Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q16512 (PKN1_HUMAN)

Protein

Serine/threonine-protein kinase N1

Gene

PKN1

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 involved in various processes such as regulation of the intermediate filaments of the actin cytoskeleton, cell migration, tumor cell invasion and transcription regulation. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14. Regulates the cytoskeletal network by phosphorylating proteins such as VIM and neurofilament proteins NEFH, NEFL and NEFM, leading to inhibit their polymerization. Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau, lowering its ability to bind to microtubules, resulting in disruption of tubulin assembly. Acts as a key coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific tag for epigenetic transcriptional activation that promotes demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C. Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser-159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able to phosphorylate RPS6 in vitro.11 Publications

<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 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 Rho proteins (RHOA, RHOB and RAC1). Activated by lipids, particularly cardiolipin and to a lesser extent by other acidic phospholipids. Activated by caspase-3 (CASP3) cleavage during apoptosis. Two specific sites, Thr-774 (activation loop of the kinase domain) and Ser-916 (turn motif), need to be phosphorylated for its full activation.2 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=20.6 µM for HDAC51 Publication

    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 sitei644ATPPROSITE-ProRule annotation1
    <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 sitei740Proton 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 bindingi621 – 629ATPPROSITE-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

    View the complete GO annotation on QuickGO ...

    GO - Biological processi

    View the complete GO annotation on QuickGO ...

    <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 functionChromatin regulator, Kinase, Serine/threonine-protein kinase, Transferase
    Biological processTranscription, 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
    R-HSA-5625886 Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		Q16512

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

    More...    SignaLinki    		Q16512

    SIGNOR Signaling Network Open Resource

    More...    SIGNORi    		Q16512

    <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 N1 (EC:2.7.11.131 Publication)
    Alternative name(s):
    Protease-activated kinase 1
    Short name:
    PAK-1
    Protein kinase C-like 1
    Protein kinase C-like PKN
    Protein kinase PKN-alpha
    Protein-kinase C-related kinase 1
    Serine-threonine protein kinase N
    <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:PKN1
    Synonyms:PAK1, PKN, PRK1, PRKCL1
    <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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
    <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 19

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...    EuPathDBi    		HostDB:ENSG00000123143.12

    Human Gene Nomenclature Database

    More...    HGNCi    		HGNC:9405 PKN1

    Online Mendelian Inheritance in Man (OMIM)

    More...    MIMi    		601032 gene

    neXtProt; the human protein knowledge platform

    More...    neXtProti    		NX_Q16512

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

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

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Endosome, 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_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>Mutagenesisi108D → A: Abolishes cleavage by caspase-3 and formation of AF1 fragment. 1 Publication1
    Mutagenesisi181R → A: Abolishes interaction with bacterial SspH1. 1 Publication1
    Mutagenesisi181R → K: Decreases interaction with bacterial SspH1. 1 Publication1
    Mutagenesisi185R → A: Abolishes interaction with bacterial SspH1. 1 Publication1
    Mutagenesisi451D → A: Abolishes cleavage by caspase-3 and formation of 70 kDa fragment. 1 Publication1
    Mutagenesisi454D → A: Abolishes cleavage by caspase-3 and formation of 70 kDa fragment. 1 Publication1
    Mutagenesisi558D → A: Abolishes cleavage by caspase-3 and formation of AF3 fragment. 1 Publication1
    Mutagenesisi560D → A: Abolishes cleavage by caspase-3 and formation of AF3 fragment. 1 Publication1
    Mutagenesisi644K → E: Abolishes Serine/threonine-protein kinase activity. 2 Publications1
    Mutagenesisi644K → R: Substantial reduction of autophosphorylation. 2 Publications1

    Organism-specific databases

    DisGeNET

    More...    DisGeNETi    		5585

    Open Targets

    More...    OpenTargetsi    		ENSG00000123143

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...    PharmGKBi    		PA33769

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...    ChEMBLi    		CHEMBL3384

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...    GuidetoPHARMACOLOGYi    		1520

