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Protein

Nuclear mitotic apparatus protein 1

Gene

Numa1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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:19255246, PubMed:24109598, PubMed:26765568). 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:26765568). Plays a role in the establishment of the mitotic spindle orientation during metaphase and elongation during anaphase in a dynein-dynactin-dependent manner (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:24109598, PubMed:26765568). 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. Binds also to other polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate (PIP3), in vitro (By similarity). Also required for proper orientation of the mitotic spindle during asymmetric cell divisions (PubMed:26765568). Plays a role in mitotic MT aster assembly. Involved in anastral spindle assembly. Positively regulates TNKS protein localization to spindle poles in mitosis. Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority of the nuclear volume (By similarity). Required for epidermal differentiation and hair follicle morphogenesis (PubMed:26765568).By similarity3 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processCell cycle, Cell division, Chromosome partition, Mitosis
LigandLipid-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-380320 Recruitment of NuMA to mitotic centrosomes
R-MMU-68875 Mitotic Prophase

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Nuclear mitotic apparatus protein 1By similarity
Alternative name(s):
Nuclear mitotic apparatus proteinBy similarity
Short name:
NuMA proteinBy similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Numa1Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 7

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

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MGIi
MGI:2443665 Numa1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Chromosome, Cytoplasm, Cytoskeleton, Membrane, Microtubule, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mutant mice with an internal in-frame deletion of exon 22 exhibit early embryonic lethality (PubMed:19255246). Mutant mice with a conditional internal in-frame deletion of exon 22 show embryonic lethality and display inhibition of primary embryonic fibroblast proliferation that display mitotic centrosome-spindle coupling, microtubule-focusing at the spindle poles and equatorial metaphase chromosome alignement defects (PubMed:19255246). Mutant mice with a conditional internal in-frame deletion of exon 22 in the embryonic epidermis show neonatal lethality and display perturbation of epidermis differentiation characterized by increased suprabasal cell divisions and mitotic spindle orientation defects (PubMed:26765568). Adult mutant mice with a conditional internal in-frame deletion of exon 22 in interfollicular and hair follicles display an almost complete absence of hair regrowth and mitotic spindle orientation defects in hair follicle matrix cells (PubMed:26765568).2 Publications

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004408791 – 2094Nuclear mitotic apparatus protein 1Add BLAST2094

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei160PhosphoserineBy similarity1
Modified residuei161PhosphothreonineBy similarity1
Modified residuei167PhosphoserineBy similarity1
Modified residuei201PhosphoserineBy similarity1
Modified residuei209PhosphothreonineBy similarity1
Modified residuei269PhosphoserineBy similarity1
Modified residuei377N6-acetyllysineBy similarity1
Modified residuei386PhosphoserineBy similarity1
Modified residuei398PhosphoserineCombined sources1
Modified residuei443N6-acetyllysineCombined sources1
Modified residuei878N6-acetyllysineBy similarity1
Modified residuei1183PhosphoserineBy similarity1
Modified residuei1221PhosphoserineBy similarity1
Modified residuei1507N6-acetyllysineBy similarity1
Modified residuei1583PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki1681Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1703PhosphoserineCombined sources1
Modified residuei1706PhosphoserineCombined sources1
Modified residuei1710PhosphoserineBy similarity1
Modified residuei1739PhosphoserineCombined sources1
Modified residuei1742PhosphoserineBy similarity1
Cross-linki1748Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki1748Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei1751PhosphoserineCombined sources1
Modified residuei1754Phosphoserine; by PLK1By similarity1
Modified residuei1756PhosphotyrosineBy similarity1
Modified residuei1758PhosphothreonineBy similarity1
Modified residuei1771Phosphoserine; by PLK1By similarity1
Modified residuei1774PhosphoserineBy similarity1
Modified residuei1782PhosphoserineCombined sources1
Modified residuei1786PhosphothreonineBy similarity1
Cross-linki1804Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1812PhosphoserineBy similarity1
Modified residuei1815PhosphoserineBy similarity1
Modified residuei1816Phosphoserine; by PLK1By similarity1
Modified residuei1818PhosphotyrosineBy similarity1
Modified residuei1822PhosphoserineBy similarity1
Modified residuei1826Phosphoserine; alternateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi1826O-linked (GlcNAc) serine; alternateBy similarity1
Modified residuei1844PhosphoserineCombined sources1
Modified residuei1869PhosphoserineBy similarity1
Modified residuei1951PhosphoserineCombined sources1
Modified residuei1973PhosphoserineBy similarity1
Modified residuei1974PhosphoserineCombined sources1
Modified residuei1982PhosphothreonineBy similarity1
Modified residuei1985PhosphoserineBy similarity1
Modified residuei1997Phosphothreonine; by CDK1By similarity1
Modified residuei2029PhosphoserineCombined sources1
Modified residuei2037PhosphothreonineCombined sources1
Modified residuei2044PhosphoserineBy similarity1
Modified residuei2059PhosphoserineBy similarity1
Modified residuei2069Phosphoserine; by CDK1By similarity1
Modified residuei2085Phosphothreonine; by CDK1By similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylation and dephosphorylation on Thr-2037 regulates the extent of cortical NUMA1 and the dynein-dynactin complex localization during mitotic metaphase and anaphase. In metaphase, phosphorylation on Thr-2037 occurs in a kinase CDK1-dependent manner; this phosphorylation maintains low levels of cortical dynein-dynactin complex at metaphase, and hence proper spindle positioning. In anaphase, dephosphorylated on Thr-2037 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. Probably also phosphorylated on Thr-1997 and Ser-2069 by CDK1; these phosphorylations may regulate its cell cortex recruitment during metaphase and anaphase. Phosphorylated on Ser-1751, Ser-1754, Ser-1771 and Ser-1816 by PLK1; these phosphorylations induce cortical dynein-dynactin complex dissociation from the NUMA1-GPSM2 complex and negatively regulates cortical dynein-dynactin complex localization.By similarity
ADP-ribosylated by TNKS at the onset of mitosis; ADP-ribosylation is not required for its localization to spindle poles.By similarity
O-glycosylated during cytokinesis at sites identical or close to phosphorylation sites, this interferes with the phosphorylation status.By similarity
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.By similarity

