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Protein

DNA-dependent protein kinase catalytic subunit

Gene

Prkdc

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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.2 Publications

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

  • ATP binding Source: UniProtKB-KW
  • DNA-dependent protein kinase activity Source: MGI
  • double-stranded DNA binding Source: MGI
  • enzyme binding Source: UniProtKB
  • poly(A) RNA binding Source: MGI
  • protein kinase activity Source: MGI
  • protein serine/threonine kinase activity Source: MGI
  • transcription factor binding Source: MGI

GO - Biological processi

  • B cell lineage commitment Source: MGI
  • brain development Source: MGI
  • cell proliferation Source: MGI
  • cellular response to insulin stimulus Source: MGI
  • double-strand break repair Source: MGI
  • double-strand break repair via nonhomologous end joining Source: MGI
  • ectopic germ cell programmed cell death Source: MGI
  • heart development Source: MGI
  • immunoglobulin V(D)J recombination Source: MGI
  • intrinsic apoptotic signaling pathway in response to DNA damage Source: MGI
  • lymphocyte differentiation Source: MGI
  • negative regulation of apoptotic process Source: MGI
  • negative regulation of cellular senescence Source: Ensembl
  • negative regulation of immunoglobulin production Source: Ensembl
  • negative regulation of protein phosphorylation Source: UniProtKB
  • negative regulation of response to gamma radiation Source: Ensembl
  • peptidyl-serine phosphorylation Source: MGI
  • positive regulation of apoptotic process Source: MGI
  • positive regulation of developmental growth Source: Ensembl
  • positive regulation of fibroblast proliferation Source: Ensembl
  • positive regulation of immune system process Source: Ensembl
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • pro-B cell differentiation Source: MGI
  • protein destabilization Source: MGI
  • regulation of circadian rhythm Source: UniProtKB
  • regulation of smooth muscle cell proliferation Source: UniProtKB
  • response to activity Source: Ensembl
  • response to gamma radiation Source: MGI
  • response to ionizing radiation Source: MGI
  • rhythmic process Source: UniProtKB-KW
  • signal transduction involved in mitotic G1 DNA damage checkpoint Source: UniProtKB
  • somitogenesis Source: MGI
  • spleen development Source: Ensembl
  • T cell differentiation in thymus Source: MGI
  • T cell lineage commitment Source: MGI
  • T cell receptor V(D)J recombination Source: MGI
  • telomere capping Source: MGI
  • telomere maintenance Source: MGI
  • thymus development Source: Ensembl
  • V(D)J recombination Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Biological rhythms, DNA damage, DNA repair

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-5693571. Nonhomologous End-Joining (NHEJ).

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
Alternative name(s):
p460
Gene namesi
Name:Prkdc
Synonyms:Xrcc7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:104779. Prkdc.

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

Disease mutation, SCID

Chemistry databases

ChEMBLiCHEMBL2176779.
GuidetoPHARMACOLOGYi2800.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002255991 – 4128DNA-dependent protein kinase catalytic subunitAdd BLAST4128

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei117N6-acetyllysineBy similarity1
Modified residuei511PhosphoserineBy similarity1
Modified residuei686PhosphoserineBy similarity1
Modified residuei840PhosphoserineBy similarity1
Modified residuei891PhosphoserineBy similarity1
Modified residuei1062PhosphoserineBy similarity1
Modified residuei1206N6-acetyllysineBy similarity1
Modified residuei1967N6-acetyllysineBy similarity1
Modified residuei2053Phosphoserine; by autocatalysisBy similarity1
Modified residuei2255N6-acetyllysineBy similarity1
Modified residuei2531PhosphothreonineBy similarity1
Modified residuei2605Phosphothreonine; by autocatalysisBy similarity1
Modified residuei2608Phosphoserine; by autocatalysisBy similarity1
Modified residuei2634Phosphothreonine; by autocatalysisBy similarity1
Modified residuei2643Phosphothreonine; by autocatalysisBy similarity1
Modified residuei3206PhosphoserineBy similarity1
Modified residuei3241N6-acetyllysineBy similarity1
Modified residuei3260N6-acetyllysineBy similarity1
Modified residuei3638N6-acetyllysineBy similarity1
Modified residuei3642N6-acetyllysineBy similarity1
Modified residuei3731PhosphoserineBy similarity1
Modified residuei3821PhosphoserineBy similarity1
Modified residuei4026PhosphoserineBy similarity1

Post-translational modificationi

Autophosphorylated on Ser-2053, Thr-2605, Thr-2634 and Thr-2643. Ser-2053 and Thr-2605 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.1 Publication
Polyubiquitinated by RNF144A, leading to proteasomal degradation.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei2017 – 2018Cleavage; by caspase-3By similarity2

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

EPDiP97313.
MaxQBiP97313.
PaxDbiP97313.
PeptideAtlasiP97313.
PRIDEiP97313.

