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Entry version 204 (22 Apr 2020)
Sequence version 1 (01 Nov 1996)
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Protein

Serine/threonine-protein kinase N2

Gene

PKN2

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

PKC-related serine/threonine-protein kinase and Rho/Rac effector protein that participates in specific signal transduction responses in the cell. Plays a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion, tumor cell invasion and transcription activation signaling processes. Phosphorylates CTTN in hyaluronan-induced astrocytes and hence decreases CTTN ability to associate with filamentous actin. Phosphorylates HDAC5, therefore lead to impair HDAC5 import. Direct RhoA target required for the regulation of the maturation of primordial junctions into apical junction formation in bronchial epithelial cells. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Stimulates FYN kinase activity that is required for establishment of skin cell-cell adhesion during keratinocytes differentiation. Regulates epithelial bladder cells speed and direction of movement during cell migration and tumor cell invasion. Inhibits Akt pro-survival-induced kinase activity. Mediates Rho protein-induced transcriptional activation via the c-fos serum response factor (SRF). Involved in the negative regulation of ciliogenesis (PubMed:27104747).12 Publications
(Microbial infection) Phosphorylates HCV NS5B leading to stimulation of HCV RNA replication.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

Kinase activity is activated upon binding to GTP-bound Rhoa/Rac1 GTPases. Activated by caspase-3 (CASP3) cleavage during apoptosis. Activated by lipids, particularly cardiolipin and to a lesser extent by other acidic phospholipids and unsaturated fatty acids. Two specific sites, Thr-816 (activation loop of the kinase domain) and Thr-958 (turn motif), need to be phosphorylated for its full activation.3 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=15.83 µM for HDAC51 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei686ATPPROSITE-ProRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei782Proton acceptorPROSITE-ProRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi663 – 671ATPPROSITE-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

    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 processApoptosis, Cell adhesion, Cell cycle, Cell division, Cilium biogenesis/degradation, Host-virus interaction, Transcription, Transcription regulation
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.7.11.13 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-5625740 RHO GTPases activate PKNs

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    Q16513

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

    More...
    SignaLinki
    Q16513

    SIGNOR Signaling Network Open Resource

    More...
    SIGNORi
    Q16513

    <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%5Fand%5Ftaxonomy%5Fsection">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 N2 (EC:2.7.11.13)
    Alternative name(s):
    PKN gamma
    Protein kinase C-like 2
    Protein-kinase C-related kinase 2
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:PKN2
    Synonyms:PRK2, PRKCL2
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:9406 PKN2

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    602549 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_Q16513

    <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 junction, Cell projection, Cytoplasm, Cytoskeleton, Membrane, 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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi117D → A: Prevents proteolytic processing by caspase-3 during apoptosis. Diminishes pro-apoptotic function; when associated with E-700. 2 Publications1
    Mutagenesisi121T → A: Does not suppress ciliogenesis; when associated with A-124. 1 Publication1
    Mutagenesisi124T → A: Does not suppress ciliogenesis; when associated with A-121. 1 Publication1
    Mutagenesisi686K → R: Does not inhibit interaction with PTPN13. 1 Publication1
    Mutagenesisi700D → E: Prevents proteolytic processing by caspase-3 during apoptosis. Diminishes pro-apoptotic function; when associated with A-117. 2 Publications1
    Mutagenesisi816T → A: Reduces catalytic activity. 1 Publication1
    Mutagenesisi958T → A: Abolishes catalytic activity. 1 Publication1
    Mutagenesisi974F → A: Abolishes interaction with PDPK1 and prevents the phosphorylation of AKT1 at 'Ser-473'. 1 Publication1
    Mutagenesisi977F → A or L: Abolishes interaction with PDPK1 and prevents the phosphorylation of AKT1 at 'Ser-473'. Reduces catalytic activity by 90%. 2 Publications1
    Mutagenesisi977F → W or Y: Reduces catalytic activity by 50%. 2 Publications1
    Mutagenesisi978D → A or S: Abolishes interaction with PDPK1 and prevents the phosphorylation of AKT1 at 'Ser-473'. 2 Publications1
    Mutagenesisi978D → A: Does not inhibit catalytic activity. 2 Publications1
    Mutagenesisi979Y → A: Abolishes interaction with PDPK1 and prevents the phosphorylation of AKT1 at 'Ser-473'. 2 Publications1
    Mutagenesisi979Y → A: Reduces catalytic activity by 50%. 2 Publications1
    Mutagenesisi979Y → F, L or W: Reduces catalytic activity by 25%. 2 Publications1
    Mutagenesisi984C → S: Inhibits interaction with PTPN13. 1 Publication1

