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Entry version 211 (05 Jun 2019)
Sequence version 3 (31 Oct 2003)
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Protein

DNA-dependent protein kinase catalytic subunit

Gene

PRKDC

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 that acts as a molecular sensor for DNA damage. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break (DSB) repair and V(D)J recombination (PubMed:11955432, PubMed:12649176, PubMed:14734805). Must be bound to DNA to express its catalytic properties. Promotes processing of hairpin DNA structures in V(D)J recombination by activation of the hairpin endonuclease artemis (DCLRE1C) (PubMed:11955432). The assembly of the DNA-PK complex at DNA ends is also required for the NHEJ ligation step (PubMed:15574326, PubMed:11955432, PubMed:12649176, PubMed:14734805). Required to protect and align broken ends of DNA (PubMed:15574326, PubMed:11955432, PubMed:12649176, PubMed:14734805). May also act as a scaffold protein to aid the localization of DNA repair proteins to the site of damage (PubMed:15574326, PubMed:11955432, PubMed:12649176, PubMed:14734805). Found at the ends of chromosomes, suggesting a further role in the maintenance of telomeric stability and the prevention of chromosomal end fusion. Also involved in modulation of transcription (PubMed:15574326, PubMed:11955432, PubMed:12649176, PubMed:14734805). Recognizes the substrate consensus sequence [ST]-Q (PubMed:15574326, PubMed:11955432, PubMed:12649176, PubMed:14734805). Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX, thereby regulating DNA damage response mechanism (PubMed:14627815, PubMed:16046194). Phosphorylates DCLRE1C, c-Abl/ABL1, histone H1, HSPCA, c-jun/JUN, p53/TP53, PARP1, POU2F1, DHX9, FH, SRF, XRCC1, XRCC1, XRCC4, XRCC5, XRCC6, WRN, MYC and RFA2 (PubMed:2507541, PubMed:2247066, PubMed:1597196, PubMed:8407951, PubMed:8464713, PubMed:9362500, PubMed:9139719, PubMed:10026262, PubMed:10467406, PubMed:12509254, PubMed:11889123, PubMed:14612514, PubMed:14704337, PubMed:16397295, PubMed:26237645, PubMed:28712728). Can phosphorylate C1D not only in the presence of linear DNA but also in the presence of supercoiled DNA (PubMed:9679063). Ability to phosphorylate p53/TP53 in the presence of supercoiled DNA is dependent on C1D (PubMed:9363941). Contributes to the determination of the circadian period length by antagonizing phosphorylation of CRY1 'Ser-588' and increasing CRY1 protein stability, most likely through an indirect mechanism (By similarity). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728).By similarity24 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 <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by wortmannin. Activity of the enzyme seems to be attenuated by autophosphorylation.1 Publication

<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 functionDNA-binding, Kinase, Serine/threonine-protein kinase, Transferase
Biological processBiological rhythms, DNA damage, DNA recombination, DNA repair, Immunity, Innate immunity
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-1834949 Cytosolic sensors of pathogen-associated DNA
R-HSA-3270619 IRF3-mediated induction of type I IFN
R-HSA-5693571 Nonhomologous End-Joining (NHEJ)
R-HSA-8866654 E3 ubiquitin ligases ubiquitinate target proteins

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P78527

<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:
DNA-dependent protein kinase catalytic subunit (EC:2.7.11.1)
Short name:
DNA-PK catalytic subunit
Short name:
DNA-PKcs
Alternative name(s):
DNPK1
p460
<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:PRKDC
Synonyms:HYRC, HYRC1
<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 8

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:9413 PRKDC

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
600899 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P78527

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

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

Keywords - Cellular componenti

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

Immunodeficiency 26 with or without neurologic abnormalities (IMD26)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of severe combined immunodeficiency characterized by reduced or absent T and B cells, recurrent candidiasis, and lower respiratory tract infections. Some patients show dysmorphic features, severe growth failure, microcephaly, seizures, and impaired neurological functions.
Related information in OMIM
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_0725693062L → R in IMD26; shows increased long palindromic (P)-nucleotide stretches in the immunoglobulin coding joints indicating a defect in hairpin opening and insufficient DCLRE1C activation. 1 PublicationCorresponds to variant dbSNP:rs587777685EnsemblClinVar.1
Natural variantiVAR_0725703574A → V in IMD26; shows impaired function in response to irradiation and a less severe defect in V(D)J end-joining suggesting that the missense mutation retained some functional capacity; consistent with a loss of function mutation. 1 PublicationCorresponds to variant dbSNP:rs587777686EnsemblClinVar.1