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...    BioMutai    		PKN1

    Domain mapping of disease mutations (DMDM)

    More...    DMDMi    		259016304

    <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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
    <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_00000557192 – 942Serine/threonine-protein kinase N1Add BLAST941

    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 residuei2N-acetylalanineCombined sources1
    Modified residuei69PhosphoserineCombined sources1
    Modified residuei205PhosphoserineCombined sources1
    Modified residuei374PhosphoserineBy similarity1
    Modified residuei448N6-acetyllysineCombined sources1
    Modified residuei533PhosphoserineCombined sources1
    Modified residuei537PhosphoserineCombined sources1
    Modified residuei540PhosphoserineCombined sources1
    Modified residuei559PhosphoserineCombined sources1
    Modified residuei562PhosphoserineCombined sources1
    Modified residuei608PhosphoserineCombined sources1
    Modified residuei774Phosphothreonine; by PDPK11 Publication1
    Modified residuei778PhosphothreonineCombined sources1
    Modified residuei914PhosphothreonineCombined sources1
    Modified residuei916PhosphoserineCombined sources1

    <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

    Autophosphorylated; preferably on serine. Phosphorylated during mitosis.2 Publications
    Activated by limited proteolysis with trypsin.By similarity
    (Microbial infection) In case of infection, polyubiquitinated by the bacterial E3 ubiquitin-protein ligase SspH1, leading to its proteasomal degradation.1 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>Sitei108 – 109Cleavage; by caspase-32
    Sitei454 – 455Cleavage; by caspase-32
    Sitei558 – 559Cleavage; by caspase-32

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...    EPDi    		Q16512

    MaxQB - The MaxQuant DataBase

    More...    MaxQBi    		Q16512

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

    More...    PaxDbi    		Q16512

    PeptideAtlas

    More...    PeptideAtlasi    		Q16512

    PRoteomics IDEntifications database

    More...    PRIDEi    		Q16512

    ProteomicsDB human proteome resource

    More...    ProteomicsDBi    		60877
    60878 [Q16512-2]
    60879 [Q16512-3]

    PTM databases

    GlyConnect protein glycosylation platform

    More...    GlyConnecti    		1737

    iPTMnet integrated resource for PTMs in systems biology context

    More...    iPTMneti    		Q16512

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

    More...    PhosphoSitePlusi    		Q16512

    Miscellaneous databases

    CutDB - Proteolytic event database

    More...    PMAP-CutDBi    		Q16512

    <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

    Found ubiquitously. Expressed in heart, brain, placenta, lung, skeletal muscle, kidney and pancreas. Expressed in numerous tumor cell lines, especially in breast tumor cells.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...    Bgeei    		ENSG00000123143 Expressed in 181 organ(s), highest expression level in apex of heart

    CleanEx database of gene expression profiles

    More...    CleanExi    		HS_PKN1

    ExpressionAtlas, Differential and Baseline Expression

    More...    ExpressionAtlasi    		Q16512 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...    Genevisiblei    		Q16512 HS

    Organism-specific databases

    Human Protein Atlas

    More...    HPAi    		CAB010278
    HPA003982

    <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

    Interacts with ZFAND6 (By similarity). Interacts with ANDR (PubMed:12514133). Interacts with PRKCB (PubMed:20228790). Interacts (via REM 1 and REM 2 repeats) with RAC1 (PubMed:14514689, PubMed:18006505). Interacts (via REM 1 repeat) with RHOA (PubMed:10619026, PubMed:8571126). Interacts with RHOB (PubMed:9478917). Interacts (via C-terminus) with PDPK1 (PubMed:10792047). Interacts with CCNT2; enhances MYOD1-dependent transcription (PubMed:16331689). Component of a signaling complex containing at least AKAP13, PKN1, MAPK14, ZAK and MAP2K3. Within this complex, AKAP13 interacts directly with PKN1, which in turn recruits MAPK14, MAP2K3 and ZAK (PubMed:21224381).By similarity10 Publications
    (Microbial infection) Interacts (via the second REM repeat) with S.typhimurium E3 ubiquitin-protein ligase SspH1 (via the leucine-rich repeat region) (PubMed:16611232, PubMed:24248594).2 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

