Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 179 (08 May 2019)
Sequence version 2 (17 Apr 2007)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Nuclear mitotic apparatus protein 1

Gene

NUMA1

Organism
Homo sapiens (Human)
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: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).By similarity2 Publications19 Publications

Miscellaneous

Also known as nuclear matrix protein-22/NMP-22/NMP22, an antigen used in diagnostic tests of bladder cancer.1 Publication

<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-HSA-380320 Recruitment of NuMA to mitotic centrosomes
R-HSA-68875 Mitotic Prophase

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q14980

<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 1Imported
Alternative name(s):
Nuclear matrix protein-221 Publication
Short name:
NMP-221 Publication
Nuclear mitotic apparatus protein2 Publications
Short name:
NuMA protein2 Publications
SP-H antigen1 Publication
<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
Synonyms:NMP221 Publication, NUMA1 Publication
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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 11

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:8059 NUMA1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
164009 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q14980

<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 & Seán O’Donoghue; 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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi1910E → A: Abolishes interaction with GPSM2. 1 Publication1
Mutagenesisi1984R → G: No effect on nuclear localization. 1 Publication1
Mutagenesisi1988K → E: Abolishes nuclear localization. 1 Publication1
Mutagenesisi2015T → A: Abolishes association with the mitotic spindle. Increases premature accumulation at the cell cortex during metaphase; when associated with A-2055 and A-2087. 2 Publications1
Mutagenesisi2055T → 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. 6 Publications1
Mutagenesisi2055T → D: Increases localization at the spindle poles. Decreases localization at the cell cortex. 1 Publication1
Mutagenesisi2055T → 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. 2 Publications1
Mutagenesisi2087S → A: Abolishes association with the mitotic spindle. Increases premature accumulation at the cell cortex during metaphase; when associated with A-2015 and A-2055. 2 Publications1
Mutagenesisi2106T → A: Abolishes association with the mitotic spindle. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
4926

MalaCards human disease database

More...
MalaCardsi
NUMA1

Open Targets

More...
OpenTargetsi
ENSG00000137497

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
520 Acute promyelocytic leukemia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA31844

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
NUMA1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
145559510

<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_00000579981 – 2115Nuclear mitotic apparatus protein 1Add BLAST2115

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 residuei162PhosphoserineCombined sources1
Modified residuei163PhosphothreonineCombined sources1
Modified residuei169PhosphoserineCombined sources1
Modified residuei203PhosphoserineCombined sources1
Modified residuei211PhosphothreonineCombined sources1
Modified residuei271PhosphoserineCombined sources1
Modified residuei379N6-acetyllysineCombined sources1
Modified residuei388PhosphoserineCombined sources1
Modified residuei395PhosphoserineCombined sources1
Modified residuei820PhosphoserineCombined sources1
Modified residuei891N6-acetyllysineCombined sources1
Modified residuei1047Phosphothreonine; by PLK11 Publication1
Modified residuei1187PhosphoserineCombined sources1
Modified residuei1225PhosphoserineCombined sources1
Modified residuei1511N6-acetyllysineCombined sources1
Modified residuei1601PhosphoserineCombined sources1
<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-linki1699Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1721PhosphoserineCombined sources1
Modified residuei1724PhosphoserineCombined sources1
Modified residuei1728PhosphoserineCombined sources1
Modified residuei1757PhosphoserineCombined sources1
Modified residuei1760PhosphoserineCombined sources1
Cross-linki1766Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki1766Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei1769Phosphoserine; by PLK1Combined sources1 Publication1
Modified residuei1772Phosphoserine; by PLK1Combined sources1 Publication1
Modified residuei1774PhosphotyrosineCombined sources1
Modified residuei1776PhosphothreonineCombined sources1
Modified residuei1788PhosphoserineCombined sources1
Modified residuei1789Phosphoserine; by PLK1Combined sources1 Publication1
Modified residuei1792PhosphoserineCombined sources1
Modified residuei1800PhosphoserineCombined sources1
Modified residuei1804PhosphothreonineCombined sources1
Cross-linki1822Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1830PhosphoserineCombined sources1
Modified residuei1833PhosphoserineCombined sources1
Modified residuei1834Phosphoserine; by PLK1Combined sources1 Publication1
Modified residuei1836PhosphotyrosineCombined sources1
Modified residuei1840PhosphoserineCombined sources1
Modified residuei1844Phosphoserine; alternateCombined sources1
<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>Glycosylationi1844O-linked (GlcNAc) serine; alternate1 Publication1
Modified residuei1862PhosphoserineCombined sources1
Modified residuei1887PhosphoserineCombined sources1
Modified residuei1969PhosphoserineCombined sources1
Modified residuei1991PhosphoserineCombined sources1
Modified residuei2000PhosphothreonineCombined sources1
Modified residuei2003PhosphoserineCombined sources1
Modified residuei2015Phosphothreonine; by CDK12 Publications1
Modified residuei2047PhosphoserineCombined sources1
Modified residuei2055Phosphothreonine; by CDK1Combined sources2 Publications1
Modified residuei2062PhosphoserineCombined sources1
Modified residuei2077PhosphoserineCombined sources1
Modified residuei2087Phosphoserine; by CDK12 Publications1
Modified residuei2106Phosphothreonine; by CDK1Combined sources2 Publications1

