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Entry version 119 (05 Jun 2019)
Sequence version 1 (01 Mar 2002)
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Protein

DNA-dependent protein kinase catalytic subunit

Gene

PRKDC

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
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 transcript 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. 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). The assembly of the DNA-PK complex at DNA ends is also required for the NHEJ ligation step. Required to protect and align broken ends of DNA. May also act as a scaffold protein to aid the localization of DNA repair proteins to the site of damage. 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. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX, thereby regulating DNA damage response mechanism. 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. Can phosphorylate C1D not only in the presence of linear DNA but also in the presence of supercoiled DNA. Ability to phosphorylate p53/TP53 in the presence of supercoiled DNA is dependent on C1D (By similarity). 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 (By similarity).By similarity

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

<p>This subsection of the <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.By similarity

<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

<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
<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
<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>OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
<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 identifieri9615 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
<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
  • UP000002254 <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: Unplaced

<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

Defects in PRKDC are the cause of severe combined immune deficiency (SCID) which is characterized by a lack of mature functional lymphocytes and a high susceptibility to lethal opportunistic infections if not chronically treated with antibiotics. The lack of B- and T-cell immunity resembles severe combined immunodeficiency syndrome in human infants.1 Publication

Keywords - Diseasei

SCID

<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_00002256321 – 4144DNA-dependent protein kinase catalytic subunitAdd BLAST4144

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 residuei127N6-acetyllysineBy similarity1
Modified residuei521PhosphoserineBy similarity1
Modified residuei851PhosphoserineBy similarity1
Modified residuei903PhosphoserineBy similarity1
Modified residuei1075PhosphoserineBy similarity1
Modified residuei1219N6-acetyllysineBy similarity1
Modified residuei1983N6-acetyllysineBy similarity1
Modified residuei2069Phosphoserine; by autocatalysisBy similarity1
Modified residuei2271N6-acetyllysineBy similarity1
Modified residuei2547PhosphothreonineBy similarity1
Modified residuei2621Phosphothreonine; by autocatalysisBy similarity1
Modified residuei2624Phosphoserine; by autocatalysisBy similarity1
Modified residuei2650Phosphothreonine; by autocatalysisBy similarity1
Modified residuei2659Phosphothreonine; by autocatalysisBy similarity1
Modified residuei2805PhosphoserineBy similarity1
Modified residuei3221PhosphoserineBy similarity1
Modified residuei3257N6-acetyllysineBy similarity1
Modified residuei3276N6-acetyllysineBy similarity1
Modified residuei3654N6-acetyllysineBy similarity1
Modified residuei3658N6-acetyllysineBy similarity1
Modified residuei3747PhosphoserineBy similarity1
Modified residuei3837PhosphoserineBy similarity1
Modified residuei4042PhosphoserineBy similarity1

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

Autophosphorylated on Ser-2069, Thr-2621, Thr-2650 and Thr-2659. Ser-2069 and Thr-2621 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 (By similarity).By similarity
S-nitrosylated by GAPDH.By similarity
Polyubiquitinated by RNF144A, leading to proteasomal degradation.By similarity

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>Sitei2033 – 2034Cleavage; by caspase-3By similarity2

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...
PaxDbi
Q8WN22

PRoteomics IDEntifications database

More...
PRIDEi
Q8WN22

<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 CRY1 and CRY2; negatively regulates CRY1 phosphorylation.

Interacts with SETX.

Interacts with NR4A3; the DNA-dependent protein kinase complex DNA-PK phosphorylates and activates NR4A3 and prevents NR4A3 ubiquitination and degradation. 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 (By similarity).

By similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9612.ENSCAFP00000009842

<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>Repeati298 – 333HEAT 1Add BLAST36
Repeati1014 – 1050HEAT 2Add BLAST37
Repeati1736 – 1769TPR 1Add BLAST34
Repeati2903 – 2935TPR 2Add BLAST33
<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>Domaini2922 – 3555FATPROSITE-ProRule annotationAdd BLAST634
Repeati2936 – 2964TPR 3Add BLAST29
Repeati2965 – 2998TPR 4Add BLAST34
Repeati3711 – 3748TPR 5Add BLAST38
Domaini3764 – 4031PI3K/PI4KPROSITE-ProRule annotationAdd BLAST268
Domaini4112 – 4144FATCPROSITE-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>Regioni1516 – 1551Interaction with C1DBy similarityAdd BLAST36
Regioni1516 – 1551Leucine-zipperAdd BLAST36
Regioni2448 – 3228KIP-bindingBy similarityAdd BLAST781

<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
COG5032 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000168371

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q8WN22

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, 2 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_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>Sequencei