    View the complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		111571, 65 interactors

    CORUM comprehensive resource of mammalian protein complexes

    More...    CORUMi    		Q16512

    Database of interacting proteins

    More...    DIPi    		DIP-34240N

    The Eukaryotic Linear Motif resource for Functional Sites in Proteins

    More...    ELMi    		Q16512

    Protein interaction database and analysis system

    More...    IntActi    		Q16512, 72 interactors

    Molecular INTeraction database

    More...    MINTi    		Q16512

    STRING: functional protein association networks

    More...    STRINGi    		9606.ENSP00000343325

    Chemistry databases

    BindingDB database of measured binding affinities

    More...    BindingDBi    		Q16512

    <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

    1942
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...    ProteinModelPortali    		Q16512

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

    More...    SMRi    		Q16512

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...    EvolutionaryTracei    		Q16512

    <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>Domaini25 – 100REM-1 1PROSITE-ProRule annotationAdd BLAST76
    Domaini112 – 193REM-1 2PROSITE-ProRule annotationAdd BLAST82
    Domaini201 – 280REM-1 3PROSITE-ProRule annotationAdd BLAST80
    Domaini325 – 461C2Add BLAST137
    Domaini615 – 874Protein kinasePROSITE-ProRule annotationAdd BLAST260
    Domaini875 – 942AGC-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>Regioni181 – 185Important for interaction with bacterial SspH1 and SspH1-mediated polyubiquitination1 Publication5

    <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 C1 domain does not bind the diacylglycerol (DAG).

    <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

    Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.Curated

    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    		ENSGT00940000154990

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...    HOVERGENi    		HBG108317

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		Q16512

    KEGG Orthology (KO)

    More...    KOi    		K06071

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		TMYAIKA

    Database of Orthologous Groups

    More...    OrthoDBi    		EOG091G00YT

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		Q16512

    TreeFam database of animal gene trees

    More...    TreeFami    		TF102005

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd08687 C2_PKN-like, 1 hit
    cd11630 HR1_PKN1_2, 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
    IPR037784 C2_PKN
    IPR011072 HR1_rho-bd
    IPR036274 HR1_rpt_sf
    IPR011009 Kinase-like_dom_sf
    IPR017892 Pkinase_C
    IPR037317 PKN1_HR1_2
    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
    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
    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_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 (3+)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.

    <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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 <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 3 described isoforms and 6 potential isoforms that are computationally mapped.Show allAlign All

