NUMA1_MOUSE
ID NUMA1_MOUSE Reviewed; 2094 AA.
AC E9Q7G0; Q80Y35;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Nuclear mitotic apparatus protein 1 {ECO:0000250|UniProtKB:Q14980};
DE AltName: Full=Nuclear mitotic apparatus protein {ECO:0000250|UniProtKB:Q14980};
DE Short=NuMA protein {ECO:0000250|UniProtKB:Q14980};
GN Name=Numa1 {ECO:0000312|MGI:MGI:2443665};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Limb;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398 AND SER-1739, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398; SER-1739 AND SER-1844,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398; SER-1703; SER-1706;
RP SER-1739; SER-1751; SER-1782; SER-1951; SER-1974; SER-2029 AND THR-2037,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-443, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [9]
RP INTERACTION WITH KHDC3.
RX PubMed=25936915; DOI=10.1016/j.stem.2015.03.017;
RA Zhao B., Zhang W.D., Duan Y.L., Lu Y.Q., Cun Y.X., Li C.H., Guo K.,
RA Nie W.H., Li L., Zhang R., Zheng P.;
RT "Filia Is an ESC-Specific Regulator of DNA Damage Response and Safeguards
RT Genomic Stability.";
RL Cell Stem Cell 16:684-698(2015).
RN [10]
RP SUBCELLULAR LOCATION.
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 [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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).
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:19255246, PubMed:24109598, PubMed:26765568). Functions to
CC tether the minus ends of MTs at the spindle poles, which is critical
CC for the establishment and maintenance of the spindle poles
CC (PubMed:26765568). 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:26765568). In metaphase,
CC part of a ternary complex composed of GPSM2 and G(i) alpha proteins,
CC that regulates the recruitment and anchorage of the dynein-dynactin
CC complex in the mitotic cell cortex regions situated above the two
CC spindle poles, and hence regulates the correct oritentation of the
CC mitotic spindle (PubMed:24109598, PubMed:26765568). 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. Binds also to other polyanionic
CC phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP),
CC lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate
CC (PIP3), in vitro (By similarity). Also required for proper orientation
CC of the mitotic spindle during asymmetric cell divisions
CC (PubMed:26765568). Plays a role in mitotic MT aster assembly. Involved
CC in anastral spindle assembly. Positively regulates TNKS protein
CC localization to spindle poles in mitosis. Highly abundant component of
CC the nuclear matrix where it may serve a non-mitotic structural role,
CC occupies the majority of the nuclear volume (By similarity). Required
CC for epidermal differentiation and hair follicle morphogenesis
CC (PubMed:26765568). {ECO:0000250|UniProtKB:Q14980,
CC ECO:0000269|PubMed:19255246, ECO:0000269|PubMed:24109598,
CC ECO:0000269|PubMed:26765568}.
CC -!- SUBUNIT: Homodimer. Also forms multiarm oligomers by association of C-
CC terminal tail domains, oligomers may further assemble to form a
CC hexagonal nuclear lattice-like network. Associates with the dynein-
CC dynactin complex; this association promotes the transport and
CC accumulation of NUMA1 at the mitotic spindle poles that is inhibited by
CC the BRISC complex in a PLK1-dependent manner. Part of a spindle
CC orientation complex at least composed of GNAI1, GPSM2 and NUMA1 (By
CC similarity). Interacts (via C-terminus) with microtubules (MTs); this
CC interaction is direct and promotes both MT bundle formation and
CC stability in a dynein-dynactin complex- and CDK1-independent manner.
CC Interacts with EPB41 and EPB41L2; these interactions are negatively
CC regulated by CDK1 during metaphase and are important for anaphase-
CC specific localization of NUMA1 in symmetrically dividing cells.
CC Interacts (via C-terminus) with GPSM2 (via TPR repeats); this
CC interaction is direct, prevented by competitive binding of INSC, is
CC inhibited in a PLK1-dependent manner, blocks the association of NUMA1
CC with MTs and inhibits NUMA1-induced MT bundle formation, prevents the
CC association of NUMA1 with SPAG5, induces mitotic spindle pole
CC localization of GPSM2, both metaphase cell cortex localization of NUMA1
CC and mitotic spindle organization. Does not interact with GPSM2 during
CC anaphase. Interacts (via C-terminus) with the nuclear importin
CC alpha/importin beta receptor; this interaction is inhibited by RanGTP.