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

Q8WN22-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFSSSQIPRV FLIPSRRELR LVLQLQESLS AGDRCSAAMA SYQLTRGLGQ
60 70 80 90 100
ECVLSSDPAV LALQTSLVFS KDFGLLVFVR KSLSIDEFRD CREEVLKFLY
110 120 130 140 150
IFLEKIGQKI TPYSLDIKTT CTSVYTKDKA AKCKIPALDL LIKLLQTLRS
160 170 180 190 200
SRLMDEFSIG ELFNKFYGEL ALKTKIQDTV LEKIYELLGV LAEVHPSEMI
210 220 230 240 250
NNSEKLFRAF LGELKIQMTS AIREPKLPVL AGCLKGLSSL MCNFTKSMEE
260 270 280 290 300
DPQTSREIFD FALKAIRPQI DLKRYAVPLA GLCLFTLHAS QFSTCLLDNY
310 320 330 340 350
VSLFEVLSKW CSHTNVEMKK AAHSALESFL KQVSFMVAKD AEMHKSKLQY
360 370 380 390 400
FMEQFYGIIR NMDSNSKDLS IAIRGYGLFA GPCKVINAKD VDFMYIELIQ
410 420 430 440 450
RCKQLFLTQI DTVDDHVYHM PSFLQSIASV LLYLDRVPEV YTPVLEHLMV
460 470 480 490 500
AQIDSFPQYS PKMQSVCCKA LVKVFLALGG KGPVLWNCIS TVVHQGLIRI
510 520 530 540 550
CSKPVILQKG VESEPEEYRA SGEVRTGKWK VPTYKDYLDL FRSLLSCDQM
560 570 580 590 600
MDSLLADEAF LFVNSSLQNL NRLLYDEFVK SVLKIIEKLD LTLEKRNVGE
610 620 630 640 650
HEDENEATGV WVIPTSDPAA NLHPAKPKDF SAFINLVEFC RDILPEKHIE
660 670 680 690 700
FFEPWVYSFA YELILQSTRL PLISGFYKLL SVAVRNAKKI KYFEGVGMKS
710 720 730 740 750
QTQAPKDPEK YSCFALFAKF GKEVTVKMKQ YKDELLASCL TFILSLPHDI
760 770 780 790 800
IELDIRAYIP ALQMAFKLGL SYTPLAEVGL NALEEWSVCI CKHIIQPHYK
810 820 830 840 850
DILPSLDGYL KTSALSDETK NSWEVSAPSQ AAQKGFNQVV LKHLKKTKNI
860 870 880 890 900
SSNEALSLEE IRIRVVQMLG FLGGQINKNL LTATSSDEMM KKCVAWDREK
910 920 930 940 950
RLSFAVPFIE MKPVIYLDVF LPRVTELALS ASDRQTKVAA CELLHSMVMF
960 970 980 990 1000
TLGKATQMPE CGQGFPPMYQ LYKRTFPALL RLACDVDQVT RQLYEPLVMQ
1010 1020 1030 1040 1050
LIHWFTNNKK FESQDTVALL ETILDGIVDP VDSTLRDFCG RCIREFLKWS
1060 1070 1080 1090 1100
IKQTTPQQQE KSPVNTKSLF KRLYSFALHP NAFKRLGASL AFNNIYREFR
1110 1120 1130 1140 1150
EEESLVEQFV FEALVTYLES LALAHTDEKP LGTIRQCCDA IDHLRHIIEK
1160 1170 1180 1190 1200
KHVSLNKVKK RRRPRGFPPS ASLCLLDMVQ WLLAHCGRPQ TECRHKSIEL
1210 1220 1230 1240 1250
FYKFVPLLPG NKSPSLWLKD ILKNKDTSFL INTFEGGGGS CDRPSGILVQ
1260 1270 1280 1290 1300
PTLFHLQGPF SLRAALQWMD MLLAALECYN TFIEEKTLKA PDVLGTETQS
1310 1320 1330 1340 1350
SLWKAVAFFL DNIAMHDITA AEKCFGTGAA GHRPSPQEGE RYNYSKCTIV
1360 1370 1380 1390 1400
VRIMEFTTTL LNTSPDGWKL LEEDLCNNKN FMTLLVKILC QPSSIGFNIG
1410 1420 1430 1440 1450
DVLVMNHLPD VCVNLMKALK KSPYKDTLEM CLKEKITVQS IEELCAVDLY
1460 1470 1480 1490 1500
GPDAYVDRAT LASVVSACKQ LHRAGVLHVV LPSQSADQRH SVGIKLLFLV
1510 1520 1530 1540 1550
YKSIAPGDER EYFPSLDPSC KRLASGLLEL AFAFGGLCEH LVDLLLDTAV
1560 1570 1580 1590 1600
LSMPASGESQ RNMVSFSHGE YFYSLFSEII NTELLRNLDM TVLKLMKSSV
1610 1620 1630 1640 1650
DNPKMVSAIL NGMLDQSFRD RASRKQQGLK LASTILHNWK KWDSWWAKDS
1660 1670 1680 1690 1700
