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Protein

Serine/threonine-protein kinase Nek2

Gene

NEK2

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

Protein kinase which is involved in the control of centrosome separation and bipolar spindle formation in mitotic cells and chromatin condensation in meiotic cells. Regulates centrosome separation (essential for the formation of bipolar spindles and high-fidelity chromosome separation) by phosphorylating centrosomal proteins such as CROCC, CEP250 and NINL, resulting in their displacement from the centrosomes. Regulates kinetochore microtubule attachment stability in mitosis via phosphorylation of NDC80. Involved in regulation of mitotic checkpoint protein complex via phosphorylation of CDC20 and MAD2L1. Plays an active role in chromatin condensation during the first meiotic division through phosphorylation of HMGA2. Phosphorylates: PPP1CC; SGO1; NECAB3 and NPM1. Essential for localization of MAD2L1 to kinetochore and MAPK1 and NPM1 to the centrosome. Phosphorylates CEP68 and CNTLN directly or indirectly (PubMed:24554434). NEK2-mediated phosphorylation of CEP68 promotes CEP68 dissociation from the centrosome and its degradation at the onset of mitosis (PubMed:25704143). Involved in the regulation of centrosome disjunction (PubMed:26220856).15 Publications
Isoform 1: Phosphorylates and activates NEK11 in G1/S-arrested cells.1 Publication
Isoform 2: Not present in the nucleolus and, in contrast to isoform 1, does not phosphorylate and activate NEK11 in G1/S-arrested cells.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Isoform 1 is inhibited by ionizing radiation in the presence of PPP1CA. Its catalytic activity is inhibited by the inhibitor CCT241950. In the presence of this inhibitor, displays an autoinhibited conformation: Tyr-70 side chain points into the active site, interacts with the activation loop, and blocks the alphaC helix.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei37ATP1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei141Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi14 – 22ATPPROSITE-ProRule annotation9

<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

  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • protein kinase activity Source: UniProtKB
  • protein phosphatase binding Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB

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

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processCell cycle, Cell division, Chromosome partition, Meiosis, Mitosis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.7.11.1 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-179409 APC-Cdc20 mediated degradation of Nek2A
R-HSA-2565942 Regulation of PLK1 Activity at G2/M Transition
R-HSA-380259 Loss of Nlp from mitotic centrosomes
R-HSA-380270 Recruitment of mitotic centrosome proteins and complexes
R-HSA-380284 Loss of proteins required for interphase microtubule organization from the centrosome
R-HSA-380320 Recruitment of NuMA to mitotic centrosomes
R-HSA-5620912 Anchoring of the basal body to the plasma membrane
R-HSA-8854518 AURKA Activation by TPX2

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P51955

SIGNOR Signaling Network Open Resource

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SIGNORi
P51955

<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:
Serine/threonine-protein kinase Nek2 (EC:2.7.11.1)
Alternative name(s):
HSPK 21
Never in mitosis A-related kinase 2
Short name:
NimA-related protein kinase 2
NimA-like protein kinase 1
<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:NEK2
Synonyms:NEK2A, NLK1
<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 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000117650.12

Human Gene Nomenclature Database

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HGNCi
HGNC:7745 NEK2

Online Mendelian Inheritance in Man (OMIM)

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MIMi
604043 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P51955

<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

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, 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 provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Retinitis pigmentosa 67 (RP67)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.
See also OMIM:615565

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>Mutagenesisi37K → R: Loss of kinase activity and of ability to activate NEK11. 2 Publications1
Mutagenesisi141D → A: Loss of autophosphorylation. 1 Publication1
Mutagenesisi170T → A: No effect on kinase activity. 1 Publication1
Mutagenesisi170T → E: Kinase activity increased by two fold. 1 Publication1
Mutagenesisi171S → A: No effect on kinase activity. 1 Publication1
Mutagenesisi171S → D: Kinase activity increased by two fold. 1 Publication1
Mutagenesisi175T → A: Kinase activity decreased by two fold. 1 Publication1
Mutagenesisi175T → E: Kinase activity increased by two fold. 1 Publication1
Mutagenesisi179T → A: Loss of kinase activity. 1 Publication1
Mutagenesisi179T → E: Loss of kinase activity. 1 Publication1
Mutagenesisi241S → A: Loss of kinase activity. 1 Publication1
Mutagenesisi241S → D: Loss of kinase activity. 1 Publication1

