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Protein

cAMP-dependent protein kinase catalytic subunit PRKX

Gene

PRKX

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

Serine/threonine protein kinase regulated by and mediating cAMP signaling in cells. Acts through phosphorylation of downstream targets that may include CREB, SMAD6 and PKD1 and has multiple functions in cellular differentiation and epithelial morphogenesis. Regulates myeloid cell differentiation through SMAD6 phosphorylation. Involved in nephrogenesis by stimulating renal epithelial cell migration and tubulogenesis. Also involved in angiogenesis through stimulation of endothelial cell proliferation, migration and vascular-like structure formation.7 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

Binding of cAMP to the PRKAR1A or PRKAR1B regulatory subunits induces dissociation of the holoenzyme heterotetramer. The released monomeric PRKX is then active and able to phosphorylate its substrates.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=127 µM for ATP (in the presence of 10 mM magnesium chloride)2 Publications
  2. KM=58 µM for kemptide (in the presence of 10 mM magnesium chloride)2 Publications
  3. KM=6.7 µM for kemptide (in the presence of 1 µM Br-cAMP at 30 degrees Celsius)2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei78ATPPROSITE-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 sitei172Proton 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 bindingi55 – 63ATPPROSITE-ProRule annotation9

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

    • ATP binding Source: UniProtKB-KW
    • cAMP-dependent protein kinase activity Source: UniProtKB

    GO - Biological processi

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

    Molecular functionDevelopmental protein, Kinase, Serine/threonine-protein kinase, Transferase
    Biological processAngiogenesis, Differentiation
    LigandATP-binding, cAMP, Nucleotide-binding

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.7.11.1 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-111931 PKA-mediated phosphorylation of CREB
    R-HSA-442720 CREB phosphorylation through the activation of Adenylate Cyclase

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P51817

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

    More...
    SignaLinki
    P51817

    SIGNOR Signaling Network Open Resource

    More...
    SIGNORi
    P51817

    <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:
    cAMP-dependent protein kinase catalytic subunit PRKX (EC:2.7.11.1)
    Short name:
    PrKX
    Short name:
    Protein kinase X
    Short name:
    Protein kinase X-linked
    Short name:
    Serine/threonine-protein kinase PRKX
    Alternative name(s):
    Protein kinase PKX1
    <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:PRKX
    Synonyms:PKX1
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome X

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000183943.5

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:9441 PRKX

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    300083 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_P51817

    <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

    Cytoplasm, Nucleus

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

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

    A chromosomal aberration involving PRKX is a cause of sex reversal disorder. Translocation t(X;Y)(p22;p11) with PRKY. Chromosomal translocations proximal to PRKY account for about 30% of the cases of sex reversal disorder in XX males and XY females.

    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>Mutagenesisi78K → R: Loss of function. 1 Publication1
    Mutagenesisi93H → Q: Constitutive kinase activity; when associated with R-202. 1 Publication1
    Mutagenesisi202W → R: Constitutive kinase activity; when associated with Q-93. 1 Publication1
    Mutagenesisi283R → L: Increases the affinity for PRKAR2A and PRKAR2B. 1 Publication1

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    5613

    Open Targets

    More...
    OpenTargetsi
    ENSG00000183943

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA33786

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL5818

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...
    GuidetoPHARMACOLOGYi
    2175

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    PRKX

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    1709648

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

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000865821 – 358cAMP-dependent protein kinase catalytic subunit PRKXAdd BLAST358

    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 residuei1N-acetylmethionineCombined sources1
    Modified residuei203PhosphothreonineBy similarity1

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

    Phosphorylated; autophosphorylates in vitro.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P51817

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P51817

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

    More...
    PaxDbi
    P51817

    PeptideAtlas

    More...
    PeptideAtlasi
    P51817

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P51817

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    56426

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P51817

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

    More...
    PhosphoSitePlusi
    P51817

    <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

    Widely expressed (at protein level). Specifically expressed in blood by macrophages and granulocytes according to PubMed:9860982.4 Publications

    <p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

    Expression is developmentally regulated being high and specific in a wide range of developing tissues including liver, kidney, brain and pancreas (at protein level).3 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 by phorbol 12-myristate 13-acetate (PMA).2 Publications

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000183943 Expressed in 176 organ(s), highest expression level in thyroid gland

    CleanEx database of gene expression profiles

    More...
    CleanExi
    HS_PRKX

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P51817 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P51817 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    HPA015324

    <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

    Like other cAMP-dependent protein kinases, the inactive holoenzyme is probably composed of 2 PRKX catalytic subunits and a dimer of regulatory subunits. Interacts (cAMP-dependent) specifically with the regulatory subunits PRKAR1A and PRKAR1B. Compared to other cAMP-dependent serine/threonine protein kinases, does not interact with the 2 other PKA regulatory subunits PRKAR2A and PRKAR2B. Interacts with cAMP-dependent protein kinase inhibitor/PKI proteins; inhibits PRKX. Interacts with GPKOW. Interacts with SMAD6. Interacts with PKD1; involved in differentiation and controlled morphogenesis of the kidney. Interacts with PIN1 (via WW domain).5 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

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    111599, 8 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    P51817, 6 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000262848

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P51817

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

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P51817

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

    More...
    SMRi
    P51817

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

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

    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>Domaini49 – 303Protein kinasePROSITE-ProRule annotationAdd BLAST255
    Domaini304 – 358AGC-kinase C-terminalAdd BLAST55

    <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

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG0616 Eukaryota
    ENOG410XPQQ LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000159832

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000233033

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG108317

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P51817

    KEGG Orthology (KO)

    More...
    KOi
    K19584

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    WWACGIL

    Database of Orthologous Groups

    More...
    OrthoDBi
    EOG091G10O8

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P51817

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF313399

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR000961 AGC-kinase_C
    IPR039811 cAMP/cGMP-dep_PK
    IPR011009 Kinase-like_dom_sf
    IPR000719 Prot_kinase_dom
    IPR017441 Protein_kinase_ATP_BS
    IPR008271 Ser/Thr_kinase_AS

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR24353 PTHR24353, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00069 Pkinase, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00133 S_TK_X, 1 hit
    SM00220 S_TKc, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    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

    <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>Sequencei

    <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.