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>Mutagenesisi1510L → P: Loss of interaction with C1D. 1 Publication1
Mutagenesisi1516 – 1517EL → PD: Loss of interaction with C1D. 1 Publication2
Mutagenesisi2609T → A: Leads to radiation sensitivity and impaired DSB joining. Gives rise to reduced phosphorylation; when associated with A-2612. 1 Publication1
Mutagenesisi2612S → A: Reduced phosphorylation; when associated with A-2609. 1
Mutagenesisi2638T → A: Alleviates phosphorylation, leaves a fully active enzyme with compromised cellular resistance to ionizing radiation without affecting DNA end joining; when associated with A-2647. 1 Publication1
Mutagenesisi2647T → A: Alleviates phosphorylation, leaves a fully active enzyme with compromised cellular resistance to ionizing radiation without affecting DNA end joining; when associated with A-2638. 1 Publication1

Keywords - Diseasei

Disease mutation, SCID

Organism-specific databases

DisGeNET

More...
DisGeNETi
5591

MalaCards human disease database

More...
MalaCardsi
PRKDC
MIMi615966 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000253729

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

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Orphaneti
317425 Severe combined immunodeficiency due to DNA-PKcs deficiency

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA33776

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3142

Drug and drug target database

More...
DrugBanki
DB00201 Caffeine
DB05210 SF1126

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2800

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
PRKDC

Domain mapping of disease mutations (DMDM)

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DMDMi
38258929

<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_00002255981 – 4128DNA-dependent protein kinase catalytic subunitAdd BLAST4128

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 residuei117N6-acetyllysineCombined sources1
Modified residuei511PhosphoserineCombined sources1
Modified residuei687PhosphoserineCombined sources1
Modified residuei828N6-acetyllysineCombined sources1
Modified residuei841PhosphoserineCombined sources1
Modified residuei893PhosphoserineCombined sources1
Modified residuei1065PhosphoserineCombined sources1
Modified residuei1209N6-acetyllysineCombined sources1
Modified residuei1970N6-acetyllysineCombined sources1
Modified residuei2056Phosphoserine; by autocatalysis2 Publications1
Modified residuei2259N6-acetyllysineCombined sources1
Modified residuei2535PhosphothreonineCombined sources1
Modified residuei2609Phosphothreonine; by autocatalysis3 Publications1
Modified residuei2612Phosphoserine; by autocatalysisCombined sources1 Publication1
Modified residuei2638Phosphothreonine; by autocatalysisCombined sources1 Publication1
Modified residuei2647Phosphothreonine; by autocatalysisCombined sources1 Publication1
Modified residuei2789PhosphoserineCombined sources1
Modified residuei3205PhosphoserineCombined sources1
Modified residuei3241N6-acetyllysineCombined sources1
Modified residuei3260N6-acetyllysineCombined sources1
Modified residuei3621N6-acetyllysineCombined sources1
Modified residuei3638N6-acetyllysineCombined sources1
Modified residuei3642N6-acetyllysineCombined sources1
Modified residuei3731PhosphoserineCombined sources1
Modified residuei3821PhosphoserineCombined sources1
Modified residuei4026PhosphoserineCombined 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 on Ser-2056, Thr-2609, Thr-2638 and Thr-2647. Ser-2056 and Thr-2609 are DNA damage-inducible phosphorylation sites (inducible with ionizing radiation, IR) dephosphorylated by PPP5C. Autophosphorylation induces a conformational change that leads to remodeling of the DNA-PK complex, requisite for efficient end processing and DNA repair.21 Publications
S-nitrosylated by GAPDH.By similarity
Polyubiquitinated by RNF144A, leading to 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>Sitei2020 – 2021Cleavage; by caspase-3Curated2

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P78527

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P78527

MaxQB - The MaxQuant DataBase

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MaxQBi
P78527

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

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PaxDbi
P78527

PeptideAtlas

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PeptideAtlasi
P78527

PRoteomics IDEntifications database

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PRIDEi
P78527

ProteomicsDB human proteome resource

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ProteomicsDBi
57634
57635 [P78527-2]

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P78527

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P78527

GlyConnect protein glycosylation platform

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GlyConnecti
1183

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P78527

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

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PhosphoSitePlusi
P78527

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P78527

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000253729 Expressed in 234 organ(s), highest expression level in kidney

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P78527 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P78527 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB005167
HPA035174

<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

DNA-PK is a heterotrimer of PRKDC and the Ku p70/YRCC6-p86/XRCC5 dimer. Formation of this complex may be promoted by interaction with ILF3. Associates with the DNA-bound Ku heterodimer, but it can also bind to and be activated by free DNA. The DNA-PK heterotrimer associates with the LIG4-XRCC4 complex to form the core of the non-homologous end joining (NHEJ) complex. Additional components of the NHEJ complex include NHEJ1/XLF and PAXX. Interacts with DNA-PKcs-interacting protein (KIP) with the region upstream the kinase domain. PRKDC alone also interacts with and phosphorylates DCLRE1C, thereby activating the latent endonuclease activity of this protein. Interacts with C1D. Interacts with TTI1 and TELO2. Interacts with CIB1. Interacts with SETX (PubMed:23149945). Interacts with NR4A3; the DNA-dependent protein kinase complex DNA-PK phosphorylates and activates NR4A3 and prevents NR4A3 ubiquitination and degradation (PubMed:25852083). Interacts with BRAT1. Part of the HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1 RNA.21 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
111577, 328 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-3403 DNA-dependent protein kinase complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P78527

Database of interacting proteins

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DIPi
DIP-24186N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P78527

Protein interaction database and analysis system

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IntActi
P78527, 141 interactors

Molecular INTeraction database

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MINTi
P78527

STRING: functional protein association networks

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STRINGi
9606.ENSP00000313420

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P78527

<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

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

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SMRi
P78527

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...