PTM databases

iPTMnetiP97313.
PhosphoSitePlusiP97313.

Expressioni

Gene expression databases

BgeeiENSMUSG00000022672.
GenevisibleiP97313. MM.

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 SETX (By similarity). Interacts with CRY1 and CRY2; negatively regulates CRY1 phosphorylation (PubMed:24158435). Interacts with NR4A3; the DNA-dependent protein kinase complex DNA-PK phosphorylates and activates NR4A3 and prevents NR4A3 ubiquitinylation and degradation (By similarity).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
EGFRP005334EBI-2272005,EBI-297353From a different organism.

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • transcription factor binding Source: MGI

Protein-protein interaction databases

BioGridi202371. 7 interactors.
IntActiP97313. 7 interactors.
MINTiMINT-4108568.
STRINGi10090.ENSMUSP00000023352.

Chemistry databases

BindingDBiP97313.

Structurei

3D structure databases

ProteinModelPortaliP97313.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati288 – 323HEAT 1Add BLAST36
Repeati1001 – 1037HEAT 2Add BLAST37
Repeati1050 – 1086HEAT 3Add BLAST37
Repeati1720 – 1753TPR 1Add BLAST34
Domaini2884 – 3539FATPROSITE-ProRule annotationAdd BLAST656
Repeati2921 – 2954TPR 2Add BLAST34
Repeati2956 – 2983TPR 3Add BLAST28
Domaini3747 – 4015PI3K/PI4KPROSITE-ProRule annotationAdd BLAST269
Domaini4096 – 4128FATCPROSITE-ProRule annotationAdd BLAST33

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1501 – 1536Interaction with C1DBy similarityAdd BLAST36
Regioni1501 – 1536Leucine-zipperAdd BLAST36
Regioni2432 – 3213KIP-bindingBy similarityAdd BLAST782

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 3 HEAT repeats.Curated
Contains 1 PI3K/PI4K domain.PROSITE-ProRule annotation
Contains 3 TPR repeats.Curated

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG0891. Eukaryota.
COG5032. LUCA.
GeneTreeiENSGT00830000128321.
HOVERGENiHBG053681.
InParanoidiP97313.
KOiK06642.
OMAiLVEQFVF.
OrthoDBiEOG091G0015.
TreeFamiTF324494.