    P51817-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MEAPGLAQAA AAESDSRKVA EETPDGAPAL CPSPEALSPE PPVYSLQDFD
    60 70 80 90 100
    TLATVGTGTF GRVHLVKEKT AKHFFALKVM SIPDVIRLKQ EQHVHNEKSV
    110 120 130 140 150
    LKEVSHPFLI RLFWTWHDER FLYMLMEYVP GGELFSYLRN RGRFSSTTGL
    160 170 180 190 200
    FYSAEIICAI EYLHSKEIVY RDLKPENILL DRDGHIKLTD FGFAKKLVDR
    210 220 230 240 250
    TWTLCGTPEY LAPEVIQSKG HGRAVDWWAL GILIFEMLSG FPPFFDDNPF
    260 270 280 290 300
    GIYQKILAGK IDFPRHLDFH VKDLIKKLLV VDRTRRLGNM KNGANDVKHH
    310 320 330 340 350
    RWFRSVDWEA VPQRKLKPPI VPKIAGDGDT SNFETYPEND WDTAAPVPQK

    DLEIFKNF
    Length:358
    Mass (Da):40,896
    Last modified:October 1, 1996 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB603834E3541CB56
    GO

    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_06174443V → A. Corresponds to variant dbSNP:rs3752362Ensembl.1

    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
    X85545 mRNA Translation: CAA59733.1
    BC041073 mRNA Translation: AAH41073.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS14125.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    I38121

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_005035.1, NM_005044.4

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Hs.390788

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000262848; ENSP00000262848; ENSG00000183943

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    5613

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:5613

    UCSC genome browser

    More...
    UCSCi
    uc010nde.4 human

    Keywords - Coding sequence diversityi

    Chromosomal rearrangement, 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
    X85545 mRNA Translation: CAA59733.1
    BC041073 mRNA Translation: AAH41073.1
    CCDSiCCDS14125.1
    PIRiI38121
    RefSeqiNP_005035.1, NM_005044.4
    UniGeneiHs.390788

    3D structure databases

    ProteinModelPortaliP51817
    SMRiP51817
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi111599, 8 interactors
    IntActiP51817, 6 interactors
    STRINGi9606.ENSP00000262848

    Chemistry databases

    BindingDBiP51817
    ChEMBLiCHEMBL5818
    GuidetoPHARMACOLOGYi2175

    PTM databases

    iPTMnetiP51817
    PhosphoSitePlusiP51817

    Polymorphism and mutation databases

    BioMutaiPRKX
    DMDMi1709648

    Proteomic databases

    EPDiP51817
    MaxQBiP51817
    PaxDbiP51817
    PeptideAtlasiP51817
    PRIDEiP51817
    ProteomicsDBi56426

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    5613
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000262848; ENSP00000262848; ENSG00000183943
    GeneIDi5613
    KEGGihsa:5613
    UCSCiuc010nde.4 human

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    5613
    DisGeNETi5613
    EuPathDBiHostDB:ENSG00000183943.5

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    PRKX

    H-Invitational Database, human transcriptome db

    More...
    H-InvDBi
    HIX0202211
    HGNCiHGNC:9441 PRKX
    HPAiHPA015324
    MIMi300083 gene
    neXtProtiNX_P51817
    OpenTargetsiENSG00000183943
    PharmGKBiPA33786

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG0616 Eukaryota
    ENOG410XPQQ LUCA
    GeneTreeiENSGT00940000159832
    HOGENOMiHOG000233033
    HOVERGENiHBG108317
    InParanoidiP51817
    KOiK19584
    OMAiWWACGIL
    OrthoDBiEOG091G10O8
    PhylomeDBiP51817
    TreeFamiTF313399

    Enzyme and pathway databases

    BRENDAi2.7.11.1 2681
    ReactomeiR-HSA-111931 PKA-mediated phosphorylation of CREB
    R-HSA-442720 CREB phosphorylation through the activation of Adenylate Cyclase
    SABIO-RKiP51817
    SignaLinkiP51817
    SIGNORiP51817

    Miscellaneous databases

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

    More...
    GenomeRNAii
    5613

    Protein Ontology

    More...
    PROi
    PR:P51817

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000183943 Expressed in 176 organ(s), highest expression level in thyroid gland
    CleanExiHS_PRKX
    ExpressionAtlasiP51817 baseline and differential
    GenevisibleiP51817 HS

    Family and domain databases

    InterProiView protein in InterPro
    IPR000961 AGC-kinase_C
    IPR039811 cAMP/cGMP-dep_PK
    IPR011009 Kinase-like_dom_sf
    IPR000719 Prot_kinase_dom
    IPR017441 Protein_kinase_ATP_BS
    IPR008271 Ser/Thr_kinase_AS
    PANTHERiPTHR24353 PTHR24353, 1 hit
    PfamiView protein in Pfam
    PF00069 Pkinase, 1 hit
    SMARTiView protein in SMART
    SM00133 S_TK_X, 1 hit
    SM00220 S_TKc, 1 hit
    SUPFAMiSSF56112 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

    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 nameiPRKX_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: P51817
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: December 5, 2018
    This is version 165 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. SIMILARITY comments
      Index of protein domains and families
    3. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    6. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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