<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 ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati288 – 323HEAT 1Add BLAST36
Repeati1004 – 1040HEAT 2Add BLAST37
Repeati1723 – 1756TPR 1Add BLAST34
<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>Domaini2906 – 3539FATPROSITE-ProRule annotationAdd BLAST634
Repeati2920 – 2948TPR 2Add BLAST29
Repeati2949 – 2982TPR 3Add BLAST34
Domaini3747 – 4015PI3K/PI4KPROSITE-ProRule annotationAdd BLAST269
Domaini4096 – 4128FATCPROSITE-ProRule annotationAdd BLAST33

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>Regioni1503 – 1538Interaction with C1D1 PublicationAdd BLAST36
Regioni1503 – 1538Leucine-zipperAdd BLAST36
Regioni2436 – 3212KIP-bindingAdd BLAST777

<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 PI3/PI4-kinase family.Curated

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0891 Eukaryota
COG5032 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155633

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P78527

KEGG Orthology (KO)

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KOi
K06642

Identification of Orthologs from Complete Genome Data

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OMAi
NYSKCTI

Database of Orthologous Groups

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OrthoDBi
26975at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P78527

TreeFam database of animal gene trees

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TreeFami
TF324494

Family and domain databases

Conserved Domains Database

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CDDi
cd05172 PIKKc_DNA-PK, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.1070.11, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR016024 ARM-type_fold
IPR037706 DNA-PK_dom
IPR003152 FATC_dom
IPR011009 Kinase-like_dom_sf
IPR012582 NUC194
IPR000403 PI3/4_kinase_cat_dom
IPR036940 PI3/4_kinase_cat_sf
IPR018936 PI3/4_kinase_CS
IPR003151 PIK-rel_kinase_FAT
IPR014009 PIK_FAT