<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-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).5 Publications
ADP-ribosylated by TNKS at the onset of mitosis; ADP-ribosylation is not required for its localization to spindle poles (PubMed:16076287).1 Publication
O-glycosylated during cytokinesis at sites identical or close to phosphorylation sites, this interferes with the phosphorylation status (PubMed:20068230).1 Publication
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.1 Publication

Keywords - PTMi

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

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q14980

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q14980

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q14980

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

More...
PaxDbi
Q14980

PeptideAtlas

More...
PeptideAtlasi
Q14980

PRoteomics IDEntifications database

More...
PRIDEi
Q14980

ProteomicsDB human proteome resource

More...
ProteomicsDBi
60272
60273 [Q14980-2]

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
Q14980

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q14980

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

More...
PhosphoSitePlusi
Q14980

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q14980

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000137497 Expressed in 239 organ(s), highest expression level in myometrium

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q14980 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q14980 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA019841
HPA019859
HPA029912

<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 (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).20 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
110980, 115 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q14980

Database of interacting proteins

More...
DIPi
DIP-32937N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
Q14980

Protein interaction database and analysis system

More...
IntActi
Q14980, 71 interactors

Molecular INTeraction database

More...
MINTi
Q14980

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000377298

<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

Secondary structure

12115
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3RO2X-ray2.30B1899-1926[»]
5GXWX-ray2.39B1984-2010[»]

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

More...
SMRi
Q14980

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
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 – 212Head (Globular)Add BLAST212
Regioni1699 – 1876Membrane-binding domain 11 PublicationAdd BLAST178
Regioni1700 – 2115Tail (Globular)Add BLAST416
Regioni1788 – 18104.1-binding domain2 PublicationsAdd BLAST23
Regioni1882 – 1985Tubulin-binding domain2 PublicationsAdd BLAST104
Regioni1892 – 1926GPSM2-binding domain4 PublicationsAdd BLAST35
Regioni1981 – 2060Membrane-binding domain 21 PublicationAdd 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 coili213 – 1699Sequence analysisAdd BLAST1487

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>Motifi1742 – 1748Tankyrase-binding domain1 Publication7
Motifi1984 – 1989Nuclear localization signal2 Publications6

<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 (PubMed:11956313). The 4.1-binding domain is necessary for its cortical stability and spindle orientation (PubMed:24109598).2 Publications

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IFJ8 Eukaryota
ENOG41125FF LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00950000183078

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000113889

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q14980

KEGG Orthology (KO)

More...
KOi
K16808

Identification of Orthologs from Complete Genome Data

More...
OMAi
LETLYFT

Database of Orthologous Groups

More...
OrthoDBi
524033at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q14980

TreeFam database of animal gene trees

More...
TreeFami
TF334442

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR026650 NUMA1

The PANTHER Classification System

More...
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>Sequences (5+)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 describes 5 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 5 described isoforms and 18 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q14980-1) [UniParc]FASTAAdd to basket
Also known as: Numa-1, p230

