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UniProtKB - P78527 (PRKDC_HUMAN)

Entry version 224 (07 Apr 2021)
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). As part of the DNA-PK complex, involved in the early steps of ribosome assembly by promoting the processing of precursor rRNA into mature 18S rRNA in the small-subunit processome (PubMed:32103174). Binding to U3 small nucleolar RNA, recruits PRKDC and XRCC5/Ku86 to the small-subunit processome (PubMed:32103174). Recognizes the substrate consensus sequence [ST]-Q (PubMed:15574326, PubMed:11955432, PubMed:12649176, PubMed:14734805). Phosphorylates 'Ser-139' of histone variant H2AX, 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 similarity25 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activity seems to be attenuated by autophosphorylation. Binding to the SL1 region of U3 small nucleolar RNA promotes auto-phosphorylation activity (PubMed:32103174). Inhibited by wortmannin (PubMed:9766667).2 Publications

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

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

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

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P78527

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%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
DNA-dependent protein kinase catalytic subunit (EC:2.7.11.12 Publications)
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%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PRKDC
Synonyms:HYRC, HYRC1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 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

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000253729.7

<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

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 variants 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%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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 variant, 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

More...Orphaneti		317425, Severe combined immunodeficiency due to DNA-PKcs deficiency

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA33776

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P78527, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3142

Drug and drug target database

More...DrugBanki		DB00201, Caffeine
DB05210, SF1126

DrugCentral

More...DrugCentrali		P78527

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2800

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		PRKDC

Domain mapping of disease mutations (DMDM)

More...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 or proteolytic cleavage.<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 autocatalysis4 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%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Autophosphorylated at two clusters, the T2609 cluster and the S2056 cluster (By similarity). 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. Autophosphorylation of the T2609 cluster is required for hematopoietic development and protein synthesis in erythrocytes precursors (By similarity).By similarity21 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

More...EPDi		P78527

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P78527

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P78527

MaxQB - The MaxQuant DataBase

More...MaxQBi		P78527

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

More...PaxDbi		P78527

PeptideAtlas

More...PeptideAtlasi		P78527

PRoteomics IDEntifications database

More...PRIDEi		P78527

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		57634 [P78527-1]
57635 [P78527-2]

2D gel databases

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

More...SWISS-2DPAGEi		P78527

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P78527

GlyConnect protein glycosylation platform

More...GlyConnecti		1183, 1 N-Linked glycan (1 site)

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P78527, 2 sites, 1 O-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P78527

MetOSite database of methionine sulfoxide sites

More...MetOSitei		P78527

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

More...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

More...Bgeei		ENSG00000253729, Expressed in ventricular zone and 244 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P78527, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P78527, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000253729, Low tissue specificity

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		111577, 438 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-3403, DNA-dependent protein kinase complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P78527

Database of interacting proteins

More...DIPi		DIP-24186N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P78527

Protein interaction database and analysis system

More...IntActi		P78527, 176 interactors

Molecular INTeraction database

More...MINTi		P78527

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000313420

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P78527

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P78527, protein

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

3D structure databases

Small Angle Scattering Biological Data Bank

More...SASBDBi		P78527

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

More...SMRi		P78527

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the '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%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>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

More...eggNOGi		KOG0891, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155633

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_224534_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P78527

Identification of Orthologs from Complete Genome Data

More...OMAi		MENTCTL

Database of Orthologous Groups

More...OrthoDBi		26975at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P78527

TreeFam database of animal gene trees

More...TreeFami		TF324494

Family and domain databases

Conserved Domains Database

More...CDDi		cd05172, PIKKc_DNA-PK, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.1070.11, 1 hit

Integrated resource of protein families, domains and functional sites

More...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

More...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

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

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48371, SSF48371, 3 hits
SSF56112, SSF56112, 1 hit

