; 105.
CORUM; Q14980; -.
DIP; DIP-32937N; -.
ELM; Q14980; -.
IntAct; Q14980; 39.
MINT; MINT-1489811; -.
STRING; 9606.ENSP00000377298; -.
iPTMnet; Q14980; -.
PhosphoSitePlus; Q14980; -.
SwissPalm; Q14980; -.
BioMuta; NUMA1; -.
DMDM; 145559510; -.
EPD; Q14980; -.
MaxQB; Q14980; -.
PaxDb; Q14980; -.
PeptideAtlas; Q14980; -.
PRIDE; Q14980; -.
DNASU; 4926; -.
Ensembl; ENST00000351960; ENSP00000260051; ENSG00000137497. [Q14980-5]
Ensembl; ENST00000358965; ENSP00000351851; ENSG00000137497. [Q14980-2]
Ensembl; ENST00000393695; ENSP00000377298; ENSG00000137497. [Q14980-1]
Ensembl; ENST00000613205; ENSP00000480172; ENSG00000137497. [Q14980-5]
Ensembl; ENST00000620566; ENSP00000478624; ENSG00000137497. [Q14980-2]
GeneID; 4926; -.
KEGG; hsa:4926; -.
UCSC; uc001ork.3; human. [Q14980-1]
CTD; 4926; -.
DisGeNET; 4926; -.
EuPathDB; HostDB:ENSG00000137497.17; -.
GeneCards; NUMA1; -.
H-InvDB; HIX0026234; -.
HGNC; HGNC:8059; NUMA1.
HPA; HPA019841; -.
HPA; HPA019859; -.
HPA; HPA029912; -.
MalaCards; NUMA1; -.
MIM; 164009; gene.
neXtProt; NX_Q14980; -.
OpenTargets; ENSG00000137497; -.
Orphanet; 520; Acute promyelocytic leukemia.
PharmGKB; PA31844; -.
eggNOG; ENOG410IFJ8; Eukaryota.
eggNOG; ENOG41125FF; LUCA.
GeneTree; ENSGT00730000111158; -.
HOGENOM; HOG000113889; -.
HOVERGEN; HBG052694; -.
InParanoid; Q14980; -.
KO; K16808; -.
OMA; HLTAQVR; -.
OrthoDB; EOG091G00XV; -.
PhylomeDB; Q14980; -.
TreeFam; TF334442; -.
Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-HSA-68875; Mitotic Prophase.
SIGNOR; Q14980; -.
ChiTaRS; NUMA1; human.
GeneWiki; Nuclear_mitotic_apparatus_protein_1; -.
GenomeRNAi; 4926; -.
PRO; PR:Q14980; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000137497; -.
CleanEx; HS_NUMA1; -.
ExpressionAtlas; Q14980; baseline and differential.
Genevisible; Q14980; HS.
GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
GO; GO:0099738; C:cell cortex region; IDA:UniProtKB.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0055028; C:cortical microtubule; IDA:UniProtKB.
GO; GO:1905720; C:cytoplasmic microtubule bundle; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:InterPro.
GO; GO:0097575; C:lateral cell cortex; ISS:UniProtKB.
GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0097427; C:microtubule bundle; IDA:UniProtKB.
GO; GO:0036449; C:microtubule minus-end; IDA:UniProtKB.
GO; GO:0035371; C:microtubule plus-end; IDA:UniProtKB.
GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
GO; GO:0061673; C:mitotic spindle astral microtubule; IDA:UniProtKB.
GO; GO:1990023; C:mitotic spindle midzone; IDA:UniProtKB.
GO; GO:0097431; C:mitotic spindle pole; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0005819; C:spindle; TAS:ProtInc.
GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB.
GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
GO; GO:0031616; C:spindle pole centrosome; IDA:UniProtKB.
GO; GO:0097718; F:disordered domain specific binding; IMP:CAFA.
GO; GO:0070840; F:dynein complex binding; IDA:UniProtKB.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0051011; F:microtubule minus-end binding; IDA:UniProtKB.
GO; GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB.
GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IMP:CAFA.
GO; GO:0032403; F:protein complex binding; IDA:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0005198; F:structural molecule activity; TAS:ProtInc.
GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
GO; GO:0055048; P:anastral spindle assembly; IMP:UniProtKB.
GO; GO:0030953; P:astral microtubule organization; IDA:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
GO; GO:0000132; P:establishment of mitotic spindle orientation; IDA:UniProtKB.
GO; GO:0060487; P:lung epithelial cell differentiation; IEA:Ensembl.
GO; GO:0051321; P:meiotic cell cycle; IEA:Ensembl.
GO; GO:0001578; P:microtubule bundle formation; IMP:UniProtKB.