CC Interacts (via C-terminus) with KPNB1; this interaction is inhibited by
CC RanGTP and the BRISC complex. Interacts with ABRAXAS2 and the BRISC
CC complex; these interactions regulate mitotic spindle assembly.
CC Interacts (via N-terminal end of the coiled-coil domain) with RAE1;
CC this interaction promotes mitotic spindle formation. Interacts (via C-
CC terminus) with SPAG5 (via C-terminus); this interaction promotes the
CC recruitment of SPAG5 to the MTs at spindle poles in a dynein-dynactin-
CC dependent manner and regulates mitotic spindle organization and proper
CC chromosome alignment during mitosis. Interacts with TNKS; this
CC interaction occurs at the onset of mitosis. Interacts with TNKS2.
CC Interacts with tubulin. Interacts with KHDC3 (via C-terminus)
CC (PubMed:25936915). {ECO:0000250|UniProtKB:Q14980,
CC ECO:0000269|PubMed:25936915}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19255246}. Nucleus,
CC nucleoplasm {ECO:0000250|UniProtKB:Q14980}. Nucleus matrix
CC {ECO:0000250|UniProtKB:Q14980}. Chromosome
CC {ECO:0000250|UniProtKB:Q14980}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:26765568}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q14980}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:19255246,
CC ECO:0000269|PubMed:24109598, ECO:0000269|PubMed:26765568}. Cytoplasm,
CC cell cortex {ECO:0000269|PubMed:24109598, ECO:0000269|PubMed:26765568,
CC ECO:0000269|PubMed:26766442}. Cell membrane
CC {ECO:0000250|UniProtKB:Q14980}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q14980}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q14980}. Lateral cell membrane
CC {ECO:0000269|PubMed:26766442}. Note=Mitotic cell cycle-dependent
CC shuttling protein that relocalizes from the interphase nucleus to the
CC spindle poles and cell cortex (PubMed:19255246, PubMed:24109598,
CC PubMed:26765568). The localization to the spindle poles is regulated by
CC AAAS (By similarity). In interphase, resides in the nuclear matrix
CC (PubMed:19255246). In prophase, restricted to the interchromatin or
CC condensed chromosome space. In prometaphase, after nuclear envelope
CC disassembly, forms aggregates both in the spindle midzone and at
CC duplicated centrosomes and astral microtubules (MTs) of the bipolar
CC spindle apparatus. Translocates from the spindle midzone towards the
CC spindle poles along spindle fibers in a MT- and dynein-dynactin-
CC dependent manner until the anaphase onset (By similarity). In
CC metaphase, recruited to the polar cortical region in a GPSM2- and
CC GNAI1-dependent manner (PubMed:24109598). Excluded from the metaphase
CC equatorial cortical region in a RanGTP-dependent manner.
CC Phosphorylation on Thr-2037 by CDK1 results in its localization at
CC spindle poles in metaphase, but not at the cell cortex (By similarity).
CC In anaphase, recruited and anchored at the cell membrane of the polar
CC cortical region in a EPB41-, EPB41L2-, phosphatidylinositol-dependent
CC and GPSM2- and G(i) alpha proteins-independent manner
CC (PubMed:24109598). Excluded from the anaphase equatorial region of the
CC cell cortex in a RACGAP1- and KIF23-dependent and RanGTP-independent
CC manner. Associated with astral MTs emanating from the spindle poles
CC during anaphase. Nonphosphorylated Thr-2037 localizes at the cell
CC cortex, weakly during metaphase and more prominently during anaphase in
CC a phosphatase PPP2CA-dependent manner. As mitosis progresses it
CC reassociates with telophase chromosomes very early during nuclear
CC reformation, before substantial accumulation of lamins on chromosomal
CC surfaces is evident. Localizes to the tips of cortical MTs in
CC prometaphase (By similarity). Localizes along MTs and specifically to
CC both MT plus and minus ends (PubMed:26765568). Accumulates also at MT
CC tips near the cell periphery. Colocalizes with GPSM2 at mitotic spindle
CC poles during mitosis. Colocalizes with SPAG5 at mitotic spindle at
CC prometaphase and at mitotic spindle poles at metaphase and anaphase.
