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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-Experimental evidence at transcript leveli

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, C1D, c-Abl/ABL1, histone H1, HSPCA, c-jun/JUN, p53/TP53, PARP1, POU2F1, DHX9, SRF, 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. 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 machanism (By similarity).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Inhibited by wortmannin. Activity of the enzyme seems to be attenuated by autophosphorylation (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Biological rhythms, DNA damage, DNA recombination, DNA repair

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Names & Taxonomyi

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
Gene namesi
Name:PRKDC
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Unplaced

Subcellular locationi

  • Nucleus By similarity
  • Nucleusnucleolus By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

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.

Keywords - Diseasei

SCID

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 41444144DNA-dependent protein kinase catalytic subunitPRO_0000225632Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei127 – 1271N6-acetyllysineBy similarity
Modified residuei521 – 5211PhosphoserineBy similarity
Modified residuei851 – 8511PhosphoserineBy similarity
Modified residuei903 – 9031PhosphoserineBy similarity
Modified residuei1075 – 10751PhosphoserineBy similarity
Modified residuei1219 – 12191N6-acetyllysineBy similarity
Modified residuei1983 – 19831N6-acetyllysineBy similarity
Modified residuei2069 – 20691Phosphoserine; by autocatalysisBy similarity
Modified residuei2271 – 22711N6-acetyllysineBy similarity
Modified residuei2547 – 25471PhosphothreonineBy similarity
Modified residuei2621 – 26211Phosphothreonine; by autocatalysisBy similarity
Modified residuei2624 – 26241Phosphoserine; by autocatalysisBy similarity
Modified residuei2650 – 26501Phosphothreonine; by autocatalysisBy similarity
Modified residuei2659 – 26591Phosphothreonine; by autocatalysisBy similarity
Modified residuei2805 – 28051PhosphoserineBy similarity
Modified residuei3221 – 32211PhosphoserineBy similarity
Modified residuei3257 – 32571N6-acetyllysineBy similarity
Modified residuei3276 – 32761N6-acetyllysineBy similarity
Modified residuei3654 – 36541N6-acetyllysineBy similarity
Modified residuei3658 – 36581N6-acetyllysineBy similarity
Modified residuei3747 – 37471PhosphoserineBy similarity
Modified residuei3837 – 38371PhosphoserineBy similarity
Modified residuei4042 – 40421PhosphoserineBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Sitei2033 – 20342Cleavage; by caspase-3By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ8WN22.
PRIDEiQ8WN22.

Interactioni

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 ubiquitinylation and degradation.By similarity

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000009842.

Structurei

3D structure databases

ProteinModelPortaliQ8WN22.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati298 – 33336HEAT 1Add
BLAST
Repeati1014 – 105037HEAT 2Add
BLAST
Repeati1736 – 176934TPR 1Add
BLAST
Domaini2899 – 3555657FATPROSITE-ProRule annotationAdd
BLAST
Repeati2903 – 293533TPR 2Add
BLAST
Repeati2936 – 296429TPR 3Add
BLAST
Repeati2965 – 299834TPR 4Add
BLAST
Repeati3711 – 374838TPR 5Add
BLAST
Domaini3764 – 4031268PI3K/PI4KPROSITE-ProRule annotationAdd
BLAST
Domaini4112 – 414433FATCPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1516 – 155136Interaction with C1DBy similarityAdd
BLAST
Regioni1516 – 155136Leucine-zipperAdd
BLAST
Regioni2448 – 3228781KIP-bindingBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the PI3/PI4-kinase family.Curated
Contains 1 FAT domain.PROSITE-ProRule annotation
Contains 1 FATC domain.PROSITE-ProRule annotation
Contains 2 HEAT repeats.Curated
Contains 1 PI3K/PI4K domain.PROSITE-ProRule annotation
Contains 5 TPR repeats.Curated

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG0891. Eukaryota.
COG5032. LUCA.
HOGENOMiHOG000168371.
HOVERGENiHBG053681.
InParanoidiQ8WN22.

Family and domain databases

Gene3Di1.10.1070.11. 3 hits.
InterProiIPR016024. ARM-type_fold.
IPR003152. FATC_dom.
IPR011009. Kinase-like_dom.
IPR012582. NUC194.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
[Graphical view]
PfamiPF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF08163. NUC194. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
[Graphical view]
SMARTiSM01343. FATC. 1 hit.
SM01344. NUC194. 1 hit.
SM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 10 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS51189. 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.
[Graphical view]

Sequencei

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
Checksum:i27CE0079556E094E
GO

Sequence databases

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

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliQ8WN22.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000009842.

Proteomic databases

PaxDbiQ8WN22.
PRIDEiQ8WN22.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG0891. Eukaryota.
COG5032. LUCA.
HOGENOMiHOG000168371.
HOVERGENiHBG053681.
InParanoidiQ8WN22.

Family and domain databases

Gene3Di1.10.1070.11. 3 hits.
InterProiIPR016024. ARM-type_fold.
IPR003152. FATC_dom.
IPR011009. Kinase-like_dom.
IPR012582. NUC194.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
[Graphical view]
PfamiPF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF08163. NUC194. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
[Graphical view]
SMARTiSM01343. FATC. 1 hit.
SM01344. NUC194. 1 hit.
SM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 10 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS51189. 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.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPRKDC_CANLF
AccessioniPrimary (citable) accession number: Q8WN22
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: March 1, 2002
Last modified: July 6, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.