Keywords - Diseasei

Retinitis pigmentosa

Organism-specific databases

DisGeNET

More...
DisGeNETi
4751

MalaCards human disease database

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MalaCardsi
NEK2
MIMi615565 phenotype

Open Targets

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OpenTargetsi
ENSG00000117650

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

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Orphaneti
791 Retinitis pigmentosa

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA31546

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3835

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2117

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
NEK2

Domain mapping of disease mutations (DMDM)

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DMDMi
1709252

<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_00000864211 – 445Serine/threonine-protein kinase Nek2Add BLAST445

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 residuei170Phosphothreonine; by autocatalysis1 Publication1
Modified residuei171Phosphoserine; by autocatalysisCombined sources1 Publication1
Modified residuei175Phosphothreonine; by autocatalysis1 Publication1
Modified residuei179Phosphothreonine; by autocatalysis1 Publication1
Modified residuei184PhosphoserineCombined sources1
Modified residuei241Phosphoserine; by autocatalysis1 Publication1
Modified residuei296PhosphoserineCombined sources1
Modified residuei300PhosphoserineCombined sources1
Modified residuei356Phosphoserine; by STK3/MST22 Publications1
Modified residuei365Phosphoserine; by STK3/MST21 Publication1
Modified residuei387Phosphoserine1 Publication1
Modified residuei390Phosphoserine1 Publication1
Modified residuei397PhosphoserineCombined sources1 Publication1
Modified residuei402Phosphoserine1 Publication1
Modified residuei406Phosphoserine; by STK3/MST21 Publication1
Modified residuei428Phosphoserine1 Publication1
Modified residuei438Phosphoserine; by STK3/MST21 Publication1

<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

Activated by autophosphorylation. Protein phosphatase 1 represses autophosphorylation and activation of isoform 1 by dephosphorylation. Phosphorylation by STK3/MST2 is necessary for its localization to the centrosome.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P51955

MaxQB - The MaxQuant DataBase

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MaxQBi
P51955

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

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PaxDbi
P51955

PeptideAtlas

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PeptideAtlasi
P51955

PRoteomics IDEntifications database

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PRIDEi
P51955

ProteomicsDB human proteome resource

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ProteomicsDBi
56453
56454 [P51955-2]
56455 [P51955-3]
56456 [P51955-4]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P51955

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

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PhosphoSitePlusi
P51955

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
P51955

<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

Isoform 1 and isoform 2 are expressed in peripheral blood T-cells and a wide variety of transformed cell types. Isoform 1 and isoform 4 are expressed in the testis. Up-regulated in various cancer cell lines, as well as primary breast tumors.2 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expression and activity peak in the G2 phase of the mitotic cycle and decrease once the cells have entered mitosis due to degradation by the anaphase promoting complex APC/C-CDC20. In G1 phase, both isoform 1 and isoform 2 are almost undetectable. However, at the G1/S transition, there is an increase in expression of both isoforms which then remain at this increased level throughout S and G2. At the onset of mitosis, isoform 1 undergoes a rapid disappearance whereas isoform 2 continues to be present at about the same level as in G2. During the rest of mitosis, isoform 1 remains absent, while isoform 2 only begins to decline upon re-entry into the next G1 phase.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000117650 Expressed in 153 organ(s), highest expression level in testis

CleanEx database of gene expression profiles

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CleanExi
HS_NEK2

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P51955 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P51955 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB017530
HPA064967

<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

Isoform 1, isoform 2 and isoform 4 form homo- and heterodimers. Interacts with NECAB3 and HMGA2 (By similarity). Isoform 1 interacts with CDC20, CTNB1, MAD1L1, MAPK, NEK11, NPM1, NDC80, PCNT and SGO1 (PubMed:14978040, PubMed:15358203, PubMed:15388344, PubMed:15161910, PubMed:17621308, PubMed:18086858, PubMed:18297113, PubMed:20599736, PubMed:20034488). Isoform 1 interacts with STK3/MST2 (via SARAH domain) and SAV1 (via SARAH domain) (PubMed:21076410). Isoform 1 and isoform 2 interact with MAD2L1 (PubMed:20034488). Isoform 1 and isoform 4 interact with PPP1CA and PPP1CC (PubMed:15659832, PubMed:17283141). Interacts with CEP68; the interaction leads to phosphorylation of CEP68. Interacts with CNTLN; the interaction leads to phosphorylation of CNTLN (PubMed:24554434). Isoform 1 interacts with CEP85 (PubMed:26220856).By similarity16 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)

