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Protein

cAMP-dependent protein kinase catalytic subunit alpha

Gene

PRKACA

Organism
Bos taurus (Bovine)
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

Phosphorylates a large number of substrates in the cytoplasm and the nucleus. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA and VASP. RORA is activated by phosphorylation. Required for glucose-mediated adipogenic differentiation increase and osteogenic differentiation inhibition from osteoblasts. Involved in the regulation of platelets in response to thrombin and collagen; maintains circulating platelets in a resting state by phosphorylating proteins in numerous platelet inhibitory pathways when in complex with NF-kappa-B (NFKB1 and NFKB2) and I-kappa-B-alpha (NFKBIA), but thrombin and collagen disrupt these complexes and free active PRKACA stimulates platelets and leads to platelet aggregation by phosphorylating VASP. Prevents the antiproliferative and anti-invasive effects of alpha-difluoromethylornithine in breast cancer cells when activated. RYR2 channel activity is potentiated by phosphorylation in presence of luminal Ca2+, leading to reduced amplitude and increased frequency of store overload-induced Ca2+ release (SOICR) characterized by an increased rate of Ca2+ release and propagation velocity of spontaneous Ca2+ waves, despite reduced wave amplitude and resting cytosolic Ca2+. PSMC5/RPT6 activation by phosphorylation stimulates proteasome. Negatively regulates tight junctions (TJs) in ovarian cancer cells via CLDN3 phosphorylation. NFKB1 phosphorylation promotes NF-kappa-B p50-p50 DNA binding. Involved in embryonic development by down-regulating the Hedgehog (Hh) signaling pathway that determines embryo pattern formation and morphogenesis. Prevents meiosis resumption in prophase-arrested oocytes via CDC25B inactivation by phosphorylation. May also regulate rapid eye movement (REM) sleep in the pedunculopontine tegmental (PPT) (By similarity). Phosphorylates APOBEC3G and AICDA (By similarity). Phosphorylates HSF1; this phosphorylation promotes HSF1 nuclear localization and transcriptional activity upon heat shock (By similarity).By similarity

<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

Allosterically activated by various compounds, including ATP. Activated by cAMP; the nucleotide acts as a dynamic and allosteric activator by coupling the two lobes of apo PKA, enhancing the enzyme dynamics synchronously and priming it for catalysis.

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 sitei73ATP1
<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 sitei167Proton acceptorPROSITE-ProRule annotation1 Publication1

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 bindingi50 – 58ATP9
Nucleotide bindingi122 – 128ATPPROSITE-ProRule annotation7
Nucleotide bindingi169 – 172ATPPROSITE-ProRule annotation4

<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
LigandATP-binding, cAMP, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.11.11 908

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-BTA-163615 PKA activation
R-BTA-164378 PKA activation in glucagon signalling
R-BTA-180024 DARPP-32 events
R-BTA-2565942 Regulation of PLK1 Activity at G2/M Transition
R-BTA-380259 Loss of Nlp from mitotic centrosomes
R-BTA-380270 Recruitment of mitotic centrosome proteins and complexes
R-BTA-380320 Recruitment of NuMA to mitotic centrosomes
R-BTA-381676 Glucagon-like Peptide-1 (GLP1) regulates insulin secretion
R-BTA-392517 Rap1 signalling
R-BTA-422356 Regulation of insulin secretion
R-BTA-432040 Vasopressin regulates renal water homeostasis via Aquaporins
R-BTA-4420097 VEGFA-VEGFR2 Pathway
R-BTA-512988 Interleukin-3, Interleukin-5 and GM-CSF signaling
R-BTA-5578775 Ion homeostasis
R-BTA-5610785 GLI3 is processed to GLI3R by the proteasome
R-BTA-5610787 Hedgehog 'off' state
R-BTA-5620912 Anchoring of the basal body to the plasma membrane
R-BTA-5621575 CD209 (DC-SIGN) signaling
R-BTA-5687128 MAPK6/MAPK4 signaling
R-BTA-8853659 RET signaling
R-BTA-8854518 AURKA Activation by TPX2
R-BTA-8963896 HDL assembly
R-BTA-983231 Factors involved in megakaryocyte development and platelet production

<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 alpha (EC:2.7.11.11)
Short name:
PKA C-alpha
<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:PRKACA
<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>OrganismiBos taurus (Bovine)
<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 identifieri9913 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
<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
  • UP000009136 <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 7

Organism-specific databases

Vertebrate Gene Nomenclature Database

More...
VGNCi
VGNC:50250 PRKACA

<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, Cell projection, Cilium, Cytoplasm, Cytoplasmic vesicle, Flagellum, Membrane, Mitochondrion, 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>Mutagenesisi3N → D: No myristoylation. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2654