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    5586

    Open Targets

    More...
    OpenTargetsi
    ENSG00000065243

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA33770

    Miscellaneous databases

    Pharos NIH Druggable Genome Knowledgebase

    More...
    Pharosi
    Q16513 Tchem

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL3032

    Drug and drug target database

    More...
    DrugBanki
    DB12010 Fostamatinib

    DrugCentral

    More...
    DrugCentrali
    Q16513

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...
    GuidetoPHARMACOLOGYi
    1521

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    PKN2

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    6225859

    <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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000557221 – 984Serine/threonine-protein kinase N2Add BLAST984

    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 residuei21PhosphoserineCombined sources1
    Modified residuei77N6-acetyllysineBy similarity1
    Modified residuei110PhosphoserineCombined sources1
    Modified residuei121PhosphothreonineCombined sources1 Publication1
    Modified residuei124PhosphothreonineCombined sources1 Publication1
    Modified residuei302PhosphoserineCombined sources1
    Modified residuei306PhosphoserineCombined sources1
    Modified residuei360PhosphoserineCombined sources1
    Modified residuei362PhosphoserineCombined sources1
    Modified residuei535PhosphoserineCombined sources1
    Modified residuei583PhosphoserineCombined sources1
    Modified residuei620PhosphoserineBy similarity1
    Modified residuei628PhosphothreonineCombined sources1
    Modified residuei631PhosphoserineCombined sources1
    Modified residuei816Phosphothreonine; by PDPK11 Publication1
    Modified residuei952PhosphoserineCombined sources1
    Modified residuei958PhosphothreonineCombined sources1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

    Autophosphorylated. Phosphorylated during mitosis. Phosphorylated by CDK10 (PubMed:27104747).3 Publications
    Activated by limited proteolysis with trypsin (By similarity). Proteolytically cleaved by caspase-3 during the induction of apoptotic cell death.By similarity1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei117 – 118Cleavage; by caspase-32
    Sitei700 – 701Cleavage; by caspase-32

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    Q16513

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    Q16513

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...
    MassIVEi
    Q16513

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    Q16513

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

    More...
    PaxDbi
    Q16513

    PeptideAtlas

    More...
    PeptideAtlasi
    Q16513

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q16513

    ProteomicsDB: a multi-organism proteome resource

    More...
    ProteomicsDBi
    60880 [Q16513-1]
    60881 [Q16513-2]
    60882 [Q16513-3]
    60883 [Q16513-4]
    60884 [Q16513-5]

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q16513

    MetOSite database of methionine sulfoxide sites

    More...
    MetOSitei
    Q16513

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

    More...
    PhosphoSitePlusi
    Q16513

    <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

    Ubiquitous. Expressed in numerous tumor cell lines, especially in bladder tumor cells.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

    Up-regulated during keratinocyte differentiation.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000065243 Expressed in intestine and 240 other tissues

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    Q16513 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q16513 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    ENSG00000065243 Low tissue specificity

    <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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Interacts (via the REM repeats) with RHOA (GTP-bound form preferentially) and interacts (via the REM repeats) with RAC1 (GTP-bound form preferentially); the interactions induce its autophosphorylation (PubMed:9121475, PubMed:20974804).

    Interacts with RHOC (PubMed:20974804).

    Interacts with NCK1 and NCK2 (PubMed:10026169).

    Interacts with NCK1 (via SH3 domains) (By similarity).

    Interacts with CD44 (PubMed:15123640).

    Interacts (via C-terminal kinase domain) with PDPK1; the interaction stimulates PDPK1 kinase activity (PubMed:10226025, PubMed:10792047, PubMed:11781095, PubMed:18835241).

    Interacts with MAP3K2; the interaction activates PRK2 kinase activity in a MAP3K2-independent kinase activity (PubMed:10818102).