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BioGridi
110826, 54 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P51955

Protein interaction database and analysis system

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IntActi
P51955, 41 interactors

Molecular INTeraction database

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MINTi
P51955

STRING: functional protein association networks

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STRINGi
9606.ENSP00000355966

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P51955

<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

1445
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P51955

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

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SMRi
P51955

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...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P51955

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini8 – 271Protein kinasePROSITE-ProRule annotationAdd BLAST264

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>Regioni264 – 445Interaction with PCNT1 PublicationAdd BLAST182
Regioni301 – 445Interaction with CEP851 PublicationAdd BLAST145
Regioni306 – 334Leucine-zipperAdd BLAST29
Regioni329 – 445Necessary for interaction with MAD1L11 PublicationAdd BLAST117
Regioni333 – 370Required for microtubule binding and for localization to the centrosomesAdd BLAST38
Regioni403 – 439Interaction with SAV1 and STK3/MST21 PublicationAdd BLAST37

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 coili303 – 362Sequence analysisAdd BLAST60
Coiled coili406 – 430Sequence analysisAdd BLAST25

<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 leucine-zipper domain is required for its dimerization and activation.1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0591 Eukaryota
ENOG410XNQP LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000156989

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG006461

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P51955

KEGG Orthology (KO)

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KOi
K20872

Identification of Orthologs from Complete Genome Data

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OMAi
AYNQKEL

Database of Orthologous Groups

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OrthoDBi
EOG091G07PD

Database for complete collections of gene phylogenies

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PhylomeDBi
P51955

TreeFam database of animal gene trees

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TreeFami
TF101184

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR008271 Ser/Thr_kinase_AS

Pfam protein domain database

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Pfami
View protein in Pfam
PF00069 Pkinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 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 (4+)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 4 <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 4 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: P51955-1) [UniParc]FASTAAdd to basket
Also known as: Nek2A

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
MPSRAEDYEV LYTIGTGSYG RCQKIRRKSD GKILVWKELD YGSMTEAEKQ
60 70 80 90 100
MLVSEVNLLR ELKHPNIVRY YDRIIDRTNT TLYIVMEYCE GGDLASVITK
110 120 130 140 150
GTKERQYLDE EFVLRVMTQL TLALKECHRR SDGGHTVLHR DLKPANVFLD
160 170 180 190 200
GKQNVKLGDF GLARILNHDT SFAKTFVGTP YYMSPEQMNR MSYNEKSDIW
210 220 230 240 250
SLGCLLYELC ALMPPFTAFS QKELAGKIRE GKFRRIPYRY SDELNEIITR
260 270 280 290 300
MLNLKDYHRP SVEEILENPL IADLVADEQR RNLERRGRQL GEPEKSQDSS
310 320 330 340 350
PVLSELKLKE IQLQERERAL KAREERLEQK EQELCVRERL AEDKLARAEN
360 370 380 390 400
LLKNYSLLKE RKFLSLASNP ELLNLPSSVI KKKVHFSGES KENIMRSENS
410 420 430 440
ESQLTSKSKC KDLKKRLHAA QLRAQALSDI EKNYQLKSRQ ILGMR
Length:445
Mass (Da):51,763
Last modified:October 1, 1996 - 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:iD33A37778ABB6D9E
GO
Isoform 2 (identifier: P51955-2) [UniParc]FASTAAdd to basket
Also known as: Nek2B

The sequence of this isoform differs from the canonical sequence as follows:
     371-384: ELLNLPSSVIKKKV → GMRINLVNRSWCYK
     385-445: Missing.

Show »
Length:384
Mass (Da):44,906
Checksum:iEBFA8B6BB07480FB
GO
Isoform 3 (identifier: P51955-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     323-326: REER → KKKK
     327-445: Missing.