Pfam protein domain database

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Pfami
View protein in Pfam
PF02259 FAT, 1 hit
PF02260 FATC, 1 hit
PF08163 NUC194, 1 hit
PF00454 PI3_PI4_kinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM01343 FATC, 1 hit
SM01344 NUC194, 1 hit
SM00146 PI3Kc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48371 SSF48371, 3 hits
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51189 FAT, 1 hit
PS51190 FATC, 1 hit
PS00915 PI3_4_KINASE_1, 1 hit
PS00916 PI3_4_KINASE_2, 1 hit
PS50290 PI3_4_KINASE_3, 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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <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 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P78527-1) [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
MAGSGAGVRC SLLRLQETLS AADRCGAALA GHQLIRGLGQ ECVLSSSPAV
60 70 80 90 100
LALQTSLVFS RDFGLLVFVR KSLNSIEFRE CREEILKFLC IFLEKMGQKI
110 120 130 140 150
APYSVEIKNT CTSVYTKDRA AKCKIPALDL LIKLLQTFRS SRLMDEFKIG
160 170 180 190 200
ELFSKFYGEL ALKKKIPDTV LEKVYELLGL LGEVHPSEMI NNAENLFRAF
210 220 230 240 250
LGELKTQMTS AVREPKLPVL AGCLKGLSSL LCNFTKSMEE DPQTSREIFN
260 270 280 290 300
FVLKAIRPQI DLKRYAVPSA GLRLFALHAS QFSTCLLDNY VSLFEVLLKW
310 320 330 340 350
CAHTNVELKK AALSALESFL KQVSNMVAKN AEMHKNKLQY FMEQFYGIIR
360 370 380 390 400
NVDSNNKELS IAIRGYGLFA GPCKVINAKD VDFMYVELIQ RCKQMFLTQT
410 420 430 440 450
DTGDDRVYQM PSFLQSVASV LLYLDTVPEV YTPVLEHLVV MQIDSFPQYS
460 470 480 490 500
PKMQLVCCRA IVKVFLALAA KGPVLRNCIS TVVHQGLIRI CSKPVVLPKG
510 520 530 540 550
PESESEDHRA SGEVRTGKWK VPTYKDYVDL FRHLLSSDQM MDSILADEAF
560 570 580 590 600
FSVNSSSESL NHLLYDEFVK SVLKIVEKLD LTLEIQTVGE QENGDEAPGV
610 620 630 640 650
WMIPTSDPAA NLHPAKPKDF SAFINLVEFC REILPEKQAE FFEPWVYSFS
660 670 680 690 700
YELILQSTRL PLISGFYKLL SITVRNAKKI KYFEGVSPKS LKHSPEDPEK
710 720 730 740 750
YSCFALFVKF GKEVAVKMKQ YKDELLASCL TFLLSLPHNI IELDVRAYVP
760 770 780 790 800
ALQMAFKLGL SYTPLAEVGL NALEEWSIYI DRHVMQPYYK DILPCLDGYL
810 820 830 840 850
KTSALSDETK NNWEVSALSR AAQKGFNKVV LKHLKKTKNL SSNEAISLEE
860 870 880 890 900
IRIRVVQMLG SLGGQINKNL LTVTSSDEMM KSYVAWDREK RLSFAVPFRE
910 920 930 940 950
MKPVIFLDVF LPRVTELALT ASDRQTKVAA CELLHSMVMF MLGKATQMPE
960 970 980 990 1000
GGQGAPPMYQ LYKRTFPVLL RLACDVDQVT RQLYEPLVMQ LIHWFTNNKK
1010 1020 1030 1040 1050
FESQDTVALL EAILDGIVDP VDSTLRDFCG RCIREFLKWS IKQITPQQQE
1060 1070 1080 1090 1100
KSPVNTKSLF KRLYSLALHP NAFKRLGASL AFNNIYREFR EEESLVEQFV
1110 1120 1130 1140 1150
FEALVIYMES LALAHADEKS LGTIQQCCDA IDHLCRIIEK KHVSLNKAKK
1160 1170 1180 1190 1200
RRLPRGFPPS ASLCLLDLVK WLLAHCGRPQ TECRHKSIEL FYKFVPLLPG
1210 1220 1230 1240 1250
NRSPNLWLKD VLKEEGVSFL INTFEGGGCG QPSGILAQPT LLYLRGPFSL
1260 1270 1280 1290 1300
QATLCWLDLL LAALECYNTF IGERTVGALQ VLGTEAQSSL LKAVAFFLES
1310 1320 1330 1340 1350
IAMHDIIAAE KCFGTGAAGN RTSPQEGERY NYSKCTVVVR IMEFTTTLLN
1360 1370 1380 1390 1400
TSPEGWKLLK KDLCNTHLMR VLVQTLCEPA SIGFNIGDVQ VMAHLPDVCV
1410 1420 1430 1440 1450
NLMKALKMSP YKDILETHLR EKITAQSIEE LCAVNLYGPD AQVDRSRLAA
1460 1470 1480 1490 1500
VVSACKQLHR AGLLHNILPS QSTDLHHSVG TELLSLVYKG IAPGDERQCL
1510 1520 1530 1540 1550
PSLDLSCKQL ASGLLELAFA FGGLCERLVS LLLNPAVLST ASLGSSQGSV
1560 1570 1580 1590 1600
IHFSHGEYFY SLFSETINTE LLKNLDLAVL ELMQSSVDNT KMVSAVLNGM
1610 1620 1630 1640 1650
LDQSFRERAN QKHQGLKLAT TILQHWKKCD SWWAKDSPLE TKMAVLALLA
1660 1670 1680 1690 1700
KILQIDSSVS FNTSHGSFPE VFTTYISLLA DTKLDLHLKG QAVTLLPFFT
1710 1720 1730 1740 1750
SLTGGSLEEL RRVLEQLIVA HFPMQSREFP PGTPRFNNYV DCMKKFLDAL
1760 1770 1780 1790 1800
ELSQSPMLLE LMTEVLCREQ QHVMEELFQS SFRRIARRGS CVTQVGLLES
1810 1820 1830 1840 1850
VYEMFRKDDP RLSFTRQSFV DRSLLTLLWH CSLDALREFF STIVVDAIDV
1860 1870 1880 1890 1900
LKSRFTKLNE STFDTQITKK MGYYKILDVM YSRLPKDDVH AKESKINQVF
1910 1920 1930 1940 1950