<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 methionineiRemoved3 Publications
<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_00000860492 – 351cAMP-dependent protein kinase catalytic subunit alphaAdd BLAST350

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi2N-myristoyl glycine1 Publication1
<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 residuei3Deamidated asparagine; partial3 Publications1
Modified residuei11Phosphoserine; by autocatalysisBy similarity1
Modified residuei49PhosphothreonineBy similarity1
Modified residuei140PhosphoserineBy similarity1
Modified residuei196PhosphothreonineBy similarity1
Modified residuei198Phosphothreonine; by PDPK11 Publication1
Modified residuei331PhosphotyrosineBy similarity1
Modified residuei339Phosphoserine1 Publication1

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

Asn-3 is deaminated to Asp in more than 25% of the proteins, giving rise to 2 major isoelectric variants, called CB and CA respectively (0.4 pH unit change). Deamidation proceeds via the so-called beta-aspartyl shift mechanism and yields either 'D-Asp-3' (major) or 'D-isoAsp-2' (minor), in addition to L-isomers. Deamidation occurs after the addition of myristate. The Asn-3 form reaches a significantly larger nuclear/cytoplasmic ratio than the 'Asp-2' form.4 Publications
Autophosphorylated. Phosphorylation is enhanced by vitamin K2. Phosphorylated on threonine and serine residues. Phosphorylation on Thr-198 is required for full activity (By similarity).By similarity
Phosphorylated at Tyr-331 by activated receptor tyrosine kinases EGFR and PDGFR; this increases catalytic efficienncy.By similarity

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

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

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PaxDbi
P00517

PeptideAtlas

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PeptideAtlasi
P00517

PRoteomics IDEntifications database

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PRIDEi
P00517

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P00517

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
P00517

<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

Ubiquitously expressed in mammalian tissues.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSBTAG00000006642 Expressed in 9 organ(s), highest expression level in heart

<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

A number of inactive tetrameric holoenzymes are produced by the combination of homo- or heterodimers of the different regulatory subunits associated with two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Activates cAMP-sensitive PKAI and PKAII holoenzymes by interacting with regulatory subunit (R) of PKA, PRKAR1A/PKR1 and PRKAR2A/PKR2, respectively. Interacts with NFKB1, NFKB2 and NFKBIA in platelets; these interactions are disrupted by thrombin and collagen. Binds to ABL1 in spermatozoa and with CDC25B in oocytes (By similarity). Interacts with APOBEC3G and AICDA (By similarity). Interacts with RAB13; downstream effector of RAB13 involved in tight junction assembly. Found in a complex at least composed of MROH2B, PRKACA and TCP11 (By similarity). Interacts with MROH2B (By similarity). Interacts with TCP11 (By similarity). Interacts with HSF1 (By similarity).By similarity1 Publication

<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

WithEntry#Exp.IntActNotes
Kcnj3P632516EBI-7251007,EBI-7250981From Rattus norvegicus.

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
159584, 13 interactors

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P00517

Protein interaction database and analysis system

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IntActi
P00517, 4 interactors

Molecular INTeraction database

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MINTi
P00517

STRING: functional protein association networks

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STRINGi
9913.ENSBTAP00000008727

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P00517

<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

1351
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P00517

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

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SMRi
P00517

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P00517

<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>Domaini44 – 298Protein kinasePROSITE-ProRule annotationAdd BLAST255
Domaini299 – 351AGC-kinase C-terminalAdd BLAST53

<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

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eggNOGi
KOG0616 Eukaryota
ENOG410XPQQ LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000162186

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG108317

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P00517

KEGG Orthology (KO)

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KOi
K04345

Identification of Orthologs from Complete Genome Data

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OMAi
HSHDIIY

Database of Orthologous Groups

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OrthoDBi
EOG091G10O8

TreeFam database of animal gene trees

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TreeFami
TF313399

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR000961 AGC-kinase_C
IPR039811 cAMP/cGMP-dep_PK
IPR011009 Kinase-like_dom_sf
IPR039035 PKA_C-alpha
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS

The PANTHER Classification System

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PANTHERi
PTHR24353 PTHR24353, 1 hit
PTHR24353:SF82 PTHR24353:SF82, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00069 Pkinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

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SUPFAMi
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
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.

<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.