Keywords - PTMi

Acetylation, ADP-ribosylation, Glycoprotein, Isopeptide bond, Lipoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

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MaxQBi
E9Q7G0

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
E9Q7G0

PeptideAtlas

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PeptideAtlasi
E9Q7G0

PRoteomics IDEntifications database

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PRIDEi
E9Q7G0

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
E9Q7G0

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
E9Q7G0

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in testis, speen, liver, lung, spinal cord and brain. Expressed in Purkinje neurons (at protein level) (PubMed:19255246).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000066306 Expressed in 292 organ(s), highest expression level in vas deferens

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
E9Q7G0 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
E9Q7G0 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer. Also forms multiarm oligomers by association of C-terminal tail domains, oligomers may further assemble to form a hexagonal nuclear lattice-like network. 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. Part of a spindle orientation complex at least composed of GNAI1, GPSM2 and NUMA1 (By similarity). 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. 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. 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. Does not interact with GPSM2 during anaphase. Interacts (via C-terminus) with the nuclear importin alpha/importin beta receptor; this interaction is inhibited by RanGTP. Interacts (via C-terminus) with KPNB1; this interaction is inhibited by RanGTP and the BRISC complex. Interacts with ABRAXAS2 and the BRISC complex; these interactions regulate mitotic spindle assembly. Interacts (via N-terminal end of the coiled-coil domain) with RAE1; this interaction promotes mitotic spindle formation. 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. Interacts with TNKS; this interaction occurs at the onset of mitosis. Interacts with TNKS2. Interacts with tubulin.By similarity

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

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IntActi
E9Q7G0, 2 interactors

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000081912

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
E9Q7G0

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 210Head (Globular)By similarityAdd BLAST210
Regioni1681 – 1858Membrane-binding domain 1By similarityAdd BLAST178
Regioni1682 – 2094Tail (Globular)By similarityAdd BLAST413
Regioni1770 – 17924.1-binding domainBy similarityAdd BLAST23
Regioni1864 – 1967Tubulin-binding domainBy similarityAdd BLAST104
Regioni1874 – 1908GPSM2-binding domainBy similarityAdd BLAST35
Regioni1963 – 2042Membrane-binding domain 2By similarityAdd BLAST80

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili211 – 1681Sequence analysisAdd BLAST1471

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi1724 – 1730Tankyrase-binding domainBy similarity7
Motifi1966 – 1971Nuclear localization signalBy similarity6

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The C-terminal tubulin-binding domain mediates direct binding to microtubules, independently of dynein-dynactin complex, and induces their bundling and stabilization. The 4.1-binding domain is necessary for its cortical stability and spindle orientation.By similarity

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IFJ8 Eukaryota
ENOG41125FF LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000154027

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000113889

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG052694

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
E9Q7G0

KEGG Orthology (KO)

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KOi
K16808

Database of Orthologous Groups

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OrthoDBi
EOG091G00XV

TreeFam database of animal gene trees

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TreeFami
TF334442

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR026650 NUMA1

The PANTHER Classification System

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PANTHERi
PTHR18902:SF24 PTHR18902:SF24, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 5 potential isoforms that are computationally mapped.Show allAlign All