HGSCITEGNE LTKTLIKLCY DAFTENMAGE NQLLERRRLY HCAAYNCAIS
1960 1970 1980 1990 2000
VICCVFNELK FYQGFLFSEK PEKNLLIFEN LIDLKRRYNF PVEVEVPMER
2010 2020 2030 2040 2050
KKKYIEIRKE AREAANGDSD GPSYMSSLSY LADSTLSEEM SQFDFSTGVQ
2060 2070 2080 2090 2100
SYSYSSQDPR PATGRFRRRE QRDPTVHDDV LELEMDELNR HECMAPLTAL
2110 2120 2130 2140 2150
VKHMHRSLGP PQGEEDSVPR DLPSWMKFLH GKLGNPIVPL NIRLFLAKLV
2160 2170 2180 2190 2200
INTEEVFRPY AKHWLSPLLQ LAASENNGGE GIHYMVVEIV ATILSWTGLA
2210 2220 2230 2240 2250
TPTGVPKDEV LANRLLNFLM KHVFHPKRAV FRHNLEIIKT LVECWKDCLS
2260 2270 2280 2290 2300
IPYRLIFEKF SGKDPNSKDN SVGIQLLGIV MANDLPPYDP QCGIQSSEYF
2310 2320 2330 2340 2350
QALVNNMSFV RYKEVYAAAA EVLGLILRYV MERKNILEES LCELVAKQLK
2360 2370 2380 2390 2400
QHQNTMEDKF IVCLNKVTKS FPPLADRFMN AVFFLLPKFH GVLKTLCLEV
2410 2420 2430 2440 2450
VLCRVEGMTE LYFQLKSKDF VQVMRHRDDE RQKVCLDIIY KMMPKLKPVE
2460 2470 2480 2490 2500
LRELLNPVVE FVSHPSTTCR EQMYNILMWI HDNYRDPESE TDNDSQEIFK
2510 2520 2530 2540 2550
LAKDVLIQGL IDENPGLQLI IRNFWSHETR LPSNTLDRLL ALNSLYSPKI
2560 2570 2580 2590 2600
EVHFLSLATN FLLEMTSMSP DYPNPMFEHP LSECEFQEYT IDSDWRFRST
2610 2620 2630 2640 2650
VLTPMFVETQ ASQGTLQTRT QEGSLSARWP VAGQIRATQQ QHDFTLTQTA
2660 2670 2680 2690 2700
DGRSSFDWLT GSSTDPLVDH TSPSSDSLLF AHKRSERLQR APLKSVGPDF
2710 2720 2730 2740 2750
GKKRLGLPGD EVDNKVKGAA GRTDLLRLRR RFMRDQEKLS LMYARKGVAE
2760 2770 2780 2790 2800
QKREKEIKSE LKMKQDAQVV LYRSYRHGDL PDIQIKHSSL ITPLQAVAQR
2810 2820 2830 2840 2850
DPIIAKQLFS SLFSGILKEM DKFKTLSEKN NITQKLLQDF NRFLNTTFSF
2860 2870 2880 2890 2900
FPPFVSCIQD ISCQHAALLS LDPAAVSAGC LASLQQPVGI RLLEEALLRL
2910 2920 2930 2940 2950
LPAELPAKRV RGKARLPPDV LRWVELAKLY RSIGEYDVLR GIFTSEIGTK
2960 2970 2980 2990 3000
QITQSALLAE ARSDYSEAAK QYDEALNKQD WVDGEPTEAE KDFWELASLD
3010 3020 3030 3040 3050
CYNHLAEWKS LEYCSTASID SENPPDLNKI WSEPFYQETY LPYMIRSKLK
3060 3070 3080 3090 3100
LLLQGEADQS LLTFIDKAMH GELQKAILEL HYSQELSLLY LLQDDVDRAK
3110 3120 3130 3140 3150
YYIQNGIQSF MQNYSSIDVL LHQSRLTKLQ SVQALTEIQE FISFISKQGN
3160 3170 3180 3190 3200
LSSQVPLKRL LNTWTNRYPD AKMDPMNIWD DIITNRCFFL SKIEEKLTPL
3210 3220 3230 3240 3250
PEDNSMNVDQ DGDPSDRMEV QEQEEDISSL IRSCKFSMKM KMIDSARKQN
3260 3270 3280 3290 3300
NFSLAMKLLK ELHKESKTRD DWLVSWVQSY CRLSHCRSRS QGCSEQVLTV
3310 3320 3330 3340 3350
LKTVSLLDEN NVSSYLSKNI LAFRDQNILL GTTYRIIANA LSSEPACLAE
3360 3370 3380 3390 3400
IEEDKARRIL ELSGSSSEDS EKVIAGLYQR AFQHLSEAVQ AAEEEAQPPS
3410 3420 3430 3440 3450
WSCGPAAGVI DAYMTLADFC DQQLRKEEEN ASVIDSAELQ AYPALVVEKM
3460 3470 3480 3490 3500
LKALKLNSNE ARLKFPRLLQ IIERYPEETL SLMTKEISSV PCWQFISWIS
3510 3520 3530 3540 3550
HMVALLDKDQ AVAVQHSVEE ITDNYPQAIV YPFIISSESY SFKDTSTGHK
3560 3570 3580 3590 3600
NKEFVARIKS KLDQGGVIQD FINALDQLSN PELLFKDWSN DVRAELAKTP
3610 3620 3630 3640 3650
VNKKNIEKMY ERMYAALGDP KAPGLGAFRR KFIQTFGKEF DKHFGKGGSK
3660 3670 3680 3690 3700
LLRMKLSDFN DITNMLLLKM NKDSKPPGNL KECSPWMSDF KVEFLRNELE
3710 3720 3730 3740 3750
IPGQYDGRGK PLPEYHVRIA GFDERVTVMA SLRRPKRIII RGHDEREHPF
3760 3770 3780 3790 3800
LVKGGEDLRQ DQRVEQLFQV MNGILAQDSA CSQRALQLRT YSVVPMTSRL
3810 3820 3830 3840 3850
GLIEWLENTV TLKDLLLNTM SQEEKAAYLS DPRAPPCEYK DWLTKMSGKH
3860 3870 3880 3890 3900
DVGAYMLMYK GANRTETVTS FRKRESKVPA DLLKRAFVRM STSPEAFLAL
3910 3920 3930 3940 3950
RSHFASSHAL ICISHWILGI GDRHLNNFMV AMETGGVIGI DFGHAFGSAT
3960 3970 3980 3990 4000
QFLPVPELMP FRLTRQFINL MLPMKETGLM YSIMVHALRA FRSDPGLLTN
4010 4020 4030 4040 4050
TMDVFVKEPS FDWKNFEQKM LKKGGSWIQE INVAEKNWYP RQKICYAKRK
4060 4070 4080 4090 4100
LAGANPAVIT CDELLLGHEK APAFRDYVAV ARGSKDHNIR AQEPESGLSE
4110 4120
ETQVKCLMDQ ATDPNILGRT WEGWEPWM
Length:4,128
Mass (Da):469,089
Last modified:October 31, 2003 - 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:iAC6E747FEB09F3E5
GO
Isoform 2 (identifier: P78527-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     3799-3829: Missing.