PROSITE; a protein domain and family database

More...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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 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 <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
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:rs8178090EnsemblClinVar.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:rs56182356EnsemblClinVar.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:rs55793951EnsemblClinVar.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:rs8178245EnsemblClinVar.1
Natural variantiVAR_0191983932M → V1 PublicationCorresponds to variant dbSNP:rs8178248Ensembl.1
Natural variantiVAR_0416213936G → S1 PublicationCorresponds to variant dbSNP:rs55670423EnsemblClinVar.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

<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%5Freferences%5Fsection">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[»]
6ZFPelectron microscopy3.24A1-4128[»]
6ZH2electron microscopy3.92A1-4128[»]
6ZH4electron microscopy3.62A1-4128[»]
6ZH6electron microscopy3.93A1-4128[»]
6ZH8electron microscopy4.14A1-4128[»]
6ZHAelectron microscopy3.91A1-4128[»]
6ZHEelectron microscopy7.24A/F1-4128[»]
7K10electron microscopy3.30A1-4128[»]
7K11electron microscopy3.21A1-4128[»]
7K19electron microscopy4.30A1-4128[»]
7K1Belectron microscopy4.30A1-4128[»]
7K1Jelectron microscopy3.90A1-4128[»]
7K1Kelectron microscopy4.10A1-4128[»]
7K1Nelectron microscopy3.90A1-4128[»]
SASBDBiP78527
SMRiP78527
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi111577, 438 interactors
ComplexPortaliCPX-3403, DNA-dependent protein kinase complex
CORUMiP78527
DIPiDIP-24186N
ELMiP78527
IntActiP78527, 176 interactors
MINTiP78527
STRINGi9606.ENSP00000313420

Chemistry databases

BindingDBiP78527
ChEMBLiCHEMBL3142
DrugBankiDB00201, Caffeine
DB05210, SF1126
DrugCentraliP78527
GuidetoPHARMACOLOGYi2800

PTM databases

CarbonylDBiP78527
GlyConnecti1183, 1 N-Linked glycan (1 site)
GlyGeniP78527, 2 sites, 1 O-linked glycan (1 site)
iPTMnetiP78527
MetOSiteiP78527
PhosphoSitePlusiP78527
SwissPalmiP78527

Genetic variation databases

BioMutaiPRKDC
DMDMi38258929

2D gel databases

SWISS-2DPAGEiP78527

Proteomic databases

EPDiP78527
jPOSTiP78527
MassIVEiP78527
MaxQBiP78527
PaxDbiP78527
PeptideAtlasiP78527
PRIDEiP78527
ProteomicsDBi57634 [P78527-1]
57635 [P78527-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		52433, 1536 antibodies

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

More...CTDi		5591
DisGeNETi5591

GeneCards: human genes, protein and diseases

More...GeneCardsi		PRKDC
HGNCiHGNC:9413, PRKDC
HPAiENSG00000253729, Low tissue specificity
MalaCardsiPRKDC
MIMi600899, gene
615966, phenotype
neXtProtiNX_P78527
OpenTargetsiENSG00000253729
Orphaneti317425, Severe combined immunodeficiency due to DNA-PKcs deficiency
PharmGKBiPA33776
VEuPathDBiHostDB:ENSG00000253729.7

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0891, Eukaryota
GeneTreeiENSGT00940000155633
HOGENOMiCLU_224534_0_0_1
InParanoidiP78527
OMAiMENTCTL
OrthoDBi26975at2759
PhylomeDBiP78527
TreeFamiTF324494

Enzyme and pathway databases

PathwayCommonsiP78527
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

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		5591, 51 hits in 230 CRISPR screens

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

More...ChiTaRSi		PRKDC, human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		DNA-PKcs

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

More...GenomeRNAii		5591
PharosiP78527, Tchem

Protein Ontology

More...PROi		PR:P78527
RNActiP78527, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000253729, Expressed in ventricular zone and 244 other tissues
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

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry 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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 31, 2003
Last modified: April 7, 2021
This is version 224 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, Reference proteome

Documents

  1. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  2. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  3. Human entries with genetic variants
    List of human entries with genetic variants
  4. Human variants curated from literature reports
    Index of human variants curated from literature reports
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families
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