Family and domain databases

Gene3Di1.10.1070.11. 3 hits.
1.25.10.10. 6 hits.
InterProiIPR011989. ARM-like.
IPR016024. 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. 9 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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced.
Isoform 1 (identifier: P97313-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAEEGTGVRC WLLQLQEFLS AADRCSAAGA SYQLIRSLGQ ECVLSTSSAV
60 70 80 90 100
QALQISLVFS RDFGLLVFIR KSLSIEDFRD CREEALKFLC VFLEKIDQKV
110 120 130 140 150
MHYSLDIKNT CTSVYTKDRT AKCKIPALDL LIKLLQILRS TRLMDEFKIG
160 170 180 190 200
ELFNKFYGEL ASKSKLPDTV LEKVYELLGV LGEVHPSEMI NHSENLFRAF
210 220 230 240 250
LGELKTQMTS TVREPKFPVL AGCLKGLSSL LCNFTKSMEE DPQTSKEIFG
260 270 280 290 300
FTFKAIRPQI EMKRYAVPLA GLRLLTLHAS QFTACLLDNY ITLFEVLSKW
310 320 330 340 350
CSHTNVELKK AAHSALESFL RQISFTVAED AELHKSRLKY FMEQFYGIIR
360 370 380 390 400
NTDSNNKELA IAIRGYGLFA GPCKVINAKD VDFMYVELIQ RCKQMFLTHA
410 420 430 440 450
DASEDHVYQM PSFLQSIASV LLYLDTVPEV YTPVLEHLMV VQIDSFPQYS
460 470 480 490 500
PKMQLVCCKA IIKLFLALSE KGPVHWNCIS AVVHQGLIRI CSKPVVLQKD
510 520 530 540 550
VESRSDNRSA SEEVRTGRWK VPTYKDYVDL FQHLLGCDQM EDFILGDETF
560 570 580 590 600
LFVNSSLKSL NHLLYDEFIR SVLKIVEKLD LTLEKQTVGE QEDGSTADVW
610 620 630 640 650
VIPTSDPAAN LHPAKPSDFS ALINLVEFCR EILPRKHVGF FEPWVYSFAY
660 670 680 690 700
ELILQSTRLP LISGFYKLLS IAVKNARKIK YFEGISPKSL KHSPEDTEKY
710 720 730 740 750
SCFALFAKFG KEVSVKMKQY KDELLASCLT FVLSLPHDII ELDVRAYVPA
760 770 780 790 800
LQMAFKLGLS HMPLAEIGLH ALKEWSVHID KSILQPYYKD ILPCLDGYLN
810 820 830 840 850
TSTLSDETKS HWGLSALSRA AQKGFNRHVV KHLKRTRNSS PDEALSLEEI
860 870 880 890 900
RIKVVQILGS LGGQINKSLV TATSGERMKK YVAWDAERRL SFAVPFREMK
910 920 930 940 950
PVIYLDVFLP RVTELALSAS DRQTKVAACE LLHSMVMFML GRATQMPEGQ
960 970 980 990 1000
GLPPMYQLYK HTFPVLLQLA CDVDQVTRQL YEPLVMQLIH WLTNNKKFES
1010 1020 1030 1040 1050
QDTVALLEAI LDGIVDPVDS TLRDFCGRCV QEFLKWSIKQ TTPQQQEKSP
1060 1070 1080 1090 1100
VNSKSLFKRL YSLALHPNAF KRLGAALAFN HIYKEFREEG SLVEQFVFEA
1110 1120 1130 1140 1150
LVTYMESLAL AHEDEKSLGT VQQCCDAIDH LRRIIEKKHV SLNKAKKRRL
1160 1170 1180 1190 1200
PQGFPPLTSL CLLDLVEWLL AHCGRPQTEC RHKSMELFYK FVPLLPGNKS
1210 1220 1230 1240 1250
PSLWLKDLIK KKGISFLINT FEGGASSSDQ PAGILAQPTL VYLQGPISLR
1260 1270 1280 1290 1300
GVLQWLDLLL AALECYNTFI EKETVQGQEV LGAEVQSSLL KSVAFFLESI
1310 1320 1330 1340 1350