P00517-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGNAAAAKKG SEQESVKEFL AKAKEDFLKK WENPAQNTAH LDQFERIKTL
60 70 80 90 100
GTGSFGRVML VKHMETGNHY AMKILDKQKV VKLKQIEHTL NEKRILQAVN
110 120 130 140 150
FPFLVKLEFS FKDNSNLYMV MEYVPGGEMF SHLRRIGRFS EPHARFYAAQ
160 170 180 190 200
IVLTFEYLHS LDLIYRDLKP ENLLIDQQGY IQVTDFGFAK RVKGRTWTLC
210 220 230 240 250
GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF ADQPIQIYEK
260 270 280 290 300
IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVN DIKNHKWFAT
310 320 330 340 350
TDWIAIYQRK VEAPFIPKFK GPGDTSNFDD YEEEEIRVSI NEKCGKEFSE

F
Length:351
Mass (Da):40,620
Last modified:January 23, 2007 - v3
<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:i59DDD227D2DEEE5D
GO

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 conflicti202T → N AA sequence (PubMed:6286662).Curated1
Sequence conflicti204E → Q AA sequence (PubMed:6286662).Curated1
Sequence conflicti206L → S AA sequence (PubMed:6286662).Curated1
Sequence conflicti287N → D AA sequence (PubMed:6262777).Curated1
Sequence conflicti287N → D AA sequence (PubMed:6311252).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
X67154 mRNA Translation: CAA47627.1

Protein sequence database of the Protein Information Resource

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PIRi
S27159 OKBO2C

NCBI Reference Sequences

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RefSeqi
NP_777009.1, NM_174584.2

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Bt.4420

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSBTAT00000008727; ENSBTAP00000008727; ENSBTAG00000006642

Database of genes from NCBI RefSeq genomes

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GeneIDi
282322

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
bta:282322

<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
X67154 mRNA Translation: CAA47627.1
PIRiS27159 OKBO2C
RefSeqiNP_777009.1, NM_174584.2
UniGeneiBt.4420

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KMUmodel-C9-351[»]
1KMWmodel-C9-351[»]
1Q24X-ray2.60A2-351[»]
1Q61X-ray2.10A2-351[»]
1Q62X-ray2.30A2-351[»]
1Q8TX-ray2.00A2-351[»]
1Q8UX-ray1.90A2-351[»]
1Q8WX-ray2.20A2-351[»]
1SMHX-ray2.04A2-351[»]
1STCX-ray2.30E2-351[»]
1SVEX-ray2.49A2-351[»]
1SVGX-ray2.02A2-351[»]
1SVHX-ray2.30A2-351[»]
1SZMX-ray2.50A/B2-351[»]
1VEBX-ray2.89A2-351[»]
1XH4X-ray2.45A2-351[»]
1XH5X-ray2.05A2-351[»]
1XH6X-ray1.90A2-351[»]
1XH7X-ray2.47A2-351[»]
1XH8X-ray1.60A2-351[»]
1XH9X-ray1.64A2-351[»]
1XHAX-ray2.46A2-351[»]
1YDRX-ray2.20E2-351[»]
1YDSX-ray2.20E2-351[»]
1YDTX-ray2.30E2-351[»]
2C1AX-ray1.95A2-351[»]
2C1BX-ray2.00A2-351[»]
2F7EX-ray2.00E1-351[»]
2F7XX-ray1.90E1-351[»]
2F7ZX-ray3.00E1-351[»]
2GFCX-ray1.87A2-351[»]
2GNFX-ray2.28A2-351[»]
2GNGX-ray1.87A2-351[»]
2GNHX-ray2.05A2-351[»]
2GNIX-ray2.27A2-351[»]
2GNJX-ray2.28A2-351[»]
2GNLX-ray2.60A2-351[»]
2JDSX-ray2.00A2-351[»]
2JDTX-ray2.15A2-351[»]
2JDVX-ray2.08A2-351[»]
2OH0X-ray2.20E1-351[»]
2OJFX-ray2.10E1-351[»]
2UVXX-ray2.00A2-351[»]
2UVYX-ray1.95A2-351[»]
2UVZX-ray1.94A2-351[»]
2UW0X-ray2.00A2-351[»]
2UW3X-ray2.19A2-351[»]
2UW4X-ray2.00A2-351[»]
2UW5X-ray2.14A2-351[»]
2UW6X-ray2.23A2-351[»]
2UW7X-ray2.10A2-351[»]
2UW8X-ray2.00A2-351[»]
2UZTX-ray2.10A16-351[»]
2UZUX-ray2.40E16-351[»]
2UZVX-ray2.50A16-351[»]
2UZWX-ray2.20E16-351[»]
2VNWX-ray2.09A1-351[»]
2VNYX-ray1.96A1-351[»]
2VO0X-ray1.94A1-351[»]
2VO3X-ray1.98A1-351[»]
2VO6X-ray1.97A1-351[»]
2VO7X-ray1.98A1-351[»]
3AG9X-ray2.00A/B1-351[»]
3BWJX-ray2.30A2-351[»]
3DNDX-ray2.26A2-351[»]
3DNEX-ray2.00A2-351[»]
3E8CX-ray2.20A/B/C/D/E/F2-351[»]
3E8EX-ray2.00A/B/E/I/L/P2-351[»]
3KKVX-ray1.80A2-351[»]
3ZO1X-ray2.00A1-351[»]
3ZO2X-ray1.98A1-351[»]
3ZO3X-ray2.10A1-351[»]
3ZO4X-ray1.65A1-351[»]
4AXAX-ray1.90A1-351[»]
4C33X-ray1.70A1-351[»]
4C34X-ray1.78A1-351[»]
4C35X-ray2.19A1-351[»]
4C36X-ray1.98A1-351[»]
4C37X-ray1.70A1-351[»]
4C38X-ray1.58A1-351[»]
4IE9X-ray1.92A1-351[»]
4IJ9X-ray2.55A2-351[»]
4YXRX-ray2.00A2-351[»]
4YXSX-ray2.11A2-351[»]
4Z83X-ray1.80E2-351[»]
4Z84X-ray1.55A1-351[»]
5VHBX-ray1.61A1-351[»]
5VI9X-ray1.95A1-351[»]
5VIBX-ray2.37A1-351[»]
ProteinModelPortaliP00517
SMRiP00517
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi159584, 13 interactors
ELMiP00517
IntActiP00517, 4 interactors
MINTiP00517
STRINGi9913.ENSBTAP00000008727