E9Q7G0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTLHATRAAT LLSWVNSLHV ADPVETVLQL QDCSIFIKII NTIHDTKEGQ
60 70 80 90 100
QILQQPLPER LDFVCSFLQK NRKHPSSTQC LVSVQKVIEG SEMELAKMIM
110 120 130 140 150
LFLYQSTMSS RNLRDWEQFE YGVQAELAVI LKFMLDHEES LNLTEDLESF
160 170 180 190 200
LEKVPYTHAS TLSEELSPPS HQTKRKIRFL EIQRIASSSS ENNFLSGSPS
210 220 230 240 250
SPMGDILQTP QFQMRRLKKQ LADERSNRDD LELELSESLK LLTEKDAQIA
260 270 280 290 300
MMQQRIDHLA LLNEKQAASS QEPSELEELR GKNESLTVRL HETLKQCQNL
310 320 330 340 350
KTEKSQMDRK ISQLSEENGD LSFKVREFAN HLQQLQGAFN DLIEEHSKAS
360 370 380 390 400
QEWAEKQARL ENELSTALQD KKCLEEKNEI LQGKLSQLED QATRLQESPA
410 420 430 440 450
PEKGEVLGDA LQLDTLKQEA AKLATDNTQL QTRVETLECE RGKQEAQLLA
460 470 480 490 500
ERSRFEDEKQ QLASLIADLQ SSVSNLSQAK EELEQASQAQ GAQLTAQLTS
510 520 530 540 550
MTGLNATLQQ RDQELASLKE QAKKEQAQML QTMQEQEQAA QGLRQQVEQL
560 570 580 590 600
SSSLKLKEQQ LEEAAKEQEA TRQDHAQQLA IVAEAREASL RERDTARQQL
610 620 630 640 650
ETVEKEKDAK LESLQQQLQA ANDARDNAQT SVTQAQQEKA ELSQKIGELH
660 670 680 690 700
ACIEASHQEQ RQVQARVTEL EAQLKAEQQK TTEREKVVQE KAQLQEQLRA
710 720 730 740 750
LEESLKITKG SLEEEKRRAA DALKEQQCRA TEMEAESRSL MEQREREQKE
760 770 780 790 800
LEQEKAGRKG LEARIQQLEE AHQAETEALR HELAEATASQ HRAESECERL
810 820 830 840 850
IREVESRQKR FEARQQEEAR YGAMFQEQLM ALKGEKTGQE VQEEAVEIHS
860 870 880 890 900
EGQPGQQQSQ LAQLHASLAK AIQQVQEKEV RAQKLVDDLS ALQEKMAATN
910 920 930 940 950
KEVACLKTLV LKAGEQQETA SLELLKEPPR AANRASDQLG EQQGRPFSST
960 970 980 990 1000
HAAVKAMERE AEQMGGELER LRAALIKSQG QQQEERGQQE REVARLTQER
1010 1020 1030 1040 1050
GQAQADLAQE KAAKAELEMR LQNTLNEQRV EFAALQEALA HALTEKEGTD
1060 1070 1080 1090 1100
QELAKLRGQE AAQRTELKEL QQTLEQLKIQ LVKKEKEHPA GGASGEDASG
1110 1120 1130 1140 1150
PGTQSETAGK TDAPGPELQA LRAEISKLEQ QCQQQQQQVE GLTHSLKSER
1160 1170 1180 1190 1200
ACRAEQDKAL ETLQGQLEEK ARELGHNQAA SASAQRELQA LRAKAQDHSK
1210 1220 1230 1240 1250
AEEEWKAQVA RGQQEAERKS SLISSLEEEV SILNRQVLEK EGESKELKRL
1260 1270 1280 1290 1300
VVAESEKSQK LEERLRLLQV ETASNSARAA ERSSALREEV QSLREEVEKQ
1310 1320 1330 1340 1350
RVVSENSRQE LASQAERAEE LGQELKAWQE KFFQKEQALS ALQLEHTSTQ
1360 1370 1380 1390 1400
ALVSELLPAK HLCQQLQAEQ AAAEKRFREE LEQSKQAAGG LQAELMRAQR
1410 1420 1430 1440 1450
ELGELGSLRQ KIVEQERAAQ QLRAEKASYA EQLSMLKKAH GLLAEENRGL
1460 1470 1480 1490 1500
GERANLGRQF LEVELDQARE KYVQELAAVR TDAETHLAEM RQEAQSTSRE
1510 1520 1530 1540 1550
LEVMTAKYEG AKVKVLEERQ RFQEERQKLT AQVEELSKKL TEHDQASKVQ
1560 1570 1580 1590 1600
QQKLKAFQAQ RGESQQEVQR LQTQLNELQA QLSQKEQAAE HYKLQMEKAK
1610 1620 1630 1640 1650
THYDAKKQQN QKLQEQLQDL EELQKENKEL RSEAERLGRE LQQAGLKTKE
1660 1670 1680 1690 1700
AEQTCRHLTA QVRSLEAQVA HADQQLRDLG KFQVATDALK SREPQVKPQL
1710 1720 1730 1740 1750
DLSIDSLDLS LEEGTPCSVA SKLPRTQPDG TSVPGEPASP ISQRLPPKVE
1760 1770 1780 1790 1800
SLESLYFTPT PARGQAPLET SLDSLGDAFP DSGRKTRSAR RRTTQIINIT
1810 1820 1830 1840 1850
MTKKLELEEP DSANSSFYST QSAPASQANL RATSSTQSLA RLGSPDDGNS
1860 1870 1880 1890 1900
ALLSLPGYRP TTRSSARRSQ ARMSSGAPQG RNSFYMGTCQ DEPEQLDDWN
1910 1920 1930 1940 1950
RIAELQQRNR VCPPHLKTCY PLESRPTLSL ATITDEEMKT GDPRETLRRA
1960 1970 1980 1990 2000
SMQPAQIAEG VGITTRQQRK RVSSETHQGP GTPESKKATS CFPRPMTPRD
2010 2020 2030 2040 2050
RHEGRKQSST ADTQKKAAPV LKQADRRQSM AFSILNTPKK LGNSLLRRGA
2060 2070 2080 2090
SKKTPAKVSP NPRSGTRRSP RIATTTTGTA TVATTPRAKG KVKH
Length:2,094
Mass (Da):235,630
Last modified:April 5, 2011 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i09074ACC3A6A1046
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F6ZQA3F6ZQA3_MOUSE
Nuclear mitotic apparatus protein 1
Numa1
741Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A1B0GSW3A0A1B0GSW3_MOUSE
Nuclear mitotic apparatus protein 1
Numa1
1,082Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A1B0GT61A0A1B0GT61_MOUSE
Nuclear mitotic apparatus protein 1
Numa1
875Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A1B0GSH2A0A1B0GSH2_MOUSE
Nuclear mitotic apparatus protein 1
Numa1
218Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A1B0GT38A0A1B0GT38_MOUSE
Nuclear mitotic apparatus protein 1
Numa1
207Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti539A → V in AAH49791 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AC167240 Genomic DNA No translation available.
BC049791 mRNA Translation: AAH49791.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS40046.1