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MTLHATRGAA LLSWVNSLHV ADPVEAVLQL QDCSIFIKII DRIHGTEEGQ
60 70 80 90 100
QILKQPVSER LDFVCSFLQK NRKHPSSPEC LVSAQKVLEG SELELAKMTM
110 120 130 140 150
LLLYHSTMSS KSPRDWEQFE YKIQAELAVI LKFVLDHEDG LNLNEDLENF
160 170 180 190 200
LQKAPVPSTC SSTFPEELSP PSHQAKREIR FLELQKVASS SSGNNFLSGS
210 220 230 240 250
PASPMGDILQ TPQFQMRRLK KQLADERSNR DELELELAEN RKLLTEKDAQ
260 270 280 290 300
IAMMQQRIDR LALLNEKQAA SPLEPKELEE LRDKNESLTM RLHETLKQCQ
310 320 330 340 350
DLKTEKSQMD RKINQLSEEN GDLSFKLREF ASHLQQLQDA LNELTEEHSK
360 370 380 390 400
ATQEWLEKQA QLEKELSAAL QDKKCLEEKN EILQGKLSQL EEHLSQLQDN
410 420 430 440 450
PPQEKGEVLG DVLQLETLKQ EAATLAANNT QLQARVEMLE TERGQQEAKL
460 470 480 490 500
LAERGHFEEE KQQLSSLITD LQSSISNLSQ AKEELEQASQ AHGARLTAQV
510 520 530 540 550
ASLTSELTTL NATIQQQDQE LAGLKQQAKE KQAQLAQTLQ QQEQASQGLR
560 570 580 590 600
HQVEQLSSSL KQKEQQLKEV AEKQEATRQD HAQQLATAAE EREASLRERD
610 620 630 640 650
AALKQLEALE KEKAAKLEIL QQQLQVANEA RDSAQTSVTQ AQREKAELSR
660 670 680 690 700
KVEELQACVE TARQEQHEAQ AQVAELELQL RSEQQKATEK ERVAQEKDQL
710 720 730 740 750
QEQLQALKES LKVTKGSLEE EKRRAADALE EQQRCISELK AETRSLVEQH
760 770 780 790 800
KRERKELEEE RAGRKGLEAR LQQLGEAHQA ETEVLRRELA EAMAAQHTAE
810 820 830 840 850
SECEQLVKEV AAWRERYEDS QQEEAQYGAM FQEQLMTLKE ECEKARQELQ
860 870 880 890 900
EAKEKVAGIE SHSELQISRQ QNELAELHAN LARALQQVQE KEVRAQKLAD
910 920 930 940 950
DLSTLQEKMA ATSKEVARLE TLVRKAGEQQ ETASRELVKE PARAGDRQPE
960 970 980 990 1000
WLEEQQGRQF CSTQAALQAM EREAEQMGNE LERLRAALME SQGQQQEERG
1010 1020 1030 1040 1050
QQEREVARLT QERGRAQADL ALEKAARAEL EMRLQNALNE QRVEFATLQE
1060 1070 1080 1090 1100
ALAHALTEKE GKDQELAKLR GLEAAQIKEL EELRQTVKQL KEQLAKKEKE
1110 1120 1130 1140 1150
HASGSGAQSE AAGRTEPTGP KLEALRAEVS KLEQQCQKQQ EQADSLERSL