Show »
Length:326
Mass (Da):37,956
Checksum:i3F3FDD8262E77964
GO
Isoform 4 (identifier: P51955-4) [UniParc]FASTAAdd to basket
Also known as: Nek2C, Nek2A-T

The sequence of this isoform differs from the canonical sequence as follows:
     371-378: Missing.

Show »
Length:437
Mass (Da):50,909
Checksum:iBF89938C50FAD817
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F6U4U2F6U4U2_HUMAN
Serine/threonine-protein kinase Nek...
NEK2
388Annotation 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>

<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 AAH65932 differs from that shown. Reason: Frameshift at position 213.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 conflicti84 – 85IV → LY in CAA80912 (PubMed:8274451).Curated2
Sequence conflicti325E → K in BAD97073 (Ref. 5) 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_019990354N → S2 PublicationsCorresponds to variant dbSNP:rs2230489Ensembl.1
Natural variantiVAR_040907410C → Y1 PublicationCorresponds to variant dbSNP:rs56102977Ensembl.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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_015576323 – 326REER → KKKK in isoform 3. 1 Publication4
Alternative sequenceiVSP_015577327 – 445Missing in isoform 3. 1 PublicationAdd BLAST119
Alternative sequenceiVSP_015578371 – 384ELLNL…IKKKV → GMRINLVNRSWCYK in isoform 2. 1 PublicationAdd BLAST14
Alternative sequenceiVSP_041758371 – 378Missing in isoform 4. 1 Publication8
Alternative sequenceiVSP_015579385 – 445Missing in isoform 2. 1 PublicationAdd BLAST61

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

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DDBJi
Links Updated
Z29066 mRNA Translation: CAA82309.1
AY045701 mRNA Translation: AAK92212.1
U11050 mRNA Translation: AAA19558.1
BT019729 mRNA Translation: AAV38534.1
AK223353 mRNA Translation: BAD97073.1
AC096637 Genomic DNA No translation available.
AL356310 Genomic DNA No translation available.
BC043502 mRNA Translation: AAH43502.2
BC052807 mRNA Translation: AAH52807.1
BC065932 mRNA Translation: AAH65932.1 Frameshift.
Z25425 mRNA Translation: CAA80912.1
AY863109 mRNA Translation: AAW56418.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS1500.1 [P51955-1]
CCDS55682.1 [P51955-2]

Protein sequence database of the Protein Information Resource

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PIRi
G01452
I38215

NCBI Reference Sequences

More...
RefSeqi
NP_001191111.1, NM_001204182.1
NP_001191112.1, NM_001204183.1 [P51955-2]
NP_002488.1, NM_002497.3 [P51955-1]
XP_005273204.1, XM_005273147.1 [P51955-4]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.153704

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000366998; ENSP00000355965; ENSG00000117650 [P51955-2]
ENST00000366999; ENSP00000355966; ENSG00000117650 [P51955-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
4751

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:4751

UCSC genome browser

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UCSCi
uc001hir.3 human [P51955-1]

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z29066 mRNA Translation: CAA82309.1
AY045701 mRNA Translation: AAK92212.1
U11050 mRNA Translation: AAA19558.1
BT019729 mRNA Translation: AAV38534.1
AK223353 mRNA Translation: BAD97073.1
AC096637 Genomic DNA No translation available.
AL356310 Genomic DNA No translation available.
BC043502 mRNA Translation: AAH43502.2
BC052807 mRNA Translation: AAH52807.1
BC065932 mRNA Translation: AAH65932.1 Frameshift.
Z25425 mRNA Translation: CAA80912.1
AY863109 mRNA Translation: AAW56418.1
CCDSiCCDS1500.1 [P51955-1]
CCDS55682.1 [P51955-2]
PIRiG01452
I38215
RefSeqiNP_001191111.1, NM_001204182.1
NP_001191112.1, NM_001204183.1 [P51955-2]
NP_002488.1, NM_002497.3 [P51955-1]
XP_005273204.1, XM_005273147.1 [P51955-4]
UniGeneiHs.153704