NCBI Reference Sequences

More...
RefSeqi
NP_598708.3, NM_133947.3
XP_006507240.1, XM_006507177.2

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.27259

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000084852; ENSMUSP00000081912; ENSMUSG00000066306

Database of genes from NCBI RefSeq genomes

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GeneIDi
101706

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:101706

UCSC genome browser

More...
UCSCi
uc009ipz.1 mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC167240 Genomic DNA No translation available.
BC049791 mRNA Translation: AAH49791.1
CCDSiCCDS40046.1
RefSeqiNP_598708.3, NM_133947.3
XP_006507240.1, XM_006507177.2
UniGeneiMm.27259

3D structure databases

SMRiE9Q7G0
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiE9Q7G0, 2 interactors
STRINGi10090.ENSMUSP00000081912

PTM databases

iPTMnetiE9Q7G0
PhosphoSitePlusiE9Q7G0

Proteomic databases

MaxQBiE9Q7G0
PaxDbiE9Q7G0
PeptideAtlasiE9Q7G0
PRIDEiE9Q7G0

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000084852; ENSMUSP00000081912; ENSMUSG00000066306
GeneIDi101706
KEGGimmu:101706
UCSCiuc009ipz.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4926
MGIiMGI:2443665 Numa1

Phylogenomic databases

eggNOGiENOG410IFJ8 Eukaryota
ENOG41125FF LUCA
GeneTreeiENSGT00940000154027
HOGENOMiHOG000113889
HOVERGENiHBG052694
InParanoidiE9Q7G0
KOiK16808
OrthoDBiEOG091G00XV
TreeFamiTF334442

Enzyme and pathway databases

ReactomeiR-MMU-380320 Recruitment of NuMA to mitotic centrosomes
R-MMU-68875 Mitotic Prophase

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Numa1 mouse

Protein Ontology

More...
PROi
PR:E9Q7G0

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000066306 Expressed in 292 organ(s), highest expression level in vas deferens
ExpressionAtlasiE9Q7G0 baseline and differential
GenevisibleiE9Q7G0 MM

Family and domain databases

InterProiView protein in InterPro
IPR026650 NUMA1
PANTHERiPTHR18902:SF24 PTHR18902:SF24, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiNUMA1_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: E9Q7G0
Secondary accession number(s): Q80Y35
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 5, 2017
Last sequence update: April 5, 2011
Last modified: December 5, 2018
This is version 67 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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