1160 1170 1180 1190 1200
EAERASRAER DSALETLQGQ LEEKAQELGH SQSALASAQR ELAAFRTKVQ
1210 1220 1230 1240 1250
DHSKAEDEWK AQVARGRQEA ERKNSLISSL EEEVSILNRQ VLEKEGESKE
1260 1270 1280 1290 1300
LKRLVMAESE KSQKLEERLR LLQAETASNS ARAAERSSAL REEVQSLREE
1310 1320 1330 1340 1350
AEKQRVASEN LRQELTSQAE RAEELGQELK AWQEKFFQKE QALSTLQLEH
1360 1370 1380 1390 1400
TSTQALVSEL LPAKHLCQQL QAEQAAAEKR HREELEQSKQ AAGGLRAELL
1410 1420 1430 1440 1450
RAQRELGELI PLRQKVAEQE RTAQQLRAEK ASYAEQLSML KKAHGLLAEE
1460 1470 1480 1490 1500
NRGLGERANL GRQFLEVELD QAREKYVQEL AAVRADAETR LAEVQREAQS
1510 1520 1530 1540 1550
TARELEVMTA KYEGAKVKVL EERQRFQEER QKLTAQVEQL EVFQREQTKQ
1560 1570 1580 1590 1600
VEELSKKLAD SDQASKVQQQ KLKAVQAQGG ESQQEAQRLQ AQLNELQAQL
1610 1620 1630 1640 1650
SQKEQAAEHY KLQMEKAKTH YDAKKQQNQE LQEQLRSLEQ LQKENKELRA
1660 1670 1680 1690 1700
EAERLGHELQ QAGLKTKEAE QTCRHLTAQV RSLEAQVAHA DQQLRDLGKF
1710 1720 1730 1740 1750
QVATDALKSR EPQAKPQLDL SIDSLDLSCE EGTPLSITSK LPRTQPDGTS
1760 1770 1780 1790 1800
VPGEPASPIS QRLPPKVESL ESLYFTPIPA RSQAPLESSL DSLGDVFLDS
1810 1820 1830 1840 1850
GRKTRSARRR TTQIINITMT KKLDVEEPDS ANSSFYSTRS APASQASLRA
1860 1870 1880 1890 1900
TSSTQSLARL GSPDYGNSAL LSLPGYRPTT RSSARRSQAG VSSGAPPGRN
1910 1920 1930 1940 1950
SFYMGTCQDE PEQLDDWNRI AELQQRNRVC PPHLKTCYPL ESRPSLSLGT
1960 1970 1980 1990 2000
ITDEEMKTGD PQETLRRASM QPIQIAEGTG ITTRQQRKRV SLEPHQGPGT
2010 2020 2030 2040 2050
PESKKATSCF PRPMTPRDRH EGRKQSTTEA QKKAAPASTK QADRRQSMAF
2060 2070 2080 2090 2100
SILNTPKKLG NSLLRRGASK KALSKASPNT RSGTRRSPRI ATTTASAATA
2110
AAIGATPRAK GKAKH
Length:2,115
Mass (Da):238,260
Last modified:April 17, 2007 - v2
<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:iDE734EC85B812CC7
GO
Isoform 2 (identifier: Q14980-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1536-1549: Missing.