ATHSARAVEQ RFGSGAPGPP SLHEEEKYNY SKCTVLVRIM EFTTTLLIAS
1360 1370 1380 1390 1400
PEDCKLLEKD LCNTNLMQVL VKMICEPMSL GFNIGDVQVM NHLPSICVNL
1410 1420 1430 1440 1450
LKALRKSPYR DMLETHLKEK VTVQSVEELC SINLCSSGAR QERSKLLSIL
1460 1470 1480 1490 1500
SACKQLHKAG FSHVISPSQS TALNHSVGMR LLSLVYKGIV PAEERQCLQS
1510 1520 1530 1540 1550
LDPSCKSLAN GLLELAFGFG GLCDHLVSLL LNSAMLSTQY LGSSQRNISF
1560 1570 1580 1590 1600
SHGEYFYSLF SEVINSELLK NLDIAVSRLM ESSSDNPKMV STVLNGMLDT
1610 1620 1630 1640 1650
SFRDRAVQKH QGLKLATAIL QNWRKCDSWW APDSAPESKT TVLSLLAKML
1660 1670 1680 1690 1700
QIDSALSFDT NHSSFSEIFT TYASLLADTK LGLHLKGQAI ILLPFFTSLR
1710 1720 1730 1740 1750
EGSLENLKHI LEKLIVCNFP MKSDEFPPDS LKYNNYVDCM KKFLDALELS
1760 1770 1780 1790 1800
QSPMLFQLMT DILCREQRHI MEELFQTTFK RIARQSPCVT QLNLLESVYT
1810 1820 1830 1840 1850
MFRKADLPSN VTRQAFVDRS LLTLLWHCDL DTLKEFFSRI VVDAIDVLKS
1860 1870 1880 1890 1900
RFTKLNEFTF DTQITKKMCY YKMLAVMYSR LLKDDVHSKE AKINQAFHGS
1910 1920 1930 1940 1950
RVAEGNELTK TLLKLCHDAF TENMVGESQL LEKRRLYHCA AYNCAISLIS
1960 1970 1980 1990 2000
CVFNELKFYQ GFLFNEKPEK NLFIFENLID LKRCYTFPIE VEVPMERKKK
2010 2020 2030 2040 2050
YIEIRKEARD AANGASGSPH YMSSLSYLTD SSLSEEMSQF DFSTGVQSYS
2060 2070 2080 2090 2100
YSSQDRKPTT GHFQRREHQD SMTQDDIMEL EMDELNQHEC MAPMIALIKH
2110 2120 2130 2140 2150
MQRNVIAPKG EEGSIPKDLP PWMKFLHDKL GNASVSLNIR LFLAKLVINT
2160 2170 2180 2190 2200
EEVFRPYAKH WLSPLLQLAV CENNREGIHY MMVEIVATIL SWTGLATPTG
2210 2220 2230 2240 2250
VPKDEVLANR LLRFLMKHVF HPKRAVFRHN LEIIKTLVEC WKECLSIPYR
2260 2270 2280 2290 2300
LIFEKFSHKD PNSKDNSVGI QLLGIVIANN LPPYDPNCDI TSAMYFEALV
2310 2320 2330 2340 2350
NNMSFVKYKE VYAAAAEVLG LILQYITERK HVIAELVCEL VIKQLKQHQN
2360 2370 2380 2390 2400
TMEDKFIVCL NKIAKGFPPL ADRFLNALFF LLPKFHGVMK TLCLEVVLCR
2410 2420 2430 2440 2450
AEEITGLYLQ LKSKDFLQVM RHRDDERQKV CLDIVYKMVA KLKPIELREL
2460 2470 2480 2490 2500
LNPVVEFVSH PSPTCREQMY NILMWIHDNY RDQESQNDED SQEIFKLAKD
2510 2520 2530 2540 2550
VLIQGLIDEN VGLQLIIRNF WSHETRLPSN TLDRLLALNS LYSPKIEVHF
2560 2570 2580 2590 2600
LSLATNFLLE MTRMSPDYLN PIFEHPLSEC EFQEYTIDPD WRFRSTVLTP
2610 2620 2630 2640 2650
MFIETQASPS ILHTQTQEGP LSDQRQKPGQ VRATQQQYDF TPTQASVERS
2660 2670 2680 2690 2700
SFDWLTGSSI DLLADHTVFS SETLSSSLLF SHKRTEKSQR MSCKSVGPDF
2710 2720 2730 2740 2750
GTKKLGLPDD EVDNQVKSGT PSQADILRLR RRFLKDREKL SLLYAKRGLM
2760 2770 2780 2790 2800
EQKLEKDIKS EFKMKQDAQV VLYRSYRHGD LPDIQIQHSG LITPLQAVAQ