Chemistry databases

BindingDBiP00517
ChEMBLiCHEMBL2654

PTM databases

iPTMnetiP00517

Proteomic databases

PaxDbiP00517
PeptideAtlasiP00517
PRIDEiP00517

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000008727; ENSBTAP00000008727; ENSBTAG00000006642
GeneIDi282322
KEGGibta:282322

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5566
VGNCiVGNC:50250 PRKACA

Phylogenomic databases

eggNOGiKOG0616 Eukaryota
ENOG410XPQQ LUCA
GeneTreeiENSGT00940000162186
HOVERGENiHBG108317
InParanoidiP00517
KOiK04345
OMAiHSHDIIY
OrthoDBiEOG091G10O8
TreeFamiTF313399

Enzyme and pathway databases

BRENDAi2.7.11.11 908
ReactomeiR-BTA-163615 PKA activation
R-BTA-164378 PKA activation in glucagon signalling
R-BTA-180024 DARPP-32 events
R-BTA-2565942 Regulation of PLK1 Activity at G2/M Transition
R-BTA-380259 Loss of Nlp from mitotic centrosomes
R-BTA-380270 Recruitment of mitotic centrosome proteins and complexes
R-BTA-380320 Recruitment of NuMA to mitotic centrosomes
R-BTA-381676 Glucagon-like Peptide-1 (GLP1) regulates insulin secretion
R-BTA-392517 Rap1 signalling
R-BTA-422356 Regulation of insulin secretion
R-BTA-432040 Vasopressin regulates renal water homeostasis via Aquaporins
R-BTA-4420097 VEGFA-VEGFR2 Pathway
R-BTA-512988 Interleukin-3, Interleukin-5 and GM-CSF signaling
R-BTA-5578775 Ion homeostasis
R-BTA-5610785 GLI3 is processed to GLI3R by the proteasome
R-BTA-5610787 Hedgehog 'off' state
R-BTA-5620912 Anchoring of the basal body to the plasma membrane
R-BTA-5621575 CD209 (DC-SIGN) signaling
R-BTA-5687128 MAPK6/MAPK4 signaling
R-BTA-8853659 RET signaling
R-BTA-8854518 AURKA Activation by TPX2
R-BTA-8963896 HDL assembly
R-BTA-983231 Factors involved in megakaryocyte development and platelet production

Miscellaneous databases

EvolutionaryTraceiP00517
PMAP-CutDBiP00517

Protein Ontology

More...
PROi
PR:P00517

Gene expression databases

BgeeiENSBTAG00000006642 Expressed in 9 organ(s), highest expression level in heart

Family and domain databases

InterProiView protein in InterPro
IPR000961 AGC-kinase_C
IPR039811 cAMP/cGMP-dep_PK
IPR011009 Kinase-like_dom_sf
IPR039035 PKA_C-alpha
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PANTHERiPTHR24353 PTHR24353, 1 hit
PTHR24353:SF82 PTHR24353:SF82, 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

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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 nameiKAPCA_BOVIN
<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: P00517
<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 21, 1986
Last sequence update: January 23, 2007
Last modified: December 5, 2018
This is version 189 of the entry and version 3 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

<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, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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