Note: No experimental confirmation available.
Show »
Length:2,101
Mass (Da):236,516
Checksum:i18D8C4A34409ADE9
GO
Isoform 3 (identifier: Q14980-3) [UniParc]FASTAAdd to basket
Also known as: Numa-m1 Publication, p195

The sequence of this isoform differs from the canonical sequence as follows:
     1725-2115: LDLSCEEGTP...TPRAKGKAKH → SQANSSQTPR...ALSLPCLLFS

Show »
Length:1,776
Mass (Da):201,453
Checksum:i4CCE2F79A2228DCD
GO
Isoform 4 (identifier: Q14980-4) [UniParc]FASTAAdd to basket
Also known as: Numa-s1 Publication, p194

The sequence of this isoform differs from the canonical sequence as follows:
     1739-2115: SKLPRTQPDG...TPRAKGKAKH → RSGGSLPPYVCLWSACCLSGCILVR

Show »
Length:1,763
Mass (Da):200,097
Checksum:iB288C63D156E3E18
GO
Isoform 5 (identifier: Q14980-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     414-1549: Missing.

Note: No experimental confirmation available.
Show »
Length:979
Mass (Da):109,279
Checksum:iA1371283C8D14140
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 18 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F5H6Y5F5H6Y5_HUMAN
Nuclear mitotic apparatus protein 1
NUMA1
691Annotation 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>
F5H4J1F5H4J1_HUMAN
Nuclear mitotic apparatus protein 1
NUMA1
851Annotation 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>
A0A087WY61A0A087WY61_HUMAN
Nuclear mitotic apparatus protein 1
NUMA1
2,099Annotation 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>
H0YFY6H0YFY6_HUMAN
Nuclear mitotic apparatus protein 1
NUMA1
964Annotation 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>
K4DIE0K4DIE0_HUMAN
Nuclear mitotic apparatus protein 1
NUMA1
353Annotation 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>
F8W6T3F8W6T3_HUMAN
Nuclear mitotic apparatus protein 1
NUMA1
91Annotation 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>
F5H0Z7F5H0Z7_HUMAN
Nuclear mitotic apparatus protein 1
NUMA1
201Annotation 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>
F5H3L6F5H3L6_HUMAN
Nuclear mitotic apparatus protein 1
NUMA1
174Annotation 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>
F5GWK2F5GWK2_HUMAN
Nuclear mitotic apparatus protein 1
NUMA1
72Annotation 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>
F5H073F5H073_HUMAN
Nuclear mitotic apparatus protein 1
NUMA1
75Annotation 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>
There are more potential isoformsShow all

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence CAA77670 differs from that shown. Reason: Frameshift at positions 1270 and 1299.Curated

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 conflicti772Q → L in CAA77670 (PubMed:1541636).Curated1
Sequence conflicti815 – 816ER → DG in CAA77670 (PubMed:1541636).Curated2
Sequence conflicti873E → K in CAA77670 (PubMed:1541636).Curated1
Sequence conflicti1589L → F in CAA77670 (PubMed:1541636).Curated1
Sequence conflicti1637S → T in Z14227 (PubMed:8408288).Curated1
Sequence conflicti1637S → T in Z14228 (PubMed:8408288).Curated1
Sequence conflicti1682S → T in Z14227 (PubMed:8408288).Curated1
Sequence conflicti1682S → T in Z14228 (PubMed:8408288).Curated1
Sequence conflicti1798L → Q in CAA77669 (PubMed:8408288).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_031679242K → R. Corresponds to variant dbSNP:rs34239655Ensembl.1
Natural variantiVAR_031680794A → G. Corresponds to variant dbSNP:rs3750913Ensembl.1
Natural variantiVAR_0316811153E → D. Corresponds to variant dbSNP:rs34311364Ensembl.1
Natural variantiVAR_0316821825V → M. Corresponds to variant dbSNP:rs7949430Ensembl.1
Natural variantiVAR_0316831836Y → H. Corresponds to variant dbSNP:rs35586429Ensembl.1
Natural variantiVAR_0512482049A → T. Corresponds to variant dbSNP:rs5743685Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_054146414 – 1549Missing in isoform 5. 1 PublicationAdd BLAST1136
Alternative sequenceiVSP_0129101536 – 1549Missing in isoform 2. 1 PublicationAdd BLAST14
Alternative sequenceiVSP_0443781725 – 2115LDLSC…GKAKH → SQANSSQTPRDSDACPHPGL VPGPSLAPSRSWPRGPGAWT VWALSLPCLLFS in isoform 3. 1 PublicationAdd BLAST391
Alternative sequenceiVSP_0443791739 – 2115SKLPR…GKAKH → RSGGSLPPYVCLWSACCLSG CILVR in isoform 4. 1 PublicationAdd BLAST377

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Z14227 mRNA No translation available.
Z14228 mRNA No translation available.
Z14229 mRNA No translation available.
Z11583 mRNA Translation: CAA77669.1
Z11584 mRNA Translation: CAA77670.1 Frameshift.
AP002490 Genomic DNA No translation available.
CH471076 Genomic DNA Translation: EAW74826.1
BC004165 mRNA Translation: AAH04165.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS31633.1 [Q14980-1]
CCDS66156.1 [Q14980-2]

Protein sequence database of the Protein Information Resource

More...
PIRi
A42184

NCBI Reference Sequences

More...
RefSeqi
NP_001273490.1, NM_001286561.1 [Q14980-2]
NP_006176.2, NM_006185.3 [Q14980-1]
XP_006718627.1, XM_006718564.1 [Q14980-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000351960; ENSP00000260051; ENSG00000137497 [Q14980-5]
ENST00000358965; ENSP00000351851; ENSG00000137497 [Q14980-2]
ENST00000393695; ENSP00000377298; ENSG00000137497 [Q14980-1]
ENST00000613205; ENSP00000480172; ENSG00000137497 [Q14980-5]
ENST00000620566; ENSP00000478624; ENSG00000137497 [Q14980-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
4926