Show »
Length:4,097
Mass (Da):465,501
Checksum:iB698F749065D319B
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0YG84H0YG84_HUMAN
DNA-dependent protein kinase cataly...
PRKDC
90Annotation 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>
F5GX40F5GX40_HUMAN
DNA-dependent protein kinase cataly...
PRKDC
70Annotation 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 conflicti405D → Y in AAC50210 (Ref. 2) Curated1
Sequence conflicti1008A → S in AAC50210 (Ref. 2) Curated1
Sequence conflicti3660N → T in AAA79184 (PubMed:7594449).Curated1
Sequence conflicti3817L → W in AAA79184 (PubMed:7594449).Curated1
Sequence conflicti3862A → P in AAA79184 (PubMed:7594449).Curated1
Sequence conflicti4031I → V in AAK40350 (Ref. 9) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0191796A → S2 PublicationsCorresponds to variant dbSNP:rs8177999EnsemblClinVar.1
Natural variantiVAR_041602263K → N in a lung adenocarcinoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs758032015Ensembl.1
Natural variantiVAR_019180333M → I2 PublicationsCorresponds to variant dbSNP:rs8178017EnsemblClinVar.1
Natural variantiVAR_041603420V → I1 PublicationCorresponds to variant dbSNP:rs55925466Ensembl.1
Natural variantiVAR_041604500G → S in a metastatic melanoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_019181605T → S2 PublicationsCorresponds to variant dbSNP:rs8178033EnsemblClinVar.1
Natural variantiVAR_041605649F → L1 PublicationCorresponds to variant dbSNP:rs55811715Ensembl.1
Natural variantiVAR_019182680I → M1 PublicationCorresponds to variant dbSNP:rs8178040EnsemblClinVar.1
Natural variantiVAR_019183695P → S2 PublicationsCorresponds to variant dbSNP:rs8178046EnsemblClinVar.1
Natural variantiVAR_0191841071N → S1 PublicationCorresponds to variant dbSNP:rs8178070EnsemblClinVar.1
Natural variantiVAR_0416061136R → H in a colorectal adenocarcinoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs781401034Ensembl.1
Natural variantiVAR_0416071190L → V1 PublicationCorresponds to variant dbSNP:rs34598508Ensembl.1
Natural variantiVAR_0416081237A → T1 PublicationCorresponds to variant dbSNP:rs191531119EnsemblClinVar.1
Natural variantiVAR_0416091279L → F1 Publication1
Natural variantiVAR_0191851314G → V1 PublicationCorresponds to variant dbSNP:rs8178090Ensembl.1
Natural variantiVAR_0416101447R → M in a lung squamous cell carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_0191861588D → V1 PublicationCorresponds to variant dbSNP:rs8178104Ensembl.1
Natural variantiVAR_0191871603Q → H1 PublicationCorresponds to variant dbSNP:rs8178106EnsemblClinVar.1
Natural variantiVAR_0416111619A → G1 PublicationCorresponds to variant dbSNP:rs56182356Ensembl.1
Natural variantiVAR_0416121680A → V in a metastatic melanoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs55735910Ensembl.1
Natural variantiVAR_0416132023S → P1 PublicationCorresponds to variant dbSNP:rs56042895EnsemblClinVar.1
Natural variantiVAR_0191882095A → V1 PublicationCorresponds to variant dbSNP:rs8178147Ensembl.1
Natural variantiVAR_0416142598R → Q1 PublicationCorresponds to variant dbSNP:rs55923149Ensembl.1
Natural variantiVAR_0191892702K → E1 PublicationCorresponds to variant dbSNP:rs8178178Ensembl.1
Natural variantiVAR_0416152810S → N in a metastatic melanoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_0191902899R → C2 PublicationsCorresponds to variant dbSNP:rs4278157EnsemblClinVar.1
Natural variantiVAR_0416162941G → A in a lung neuroendocrine carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_0725693062L → R in IMD26; shows increased long palindromic (P)-nucleotide stretches in the immunoglobulin coding joints indicating a defect in hairpin opening and insufficient DCLRE1C activation. 1 PublicationCorresponds to variant dbSNP:rs587777685EnsemblClinVar.1
Natural variantiVAR_0416173085E → D1 PublicationCorresponds to variant dbSNP:rs56135402Ensembl.1
Natural variantiVAR_0191913149G → D2 PublicationsCorresponds to variant dbSNP:rs8178208EnsemblClinVar.1
Natural variantiVAR_0416183198T → S1 PublicationCorresponds to variant dbSNP:rs55793951Ensembl.1
Natural variantiVAR_0191923201P → S2 PublicationsCorresponds to variant dbSNP:rs8178216EnsemblClinVar.1
Natural variantiVAR_0191933404G → E2 PublicationsCorresponds to variant dbSNP:rs8178225EnsemblClinVar.1
Natural variantiVAR_0191943434I → T2 PublicationsCorresponds to variant dbSNP:rs7830743EnsemblClinVar.1
Natural variantiVAR_0191953459N → S1 PublicationCorresponds to variant dbSNP:rs8178228EnsemblClinVar.1
Natural variantiVAR_0191963562L → M2 PublicationsCorresponds to variant dbSNP:rs8178232EnsemblClinVar.1
Natural variantiVAR_0725703574A → V in IMD26; shows impaired function in response to irradiation and a less severe defect in V(D)J end-joining suggesting that the missense mutation retained some functional capacity; consistent with a loss of function mutation. 1 PublicationCorresponds to variant dbSNP:rs587777686EnsemblClinVar.1
Natural variantiVAR_0416193584L → F1 PublicationCorresponds to variant dbSNP:rs55866966EnsemblClinVar.1
Natural variantiVAR_0505343702P → L. Corresponds to variant dbSNP:rs8178236Ensembl.1
Natural variantiVAR_0416203800L → I1 PublicationCorresponds to variant dbSNP:rs56216442Ensembl.1
Natural variantiVAR_0191973836P → L2 PublicationsCorresponds to variant dbSNP:rs8178245Ensembl.1
Natural variantiVAR_0191983932M → V1 PublicationCorresponds to variant dbSNP:rs8178248Ensembl.1
Natural variantiVAR_0416213936G → S1 PublicationCorresponds to variant dbSNP:rs55670423Ensembl.1
Natural variantiVAR_0416223937V → M1 PublicationCorresponds to variant dbSNP:rs56090750Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0047083799 – 3829Missing in isoform 2. 1 PublicationAdd BLAST31