CC Colocalizes with ABRO1 at mitotic spindle poles. Colocalized with TNKS
CC from prophase through to anaphase in mitosis. Colocalizes with tubulin
CC alpha. CCSAP is essential for its centrosomal localization (By
CC similarity). In horizontally retinal progenitor dividing cells,
CC localized to the lateral cortical region (PubMed:26766442).
CC {ECO:0000250|UniProtKB:Q14980, ECO:0000269|PubMed:19255246,
CC ECO:0000269|PubMed:24109598, ECO:0000269|PubMed:26765568,
CC ECO:0000269|PubMed:26766442}.
CC -!- TISSUE SPECIFICITY: Expressed in testis, speen, liver, lung, spinal
CC cord and brain. Expressed in Purkinje neurons (at protein level)
CC (PubMed:19255246). {ECO:0000269|PubMed:19255246}.
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. The 4.1-binding domain is necessary
CC for its cortical stability and spindle orientation.
CC {ECO:0000250|UniProtKB:Q14980}.
CC -!- PTM: Phosphorylation and dephosphorylation on Thr-2037 regulates the
CC extent of cortical NUMA1 and the dynein-dynactin complex localization
CC during mitotic metaphase and anaphase. In metaphase, phosphorylation on
CC Thr-2037 occurs in a kinase CDK1-dependent manner; this phosphorylation
CC maintains low levels of cortical dynein-dynactin complex at metaphase,
CC and hence proper spindle positioning. In anaphase, dephosphorylated on
CC Thr-2037 by phosphatase PPP2CA; this dephosphorylation stimulates its
CC membrane association and with the dynein-dynactin complex its
CC enrichment at the cell cortex, and hence robust spindle elongation.
CC Probably also phosphorylated on Thr-1997 and Ser-2069 by CDK1; these
CC phosphorylations may regulate its cell cortex recruitment during
CC metaphase and anaphase. Phosphorylated on Ser-1751, Ser-1754, Ser-1771
CC and Ser-1816 by PLK1; these phosphorylations induce cortical dynein-
CC dynactin complex dissociation from the NUMA1-GPSM2 complex and
CC negatively regulates cortical dynein-dynactin complex localization.
CC {ECO:0000250|UniProtKB:Q14980}.
CC -!- PTM: ADP-ribosylated by TNKS at the onset of mitosis; ADP-ribosylation
CC is not required for its localization to spindle poles.
CC {ECO:0000250|UniProtKB:Q14980}.
CC -!- PTM: O-glycosylated during cytokinesis at sites identical or close to
CC phosphorylation sites, this interferes with the phosphorylation status.
CC {ECO:0000250|UniProtKB:Q14980}.
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:0000250|UniProtKB:Q14980}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice with an internal in-frame deletion of
CC exon 22 exhibit early embryonic lethality (PubMed:19255246). Mutant
CC mice with a conditional internal in-frame deletion of exon 22 show
CC embryonic lethality and display inhibition of primary embryonic
CC fibroblast proliferation that display mitotic centrosome-spindle
CC coupling, microtubule-focusing at the spindle poles and equatorial
CC metaphase chromosome alignement defects (PubMed:19255246). Mutant mice
CC with a conditional internal in-frame deletion of exon 22 in the
CC embryonic epidermis show neonatal lethality and display perturbation of
CC epidermis differentiation characterized by increased suprabasal cell
CC divisions and mitotic spindle orientation defects (PubMed:26765568).
CC Adult mutant mice with a conditional internal in-frame deletion of exon
CC 22 in interfollicular and hair follicles display an almost complete
CC absence of hair regrowth and mitotic spindle orientation defects in
CC hair follicle matrix cells (PubMed:26765568).