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:4926

UCSC genome browser

More...
UCSCi
uc001ork.3 human [Q14980-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z14227 mRNA No translation available.
Z14228 mRNA No translation available.
Z14229 mRNA No translation available.
Z11583 mRNA Translation: CAA77669.1
Z11584 mRNA Translation: CAA77670.1 Frameshift.
AP002490 Genomic DNA No translation available.
CH471076 Genomic DNA Translation: EAW74826.1
BC004165 mRNA Translation: AAH04165.1
CCDSiCCDS31633.1 [Q14980-1]
CCDS66156.1 [Q14980-2]
PIRiA42184
RefSeqiNP_001273490.1, NM_001286561.1 [Q14980-2]
NP_006176.2, NM_006185.3 [Q14980-1]
XP_006718627.1, XM_006718564.1 [Q14980-1]

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3RO2X-ray2.30B1899-1926[»]
5GXWX-ray2.39B1984-2010[»]
SMRiQ14980
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110980, 115 interactors
CORUMiQ14980
DIPiDIP-32937N
ELMiQ14980
IntActiQ14980, 71 interactors
MINTiQ14980
STRINGi9606.ENSP00000377298

PTM databases

CarbonylDBiQ14980
iPTMnetiQ14980
PhosphoSitePlusiQ14980
SwissPalmiQ14980

Polymorphism and mutation databases

BioMutaiNUMA1
DMDMi145559510

Proteomic databases

EPDiQ14980
jPOSTiQ14980
MaxQBiQ14980
PaxDbiQ14980
PeptideAtlasiQ14980
PRIDEiQ14980
ProteomicsDBi60272
60273 [Q14980-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
4926
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000351960; ENSP00000260051; ENSG00000137497 [Q14980-5]
ENST00000358965; ENSP00000351851; ENSG00000137497 [Q14980-2]
ENST00000393695; ENSP00000377298; ENSG00000137497 [Q14980-1]
ENST00000613205; ENSP00000480172; ENSG00000137497 [Q14980-5]
ENST00000620566; ENSP00000478624; ENSG00000137497 [Q14980-2]
GeneIDi4926
KEGGihsa:4926
UCSCiuc001ork.3 human [Q14980-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4926
DisGeNETi4926

GeneCards: human genes, protein and diseases

More...
GeneCardsi
NUMA1

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0026234
HGNCiHGNC:8059 NUMA1
HPAiHPA019841
HPA019859
HPA029912
MalaCardsiNUMA1
MIMi164009 gene
neXtProtiNX_Q14980
OpenTargetsiENSG00000137497
Orphaneti520 Acute promyelocytic leukemia
PharmGKBiPA31844

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IFJ8 Eukaryota
ENOG41125FF LUCA
GeneTreeiENSGT00950000183078
HOGENOMiHOG000113889
InParanoidiQ14980
KOiK16808
OMAiLETLYFT
OrthoDBi524033at2759
PhylomeDBiQ14980
TreeFamiTF334442

Enzyme and pathway databases

ReactomeiR-HSA-380320 Recruitment of NuMA to mitotic centrosomes
R-HSA-68875 Mitotic Prophase
SIGNORiQ14980

Miscellaneous databases

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

More...
ChiTaRSi
NUMA1 human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Nuclear_mitotic_apparatus_protein_1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
4926

Protein Ontology

More...
PROi
PR:Q14980

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000137497 Expressed in 239 organ(s), highest expression level in myometrium
ExpressionAtlasiQ14980 baseline and differential
GenevisibleiQ14980 HS

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_HUMAN
<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: Q14980
Secondary accession number(s): H0YH75, Q14981, Q9BTE9
<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 19, 2004
Last sequence update: April 17, 2007
Last modified: May 8, 2019
This is version 179 of the entry and version 2 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again