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
U47077 mRNA Translation: AAB39925.5
U34994 mRNA Translation: AAC50210.3
AY316117 Genomic DNA Translation: AAP69525.1
U63630 Genomic DNA Translation: AAC52019.2
U90415 Genomic DNA Translation: AAB51722.1
L27425 Genomic DNA Translation: AAA79244.1
AB052953 Genomic DNA Translation: BAB79635.1
U35835 mRNA Translation: AAA79184.1
AY030284 Genomic DNA Translation: AAK40350.1
AB208860 mRNA Translation: BAD92097.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS75734.1 [P78527-2]
CCDS75735.1 [P78527-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A57099
G02083

NCBI Reference Sequences

More...
RefSeqi
NP_001075109.1, NM_001081640.1 [P78527-2]
NP_008835.5, NM_006904.6 [P78527-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000314191; ENSP00000313420; ENSG00000253729 [P78527-1]
ENST00000338368; ENSP00000345182; ENSG00000253729 [P78527-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5591

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:5591

UCSC genome browser

More...
UCSCi
uc033bkh.1 human [P78527-1]

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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U47077 mRNA Translation: AAB39925.5
U34994 mRNA Translation: AAC50210.3
AY316117 Genomic DNA Translation: AAP69525.1
U63630 Genomic DNA Translation: AAC52019.2
U90415 Genomic DNA Translation: AAB51722.1
L27425 Genomic DNA Translation: AAA79244.1
AB052953 Genomic DNA Translation: BAB79635.1
U35835 mRNA Translation: AAA79184.1
AY030284 Genomic DNA Translation: AAK40350.1
AB208860 mRNA Translation: BAD92097.1
CCDSiCCDS75734.1 [P78527-2]
CCDS75735.1 [P78527-1]
PIRiA57099
G02083
RefSeqiNP_001075109.1, NM_001081640.1 [P78527-2]
NP_008835.5, NM_006904.6 [P78527-1]