APESKTAVLT LLAKILQIDS SVSFNTNHSA FPEVFTTYTS LLADSNLGLH
1710 1720 1730 1740 1750
LMGQAVILLP FFTNLTGGNL EDLEHVLEKL IVSNFPMKSE EFPVGTLRYS
1760 1770 1780 1790 1800
NYVDCMKKFL DALELSQSPV LLQLMAEILC REQQHVMEEL FQSTFKKIAR
1810 1820 1830 1840 1850
KSSCVTQLAL LESVYRMFKR DDLLSNVTRQ AFVDRSLLTL LWHCGLNALR
1860 1870 1880 1890 1900
EFFGKIVVET IDVLKSRFTK LNESTFDTQI TKKMGFYKML DVMYSRLSKD
1910 1920 1930 1940 1950
DVHSKESKIN QVFHGSCITE GNELTKTLIK LCYDAFTENM AGENQLLERR
1960 1970 1980 1990 2000
RLYHCAAYNC AISVICCVFT ELKFYQGFLF SEKPEKNLLI LENLIDLKRC
2010 2020 2030 2040 2050
YTFPIEVEVP MERRKKYIEI RKEAREAVNG DSDGPHYLSS LSYLADSSLS
2060 2070 2080 2090 2100
EEMSQFDFST GVQSYSYGSQ DPKSTHGHFR RREHKDPMVQ DAVLELEMDE
2110 2120 2130 2140 2150
LNQHECMATM TALIKHMQRN QILSKDEGSV PRNLPPWMKF LHDKLGNPSV
2160 2170 2180 2190 2200
SLNIRLFLAK LVINTEEVFR PYAKYWLSPL LQLVVSENNG GEGIHYMVVE
2210 2220 2230 2240 2250
IVVTVLSWTG LATPVGVPKD EVLANRLLHF LMEHVFHQKR AVFRHNLEII
2260 2270 2280 2290 2300
KTLVECWKDC LSVPYRLIFE KFSSKDPNSK DNSVGIQLLG IVMANNLPPY
2310 2320 2330 2340 2350
DPKCGIERIK YFEALVSNMS FVKYKEVYAA AAEVLGLTLR YITERENILE
2360 2370 2380 2390 2400
NVVYELVIKQ LKQHQNTMED KFIVCLNKVV KNFPPLADRF MNAVFFLLPK
2410 2420 2430 2440 2450
FHGVMKTLCL EVVLCRAEEI TNIYLELKSK DFIQVMRHRD DERQKVCLDI
2460 2470 2480 2490 2500
IYKMMAKLKP VELRDLLNSV VEFISHPSPV CREQMYNILM WIHDNYRDPE
2510 2520 2530 2540 2550
SQADDDSREV FKLAKDVLIQ GLIDENAGLQ LIIRNFWSHE TRLPSNTLDR
2560 2570 2580 2590 2600
LLALNSLYSP KIEVHFLSLA TDFLLEMTSL SPDYANPVFE HPLSECEFQE
2610 2620 2630 2640 2650
YTIDSDWRFR STVLTPMFIE TQASQSTLQT RTQERSLPAQ GVMARQIRAT
2660 2670 2680 2690 2700
QQQYDFTPTQ TADGRSSFNW LTGSSIDPLV DYTVSSSDSS SSSLLFAQKR
2710 2720 2730 2740 2750
NEKSQRAPLK SVGPDFGEKK LGLPGDKVDN KAKGIDNRTE ILRLRRRFIK
2760 2770 2780 2790 2800
DQEKLSLIYA RKGIAEQKRE KEIKSELKMK HDAQVILYRS YRQGDLPDIQ
2810 2820 2830 2840 2850
IKYSSLVTPL QAVAQRDPVV AKQLFGSLFS GIIKEMDKYK TMSEKNNITQ
2860 2870 2880 2890 2900
KLLQDFSHFL NSTFSFFPPF VSCIQEISCQ HTDLLSLDPG SIRASCLASL
2910 2920 2930 2940 2950
QQPVGVRLLE EALLHLGPQE PPAKQFKGRM RVSPDVVRWM ELAKLYRSIG
2960 2970 2980 2990 3000
EYDILRGIFS SEIGTKQITQ SAIFAEARSD YSEAAKQYNE ALNKEEWVDG
3010 3020 3030 3040 3050
EPTEAEKDFW ELASLDCYNQ LAEWKSLAYC SIVSVDNENP PDLNKMWSEP
3060 3070 3080 3090 3100
FYRETYLPYM IRSKLKLLLQ GEADQSLLTF IDEAVNKDLQ KALIELHYSQ
3110 3120 3130 3140 3150
ELSLLYILQD DIDRAKYYIE NCIQIFMQNY SSIDVLLHRS RLTKLQSVQT
3160 3170 3180 3190 3200
MIEIQEFISF ISRQGNLSSQ APLKRLLKSW TNRYPDARMD PVHIWDDIIT
3210 3220 3230 3240 3250
NRCFFLSKIE EKLTLPLGDH SLSMDEERDS SDKMEVQEQG EEVCSLIKNC
3260 3270 3280 3290 3300
MFSMKMKMVE SARKQHNFSL AMKLLKELRR ESKTRDDWQV KWVHTYCRLS
3310 3320 3330 3340 3350
HSRIQGQSCL QQILSALKTV SLLAGESTSS YFSKNVLAFH DQNILLGTTY
3360 3370 3380 3390 3400