CC {ECO:0000269|PubMed:19255246, ECO:0000269|PubMed:26765568}.
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DR EMBL; AC167240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC049791; AAH49791.1; -; mRNA.
DR CCDS; CCDS40046.1; -.
DR RefSeq; NP_598708.3; NM_133947.3.
DR RefSeq; XP_006507240.1; XM_006507177.2.
DR AlphaFoldDB; E9Q7G0; -.
DR SMR; E9Q7G0; -.
DR IntAct; E9Q7G0; 2.
DR STRING; 10090.ENSMUSP00000081912; -.
DR GlyGen; E9Q7G0; 1 site.
DR iPTMnet; E9Q7G0; -.
DR PhosphoSitePlus; E9Q7G0; -.
DR EPD; E9Q7G0; -.
DR jPOST; E9Q7G0; -.
DR MaxQB; E9Q7G0; -.
DR PaxDb; E9Q7G0; -.
DR PeptideAtlas; E9Q7G0; -.
DR PRIDE; E9Q7G0; -.
DR ProteomicsDB; 287857; -.
DR Antibodypedia; 16895; 437 antibodies from 38 providers.
DR DNASU; 101706; -.
DR Ensembl; ENSMUST00000084852; ENSMUSP00000081912; ENSMUSG00000066306.
DR GeneID; 101706; -.
DR KEGG; mmu:101706; -.
DR UCSC; uc009ipz.1; mouse.
DR CTD; 4926; -.
DR MGI; MGI:2443665; Numa1.
DR VEuPathDB; HostDB:ENSMUSG00000066306; -.
DR eggNOG; ENOG502QTDA; Eukaryota.
DR GeneTree; ENSGT00950000183078; -.
DR HOGENOM; CLU_233598_0_0_1; -.
DR InParanoid; E9Q7G0; -.
DR OMA; QCRRQQE; -.
DR PhylomeDB; E9Q7G0; -.
DR TreeFam; TF334442; -.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-68875; Mitotic Prophase.
DR BioGRID-ORCS; 101706; 24 hits in 75 CRISPR screens.
DR ChiTaRS; Numa1; mouse.
DR PRO; PR:E9Q7G0; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; E9Q7G0; protein.
DR Bgee; ENSMUSG00000066306; Expressed in undifferentiated genital tubercle and 263 other tissues.
DR ExpressionAtlas; E9Q7G0; baseline and differential.
DR Genevisible; E9Q7G0; MM.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0099738; C:cell cortex region; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0055028; C:cortical microtubule; ISS:UniProtKB.
DR GO; GO:1905720; C:cytoplasmic microtubule bundle; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:InterPro.
DR GO; GO:0097575; C:lateral cell cortex; IMP:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0097427; C:microtubule bundle; ISS:UniProtKB.
DR GO; GO:0036449; C:microtubule minus-end; ISS:UniProtKB.
DR GO; GO:0035371; C:microtubule plus-end; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0061673; C:mitotic spindle astral microtubule; ISS:UniProtKB.
DR GO; GO:1990023; C:mitotic spindle midzone; ISS: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:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005876; C:spindle microtubule; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; ISO:MGI.
DR GO; GO:0031616; C:spindle pole centrosome; ISS:UniProtKB.
DR GO; GO:0097718; F:disordered domain specific binding; ISO:MGI.
DR GO; GO:0070840; F:dynein complex binding; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0051011; F:microtubule minus-end binding; ISS:UniProtKB.
DR GO; GO:0051010; F:microtubule plus-end binding; ISS:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0015631; F:tubulin binding; ISS:UniProtKB.
DR GO; GO:0055048; P:anastral spindle assembly; ISO:MGI.
DR GO; GO:0030953; P:astral microtubule organization; ISS: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; IMP:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:Ensembl.
DR GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IMP:UniProtKB.
DR GO; GO:0051984; P:positive regulation of chromosome segregation; ISS:UniProtKB.
DR GO; GO:1905820; P:positive regulation of chromosome separation; ISO:MGI.