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
5LUQX-ray4.30A/B2-2575[»]
A/B2774-4127[»]
5W1Relectron microscopy4.40A1-4128[»]
5Y3Relectron microscopy6.60C10-4128[»]
SMRiP78527
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111577, 328 interactors
ComplexPortaliCPX-3403 DNA-dependent protein kinase complex
CORUMiP78527
DIPiDIP-24186N
ELMiP78527
IntActiP78527, 141 interactors
MINTiP78527
STRINGi9606.ENSP00000313420

Chemistry databases

BindingDBiP78527
ChEMBLiCHEMBL3142
DrugBankiDB00201 Caffeine
DB05210 SF1126
GuidetoPHARMACOLOGYi2800

PTM databases

CarbonylDBiP78527
GlyConnecti1183
iPTMnetiP78527
PhosphoSitePlusiP78527
SwissPalmiP78527

Polymorphism and mutation databases

BioMutaiPRKDC
DMDMi38258929

2D gel databases

SWISS-2DPAGEiP78527

Proteomic databases

EPDiP78527
jPOSTiP78527
MaxQBiP78527
PaxDbiP78527
PeptideAtlasiP78527
PRIDEiP78527
ProteomicsDBi57634
57635 [P78527-2]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000314191; ENSP00000313420; ENSG00000253729 [P78527-1]
ENST00000338368; ENSP00000345182; ENSG00000253729 [P78527-2]
GeneIDi5591
KEGGihsa:5591
UCSCiuc033bkh.1 human [P78527-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
5591
DisGeNETi5591

GeneCards: human genes, protein and diseases

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GeneCardsi
PRKDC
HGNCiHGNC:9413 PRKDC
HPAiCAB005167
HPA035174
MalaCardsiPRKDC
MIMi600899 gene
615966 phenotype
neXtProtiNX_P78527
OpenTargetsiENSG00000253729
Orphaneti317425 Severe combined immunodeficiency due to DNA-PKcs deficiency
PharmGKBiPA33776

GenAtlas: human gene database

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GenAtlasi
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Phylogenomic databases

eggNOGiKOG0891 Eukaryota
COG5032 LUCA
GeneTreeiENSGT00940000155633
InParanoidiP78527
KOiK06642
OMAiNYSKCTI
OrthoDBi26975at2759
PhylomeDBiP78527
TreeFamiTF324494

Enzyme and pathway databases

ReactomeiR-HSA-1834949 Cytosolic sensors of pathogen-associated DNA
R-HSA-3270619 IRF3-mediated induction of type I IFN
R-HSA-5693571 Nonhomologous End-Joining (NHEJ)
R-HSA-8866654 E3 ubiquitin ligases ubiquitinate target proteins
SIGNORiP78527

Miscellaneous databases

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

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ChiTaRSi
PRKDC human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
DNA-PKcs

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

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GenomeRNAii
5591

Protein Ontology

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PROi
PR:P78527

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSG00000253729 Expressed in 234 organ(s), highest expression level in kidney
ExpressionAtlasiP78527 baseline and differential
GenevisibleiP78527 HS

Family and domain databases

CDDicd05172 PIKKc_DNA-PK, 1 hit
Gene3Di1.10.1070.11, 1 hit
InterProiView protein in InterPro
IPR016024 ARM-type_fold
IPR037706 DNA-PK_dom
IPR003152 FATC_dom
IPR011009 Kinase-like_dom_sf
IPR012582 NUC194
IPR000403 PI3/4_kinase_cat_dom
IPR036940 PI3/4_kinase_cat_sf
IPR018936 PI3/4_kinase_CS
IPR003151 PIK-rel_kinase_FAT
IPR014009 PIK_FAT
PfamiView protein in Pfam
PF02259 FAT, 1 hit
PF02260 FATC, 1 hit
PF08163 NUC194, 1 hit
PF00454 PI3_PI4_kinase, 1 hit
SMARTiView protein in SMART
SM01343 FATC, 1 hit
SM01344 NUC194, 1 hit
SM00146 PI3Kc, 1 hit
SUPFAMiSSF48371 SSF48371, 3 hits
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS51189 FAT, 1 hit
PS51190 FATC, 1 hit
PS00915 PI3_4_KINASE_1, 1 hit
PS00916 PI3_4_KINASE_2, 1 hit
PS50290 PI3_4_KINASE_3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<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 nameiPRKDC_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: P78527
Secondary accession number(s): P78528
, Q13327, Q13337, Q14175, Q59H99, Q7Z611, Q96SE6, Q9UME3
<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: April 27, 2001
Last sequence update: October 31, 2003
Last modified: June 5, 2019
This is version 211 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
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 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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