2810 2820 2830 2840 2850
KDPIIAKQLF SSLFSGILKE MNKFKTTSEK NIITQNLLQD FNRFLNTTFL
2860 2870 2880 2890 2900
FFPPFVSCIQ EISCQHPDFL TLDPASVRVG CLASLQQPGG IRLLEEALLR
2910 2920 2930 2940 2950
LMPKEPPTKR VRGKTCLPPD VLRWMELAKL YRSIGEYDVL RGIFSSELGT
2960 2970 2980 2990 3000
TQDTQNALLA EARSDYCQAA KLYDEALNKL EWVDGEPTEA EKEFWELASL
3010 3020 3030 3040 3050
DCYNNLSKWK ELEYCSTVNI VSENSLDLSK MWSEPFYQET YLPYVIRSKL
3060 3070 3080 3090 3100
KLLLQGEGNQ SLLTFVDEAM NKELQKTVLE LQYSQELSLL YILQDDIDRA
3110 3120 3130 3140 3150
TYYIKNGIQI FMQNYSSIDV LLYRSRLAKL QSVQTLAEIE EFLSFICKHG
3160 3170 3180 3190 3200
DLSSLGPLRR LLKTWTSRYP DVVTDPMHIW DDIITNRCFF LSKIEERLTA
3210 3220 3230 3240 3250
PSGDHSMSVD EDEESIDREV YEPKEDVRCM LQSCRFTMKM KMIESAWKQS
3260 3270 3280 3290 3300
NFSLSMKLLK EMHKESKTRE IWRVQWLHSY SQLNHCRSHT QSPREQVLNM
3310 3320 3330 3340 3350
LKTITLLDES DISNYLNKNI QASCDQSILL GTTCRIMADA LSREPACLSD
3360 3370 3380 3390 3400
LEENKVNSIL TLSGSNAENT ETVITGLYQR AFHHLSKAVQ SAEEETQLSC
3410 3420 3430 3440 3450
WGHEAAAERA HAYMTLVGFC DQQLRKVEES ASQKTSAEME AYPALVVEKM
3460 3470 3480 3490 3500
LRALKLNSSE ARLKFPRLLQ IIEQYSEETL NIMTKEISSI PCWQFIGWIS
3510 3520 3530 3540 3550
HMMALLDKEE AIAVQHTVEE IADNYPQAII YPFIISSESY SFKNTSSGHN
3560 3570 3580 3590 3600
NKAFVERIKS KLDHGEVIHS FINALDQLSN PDLLFKDWVS DTKDELGKNP
3610 3620 3630 3640 3650
VNKKNIEKLY ERMYAALGDL RAPGLGPFRR RFIQAFGKEF VKSFGNGGSK
3660 3670 3680 3690 3700
LLTMKVDDFC KITGSLLVRM KKDSKLPGNL KEYSPWMSEF KAQFLKNELE
3710 3720 3730 3740 3750
IPGQYDGKSK PLPEYHVRIS GFDERVKVML SLRKPKRIVI RGHDEKEYPF
3760 3770 3780 3790 3800
LVKGGEDLRQ DQRIEQIFEV MNAILSQDAA CSQRNMQLRT YRVVPMTSRL
3810 3820 3830 3840 3850
GLIEWIENTM TLKDLLLSNM SQEEKVANNS DPKAPIRDYK DWLMKVSGKS
3860 3870 3880 3890 3900
DAGAYVLMYS RANRTETVVA FRRRESQVPP DLLKRAFVKM STSPEAFLAL
3910 3920 3930 3940 3950
RSHFASSHAL LCISHWLLGI GDRHLNNFMV AMETGSVIGI DFGHAFGSAT
3960 3970 3980 3990 4000
QFLPVPELMP FRLTRQFVSL MLPMKETGLM CTVMVHALRA FRSCAGLLTD
4010 4020 4030 4040 4050
TMEIFVKEPS FDWKSFEQTM LRKGGSWIQE INVTEKNWYP QHKIRYAKRK
4060 4070 4080 4090 4100
LAGANPAVIT CDELYLGHEA SSAFRSYTAV ARGNRDYNIR AQEPESGLSE
4110 4120
ETQVKCLVDQ ATDPNILGRT WEGWEPWM
Length:4,128
Mass (Da):471,471
Last modified:July 27, 2011 - v3
Checksum:iB143922D57F4331E
GO
Isoform 2 (identifier: P97313-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     842-852: DEALSLEEIRI → VRNPFLILYLK
     853-4128: Missing.