    Interacts (via C-terminal domain) with AKT1; the interaction occurs with the C-terminal cleavage product of PRK2 in apoptotic cells (PubMed:10926925).

    Interacts (via C-terminus) with PTPN13 (via PDZ 3 domain) (PubMed:11356191).

    Interacts with CDK10 (PubMed:27104747).

    By similarity13 Publications

    (Microbial infection) Interacts with HCV NS5B (via N-terminal finger domain).

    1 Publication

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

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    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    111572, 98 interactors

    The Eukaryotic Linear Motif resource for Functional Sites in Proteins

    More...
    ELMi
    Q16513

    Protein interaction database and analysis system

    More...
    IntActi
    Q16513, 69 interactors

    Molecular INTeraction database

    More...
    MINTi
    Q16513

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000359552

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    Q16513

    Miscellaneous databases

    RNAct, Protein-RNA interaction predictions for model organisms.

    More...
    RNActi
    Q16513 protein

    <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

    1984
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

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

    More...
    SMRi
    Q16513

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    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

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">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>Domaini33 – 109REM-1 1PROSITE-ProRule annotationAdd BLAST77
    Domaini121 – 203REM-1 2PROSITE-ProRule annotationAdd BLAST83
    Domaini204 – 284REM-1 3PROSITE-ProRule annotationAdd BLAST81
    Domaini353 – 473C2PROSITE-ProRule annotationAdd BLAST121
    Domaini657 – 916Protein kinasePROSITE-ProRule annotationAdd BLAST260
    Domaini917 – 984AGC-kinase C-terminalAdd BLAST68

    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>Regioni382 – 463Necessary to rescue apical junction formationBy similarityAdd BLAST82
    Regioni917 – 977Necessary for the catalytic activityAdd BLAST61
    Regioni978 – 984Negatively regulates the responsiveness of the catalytic activity by cardiolipin and is required for optimal activation by the GTP-bound RhoA7

    <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 N-terminal regioninterferes with the interaction between AKT1 and the C-terminal regionof PKN2.
    The C1 domain does not bind the diacylglycerol (DAG).
    The apoptotic C-terminal cleavage product inhibits EGF-induced kinase activity of AKT1 phosphorylation at 'Thr-308' and 'Ser-473' sites, PDPK1 autophosphorylation and kinases PRKCD and PRKCZ phosphorylations.

    <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, Repeat

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG0694 Eukaryota
    ENOG410XNPH LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000154339

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_000288_132_1_1

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q16513

    KEGG Orthology (KO)

    More...
    KOi
    K23691

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    RHISWEW

    Database of Orthologous Groups

    More...
    OrthoDBi
    520651at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q16513

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF102005

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd08687 C2_PKN-like, 1 hit
    cd11622 HR1_PKN_1, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR000961 AGC-kinase_C
    IPR000008 C2_dom
    IPR037784 C2_PKN
    IPR011072 HR1_rho-bd
    IPR036274 HR1_rpt_sf
    IPR011009 Kinase-like_dom_sf
    IPR017892 Pkinase_C
    IPR037313 PKN_HR1_1
    IPR000719 Prot_kinase_dom
    IPR017441 Protein_kinase_ATP_BS
    IPR008271 Ser/Thr_kinase_AS

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02185 HR1, 3 hits
    PF00069 Pkinase, 1 hit
    PF00433 Pkinase_C, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00239 C2, 1 hit
    SM00742 Hr1, 3 hits
    SM00133 S_TK_X, 1 hit
    SM00220 S_TKc, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF46585 SSF46585, 3 hits
    SSF56112 SSF56112, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51285 AGC_KINASE_CTER, 1 hit
    PS50004 C2, 1 hit
    PS00107 PROTEIN_KINASE_ATP, 1 hit
    PS50011 PROTEIN_KINASE_DOM, 1 hit
    PS00108 PROTEIN_KINASE_ST, 1 hit
    PS51860 REM_1, 3 hits

    <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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<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 3 potential isoforms that are computationally mapped.Show allAlign All

