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Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7

DescriptionSubName: Full=3-phosphoinositide-dependent protein kinase 1b {ECO:0000313|Ensembl:ENSDARP00000019085}; SubName: Full=Zgc:77318 {ECO:0000313|EMBL:AAH65959.1};
MyHits logo
MyHits synonymsQ6NZV1_DANRE , Q6NZV1 , 20A0FED4E0A79D6F
match map segment
ipat:PROTEIN_KINASE_ATP ipfam:PH_3 ipfam:Pkinase ismart:S_TKc ipat:PROTEIN_KINASE_ST iprf:PROTEIN_KINASE_DOM  
Legends: 1, ipat:PROTEIN_KINASE_ATP [T]; 2, ipat:PROTEIN_KINASE_ST [T].
ID   Q6NZV1_DANRE            Unreviewed;       537 AA.
AC   Q6NZV1;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   10-MAY-2017, entry version 120.
DE   SubName: Full=3-phosphoinositide-dependent protein kinase 1b {ECO:0000313|Ensembl:ENSDARP00000019085};
DE   SubName: Full=Zgc:77318 {ECO:0000313|EMBL:AAH65959.1};
GN   Name=pdpk1b {ECO:0000313|Ensembl:ENSDARP00000019085,
GN   ECO:0000313|ZFIN:ZDB-GENE-040426-1820};
GN   Synonyms=zgc:77318 {ECO:0000313|EMBL:AAH65959.1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|EMBL:AAH65959.1};
RN   [1] {ECO:0000313|EMBL:AAH65959.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo {ECO:0000313|EMBL:AAH65959.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSDARP00000019085}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000019085};
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSDARP00000019085, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000019085,
RC   ECO:0000313|Proteomes:UP000000437};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
RA   Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
RA   McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
RA   Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
RA   Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
RA   Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
RA   Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
RA   Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J.,
RA   Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P.,
RA   Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G.,
RA   Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D.,
RA   Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K.,
RA   Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C.,
RA   Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J.,
RA   Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S.,
RA   Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A.,
RA   Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D.,
RA   Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z.,
RA   Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J.,
RA   Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C.,
RA   Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C.,
RA   Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J.,
RA   Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
RA   Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
RA   Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
RA   Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the
RT   human genome.";
RL   Nature 496:498-503(2013).
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DR   EMBL; CU469584; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC065959; AAH65959.1; -; mRNA.
DR   RefSeq; NP_991262.1; NM_205699.1.
DR   UniGene; Dr.29812; -.
DR   STRING; 7955.ENSDARP00000019085; -.
DR   Ensembl; ENSDART00000003789; ENSDARP00000019085; ENSDARG00000018285.
DR   GeneID; 403000; -.
DR   KEGG; dre:403000; -.
DR   CTD; 403000; -.
DR   ZFIN; ZDB-GENE-040426-1820; pdpk1b.
DR   eggNOG; KOG0592; Eukaryota.
DR   eggNOG; ENOG410XRT8; LUCA.
DR   GeneTree; ENSGT00550000074819; -.
DR   HOGENOM; HOG000233026; -.
DR   HOVERGEN; HBG098357; -.
DR   KO; K06276; -.
DR   OMA; QENFTSH; -.
DR   OrthoDB; EOG091G06CX; -.
DR   TreeFam; TF105423; -.
DR   Reactome; R-DRE-114604; GPVI-mediated activation cascade.
DR   Reactome; R-DRE-1257604; PIP3 activates AKT signaling.
DR   Reactome; R-DRE-165158; Activation of AKT2.
DR   Reactome; R-DRE-202424; Downstream TCR signaling.
DR   Reactome; R-DRE-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
DR   Reactome; R-DRE-2871837; FCERI mediated NF-kB activation.
DR   Reactome; R-DRE-354192; Integrin alphaIIb beta3 signaling.
DR   Reactome; R-DRE-389357; CD28 dependent PI3K/Akt signaling.
DR   Reactome; R-DRE-392451; G beta:gamma signalling through PI3Kgamma.
DR   Reactome; R-DRE-444257; RSK activation.
DR   Reactome; R-DRE-5218920; VEGFR2 mediated vascular permeability.
DR   Reactome; R-DRE-5218921; VEGFR2 mediated cell proliferation.
DR   Reactome; R-DRE-5607764; CLEC7A (Dectin-1) signaling.
DR   Reactome; R-DRE-5625740; RHO GTPases activate PKNs.
DR   Reactome; R-DRE-6804757; Regulation of TP53 Degradation.
DR   Proteomes; UP000000437; Chromosome 24.
DR   Bgee; ENSDARG00000018285; -.
DR   GO; GO:0005622; C:intracellular; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR   CDD; cd01262; PH_PDK1; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR033931; PDK1-typ_PH.
DR   InterPro; IPR011993; PH_dom-like.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF14593; PH_3; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF50729; SSF50729; 2.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000437};
KW   Proteomics identification {ECO:0000213|PeptideAtlas:Q6NZV1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437}.
FT   DOMAIN       60    320       Protein kinase.
FT                                {ECO:0000259|PROSITE:PS50011}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        66     89       ipat:PROTEIN_KINASE_ATP [T]
FT   MYHIT       428    528       ipfam:PH_3 [T]
FT   MYHIT        61    308       ipfam:Pkinase [T]
FT   MYHIT        60    320       ismart:S_TKc [T]
FT   MYHIT       179    191       ipat:PROTEIN_KINASE_ST [T]
FT   MYHIT        60    320       iprf:PROTEIN_KINASE_DOM [T]
SQ   SEQUENCE   537 AA;  61490 MW;  20A0FED4E0A79D6F CRC64;
     MARATSQIYD VASLHSSVLI SCPSMVRGQQ DTPRLHGNSM EGPAPNAQPA QPRKKRPEDF
     RFGKILGEGS FSTVVLAKEH TTGKEYAIKI LEKRHIMKEN KAQYVKRERD IMSHLDHPFF
     VKLYFTFQDE EKLYFGLSYA KNGELLKYIR KIGSFDETCT RFYSAEIVCA LEYLHQKGII
     HRDLKPENIL LSEEMHIQIT DFGTAKQLSS DSKQARANSF VGTAQYVSPE LLTEKSACKS
     SDLWALGCII YQLVAGLPPF RAGNEYLIFQ KIIKLEYEFP EKFFPKAKDL VEQLLSLDSC
     KRIGCDEMGG YGPLKSHPFF ESVGWDDLHL QTPPKLTAYL PAMSEDDEDC YGNYDDLLSQ
     FSCMQVAQPG PAPLVPVTGE TSQPTYNPSP SVDQFIHIHE LDSNSMELDL QYSNEEKRIL
     LDKQSAANPW HQFVENNLIL KMGPVDKRKG LFARRRQLLL TEGPHLYYVD PVNKVLKGEI
     PWSPELRPEA KNFKTFFVHT PNRTYYLMDP SGNADKWCKK IQEVWRKIYH KHQSPSL
//