GO; GO:0006997; P:nucleus organization; TAS:ProtInc.
GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISS:UniProtKB.
GO; GO:0051984; P:positive regulation of chromosome segregation; IMP:UniProtKB.
GO; GO:1905820; P:positive regulation of chromosome separation; IMP:UniProtKB.
GO; GO:0051798; P:positive regulation of hair follicle development; ISS:UniProtKB.
GO; GO:0032388; P:positive regulation of intracellular transport; IMP:UniProtKB.
GO; GO:0045618; P:positive regulation of keratinocyte differentiation; ISS:UniProtKB.
GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:UniProtKB.
GO; GO:1902846; P:positive regulation of mitotic spindle elongation; IMP:UniProtKB.
GO; GO:1904778; P:positive regulation of protein localization to cell cortex; IMP:UniProtKB.
GO; GO:1902365; P:positive regulation of protein localization to spindle pole body; IDA:UniProtKB.
GO; GO:1905832; P:positive regulation of spindle assembly; IMP:UniProtKB.
GO; GO:0090235; P:regulation of metaphase plate congression; IMP:UniProtKB.
GO; GO:0060236; P:regulation of mitotic spindle organization; IDA:UniProtKB.
InterPro; IPR026650; NUMA1.
PANTHER; PTHR18902:SF24; PTHR18902:SF24; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ADP-ribosylation; Alternative splicing;
Cell cycle; Cell division; Cell membrane; Chromosome;
Chromosome partition; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Glycoprotein; Isopeptide bond; Lipid-binding;
Lipoprotein; Membrane; Microtubule; Mitosis; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Ubl conjugation.
CHAIN 1 2115 Nuclear mitotic apparatus protein 1.
/FTId=PRO_0000057998.
REGION 1 212 Head (Globular).
REGION 1699 1876 Membrane-binding domain 1.
{ECO:0000269|PubMed:24996901}.
REGION 1700 2115 Tail (Globular).
REGION 1788 1810 4.1-binding domain.
{ECO:0000269|PubMed:24109598,
ECO:0000269|PubMed:24996901}.
REGION 1882 1985 Tubulin-binding domain.
{ECO:0000269|PubMed:11956313,
ECO:0000269|PubMed:12445386}.
REGION 1892 1926 GPSM2-binding domain.
{ECO:0000269|PubMed:11781568,
ECO:0000269|PubMed:12445386,
ECO:0000269|PubMed:21816348,
ECO:0000269|PubMed:24109598}.
REGION 1981 2060 Membrane-binding domain 2.
{ECO:0000269|PubMed:24371089}.
COILED 213 1699 {ECO:0000255}.
MOTIF 1742 1748 Tankyrase-binding domain.
{ECO:0000269|PubMed:12080061}.
MOTIF 1984 1989 Nuclear localization signal.
{ECO:0000269|PubMed:26765568,
ECO:0000269|PubMed:7962183}.
MOD_RES 162 162 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 163 163 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 169 169 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 203 203 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
MOD_RES 211 211 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 271 271 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 379 379 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 388 388 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 395 395 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 820 820 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 891 891 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1047 1047 Phosphothreonine; by PLK1.
{ECO:0000269|PubMed:22327364}.
MOD_RES 1187 1187 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1225 1225 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 1511 1511 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1601 1601 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 1721 1721 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1724 1724 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1728 1728 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1757 1757 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19367720,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1760 1760 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 1769 1769 Phosphoserine; by PLK1.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:22327364}.
MOD_RES 1772 1772 Phosphoserine; by PLK1.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:22327364}.
MOD_RES 1774 1774 Phosphotyrosine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1776 1776 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 1788 1788 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569}.
MOD_RES 1789 1789 Phosphoserine; by PLK1.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:22327364}.
MOD_RES 1792 1792 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1800 1800 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 1804 1804 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1830 1830 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1833 1833 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1834 1834 Phosphoserine; by PLK1.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:22327364}.
MOD_RES 1836 1836 Phosphotyrosine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1840 1840 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1844 1844 Phosphoserine; alternate.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1862 1862 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1887 1887 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1969 1969 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1991 1991 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 2000 2000 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 2003 2003 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 2015 2015 Phosphothreonine; by CDK1.
{ECO:0000269|PubMed:23921553,
ECO:0000269|PubMed:7769006}.
MOD_RES 2047 2047 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2055 2055 Phosphothreonine; by CDK1.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:23921553,
ECO:0000269|PubMed:7769006}.
MOD_RES 2062 2062 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2077 2077 Phosphoserine.
{ECO:0000244|PubMed:17924679}.
MOD_RES 2087 2087 Phosphoserine; by CDK1.
{ECO:0000269|PubMed:23921553,
ECO:0000269|PubMed:7769006}.