    Isoform 1 (identifier: Q16513-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
    MASNPERGEI LLTELQGDSR SLPFSENVSA VQKLDFSDTM VQQKLDDIKD
    60 70 80 90 100
    RIKREIRKEL KIKEGAENLR KVTTDKKSLA YVDNILKKSN KKLEELHHKL
    110 120 130 140 150
    QELNAHIVVS DPEDITDCPR TPDTPNNDPR CSTSNNRLKA LQKQLDIELK
    160 170 180 190 200
    VKQGAENMIQ MYSNGSSKDR KLHGTAQQLL QDSKTKIEVI RMQILQAVQT
    210 220 230 240 250
    NELAFDNAKP VISPLELRME ELRHHFRIEF AVAEGAKNVM KLLGSGKVTD
    260 270 280 290 300
    RKALSEAQAR FNESSQKLDL LKYSLEQRLN EVPKNHPKSR IIIEELSLVA
    310 320 330 340 350
    ASPTLSPRQS MISTQNQYST LSKPAALTGT LEVRLMGCQD ILENVPGRSK
    360 370 380 390 400
    ATSVALPGWS PSETRSSFMS RTSKSKSGSS RNLLKTDDLS NDVCAVLKLD
    410 420 430 440 450
    NTVVGQTSWK PISNQSWDQK FTLELDRSRE LEISVYWRDW RSLCAVKFLR
    460 470 480 490 500
    LEDFLDNQRH GMCLYLEPQG TLFAEVTFFN PVIERRPKLQ RQKKIFSKQQ
    510 520 530 540 550
    GKTFLRAPQM NINIATWGRL VRRAIPTVNH SGTFSPQAPV PTTVPVVDVR
    560 570 580 590 600
    IPQLAPPASD STVTKLDFDL EPEPPPAPPR ASSLGEIDES SELRVLDIPG
    610 620 630 640 650
    QDSETVFDIQ NDRNSILPKS QSEYKPDTPQ SGLEYSGIQE LEDRRSQQRF
    660 670 680 690 700
    QFNLQDFRCC AVLGRGHFGK VLLAEYKNTN EMFAIKALKK GDIVARDEVD
    710 720 730 740 750
    SLMCEKRIFE TVNSVRHPFL VNLFACFQTK EHVCFVMEYA AGGDLMMHIH
    760 770 780 790 800
    TDVFSEPRAV FYAACVVLGL QYLHEHKIVY RDLKLDNLLL DTEGFVKIAD
    810 820 830 840 850
    FGLCKEGMGY GDRTSTFCGT PEFLAPEVLT ETSYTRAVDW WGLGVLIYEM
    860 870 880 890 900
    LVGESPFPGD DEEEVFDSIV NDEVRYPRFL STEAISIMRR LLRRNPERRL
    910 920 930 940 950
    GASEKDAEDV KKHPFFRLID WSALMDKKVK PPFIPTIRGR EDVSNFDDEF
    960 970 980
    TSEAPILTPP REPRILSEEE QEMFRDFDYI ADWC
    Length:984
    Mass (Da):112,035
    Last modified:November 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:i687EC417A0F51C1D
    GO
    Isoform 2 (identifier: Q16513-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         375-390: Missing.

    Show »
    Length:968
    Mass (Da):110,345
    Checksum:iBE8D7EDA728D78EE
    GO
    Isoform 3 (identifier: Q16513-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         428-475: Missing.

    Show »
    Length:936
    Mass (Da):106,217
    Checksum:i43128E92FEDC05B4
    GO
    Isoform 4 (identifier: Q16513-4) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-157: Missing.

    Show »
    Length:827
    Mass (Da):94,136
    Checksum:iB08B24A67D1697CE
    GO
    Isoform 5 (identifier: Q16513-5) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-326: Missing.
         327-329: LTG → MNS

    Show »
    Length:658
    Mass (Da):75,171
    Checksum:iD0B6E1DEA98B3C0D
    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 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    B1AL79B1AL79_HUMAN
    Protein kinase N2, isoform CRA_b
    PKN2 hCG_23733
    604Annotation 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>
    H0Y429H0Y429_HUMAN
    Serine/threonine-protein kinase N2
    PKN2
    65Annotation 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>
    H0Y5V5H0Y5V5_HUMAN
    Serine/threonine-protein kinase N2
    PKN2
    211Annotation score:

    Annotation score:1 out of 5

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

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti483I → V in BAG62673 (PubMed:14702039).Curated1
    Sequence conflicti565K → R in BAG60783 (PubMed:14702039).Curated1
    Sequence conflicti625K → R in BAG62673 (PubMed:14702039).Curated1
    Sequence conflicti795F → L in AAI25200 (PubMed:15489334).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_05056294E → D. Corresponds to variant dbSNP:rs12039846Ensembl.1
    Natural variantiVAR_050563197A → E. Corresponds to variant dbSNP:rs35207128Ensembl.1
    Natural variantiVAR_050564655Q → R. Corresponds to variant dbSNP:rs12085658Ensembl.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_0421801 – 326Missing in isoform 5. 1 PublicationAdd BLAST326
    Alternative sequenceiVSP_0421811 – 157Missing in isoform 4. 1 PublicationAdd BLAST157
    Alternative sequenceiVSP_042182327 – 329LTG → MNS in isoform 5. 1 Publication3
    Alternative sequenceiVSP_042183375 – 390Missing in isoform 2. 1 PublicationAdd BLAST16
    Alternative sequenceiVSP_042184428 – 475Missing in isoform 3. 1 PublicationAdd BLAST48

    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
    U33052 mRNA Translation: AAC50208.1
    S75548 mRNA Translation: AAB33346.1
    AK298595 mRNA Translation: BAG60783.1
    AK300304 mRNA Translation: BAG62057.1
    AK301066 mRNA Translation: BAG62673.1
    AC119426 Genomic DNA No translation available.
    AL136381 Genomic DNA No translation available.
    CH471097 Genomic DNA Translation: EAW73161.1
    CH471097 Genomic DNA Translation: EAW73164.1
    BC125199 mRNA Translation: AAI25200.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS714.1 [Q16513-1]
    CCDS81350.1 [Q16513-3]

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S67527

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001307636.1, NM_001320707.1 [Q16513-3]
    NP_001307637.1, NM_001320708.1 [Q16513-4]
    NP_001307638.1, NM_001320709.1 [Q16513-2]
    NP_006247.1, NM_006256.3 [Q16513-1]
    XP_011540074.1, XM_011541772.2 [Q16513-5]

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000370513; ENSP00000359544; ENSG00000065243 [Q16513-3]
    ENST00000370521; ENSP00000359552; ENSG00000065243 [Q16513-1]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    5586

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:5586

    UCSC genome browser

    More...
    UCSCi
    uc001dmn.4 human [Q16513-1]

    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
    U33052 mRNA Translation: AAC50208.1
    S75548 mRNA Translation: AAB33346.1
    AK298595 mRNA Translation: BAG60783.1
    AK300304 mRNA Translation: BAG62057.1
    AK301066 mRNA Translation: BAG62673.1
    AC119426 Genomic DNA No translation available.
    AL136381 Genomic DNA No translation available.
    CH471097 Genomic DNA Translation: EAW73161.1
    CH471097 Genomic DNA Translation: EAW73164.1
    BC125199 mRNA Translation: AAI25200.1
    CCDSiCCDS714.1 [Q16513-1]
    CCDS81350.1 [Q16513-3]
    PIRiS67527
    RefSeqiNP_001307636.1, NM_001320707.1 [Q16513-3]
    NP_001307637.1, NM_001320708.1 [Q16513-4]
    NP_001307638.1, NM_001320709.1 [Q16513-2]
    NP_006247.1, NM_006256.3 [Q16513-1]
    XP_011540074.1, XM_011541772.2 [Q16513-5]

    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
    4CRSX-ray2.75A646-984[»]
    4RRVX-ray1.41B969-983[»]
    6CCYX-ray2.18A969-983[»]
    6GBENMR-B973-984[»]
    SMRiQ16513
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi111572, 98 interactors
    ELMiQ16513
    IntActiQ16513, 69 interactors
    MINTiQ16513
    STRINGi9606.ENSP00000359552

    Chemistry databases

    BindingDBiQ16513
    ChEMBLiCHEMBL3032
    DrugBankiDB12010 Fostamatinib
    DrugCentraliQ16513
    GuidetoPHARMACOLOGYi1521