    Isoform 1 (identifier: Q16512-1) [UniParc]FASTAAdd to basket

    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
    MASDAVQSEP RSWSLLEQLG LAGADLAAPG VQQQLELERE RLRREIRKEL 
            60         70         80         90        100
    KLKEGAENLR RATTDLGRSL GPVELLLRGS SRRLDLLHQQ LQELHAHVVL 
           110        120        130        140        150
    PDPAATHDGP QSPGAGGPTC SATNLSRVAG LEKQLAIELK VKQGAENMIQ 
           160        170        180        190        200
    TYSNGSTKDR KLLLTAQQML QDSKTKIDII RMQLRRALQA GQLENQAAPD 
           210        220        230        240        250
    DTQGSPDLGA VELRIEELRH HFRVEHAVAE GAKNVLRLLS AAKAPDRKAV 
           260        270        280        290        300
    SEAQEKLTES NQKLGLLREA LERRLGELPA DHPKGRLLRE ELAAASSAAF 
           310        320        330        340        350
    STRLAGPFPA THYSTLCKPA PLTGTLEVRV VGCRDLPETI PWNPTPSMGG 
           360        370        380        390        400
    PGTPDSRPPF LSRPARGLYS RSGSLSGRSS LKAEAENTSE VSTVLKLDNT 
           410        420        430        440        450
    VVGQTSWKPC GPNAWDQSFT LELERARELE LAVFWRDQRG LCALKFLKLE 
           460        470        480        490        500
    DFLDNERHEV QLDMEPQGCL VAEVTFRNPV IERIPRLRRQ KKIFSKQQGK 
           510        520        530        540        550
    AFQRARQMNI DVATWVRLLR RLIPNATGTG TFSPGASPGS EARTTGDISV 
           560        570        580        590        600
    EKLNLGTDSD SSPQKSSRDP PSSPSSLSSP IQESTAPELP SETQETPGPA 
           610        620        630        640        650
    LCSPLRKSPL TLEDFKFLAV LGRGHFGKVL LSEFRPSGEL FAIKALKKGD 
           660        670        680        690        700
    IVARDEVESL MCEKRILAAV TSAGHPFLVN LFGCFQTPEH VCFVMEYSAG 
           710        720        730        740        750
    GDLMLHIHSD VFSEPRAIFY SACVVLGLQF LHEHKIVYRD LKLDNLLLDT 
           760        770        780        790        800
    EGYVKIADFG LCKEGMGYGD RTSTFCGTPE FLAPEVLTDT SYTRAVDWWG 
           810        820        830        840        850
    LGVLLYEMLV GESPFPGDDE EEVFDSIVND EVRYPRFLSA EAIGIMRRLL 
           860        870        880        890        900
    RRNPERRLGS SERDAEDVKK QPFFRTLGWE ALLARRLPPP FVPTLSGRTD 
           910        920        930        940 
    VSNFDEEFTG EAPTLSPPRD ARPLTAAEQA AFLDFDFVAG GC
    Length:942
    Mass (Da):103,932
    Last modified:September 22, 2009 - v2
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i61360295EC70BB8E
    GO
    Isoform 2 (identifier: Q16512-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-7: MASDAVQ → MAEANNPSEQELE

    Note: No experimental confirmation available.
    Show »
    Length:948
    Mass (Da):104,673
    Checksum:i882D58AABCFDCEE1
    GO
    Isoform 3 (identifier: Q16512-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         603-603: S → R
         604-942: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:603
    Mass (Da):66,060
    Checksum:i9CC7C140CE6C5547
    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 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    		Gene namesLengthAnnotation
    K7EM57K7EM57_HUMAN
    Serine/threonine-protein kinase N1
    PKN1
    		263Annotation 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>
    K7EKY9K7EKY9_HUMAN
    Serine/threonine-protein kinase N1
    PKN1
    		255Annotation 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>
    K7EL10K7EL10_HUMAN
    Serine/threonine-protein kinase N1
    PKN1
    		198Annotation 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>
    K7EN76K7EN76_HUMAN
    Serine/threonine-protein kinase N1
    PKN1
    		151Annotation 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>
    K7ES10K7ES10_HUMAN
    Serine/threonine-protein kinase N1
    PKN1
    		226Annotation 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>
    K7EPK3K7EPK3_HUMAN
    Serine/threonine-protein kinase N1
    PKN1
    		14Annotation 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 conflicti191G → D in AAB33345 (PubMed:7851406).Curated1
    Sequence conflicti191G → D in AAC50209 (PubMed:7851406).Curated1
    Sequence conflicti562S → P in BAG36611 (PubMed:14702039).Curated1
    Sequence conflicti736I → T no nucleotide entry (PubMed:7988719).Curated1
    Sequence conflicti750T → A no nucleotide entry (PubMed:7988719).Curated1
    Sequence conflicti800G → A no nucleotide entry (PubMed:7988719).Curated1
    Sequence conflicti812E → G in BAG36611 (PubMed:14702039).Curated1
    Sequence conflicti887L → P in BAG53845 (PubMed:14702039).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_042337185R → C in a metastatic melanoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs267605306Ensembl.1
    Natural variantiVAR_042338197A → E1 Publication1
    Natural variantiVAR_042339436R → W1 PublicationCorresponds to variant dbSNP:rs35132656Ensembl.1
    Natural variantiVAR_042340520R → Q1 PublicationCorresponds to variant dbSNP:rs56273055Ensembl.1
    Natural variantiVAR_042341555L → I2 PublicationsCorresponds to variant dbSNP:rs34309238Ensembl.1
    Natural variantiVAR_042342635R → Q1 PublicationCorresponds to variant dbSNP:rs35416389Ensembl.1
    Natural variantiVAR_042343718I → V2 PublicationsCorresponds to variant dbSNP:rs2230539Ensembl.1
    Natural variantiVAR_042344873F → L in a breast infiltrating ductal carcinoma sample; somatic mutation. 1 Publication1
    Natural variantiVAR_014937901V → I3 PublicationsCorresponds to variant dbSNP:rs10846Ensembl.1
    Natural variantiVAR_042345921A → V in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication1