MOD_RES 2106 2106 Phosphothreonine; by CDK1.
{ECO:0000244|PubMed:16964243,
ECO:0000269|PubMed:23921553,
ECO:0000269|PubMed:7769006}.
CARBOHYD 1844 1844 O-linked (GlcNAc) serine; alternate.
{ECO:0000269|PubMed:20068230}.
CROSSLNK 1699 1699 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1766 1766 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 1766 1766 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1822 1822 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 414 1549 Missing (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_054146.
VAR_SEQ 1536 1549 Missing (in isoform 2).
{ECO:0000303|PubMed:1541636}.
/FTId=VSP_012910.
VAR_SEQ 1725 2115 LDLSCEEGTPLSITSKLPRTQPDGTSVPGEPASPISQRLPP
KVESLESLYFTPIPARSQAPLESSLDSLGDVFLDSGRKTRS
ARRRTTQIINITMTKKLDVEEPDSANSSFYSTRSAPASQAS
LRATSSTQSLARLGSPDYGNSALLSLPGYRPTTRSSARRSQ
AGVSSGAPPGRNSFYMGTCQDEPEQLDDWNRIAELQQRNRV
CPPHLKTCYPLESRPSLSLGTITDEEMKTGDPQETLRRASM
QPIQIAEGTGITTRQQRKRVSLEPHQGPGTPESKKATSCFP
RPMTPRDRHEGRKQSTTEAQKKAAPASTKQADRRQSMAFSI
LNTPKKLGNSLLRRGASKKALSKASPNTRSGTRRSPRIATT
TASAATAAAIGATPRAKGKAKH -> SQANSSQTPRDSDAC
PHPGLVPGPSLAPSRSWPRGPGAWTVWALSLPCLLFS (in
isoform 3). {ECO:0000303|PubMed:8505359}.
/FTId=VSP_044378.
VAR_SEQ 1739 2115 SKLPRTQPDGTSVPGEPASPISQRLPPKVESLESLYFTPIP
ARSQAPLESSLDSLGDVFLDSGRKTRSARRRTTQIINITMT
KKLDVEEPDSANSSFYSTRSAPASQASLRATSSTQSLARLG
SPDYGNSALLSLPGYRPTTRSSARRSQAGVSSGAPPGRNSF
YMGTCQDEPEQLDDWNRIAELQQRNRVCPPHLKTCYPLESR
PSLSLGTITDEEMKTGDPQETLRRASMQPIQIAEGTGITTR
QQRKRVSLEPHQGPGTPESKKATSCFPRPMTPRDRHEGRKQ
STTEAQKKAAPASTKQADRRQSMAFSILNTPKKLGNSLLRR
GASKKALSKASPNTRSGTRRSPRIATTTASAATAAAIGATP
RAKGKAKH -> RSGGSLPPYVCLWSACCLSGCILVR (in
isoform 4). {ECO:0000303|PubMed:8505359}.
/FTId=VSP_044379.
VARIANT 242 242 K -> R (in dbSNP:rs34239655).
/FTId=VAR_031679.
VARIANT 794 794 A -> G (in dbSNP:rs3750913).
/FTId=VAR_031680.
VARIANT 1153 1153 E -> D (in dbSNP:rs34311364).
/FTId=VAR_031681.
VARIANT 1825 1825 V -> M (in dbSNP:rs7949430).
/FTId=VAR_031682.
VARIANT 1836 1836 Y -> H (in dbSNP:rs35586429).
/FTId=VAR_031683.
VARIANT 2049 2049 A -> T (in dbSNP:rs5743685).
/FTId=VAR_051248.
MUTAGEN 1910 1910 E->A: Abolishes interaction with GPSM2.
{ECO:0000269|PubMed:21816348}.
MUTAGEN 1984 1984 R->G: No effect on nuclear localization.
{ECO:0000269|PubMed:7962183}.
MUTAGEN 1988 1988 K->E: Abolishes nuclear localization.
{ECO:0000269|PubMed:7962183}.
MUTAGEN 2015 2015 T->A: Abolishes association with the
mitotic spindle. Increases premature
accumulation at the cell cortex during
metaphase; when associated with A-2055
and A-2087. {ECO:0000269|PubMed:23870127,
ECO:0000269|PubMed:7769006}.
MUTAGEN 2055 2055 T->A: Increases premature accumulation at
the cell membrane of the polar cortical
region in prophase and metaphase. Reduces
association with the mitotic spindle.
Increased randomization of spindle
orientation. Increases premature
accumulation at the cell cortex during
metaphase; when associated with A-2015
and A-2087. {ECO:0000269|PubMed:23870127,
ECO:0000269|PubMed:23921553,
ECO:0000269|PubMed:24109598,
ECO:0000269|PubMed:24371089,
ECO:0000269|PubMed:24996901,
ECO:0000269|PubMed:7769006}.