DR GO; GO:0051798; P:positive regulation of hair follicle development; IMP:UniProtKB.
DR GO; GO:0032388; P:positive regulation of intracellular transport; ISS:UniProtKB.
DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IMP:UniProtKB.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISS:UniProtKB.
DR GO; GO:1902846; P:positive regulation of mitotic spindle elongation; ISO:MGI.
DR GO; GO:1904778; P:positive regulation of protein localization to cell cortex; ISS:UniProtKB.
DR GO; GO:1902365; P:positive regulation of protein localization to spindle pole body; ISS:UniProtKB.
DR GO; GO:1905832; P:positive regulation of spindle assembly; ISS:UniProtKB.
DR GO; GO:0090235; P:regulation of metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; ISS:UniProtKB.
DR InterPro; IPR026650; NUMA1.
DR PANTHER; PTHR18902:SF24; PTHR18902:SF24; 1.
PE 1: Evidence at protein level;
KW Acetylation; ADP-ribosylation; Cell cycle; Cell division; Cell membrane;
KW Chromosome; Chromosome partition; Coiled coil; Cytoplasm; Cytoskeleton;
KW Glycoprotein; Isopeptide bond; Lipid-binding; Lipoprotein; Membrane;
KW Microtubule; Mitosis; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..2094
FT /note="Nuclear mitotic apparatus protein 1"
FT /id="PRO_0000440879"
FT REGION 1..210
FT /note="Head (Globular)"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT REGION 617..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1173..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1681..1858
FT /note="Membrane-binding domain 1"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT REGION 1682..2094
FT /note="Tail (Globular)"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT REGION 1718..1743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1760..1795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1770..1792
FT /note="4.1-binding domain"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT REGION 1807..1883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1864..1967
FT /note="Tubulin-binding domain"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT REGION 1874..1908
FT /note="GPSM2-binding domain"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT REGION 1937..2094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1963..2042
FT /note="Membrane-binding domain 2"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT COILED 211..1681
FT /evidence="ECO:0000255"
FT MOTIF 1724..1730
FT /note="Tankyrase-binding domain"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOTIF 1966..1971
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT COMPBIAS 1126..1143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1720..1738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1812..1844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1855..1883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1958..1985
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1996..2010
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2057..2084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 161
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 209
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 377
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 443
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 878
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 1183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 1221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 1507
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 1583
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 1703
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1706
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1710
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 1739
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 1742
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 1751
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1754
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 1756
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 1758
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 1771
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 1774