    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_0381431 – 7MASDAVQ → MAEANNPSEQELE in isoform 2. 1 Publication7
    Alternative sequenceiVSP_039213603S → R in isoform 3. 1 Publication1
    Alternative sequenceiVSP_039214604 – 942Missing in isoform 3. 1 PublicationAdd BLAST339

    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
    		D26181 mRNA Translation: BAA05169.1
    S75546 mRNA Translation: AAB33345.1
    U33053 mRNA Translation: AAC50209.1
    AK123007 mRNA Translation: BAG53845.1
    AK292130 mRNA Translation: BAF84819.1
    AK313886 mRNA Translation: BAG36611.1
    AC008569 Genomic DNA No translation available.
    BC040061 mRNA Translation: AAH40061.1
    BC094766 mRNA Translation: AAH94766.1

    The Consensus CDS (CCDS) project

    More...    CCDSi    		CCDS42513.1 [Q16512-1]
    CCDS42514.1 [Q16512-2]

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		JC2129
    S51162

    NCBI Reference Sequences

    More...    RefSeqi    		NP_002732.3, NM_002741.3 [Q16512-1]
    NP_998725.1, NM_213560.1 [Q16512-2]

    UniGene gene-oriented nucleotide sequence clusters

    More...    UniGenei    		Hs.466044

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...    Ensembli    		ENST00000242783; ENSP00000242783; ENSG00000123143 [Q16512-1]
    ENST00000342216; ENSP00000343325; ENSG00000123143 [Q16512-2]

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		5585

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		hsa:5585

    UCSC genome browser

    More...    UCSCi    		uc002myp.4 human [Q16512-1]

    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
    		D26181 mRNA Translation: BAA05169.1
    S75546 mRNA Translation: AAB33345.1
    U33053 mRNA Translation: AAC50209.1
    AK123007 mRNA Translation: BAG53845.1
    AK292130 mRNA Translation: BAF84819.1
    AK313886 mRNA Translation: BAG36611.1
    AC008569 Genomic DNA No translation available.
    BC040061 mRNA Translation: AAH40061.1
    BC094766 mRNA Translation: AAH94766.1
    CCDSiCCDS42513.1 [Q16512-1]
    CCDS42514.1 [Q16512-2]
    PIRiJC2129
    S51162
    RefSeqiNP_002732.3, NM_002741.3 [Q16512-1]
    NP_998725.1, NM_213560.1 [Q16512-2]
    UniGeneiHs.466044

    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
    1CXZX-ray2.20B13-98[»]
    1URFNMR-A122-199[»]
    2RMKNMR-B122-199[»]
    4NKGX-ray2.90B/D122-199[»]
    4OTDX-ray2.00A605-942[»]
    4OTGX-ray2.60A605-942[»]
    4OTHX-ray1.80A605-942[»]
    4OTIX-ray1.93A605-942[»]
    ProteinModelPortaliQ16512
    SMRiQ16512
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi111571, 65 interactors
    CORUMiQ16512
    DIPiDIP-34240N
    ELMiQ16512
    IntActiQ16512, 72 interactors
    MINTiQ16512
    STRINGi9606.ENSP00000343325