MUTAGEN 2055 2055 T->D: Increases localization at the
spindle poles. Decreases localization at
the cell cortex.
{ECO:0000269|PubMed:24109598}.
MUTAGEN 2055 2055 T->E: Absence of cell membrane
association even in anaphase. Increased
localization at spindle poles and
chromosome congression defects. Does not
localize to the cortex in either
metaphase or anaphase. Increased
randomization of spindle orientation.
{ECO:0000269|PubMed:23921553,
ECO:0000269|PubMed:24371089}.
MUTAGEN 2087 2087 S->A: Abolishes association with the
mitotic spindle. Increases premature
accumulation at the cell cortex during
metaphase; when associated with A-2015
and A-2055. {ECO:0000269|PubMed:23870127,
ECO:0000269|PubMed:7769006}.
MUTAGEN 2106 2106 T->A: Abolishes association with the
mitotic spindle.
{ECO:0000269|PubMed:7769006}.
CONFLICT 772 772 Q -> L (in Ref. 2; CAA77670).
{ECO:0000305}.
CONFLICT 815 816 ER -> DG (in Ref. 2; CAA77670).
{ECO:0000305}.
CONFLICT 873 873 E -> K (in Ref. 2; CAA77670).
{ECO:0000305}.
CONFLICT 1589 1589 L -> F (in Ref. 2; CAA77670).
{ECO:0000305}.
CONFLICT 1637 1637 S -> T (in Ref. 3; Z14227/Z14228).
{ECO:0000305}.
CONFLICT 1682 1682 S -> T (in Ref. 3; Z14227/Z14228).
{ECO:0000305}.
CONFLICT 1798 1798 L -> Q (in Ref. 3; CAA77669).
{ECO:0000305}.
TURN 1917 1919 {ECO:0000244|PDB:3RO2}.
HELIX 1920 1922 {ECO:0000244|PDB:3RO2}.
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


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GTX30688 NuMA (Nuclear Mitotic Apparatus) 100 µl
GTX30688 NuMA (Nuclear Mitotic Apparatus) 100 µl
EH3450 Nuclear Mitotic Apparatus Protein 1 Elisa Kit 96T
QY-E10566 Rat Nuclear Mitotic AppaRatus Protein 1(NUMA1)ELISA Kit 96T
201-11-1079 Rat Nuclear Mitotic Apparatus Protein 1,NUMA1 ELISA Kit 96T
NUMBL NUMA1 Gene nuclear mitotic apparatus protein 1
UB-E10566 Rat Nuclear Mitotic AppaRatus Protein 1(NUMA1)ELISA Kit 96T
201-11-1079 Rat Nuclear Mitotic AppaRatus Protein 1(NUMA1)ELISA Kit 96T
201-20-3904 NUMA1{nuclear mitotic apparatus protein 1}rabbit.pAb 0.2ml
E-EL-MK1146 Monkey NUMA1 (Nuclear Mitotic Apparatus Protein 1) ELISA Kit 96T
201-12-3209 Human Nuclear Mitotic Apparatus Protein 1(NUMA1)ELISA Kit 96T
E-EL-Ch0812 Chicken NUMA1 (Nuclear Mitotic Apparatus Protein 1) ELISA Kit 96T
E0839Mo Mouse Nuclear Mitotic Apparatus Protein 1,NUMA1 ELISA Kit 48T
CSB-EL016185HU Human Nuclear mitotic apparatus protein 1(NUMA1) ELISA kit 96T
E0840Mo Mouse Nuclear Mitotic Apparatus Protein 1,NUMA1 ELISA Kit 48T
YHB0998Mo Mouse Nuclear Mitotic Apparatus Protein 1,NUMA1 ELISA Kit 96T
201-02-0841 Mouse Nuclear Mitotic Apparatus Protein 1(NUMA1)ELISA Kit 96T
E2971Hu Human Nuclear Mitotic Apparatus Protein 1,NUMA1 ELISA Kit 48T
201-12-3209 Human Nuclear Mitotic Apparatus Protein 1,NUMA1 ELISA Kit 96T
201-12-3209 Human Nuclear Mitotic Apparatus Protein 1,NUMA1 ELISA Kit 48T
UB-E03825 Human Nuclear Mitotic Apparatus Protein 1(NUMA1)ELISA Kit 96T
E0840Mo Mouse Nuclear Mitotic Apparatus Protein 1,NUMA1 ELISA Kit 96T
E2971Hu Human Nuclear Mitotic Apparatus Protein 1,NUMA1 ELISA Kit 96T


 

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