    PTM databases

    iPTMnetiQ16513
    MetOSiteiQ16513
    PhosphoSitePlusiQ16513

    Polymorphism and mutation databases

    BioMutaiPKN2
    DMDMi6225859

    Proteomic databases

    EPDiQ16513
    jPOSTiQ16513
    MassIVEiQ16513
    MaxQBiQ16513
    PaxDbiQ16513
    PeptideAtlasiQ16513
    PRIDEiQ16513
    ProteomicsDBi60880 [Q16513-1]
    60881 [Q16513-2]
    60882 [Q16513-3]
    60883 [Q16513-4]
    60884 [Q16513-5]

    Protocols and materials databases

    Antibodypedia a portal for validated antibodies

    More...
    Antibodypediai
    33594 228 antibodies

    The DNASU plasmid repository

    More...
    DNASUi
    5586

    Genome annotation databases

    EnsembliENST00000370513; ENSP00000359544; ENSG00000065243 [Q16513-3]
    ENST00000370521; ENSP00000359552; ENSG00000065243 [Q16513-1]
    GeneIDi5586
    KEGGihsa:5586
    UCSCiuc001dmn.4 human [Q16513-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    5586
    DisGeNETi5586

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    PKN2
    HGNCiHGNC:9406 PKN2
    HPAiENSG00000065243 Low tissue specificity
    MIMi602549 gene
    neXtProtiNX_Q16513
    OpenTargetsiENSG00000065243
    PharmGKBiPA33770

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG0694 Eukaryota
    ENOG410XNPH LUCA
    GeneTreeiENSGT00940000154339
    HOGENOMiCLU_000288_132_1_1
    InParanoidiQ16513
    KOiK23691
    OMAiRHISWEW
    OrthoDBi520651at2759
    PhylomeDBiQ16513
    TreeFamiTF102005

    Enzyme and pathway databases

    BRENDAi2.7.11.13 2681
    ReactomeiR-HSA-5625740 RHO GTPases activate PKNs
    SABIO-RKiQ16513
    SignaLinkiQ16513
    SIGNORiQ16513

    Miscellaneous databases

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

    More...
    ChiTaRSi
    PKN2 human

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    PKN2

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

    More...
    GenomeRNAii
    5586
    PharosiQ16513 Tchem

    Protein Ontology

    More...
    PROi
    PR:Q16513
    RNActiQ16513 protein

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000065243 Expressed in intestine and 240 other tissues
    ExpressionAtlasiQ16513 baseline and differential
    GenevisibleiQ16513 HS

    Family and domain databases

    CDDicd08687 C2_PKN-like, 1 hit
    cd11622 HR1_PKN_1, 1 hit
    InterProiView protein in InterPro
    IPR000961 AGC-kinase_C
    IPR000008 C2_dom
    IPR037784 C2_PKN
    IPR011072 HR1_rho-bd
    IPR036274 HR1_rpt_sf
    IPR011009 Kinase-like_dom_sf
    IPR017892 Pkinase_C
    IPR037313 PKN_HR1_1
    IPR000719 Prot_kinase_dom
    IPR017441 Protein_kinase_ATP_BS
    IPR008271 Ser/Thr_kinase_AS
    PfamiView protein in Pfam
    PF02185 HR1, 3 hits
    PF00069 Pkinase, 1 hit
    PF00433 Pkinase_C, 1 hit
    SMARTiView protein in SMART
    SM00239 C2, 1 hit
    SM00742 Hr1, 3 hits
    SM00133 S_TK_X, 1 hit
    SM00220 S_TKc, 1 hit
    SUPFAMiSSF46585 SSF46585, 3 hits
    SSF56112 SSF56112, 1 hit
    PROSITEiView protein in PROSITE
    PS51285 AGC_KINASE_CTER, 1 hit
    PS50004 C2, 1 hit
    PS00107 PROTEIN_KINASE_ATP, 1 hit
    PS50011 PROTEIN_KINASE_DOM, 1 hit
    PS00108 PROTEIN_KINASE_ST, 1 hit
    PS51860 REM_1, 3 hits

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    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 nameiPKN2_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: Q16513
    Secondary accession number(s): B4DQ21
    , B4DTP5, B4DVG1, D3DT24, Q08AF4, Q9H1W4
    <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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1996
    Last modified: April 22, 2020
    This is version 204 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, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families
    4. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    5. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    6. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    7. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    UniProt is an ELIXIR core data resource
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