Note: No experimental confirmation available.
Show »
Length:852
Mass (Da):96,914
Checksum:i813746121866A369
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti3300M → T in BAA19566 (PubMed:9122213).Curated1
Sequence conflicti3300M → T in BAA28873 (PubMed:9582343).Curated1
Sequence conflicti3300M → T in BAA28875 (PubMed:9582343).Curated1
Sequence conflicti3300M → T in BAB91149 (PubMed:9339376).Curated1
Sequence conflicti3844M → V in AAB36939 (PubMed:8816463).Curated1
Sequence conflicti3844M → V in AAB36940 (PubMed:8816463).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti2140R → C.3 Publications1
Natural varianti3191L → P.1
Natural varianti4046 – 4128Missing in SCID. 1 PublicationAdd BLAST83

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_017361842 – 852DEALSLEEIRI → VRNPFLILYLK in isoform 2. 1 PublicationAdd BLAST11
Alternative sequenceiVSP_017362853 – 4128Missing in isoform 2. 1 PublicationAdd BLAST3276

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87521 mRNA. Translation: BAA19566.1.
AB007544 mRNA. Translation: BAA28873.1.
AB011543 mRNA. Translation: BAA28875.1.
AB030754 Genomic DNA. Translation: BAB91149.1.
AK084827 mRNA. Translation: BAE43387.1.
AK088981 mRNA. Translation: BAC40685.1.
AC111103 Genomic DNA. No translation available.
AC154586 Genomic DNA. No translation available.
CT010522 Genomic DNA. No translation available.
CT030649 Genomic DNA. No translation available.
AB000629 Genomic DNA. Translation: BAA34640.1.
DQ235257 mRNA. Translation: ABB36568.1.
DQ235258 mRNA. Translation: ABB36569.1.
D83786 mRNA. Translation: BAA12115.1.
U78157 mRNA. Translation: AAB36939.1.
U78158 mRNA. Translation: AAB36940.1.
CCDSiCCDS27978.1. [P97313-1]
PIRiJC6306.
RefSeqiNP_035289.2. NM_011159.2. [P97313-1]
UniGeneiMm.71.

Genome annotation databases

EnsembliENSMUST00000023352; ENSMUSP00000023352; ENSMUSG00000022672. [P97313-1]
GeneIDi19090.
KEGGimmu:19090.
UCSCiuc007yhs.1. mouse. [P97313-2]
uc007yht.1. mouse. [P97313-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87521 mRNA. Translation: BAA19566.1.
AB007544 mRNA. Translation: BAA28873.1.
AB011543 mRNA. Translation: BAA28875.1.
AB030754 Genomic DNA. Translation: BAB91149.1.
AK084827 mRNA. Translation: BAE43387.1.
AK088981 mRNA. Translation: BAC40685.1.
AC111103 Genomic DNA. No translation available.
AC154586 Genomic DNA. No translation available.
CT010522 Genomic DNA. No translation available.
CT030649 Genomic DNA. No translation available.
AB000629 Genomic DNA. Translation: BAA34640.1.
DQ235257 mRNA. Translation: ABB36568.1.
DQ235258 mRNA. Translation: ABB36569.1.
D83786 mRNA. Translation: BAA12115.1.
U78157 mRNA. Translation: AAB36939.1.
U78158 mRNA. Translation: AAB36940.1.
CCDSiCCDS27978.1. [P97313-1]
PIRiJC6306.
RefSeqiNP_035289.2. NM_011159.2. [P97313-1]
UniGeneiMm.71.

3D structure databases

ProteinModelPortaliP97313.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202371. 7 interactors.
IntActiP97313. 7 interactors.
MINTiMINT-4108568.
STRINGi10090.ENSMUSP00000023352.

Chemistry databases

BindingDBiP97313.
ChEMBLiCHEMBL2176779.
GuidetoPHARMACOLOGYi2800.

PTM databases

iPTMnetiP97313.
PhosphoSitePlusiP97313.

Proteomic databases

EPDiP97313.
MaxQBiP97313.
PaxDbiP97313.
PeptideAtlasiP97313.
PRIDEiP97313.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023352; ENSMUSP00000023352; ENSMUSG00000022672. [P97313-1]
GeneIDi19090.
KEGGimmu:19090.
UCSCiuc007yhs.1. mouse. [P97313-2]
uc007yht.1. mouse. [P97313-1]

Organism-specific databases

CTDi5591.
MGIiMGI:104779. Prkdc.

Phylogenomic databases

eggNOGiKOG0891. Eukaryota.
COG5032. LUCA.
GeneTreeiENSGT00830000128321.
HOVERGENiHBG053681.
InParanoidiP97313.
KOiK06642.
OMAiLVEQFVF.
OrthoDBiEOG091G0015.
TreeFamiTF324494.

Enzyme and pathway databases

ReactomeiR-MMU-5693571. Nonhomologous End-Joining (NHEJ).

Miscellaneous databases

PROiP97313.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000022672.
GenevisibleiP97313. MM.

Family and domain databases

Gene3Di1.10.1070.11. 3 hits.
1.25.10.10. 6 hits.
InterProiIPR011989. ARM-like.
IPR016024. 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. 9 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_MOUSE
AccessioniPrimary (citable) accession number: P97313
Secondary accession number(s): E9QN15
, O88187, P97928, Q307W9, Q3V2W8, Q8C2A7, Q9Z341
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 165 of the entry and version 3 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. 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.