    Chemistry databases

    BindingDBiQ16512
    ChEMBLiCHEMBL3384
    GuidetoPHARMACOLOGYi1520

    PTM databases

    GlyConnecti1737
    iPTMnetiQ16512
    PhosphoSitePlusiQ16512

    Polymorphism and mutation databases

    BioMutaiPKN1
    DMDMi259016304

    Proteomic databases

    EPDiQ16512
    MaxQBiQ16512
    PaxDbiQ16512
    PeptideAtlasiQ16512
    PRIDEiQ16512
    ProteomicsDBi60877
    60878 [Q16512-2]
    60879 [Q16512-3]

    Protocols and materials databases

    The DNASU plasmid repository

    More...    DNASUi    		5585
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000242783; ENSP00000242783; ENSG00000123143 [Q16512-1]
    ENST00000342216; ENSP00000343325; ENSG00000123143 [Q16512-2]
    GeneIDi5585
    KEGGihsa:5585
    UCSCiuc002myp.4 human [Q16512-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...    CTDi    		5585
    DisGeNETi5585
    EuPathDBiHostDB:ENSG00000123143.12

    GeneCards: human genes, protein and diseases

    More...    GeneCardsi    		PKN1

    H-Invitational Database, human transcriptome db

    More...    H-InvDBi    		HIX0027472
    HGNCiHGNC:9405 PKN1
    HPAiCAB010278
    HPA003982
    MIMi601032 gene
    neXtProtiNX_Q16512
    OpenTargetsiENSG00000123143
    PharmGKBiPA33769

    GenAtlas: human gene database

    More...    GenAtlasi    		Search...

    Phylogenomic databases

    eggNOGiKOG0694 Eukaryota
    ENOG410XNPH LUCA
    GeneTreeiENSGT00940000154990
    HOVERGENiHBG108317
    InParanoidiQ16512
    KOiK06071
    OMAiTMYAIKA
    OrthoDBiEOG091G00YT
    PhylomeDBiQ16512
    TreeFamiTF102005

    Enzyme and pathway databases

    BRENDAi2.7.11.13 2681
    ReactomeiR-HSA-5625740 RHO GTPases activate PKNs
    R-HSA-5625886 Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3
    SABIO-RKiQ16512
    SignaLinkiQ16512
    SIGNORiQ16512

    Miscellaneous databases

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

    More...    ChiTaRSi    		PKN1 human
    EvolutionaryTraceiQ16512

    The Gene Wiki collection of pages on human genes and proteins

    More...    GeneWikii    		Protein_kinase_N1

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

    More...    GenomeRNAii    		5585
    PMAP-CutDBiQ16512

    Protein Ontology

    More...    PROi    		PR:Q16512

    The Stanford Online Universal Resource for Clones and ESTs

    More...    SOURCEi    		Search...

    Gene expression databases

    BgeeiENSG00000123143 Expressed in 181 organ(s), highest expression level in apex of heart
    CleanExiHS_PKN1
    ExpressionAtlasiQ16512 baseline and differential
    GenevisibleiQ16512 HS

    Family and domain databases

    CDDicd08687 C2_PKN-like, 1 hit
    cd11630 HR1_PKN1_2, 1 hit
    cd11622 HR1_PKN_1, 1 hit
    InterProiView protein in InterPro
    IPR000961 AGC-kinase_C
    IPR037784 C2_PKN
    IPR011072 HR1_rho-bd
    IPR036274 HR1_rpt_sf
    IPR011009 Kinase-like_dom_sf
    IPR017892 Pkinase_C
    IPR037317 PKN1_HR1_2
    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
    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
    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...

    <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 nameiPKN1_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: Q16512
    Secondary accession number(s): A8K7W5
    , B2R9R4, B3KVN3, Q15143, Q504U4, Q8IUV5, Q9UD44
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: September 22, 2009
    Last modified: December 5, 2018
    This is version 214 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    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
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

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

    Do not show this banner again