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JAVX-ray2.20A1-271[»]
2W5AX-ray1.55A1-271[»]
2W5BX-ray2.40A1-271[»]
2W5HX-ray2.33A1-271[»]
2WQOX-ray2.17A1-271[»]
2XK3X-ray2.20A1-271[»]
2XK4X-ray2.10A1-271[»]
2XK6X-ray2.20A1-271[»]
2XK7X-ray1.99A1-271[»]
2XK8X-ray2.00A1-271[»]
2XKCX-ray2.50A1-271[»]
2XKDX-ray1.96A1-271[»]
2XKEX-ray2.20A1-271[»]
2XKFX-ray2.35A1-271[»]
2XNMX-ray1.85A1-271[»]
2XNNX-ray2.50A1-271[»]
2XNOX-ray1.98A1-271[»]
2XNPX-ray1.98A1-271[»]
4A4XX-ray2.40A1-271[»]
4AFEX-ray2.60A1-271[»]
5M51X-ray1.90A1-271[»]
5M53X-ray1.90A1-271[»]
5M55X-ray2.40A1-271[»]
5M57X-ray2.30A1-271[»]
6H0OX-ray2.00A1-271[»]
ProteinModelPortaliP51955
SMRiP51955
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110826, 54 interactors
CORUMiP51955
IntActiP51955, 41 interactors
MINTiP51955
STRINGi9606.ENSP00000355966

Chemistry databases

BindingDBiP51955
ChEMBLiCHEMBL3835
GuidetoPHARMACOLOGYi2117

PTM databases

iPTMnetiP51955
PhosphoSitePlusiP51955

Polymorphism and mutation databases

BioMutaiNEK2
DMDMi1709252

Proteomic databases

EPDiP51955
MaxQBiP51955
PaxDbiP51955
PeptideAtlasiP51955
PRIDEiP51955
ProteomicsDBi56453
56454 [P51955-2]
56455 [P51955-3]
56456 [P51955-4]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
4751
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366998; ENSP00000355965; ENSG00000117650 [P51955-2]
ENST00000366999; ENSP00000355966; ENSG00000117650 [P51955-1]
GeneIDi4751
KEGGihsa:4751
UCSCiuc001hir.3 human [P51955-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4751
DisGeNETi4751
EuPathDBiHostDB:ENSG00000117650.12

GeneCards: human genes, protein and diseases

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GeneCardsi
NEK2
HGNCiHGNC:7745 NEK2
HPAiCAB017530
HPA064967
MalaCardsiNEK2
MIMi604043 gene
615565 phenotype
neXtProtiNX_P51955
OpenTargetsiENSG00000117650
Orphaneti791 Retinitis pigmentosa
PharmGKBiPA31546

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0591 Eukaryota
ENOG410XNQP LUCA
GeneTreeiENSGT00940000156989
HOVERGENiHBG006461
InParanoidiP51955
KOiK20872
OMAiAYNQKEL
OrthoDBiEOG091G07PD
PhylomeDBiP51955
TreeFamiTF101184

Enzyme and pathway databases

BRENDAi2.7.11.1 2681
ReactomeiR-HSA-179409 APC-Cdc20 mediated degradation of Nek2A
R-HSA-2565942 Regulation of PLK1 Activity at G2/M Transition
R-HSA-380259 Loss of Nlp from mitotic centrosomes
R-HSA-380270 Recruitment of mitotic centrosome proteins and complexes
R-HSA-380284 Loss of proteins required for interphase microtubule organization from the centrosome
R-HSA-380320 Recruitment of NuMA to mitotic centrosomes
R-HSA-5620912 Anchoring of the basal body to the plasma membrane
R-HSA-8854518 AURKA Activation by TPX2
SignaLinkiP51955
SIGNORiP51955

Miscellaneous databases

EvolutionaryTraceiP51955

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
NEK2

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

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GenomeRNAii
4751
PMAP-CutDBiP51955

Protein Ontology

More...
PROi
PR:P51955

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000117650 Expressed in 153 organ(s), highest expression level in testis
CleanExiHS_NEK2
ExpressionAtlasiP51955 baseline and differential
GenevisibleiP51955 HS

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 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 nameiNEK2_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: P51955
Secondary accession number(s): Q53FD6
, Q5I1Z9, Q5VXZ1, Q6NZX8, Q7Z634, Q86XH2, Q96QN9
<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: October 1, 1996
Last sequence update: October 1, 1996
Last modified: December 5, 2018
This is version 202 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
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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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