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 1782
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1786
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 1812
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 1815
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 1816
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 1818
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 1822
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 1826
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 1844
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 1869
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 1951
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1973
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 1974
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1982
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 1985
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 1997
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 2029
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2037
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2044
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 2059
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 2069
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT MOD_RES 2085
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT CARBOHYD 1826
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT CROSSLNK 1681
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT CROSSLNK 1748
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT CROSSLNK 1748
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT CROSSLNK 1804
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14980"
FT CONFLICT 539
FT /note="A -> V (in Ref. 2; AAH49791)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2094 AA; 235630 MW; 09074ACC3A6A1046 CRC64;
MTLHATRAAT LLSWVNSLHV ADPVETVLQL QDCSIFIKII NTIHDTKEGQ QILQQPLPER
LDFVCSFLQK NRKHPSSTQC LVSVQKVIEG SEMELAKMIM LFLYQSTMSS RNLRDWEQFE
YGVQAELAVI LKFMLDHEES LNLTEDLESF LEKVPYTHAS TLSEELSPPS HQTKRKIRFL
EIQRIASSSS ENNFLSGSPS SPMGDILQTP QFQMRRLKKQ LADERSNRDD LELELSESLK
LLTEKDAQIA MMQQRIDHLA LLNEKQAASS QEPSELEELR GKNESLTVRL HETLKQCQNL
KTEKSQMDRK ISQLSEENGD LSFKVREFAN HLQQLQGAFN DLIEEHSKAS QEWAEKQARL
ENELSTALQD KKCLEEKNEI LQGKLSQLED QATRLQESPA PEKGEVLGDA LQLDTLKQEA
AKLATDNTQL QTRVETLECE RGKQEAQLLA ERSRFEDEKQ QLASLIADLQ SSVSNLSQAK
EELEQASQAQ GAQLTAQLTS MTGLNATLQQ RDQELASLKE QAKKEQAQML QTMQEQEQAA
QGLRQQVEQL SSSLKLKEQQ LEEAAKEQEA TRQDHAQQLA IVAEAREASL RERDTARQQL
ETVEKEKDAK LESLQQQLQA ANDARDNAQT SVTQAQQEKA ELSQKIGELH ACIEASHQEQ
RQVQARVTEL EAQLKAEQQK TTEREKVVQE KAQLQEQLRA LEESLKITKG SLEEEKRRAA
DALKEQQCRA TEMEAESRSL MEQREREQKE LEQEKAGRKG LEARIQQLEE AHQAETEALR
HELAEATASQ HRAESECERL IREVESRQKR FEARQQEEAR YGAMFQEQLM ALKGEKTGQE
VQEEAVEIHS EGQPGQQQSQ LAQLHASLAK AIQQVQEKEV RAQKLVDDLS ALQEKMAATN
KEVACLKTLV LKAGEQQETA SLELLKEPPR AANRASDQLG EQQGRPFSST HAAVKAMERE
AEQMGGELER LRAALIKSQG QQQEERGQQE REVARLTQER GQAQADLAQE KAAKAELEMR
LQNTLNEQRV EFAALQEALA HALTEKEGTD QELAKLRGQE AAQRTELKEL QQTLEQLKIQ
LVKKEKEHPA GGASGEDASG PGTQSETAGK TDAPGPELQA LRAEISKLEQ QCQQQQQQVE
GLTHSLKSER ACRAEQDKAL ETLQGQLEEK ARELGHNQAA SASAQRELQA LRAKAQDHSK
AEEEWKAQVA RGQQEAERKS SLISSLEEEV SILNRQVLEK EGESKELKRL VVAESEKSQK
LEERLRLLQV ETASNSARAA ERSSALREEV QSLREEVEKQ RVVSENSRQE LASQAERAEE
LGQELKAWQE KFFQKEQALS ALQLEHTSTQ ALVSELLPAK HLCQQLQAEQ AAAEKRFREE
LEQSKQAAGG LQAELMRAQR ELGELGSLRQ KIVEQERAAQ QLRAEKASYA EQLSMLKKAH
GLLAEENRGL GERANLGRQF LEVELDQARE KYVQELAAVR TDAETHLAEM RQEAQSTSRE
LEVMTAKYEG AKVKVLEERQ RFQEERQKLT AQVEELSKKL TEHDQASKVQ QQKLKAFQAQ
RGESQQEVQR LQTQLNELQA QLSQKEQAAE HYKLQMEKAK THYDAKKQQN QKLQEQLQDL
EELQKENKEL RSEAERLGRE LQQAGLKTKE AEQTCRHLTA QVRSLEAQVA HADQQLRDLG
KFQVATDALK SREPQVKPQL DLSIDSLDLS LEEGTPCSVA SKLPRTQPDG TSVPGEPASP
ISQRLPPKVE SLESLYFTPT PARGQAPLET SLDSLGDAFP DSGRKTRSAR RRTTQIINIT
MTKKLELEEP DSANSSFYST QSAPASQANL RATSSTQSLA RLGSPDDGNS ALLSLPGYRP
TTRSSARRSQ ARMSSGAPQG RNSFYMGTCQ DEPEQLDDWN RIAELQQRNR VCPPHLKTCY
PLESRPTLSL ATITDEEMKT GDPRETLRRA SMQPAQIAEG VGITTRQQRK RVSSETHQGP
GTPESKKATS CFPRPMTPRD RHEGRKQSST ADTQKKAAPV LKQADRRQSM AFSILNTPKK
LGNSLLRRGA SKKTPAKVSP NPRSGTRRSP RIATTTTGTA TVATTPRAKG KVKH