SIIANALRRE PACLAEIEES RARRILDLSG SSLENAEKVI AVLYQRAFHH
3410 3420 3430 3440 3450
LSEAVRTAEE EAQPSLRGQG PVASLTDAYM TLADFCDQQL RKEEESASVT
3460 3470 3480 3490 3500
ESVELQTYPG LVVDNMLKAL KLHSSEARLK FPRLLQIIEL YPEETLSLMT
3510 3520 3530 3540 3550
KEISSTPCWQ FIGWISHMVA LLDQEEAVAV QCTVEEIADN YPQAIVYPFI
3560 3570 3580 3590 3600
ISSESYSFKD TSTGHKNKEF VARIKTKLDL GGVIQDFISA LEQLSNPEML
3610 3620 3630 3640 3650
FKDWTDDMKA ELAKNPVSKK NIEKMYERMY AALGDLRAPG LGAFRRRFIQ
3660 3670 3680 3690 3700
VFGKEFDKHF GKGGSKLPGM KLRDFGSITD SLFYKMCTDS KPPGNLKECS
3710 3720 3730 3740 3750
PWMSDFKVEF LRNELEIPGQ YDGKGKPLPE YHARIAGFDE RIKVMASIRK
3760 3770 3780 3790 3800
PKRIIIRGRD EKEYPLLVKG GEDLRQDQRI EQLFEVMNVL LSQDTACSQR
3810 3820 3830 3840 3850
NMQLKTYHVI PMTSRLGLIE WIENTLTLKD FLLSNMSREE KAAYTSDPKA
3860 3870 3880 3890 3900
PPCEYRDWLA KMSGKYDVGA YMSMFKAASR TETVTSFRRR ESRVPADLLK
3910 3920 3930 3940 3950
RAFLKMSTGP AAFLALRSHF ASSHALMCIS HWILGIGDRH LNNFMVSMET
3960 3970 3980 3990 4000
GGLIGIDFGH AFGSATQFLP VPELMPFRLT RQFINLMLPM KEAGVVYSIM
4010 4020 4030 4040 4050
VHALRAFRSH SDLLTNTMDV FVKEPSFDWK NFEQKMLKKG GSWIQEINVT
4060 4070 4080 4090 4100
EKNWYPRQKI HYAKRKLAGA NPAVITCDEL FLGHEKALAF GDYVAVARGS
4110 4120 4130 4140
KDHNIRAQQP ENGLSEEAQV KCLIDQATDP NILGRTWIGW EPWM
Length:4,144
Mass (Da):473,061
Last modified:March 1, 2002 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i27CE0079556E094E
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AF448227 mRNA Translation: AAL40979.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF448227 mRNA Translation: AAL40979.1

3D structure databases

Database of comparative protein structure models

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ModBasei
Search...

SWISS-MODEL Interactive Workspace

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SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

STRINGi9612.ENSCAFP00000009842

Proteomic databases

PaxDbiQ8WN22
PRIDEiQ8WN22

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG0891 Eukaryota
COG5032 LUCA
HOGENOMiHOG000168371
InParanoidiQ8WN22

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, 2 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
Search...

MobiDB: a database of protein disorder and mobility annotations

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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_CANLF
<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: Q8WN22
<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: March 7, 2006
Last sequence update: March 1, 2002
Last modified: June 5, 2019
This is version 119 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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